** ******************************************************************************* ** ** **************************** ** *** PROSITE ProRule file *** ** **************************** ** ** Release 2024_02 of 27-Mar-2024. ** ** ******************************************************************************* ** ** PROSITE is developed by the SIB Swiss Institute of Bioinformatics under ** the responsibility of Alan Bridge. ** ** This release was prepared by the PROSITE team: Delphine Baratin, Beatrice ** Cuche, Edouard de Castro, Nicole Redaschi and Christian Sigrist. ** ** See: https://prosite.expasy.org ** Email: prosite@expasy.org ** ** ******************************************************************************* ** ** PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and ** distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives ** CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html ** ** ******************************************************************************* // AC PRU00021; DC Domain; TR PROSITE; PS50844; AFP_LIKE; 1; level=0 XX Names: AFP-like domain Function: Undefined XX FT From: PS50844 FT DOMAIN from..to FT /note="AFP-like #" XX Chop: Nter=0; Cter=0; Size: 59-63; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q58465; Scope: Eukaryota; Euteleostomi Bacteria; Bacillus Archaea; Methanocaldococcus Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00022; DC Domain; TR PROSITE; PS01178; ANAPHYLATOXIN_2; 1; level=0 XX Names: Anaphylatoxin-like domain Function: Undefined XX DR PROSITE; PS01177; ANAPHYLATOXIN_1; 1; trigger=no XX case KW Disulfide bond end case FT From: PS01178 FT DOMAIN from..to FT /note="Anaphylatoxin-like #" FT DISULFID 1..26 FT Tag: disulf; Condition: C-x*-C FT DISULFID 2..33 FT Tag: disulf; Condition: C-x*-C FT DISULFID 15..34 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 32-43; Related: None; Repeats: 1-3; Topology: Not cytoplasmic; Example: P01032; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00023; DC Domain; TR PROSITE; PS50088; ANK_REPEAT; 1; level=0 XX Names: ANK repeat Function: Many ankyrin repeat regions are known to function as protein-protein interaction domains. XX XX DR PROSITE; PS50297; ANK_REP_REGION; 1; trigger=no XX KW ANK repeat XX FT From: PS50088 FT REPEAT from..to FT /note="ANK #" XX Chop: Nter=0; Cter=0; Size: 11-51; Related: RRU00006!!; Repeats: 1-27; Topology: Undefined; Example: P16157; Scope: Eukaryota Bacteria Archaea Viruses; Chordopoxvirinae Comments: None XX # Revision 1.10 2019/11/20 // AC PRU00024; DC Domain; TR PROSITE; PS50119; ZF_BBOX; 1; level=0 XX Names: Zinc finger B-box-type Function: It is found essentially in transcription factors, ribonucleoproteins and proto-oncoproteins, but no function is clearly assigned to this domain. XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50119 case and and and FT ZN_FING from..to FT /note="B box-type #" else case and and and FT ZN_FING from..to FT /note="B box-type #; atypical" else FT ZN_FING from..to FT /note="B box-type #; degenerate" end case FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 35 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 31-54; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q92021; Scope: Eukaryota Comments: None XX # Revision 1.16 2022/11/19 // AC PRU00025; DC Domain; TR PROSITE; PS50063; BH4_2; 1; level=0 XX Names: BH4 motif Function: Undefined XX DR PROSITE; PS01260; BH4_1; 1; trigger=no XX GO GO:0006915; P:apoptotic process XX KW Apoptosis XX FT From: PS50063 FT MOTIF from..to FT /note="BH4 #" XX Chop: Nter=0; Cter=0; Size: 17-21; Related: None; Repeats: 1; Topology: Undefined; Example: P41957; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00026; DC Domain; TR PROSITE; PS50197; BEACH; 1; level=0 XX Names: BEACH Function: Undefined XX FT From: PS50197 FT DOMAIN from..to FT /note="BEACH #" XX Chop: Nter=0; Cter=0; Size: 103-303; Related: None; Repeats: 1; Topology: Undefined; Example: Q10122; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00027; DC Domain; TR PROSITE; PS50808; ZF_BED; 1; level=0 XX Names: Zinc finger BED-type Function: Undefined XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50808 case and and and FT ZN_FING from..to FT /note="BED-type #" else case and and and FT ZN_FING from..to FT /note="BED-type #; atypical" else FT ZN_FING from..to FT /note="BED-type #; degenerate" end case FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 49-62; Related: None; Repeats: 1-4; Topology: Undefined; Example: P34478; Scope: Eukaryota Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00028; DC Domain; TR PROSITE; PS50915; CRYSTALLIN_BETA_GAMMA; 1; level=0 XX Names: Beta/gamma crystallin 'Greek key' motif Function: Undefined XX FT From: PS50915 FT DOMAIN from..to FT /note="Beta/gamma crystallin 'Greek key' #" XX Chop: Nter=0; Cter=0; Size: 33-56; Related: None; Repeats: 1-12; Topology: Undefined; Example: P43320; Scope: Eukaryota Bacteria; Myxococcus Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00029; DC Domain; TR PROSITE; PS50143; BIR_REPEAT_2; 1; level=0 XX Names: BIR Function: All IAP proteins contain from one to three BIRs, and all known interactions between inhibitor of apoptosis proteins (IAPs) and other proteins are mediated by one or more BIRs. XX DR PROSITE; PS01282; BIR_REPEAT_1; 1; trigger=no XX case GO GO:0046872; F:metal ion binding KW Zinc KW Metal-binding end case XX FT From: PS50143 FT REPEAT from..to FT /note="BIR #" FT BINDING 35 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 64-98; Related: None; Repeats: 1-3; Topology: Undefined; Example: O14064; Scope: Eukaryota Viruses Comments: None XX # Revision 1.11 2022/11/19 // AC PRU00030; DC Domain; TR PROSITE; PS50925; BLUF; 1; level=0 XX Names: BLUF domain Function: Undefined XX FT From: PS50925 FT DOMAIN from..to FT /note="BLUF #" XX Chop: Nter=0; Cter=0; Size: 93-93; Related: None; Repeats: 1; Topology: Undefined; Example: P75990; Scope: Bacteria; Escherichia Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00031; DC Domain; TR PROSITE; PS50279; BPTI_KUNITZ_2; 1; level=0 XX Names: BPTI/Kunitz inhibitor domain Function: Undefined XX XX DR PROSITE; PS00280; BPTI_KUNITZ_1; 1; trigger=no XX GO GO:0004866; F:endopeptidase inhibitor activity GO GO:0004867; F:serine-type endopeptidase inhibitor activity XX KW Protease inhibitor KW Serine protease inhibitor case KW Disulfide bond end case XX FT From: PS50279 FT DOMAIN from..to FT /note="BPTI/Kunitz inhibitor #" FT DISULFID 1..51 FT Tag: disulf; Condition: C-x*-C FT DISULFID 10..34 FT Tag: disulf; Condition: C-x*-C FT DISULFID 26..47 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 51-76; Related: None; Repeats: 1-5; Topology: Undefined; Example: Q60495; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00032; DC Domain; TR PROSITE; PS50138; BRCA2_REPEAT; 1; level=0 XX Names: BRCA2 Function: Undefined XX FT From: PS50138 FT REPEAT from..to FT /note="BRCA2 #" XX Chop: Nter=0; Cter=0; Size: 18-35; Related: None; Repeats: 1-8; Topology: Undefined; Example: P51587; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00033; DC Domain; TR PROSITE; PS50172; BRCT; 1; level=0 XX Names: BRCT Function: Undefined XX FT From: PS50172 FT DOMAIN from..to FT /note="BRCT #" XX Chop: Nter=0; Cter=0; Size: 24-129; Related: None; Repeats: 1-5; Topology: Undefined; Example: P41882; Scope: Eukaryota Archaea; Halobacteriaceae Bacteria Viruses Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00034; DC Domain; TR PROSITE; PS50833; BRIX; 1; level=0 XX Names: Brix domain Function: Undefined XX FT From: PS50833 FT DOMAIN from..to FT /note="Brix #" XX Chop: Nter=0; Cter=0; Size: 152-323; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TDN6; Scope: Eukaryota Archaea Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00035; DC Domain; TR PROSITE; PS50014; BROMODOMAIN_2; 1; level=0 XX Names: Bromodomain Function: Undefined XX DR PROSITE; PS00633; BROMODOMAIN_1; 1; trigger=no XX KW Bromodomain XX FT From: PS50014 FT DOMAIN from..to FT /note="Bromo #" XX Chop: Nter=0; Cter=0; Size: 23-96; Related: None; Repeats: 1-2; Topology: Undefined; Example: P54816; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00036; DC Domain; TR PROSITE; PS50858; BSD; 1; level=0 XX Names: BSD Function: Undefined XX FT From: PS50858 FT DOMAIN from..to FT /note="BSD #" XX Chop: Nter=0; Cter=0; Size: 52-60; Related: None; Repeats: 1-2; Topology: Undefined; Example: P54858; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00037; DC Domain; TR PROSITE; PS50097; BTB; 1; level=0 XX Names: BTB domain Function: It is a homodimerization domain. XX FT From: PS50097 FT DOMAIN from..to FT /note="BTB #" XX Chop: Nter=0; Cter=0; Size: 40-177; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q96DT7; Scope: Eukaryota Viruses; Chordopoxvirinae Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00038; DC Domain; TR PROSITE; PS50927; BULB_LECTIN; 1; level=0 XX Names: Bulb-type lectin Function: Although this domain is a mannose-binding lectin in the bulb super- family, curculin is considered as a non-functional mannose-binding protein devoid of mannose-binding activity. XX XX GO GO:0030246; F:carbohydrate binding XX KW Lectin case KW Disulfide bond end case XX FT From: PS50927 FT DOMAIN from..to FT /note="Bulb-type lectin #" FT DISULFID 31..58 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 106-130; Related: None; Repeats: 1; Topology: Undefined; Example: P49329; Scope: Eukaryota Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00039; DC Domain; TR PROSITE; PS01225; CTCK_2; 1; level=0 XX Names: C-terminal cystine knot (CTCK) domain Function: Undefined XX XX case KW Disulfide bond end case FT From: PS01225 FT DOMAIN from..to FT /note="CTCK #" FT DISULFID 1..51 FT Tag: disulf; Condition: C-x*-C FT DISULFID 16..65 FT Tag: disulf; Condition: C-x*-C FT DISULFID 27..81 FT Tag: disulf; Condition: C-x*-C FT DISULFID 31..83 FT Tag: disulf; Condition: C-x*-C FT DISULFID ?..87 FT Tag: disulf; Condition: C XX Chop: Nter=0; Cter=0; Size: 72-106; Related: None; Repeats: 1; Topology: Undefined; Example: O95813; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.12 2019/11/20 // AC PRU00040; DC Domain; TR PROSITE; PS50041; C_TYPE_LECTIN_2; 1; level=0 XX Names: C-type lectin domain Function: The C-type lectin domain seems to function as a calcium-dependent carbohydrate-recognition domain. XX DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1; trigger=no XX GO GO:0030246; F:carbohydrate binding XX KW Lectin case KW Disulfide bond end case XX FT From: PS50041 FT DOMAIN from..to FT /note="C-type lectin #" FT DISULFID 22..116 FT Tag: disulf; Condition: C-x*-C FT DISULFID 95..108 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 71-166; Related: None; Repeats: 1-10; Topology: Undefined; Example: Q9NNX6; Scope: Eukaryota; Metazoa Viruses; Avipoxvirus Comments: None XX # Revision 1.13 2019/11/20 // AC PRU00041; DC Domain; TR PROSITE; PS50004; C2; 1; level=0 XX Names: C2 domain Function: The C2 domain is thought to be involved in calcium-dependent phospholipid binding. XX case and and CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 3 Ca(2+) ions per C2 domain. else case or or CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; end case XX case or or GO GO:0005509; F:calcium ion binding XX KW Metal-binding KW Calcium end case XX FT From: PS50004 FT DOMAIN from..to FT /note="C2 #" case FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: L end case FT BINDING 34 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 34 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: D FT BINDING 40 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: D case FT BINDING 91 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Condition: F end case FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: D FT BINDING 92 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 3; Condition: D FT BINDING 95 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 3; Condition: S case FT BINDING 96 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 3; Condition: K end case FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: D FT BINDING 98 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 3; Condition: D XX Chop: Nter=0; Cter=0; Size: 16-133; Related: None; Repeats: 1-5; Topology: Undefined; Example: Q6XYQ8; Scope: Eukaryota Comments: None XX # Revision 1.15 2022/11/19 // AC PRU00042; DC Domain; TR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1; level=0 XX Names: Zinc finger C2H2-type Function: Undefined XX DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1; trigger=no XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50157 case and and and FT ZN_FING 1..23 FT /note="C2H2-type #" else case and and and FT ZN_FING 1..23 FT /note="C2H2-type #; atypical" else FT ZN_FING 1..23 FT /note="C2H2-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 6-40; Related: None; Repeats: 1-37; Topology: Undefined; Example: Q8ST83; Scope: Eukaryota Bacteria; Pseudomonadota Archaea; Methanocaldococcus Viruses Comments: None XX # Revision 1.11 2023/01/26 // AC PRU00043; DC Domain; TR PROSITE; PS50268; CADHERIN_2; 1; level=0 XX Names: Cadherin Function: It is suggested that the calcium-binding region of cadherins is located in the cadherin domain. XX DR PROSITE; PS00232; CADHERIN_1; 1; trigger=no XX GO GO:0005509; F:calcium ion binding KW Calcium XX FT From: PS50268 FT DOMAIN from..to FT /note="Cadherin #" XX Chop: Nter=0; Cter=0; Size: 11-197; Related: None; Repeats: 1-34; Topology: Not cytoplasmic; Example: O60245; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00044; DC Domain; TR PROSITE; PS50021; CH; 1; level=0 XX Names: Calponin-homology (CH) domain Function: Some but not all CH domains are able to bind actin. XX FT From: PS50021 FT DOMAIN from..to FT /note="Calponin-homology (CH) #" XX Chop: Nter=0; Cter=0; Size: 64-162; Related: None; Repeats: 1-4; Topology: Cytoplasmic; Example: Q01995; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00045; DC Domain; TR PROSITE; PS50245; CAP_GLY_2; 1; level=0 XX Names: CAP-Gly Function: Undefined XX DR PROSITE; PS00845; CAP_GLY_1; 1; trigger=no FT From: PS50245 FT DOMAIN from..to FT /note="CAP-Gly #" XX Chop: Nter=0; Cter=0; Size: 43-51; Related: None; Repeats: 1-2; Topology: Undefined; Example: P11709; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00046; DC Domain; TR PROSITE; PS50209; CARD; 1; level=0 XX Names: CARD Function: Undefined XX FT From: PS50209 FT DOMAIN from..to FT /note="CARD #" XX Chop: Nter=0; Cter=0; Size: 67-99; Related: None; Repeats: 1-2; Topology: Undefined; Example: O95999; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00047; DC Domain; TR PROSITE; PS50158; ZF_CCHC; 1; level=0 XX Names: Zinc finger CCHC-type Function: Undefined XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50158 case and and and FT ZN_FING from..to FT /note="CCHC-type #" else case and and and FT ZN_FING from..to FT /note="CCHC-type #; atypical" else FT ZN_FING from..to FT /note="CCHC-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 14-20; Related: None; Repeats: 1-9; Topology: Undefined; Example: P03543; Scope: Eukaryota Viruses Comments: None XX # Revision 1.10 2019/11/20 // AC PRU00048; DC Domain; TR PROSITE; PS50911; CHAP; 1; level=0 XX Names: CHAP Function: Undefined XX XX GO GO:0016787; F:hydrolase activity XX KW Hydrolase XX FT From: PS50911 FT DOMAIN from..to FT /note="Peptidase C51 #" XX Chop: Nter=0; Cter=0; Size: 130-147; Related: None; Repeats: 1; Topology: Undefined; Example: P0AES0; Scope: Eukaryota; Crithidia Bacteria Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00049; DC Domain; TR PROSITE; PS50839; CHASE; 1; level=0 XX Names: CHASE Function: Undefined XX FT From: PS50839 FT DOMAIN from..to FT /note="CHASE #" XX Chop: Nter=0; Cter=0; Size: 232-232; Related: None; Repeats: 1; Topology: Undefined; Example: Q03101; Scope: Eukaryota; Dictyostelium Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00050; DC Domain; TR PROSITE; PS50122; CHEB; 1; level=0 XX Names: cheB-type methylesterase domain Function: Undefined XX XX case GO GO:0016787; F:hydrolase activity GO GO:0006935; P:chemotaxis KW Hydrolase KW Chemotaxis end case XX FT From: PS50122 FT DOMAIN from..to FT /note="CheB-type methylesterase #" FT ACT_SITE 13 FT Group: 1; Condition: S FT ACT_SITE 40 FT Group: 1; Condition: H FT ACT_SITE 136 FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 141-197; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q8P7A6; Scope: Bacteria Archaea; Euryarchaeota Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00051; DC Domain; TR PROSITE; PS50123; CHER; 1; level=0 XX Names: cheR-type methyltransferase Function: Undefined XX FT From: PS50123 FT DOMAIN from..to FT /note="CheR-type methyltransferase #" XX Chop: Nter=0; Cter=0; Size: 256-280; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KCB8; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00052; DC Domain; TR PROSITE; PS50851; CHEW; 1; level=0 XX Names: cheW-like Function: Undefined XX FT From: PS50851 FT DOMAIN from..to FT /note="CheW-like #" XX Chop: Nter=0; Cter=0; Size: 129-145; Related: None; Repeats: 1; Topology: Undefined; Example: P0A964; Scope: Bacteria Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00053; DC Domain; TR PROSITE; PS50013; CHROMO_2; 1; level=0 XX Names: Chromo Function: Undefined XX DR PROSITE; PS00598; CHROMO_1; 1; trigger=no FT From: PS50013 case FT DOMAIN from..to FT /note="Chromo #2; shadow subtype" else FT DOMAIN from..to FT /note="Chromo #" end case XX Chop: Nter=0; Cter=0; Size: 43-104; Related: None; Repeats: 1-2; Topology: Undefined; Example: P83916; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00054; DC Domain; TR PROSITE; PS50263; CN_HYDROLASE; 1; level=0 XX Names: CN hydrolase domain Carbon-nitrogen hydrolase domain Function: Undefined XX case GO GO:0016787; F:hydrolase activity KW Hydrolase end case FT From: PS50263 FT DOMAIN from..to FT /note="CN hydrolase #" FT ACT_SITE 41 FT /note="Proton acceptor" FT Group: 1; Condition: E FT ACT_SITE 114 FT Group: 1; Condition: K FT ACT_SITE 158 FT /note="Nucleophile" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 196-322; Related: None; Repeats: 1; Topology: Undefined; Example: Q9RQ17; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00055; DC Domain; TR PROSITE; PS50073; COPPER_FIST_2; 1; level=0 XX Names: Copper-fist DNA-binding domain Function: Undefined XX DR PROSITE; PS01119; COPPER_FIST_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription case GO GO:0046872; F:metal ion binding end case XX KW DNA-binding KW Transcription KW Transcription regulation case KW Zinc KW Metal-binding end case XX FT From: PS50073 FT DNA_BIND from..to FT /note="Copper-fist #" FT BINDING 11 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 40-40; Related: None; Repeats: 1; Topology: Undefined; Example: P41772; Scope: Eukaryota; Ascomycota Comments: None XX # Revision 1.11 2022/11/19 // AC PRU00056; DC Domain; TR PROSITE; PS50191; CRAL_TRIO; 1; level=0 XX Names: CRAL-TRIO Function: Undefined XX FT From: PS50191 FT DOMAIN from..to FT /note="CRAL-TRIO #" XX Chop: Nter=0; Cter=0; Size: 88-193; Related: None; Repeats: 1; Topology: Undefined; Example: P21359; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00057; DC Domain; TR PROSITE; PS50108; CRIB; 1; level=0 XX Names: CRIB Function: Undefined XX FT From: PS50108 FT DOMAIN from..to FT /note="CRIB #" XX Chop: Nter=0; Cter=0; Size: 13-15; Related: None; Repeats: 1; Topology: Undefined; Example: Q9H3Q1; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00058; DC Domain; TR PROSITE; PS50897; CTLH; 1; level=0 XX Names: CTLH Function: Undefined XX FT From: PS50897 FT DOMAIN from..to FT /note="CTLH #" XX Chop: Nter=0; Cter=0; Size: 53-84; Related: None; Repeats: 1; Topology: Undefined; Example: Q96G75; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00059; DC Domain; TR PROSITE; PS01180; CUB; 1; level=0 XX Names: CUB Function: The CUB domain [1,2,E1] is an extracellular domain of approximately 110 residues which is found in functionally diverse, mostly developmentally regulated proteins. XX XX case KW Disulfide bond end case FT From: PS01180 FT DOMAIN from..to FT /note="CUB #" FT DISULFID 1..28 FT Tag: disulf; Condition: C-x*-C FT DISULFID 58..75 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 101-138; Related: None; Repeats: 1-5; Topology: Undefined; Example: Q8TDF5; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00060; DC Domain; TR PROSITE; PS50042; CNMP_BINDING_3; 1; level=0 XX Names: CNMP Function: Undefined XX DR PROSITE; PS00889; CNMP_BINDING_2; 1; trigger=no DR PROSITE; PS00888; CNMP_BINDING_1; 1; trigger=no FT From: PS50042 FT REGION from..to FT /note="cNMP-binding domain #" XX Chop: Nter=0; Cter=0; Size: 101-146; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q96L42; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.8 2021/12/16 // AC PRU00061; DC Domain; TR PROSITE; PS50824; DAPIN; 1; level=0 XX Names: Pyrin domain pyrin N-terminal homology domain (PYD) PAAD (after the protein families pyrin, AIM, ASC death-domain-like) domain DAPIN (Domain in Apoptosis and INterferon response) domain Function: The pyrin domain is a protein-protein interaction domain capable of binding to other pyrin domains. XX FT From: PS50824 FT DOMAIN from..to FT /note="Pyrin #" XX Chop: Nter=0; Cter=0; Size: 87-103; Related: None; Repeats: 1; Topology: Undefined; Example: O15553; Scope: Eukaryota; Euteleostomi Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00062; DC Domain; TR PROSITE; PS50010; DH_2; 1; level=0 XX Names: Dbl homology (DH) domain Function: Undefined XX XX DR PROSITE; PS00741; DH_1; 1; trigger=no XX FT From: PS50010 FT DOMAIN from..to FT /note="DH #" XX Chop: Nter=0; Cter=0; Size: 160-215; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9NR80; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00063; DC Domain; TR PROSITE; PS50827; DDT; 1; level=0 XX Names: DDT domain Function: A DNA-binding function for the DDT domain has been proposed. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS50827 FT DOMAIN from..to FT /note="DDT #" XX Chop: Nter=0; Cter=0; Size: 61-66; Related: None; Repeats: 1; Topology: Undefined; Example: Q9NRL2; Scope: Eukaryota Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00064; DC Domain; TR PROSITE; PS50017; DEATH_DOMAIN; 1; level=0 XX Names: Death Function: Undefined XX FT From: PS50017 FT DOMAIN from..to FT /note="Death #" XX Chop: Nter=0; Cter=0; Size: 27-111; Related: None; Repeats: 1-2; Topology: Undefined; Example: P16157; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00065; DC Domain; TR PROSITE; PS50168; DED; 1; level=0 XX Names: DED Function: Undefined XX FT From: PS50168 FT DOMAIN from..to FT /note="DED #" XX Chop: Nter=0; Cter=0; Size: 71-81; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q14790; Scope: Eukaryota; Eutheria Viruses Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00066; DC Domain; TR PROSITE; PS50186; DEP; 1; level=0 XX Names: DEP Function: Undefined XX FT From: PS50186 FT DOMAIN from..to FT /note="DEP #" XX Chop: Nter=0; Cter=0; Size: 75-87; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9Z2H2; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00067; DC Domain; TR PROSITE; PS50216; DHHC; 1; level=0 XX Names: DHHC domain Function: The Cys residue within the DHHC domain forms a stable acyl intermediate and transfers the acyl chain to the Cys residues of a target protein. XX case GO GO:0019706; F:protein-cysteine S-palmitoyltransferase activity XX KW Acyltransferase KW Lipoprotein KW Palmitate KW Transferase end case XX FT From: PS50216 FT DOMAIN from..to FT /note="DHHC #" FT ACT_SITE 31 FT /note="S-palmitoyl cysteine intermediate" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 51-54; Related: None; Repeats: 1; Topology: Undefined; Example: P39010; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00068; DC Domain; TR PROSITE; PS50214; DISINTEGRIN_2; 1; level=0 XX Names: Disintegrin-like Function: Undefined XX DR PROSITE; PS00427; DISINTEGRIN_1; 1; trigger=no DR PROSITE; PS00016; RGD; 1; trigger=yes XX case KW Disulfide bond end case FT From: PS50214 FT DOMAIN from..to FT /note="Disintegrin #" FT DISULFID 60..80 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 57-98; Related: None; Repeats: 1; Topology: Undefined; Example: Q8K410; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00069; DC Domain; TR PROSITE; PS50841; DIX; 1; level=0 XX Names: DIX domain Function: Undefined XX XX KW Wnt signaling pathway XX FT From: PS50841 FT DOMAIN from..to FT /note="DIX #" XX Chop: Nter=0; Cter=0; Size: 82-85; Related: None; Repeats: 1; Topology: Undefined; Example: O15169; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00070; DC Domain; TR PROSITE; PS50809; DM_2; 1; level=0 XX Names: DM DNA-binding domain Function: The DM domain binds DNA as a dimer, allowing the recognition of pseudopalindromic sequences. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS40000; DM_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW DNA-binding KW Metal-binding KW Zinc KW Nucleus XX FT From: PS50809 FT DNA_BIND from..to FT /note="DM #" XX Chop: Nter=0; Cter=0; Size: 47-49; Related: None; Repeats: 1-2; Topology: Undefined; Example: P23023; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.11 2019/11/20 // AC PRU00071; DC Domain; TR PROSITE; PS50884; ZF_DOF_2; 1; level=0 XX Names: Zinc finger Dof-type Function: Like other zinc fingers the Dof domain has a dual activity: it binds DNA in a sequence-specific manner with the core binding site formed by the AAAG sequence and it can also mediates protein-protein interaction. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS01361; ZF_DOF_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW Nucleus KW DNA-binding KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50884 case and and and FT ZN_FING from..to FT /note="Dof-type #" else case and and and FT ZN_FING from..to FT /note="Dof-type #; atypical" else FT ZN_FING from..to FT /note="Dof-type #; degenerate" end case FT BINDING 3 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 55-55; Related: None; Repeats: 1; Topology: Undefined; Example: Q43385; Scope: Eukaryota; Magnoliopsida Comments: None XX # Revision 1.16 2022/11/19 // AC PRU00072; DC Domain; TR PROSITE; PS50309; DC; 1; level=0 XX Names: Doublecortin Function: Undefined XX FT From: PS50309 FT DOMAIN from..to FT /note="Doublecortin #" XX Chop: Nter=0; Cter=0; Size: 80-87; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9UHG0; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00073; DC Domain; TR PROSITE; PS50139; Z_BINDING; 1; level=0 XX Names: Z-binding domain ZBD Zalpha Zbeta Function: The Z-binding domain (ZBD), also referred to as Zalpha or Zbeta is a 78-amino-acid protein fold that specifically binds to Z-DNA as well as to Z- RNA but not to B-DNA. ZBDs might play an important role of in innate antiviral immune responses. XX FT From: PS50139 FT DOMAIN from..to FT /note="Z-binding #" XX Chop: Nter=0; Cter=0; Size: 66-70; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q99MU3; Scope: Eukaryota; Eutheria Viruses; Orthopoxvirus Comments: None XX # Revision 1.6 2020/04/08 // AC PRU00074; DC Domain; TR PROSITE; PS50883; EAL; 1; level=0 XX Names: EAL Function: Undefined XX FT From: PS50883 FT DOMAIN from..to FT /note="EAL #" XX Chop: Nter=0; Cter=0; Size: 47-261; Related: None; Repeats: 1; Topology: Undefined; Example: P14203; Scope: Bacteria Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00075; DC Domain; TR PROSITE; PS50912; EAR; 1; level=0 XX Names: EAR repeat Function: A common functional feature found in all characterized domains of this class is a participation in protein-protein interactions. XX FT From: PS50912 FT REPEAT from..to FT /note="EAR #" XX Chop: Nter=0; Cter=0; Size: 44-58; Related: None; Repeats: 6-7; Topology: Undefined; Example: Q8N135; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00076; DC Domain; TR PROSITE; PS50026; EGF_3; 1; level=0 XX Names: EGF-like domain Function: Undefined XX XX DR PROSITE; PS00022; EGF_1; 1; trigger=no DR PROSITE; PS01186; EGF_2; 1; trigger=no DR PROSITE; PS01187; EGF_CA; 0-1; trigger=no XX case GO GO:0005509; F:calcium ion binding KW Calcium end case KW EGF-like domain case KW Disulfide bond end case XX FT From: PS50026 case FT DOMAIN from..to FT /note="EGF-like #; calcium-binding" else FT DOMAIN from..to FT /note="EGF-like #" end case FT DISULFID 5..15 FT Tag: disulf; Condition: C-x*-C FT DISULFID 9..26 FT Tag: disulf; Condition: C-x*-C FT DISULFID 28..37 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 13-99; Related: None; Repeats: 1-52; Topology: Undefined; Example: P01135; Scope: Eukaryota Viruses; Chordopoxvirinae Comments: None XX # Revision 1.19 2019/11/20 // AC PRU00077; DC Domain; TR PROSITE; PS50031; EH; 1; level=0 XX Names: EH Function: Undefined XX FT From: PS50031 FT DOMAIN from..to FT /note="EH #" XX Chop: Nter=0; Cter=0; Size: 89-114; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q9JKC9; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00078; DC Domain; TR PROSITE; PS50843; EXPANSIN_CBD; 1; level=0 XX Names: Expansin-like CBD Function: Undefined XX FT From: PS50843 FT DOMAIN from..to FT /note="Expansin-like CBD #" XX Chop: Nter=0; Cter=0; Size: 80-84; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LZT4; Scope: Eukaryota; Magnoliopsida Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00079; DC Domain; TR PROSITE; PS50842; EXPANSIN_EG45; 1; level=0 XX Names: Expansin-like EG45 Function: Undefined XX XX case KW Disulfide bond end case FT From: PS50842 FT DOMAIN from..to FT /note="Expansin-like EG45 #" FT DISULFID 4..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 35..106 FT Tag: disulf; Condition: C-x*-C FT DISULFID 40..46 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 100-116; Related: None; Repeats: 1; Topology: Undefined; Example: P58738; Scope: Eukaryota Comments: None XX # Revision 1.10 2019/11/20 // AC PRU00080; DC Domain; TR PROSITE; PS50181; FBOX; 1; level=0 XX Names: F-box Function: Undefined XX **CC -!- PATHWAY: Ubiquitin conjugation; third step. **CC -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex **CC . **XX **KW Ubl conjugation pathway XX FT From: PS50181 FT DOMAIN from..to FT /note="F-box #" XX Chop: Nter=0; Cter=0; Size: 28-153; Related: None; Repeats: 1; Topology: Undefined; Example: P41002; Scope: Eukaryota Viruses Comments: None XX # Revision 1.10 2019/11/20 // AC PRU00081; DC Domain; TR PROSITE; PS50022; FA58C_3; 1; level=0 XX Names: F5/8 type C Function: Undefined XX DR PROSITE; PS01286; FA58C_2; 1; trigger=no DR PROSITE; PS01285; FA58C_1; 1; trigger=no XX case KW Disulfide bond end case FT From: PS50022 FT DOMAIN from..to FT /note="F5/8 type C #" FT DISULFID 1..150 FT Tag: disulf; Condition: C-x*-C FT DISULFID 137..141 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 139-173; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q8QFX6; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00082; DC Domain; TR PROSITE; PS50213; FAS1; 1; level=0 XX Names: FAS1 Function: Undefined XX FT From: PS50213 FT DOMAIN from..to FT /note="FAS1 #" XX Chop: Nter=0; Cter=0; Size: 123-155; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q9SJ81; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00084; DC Domain; TR PROSITE; PS50057; FERM_3; 1; level=0 XX Names: FERM Function: Undefined XX DR PROSITE; PS00661; FERM_2; 1; trigger=no DR PROSITE; PS00660; FERM_1; 1; trigger=no FT From: PS50057 FT DOMAIN from..to FT /note="FERM #" XX Chop: Nter=0; Cter=0; Size: 282-518; Related: None; Repeats: 1-2; Topology: Undefined; Example: P11171; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00085; DC Domain; TR PROSITE; PS50905; FERRITIN_LIKE; 1; level=0 XX Names: Ferritin-like diiron domain Function: Proteins containing a ferritin-like diiron domain possess the ability to catalyze oxidation of Fe(2+) to Fe(3+) by O2, i.e. ferroxidase activity. XX case or KW Metal-binding KW Iron end case XX FT From: PS50905 FT DOMAIN from..to FT /note="Ferritin-like diiron #" FT BINDING 18 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 1; Condition: E FT BINDING 96 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 1; Condition: E FT BINDING 99 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 1; Condition: E FT BINDING 132 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 1; Condition: H XX FT BINDING 18 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 2; Condition: E FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 2; Condition: E FT BINDING 51 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 2; Condition: E FT BINDING 52 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Optional; Group: 2; Condition: M FT BINDING 54 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 2; Condition: H FT BINDING 99 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 2; Condition: E FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 2; Condition: E FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 2; Condition: E FT BINDING 132 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#2" FT Group: 2; Condition: H XX case and Warn: Both types of iron binding amino acid-groups are present! end case Chop: Nter=0; Cter=0; Size: 124-191; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9AGG3; Scope: Bacteria Archaea Eukaryota Plastid Comments: None XX # Revision 1.11 2022/11/19 // AC PRU00086; DC Domain; TR PROSITE; PS50006; FHA_DOMAIN; 1; level=0 XX Names: FHA Function: Undefined XX FT From: PS50006 FT DOMAIN from..to FT /note="FHA #" XX Chop: Nter=0; Cter=0; Size: 50-81; Related: None; Repeats: 1-2; Topology: Undefined; Example: P55196; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00087; DC Domain; TR PROSITE; PS50194; FILAMIN_REPEAT; 1; level=0 XX Names: Filamin Function: Undefined XX FT From: PS50194 FT REPEAT from..to FT /note="Filamin #" XX Chop: Nter=0; Cter=0; Size: 63-110; Related: None; Repeats: 1-24; Topology: Undefined; Example: O75382; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00088; DC Domain; TR PROSITE; PS50902; FLAVODOXIN_LIKE; 1; level=0 XX Names: Flavodoxin-like domain Function: The flavodoxin-like domain is involved in electron transfer reactions. XX CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; XX GO GO:0010181; F:FMN binding XX KW Flavoprotein KW FMN XX FT From: PS50902 FT DOMAIN from..to FT /note="Flavodoxin-like #" FT BINDING 7 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: [TS] FT BINDING 8 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: E FT BINDING 9 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: T FT BINDING 11 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: [KR] FT BINDING 12 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: S FT BINDING 56 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: S FT BINDING 57 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: T FT BINDING 93 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: S FT BINDING 98 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: [HR] FT BINDING 100 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: C FT BINDING 129 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: E FT BINDING 133 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Group: 1; Condition: Q case not FT BINDING 7..11 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT BINDING 88..119 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" end case XX Chop: Nter=0; Cter=0; Size: 136-200; Related: None; Repeats: 1; Topology: Undefined; Example: P29476; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None XX # Revision 1.9 2023/07/13 // AC PRU00089; DC Domain; TR PROSITE; PS50039; FORK_HEAD_3; 1; level=0 XX Names: Fork-head DNA-binding domain Function: Undefined XX CC -!- SUBCELLULAR LOCATION: Nucleus. DR PROSITE; PS00658; FORK_HEAD_2; 1; trigger=no DR PROSITE; PS00657; FORK_HEAD_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW Nucleus KW DNA-binding XX FT From: PS50039 FT DNA_BIND from..to FT /note="Fork-head #" XX Chop: Nter=0; Cter=0; Size: 77-100; Related: None; Repeats: 1; Topology: Undefined; Example: Q12950; Scope: Eukaryota Viruses; unclassified Alpharetrovirus Comments: None XX # Revision 1.12 2019/11/20 // AC PRU00090; DC Domain; TR PROSITE; PS50038; FZ; 1; level=0 XX Names: FZ Function: Several fz domains have been shown to be both necessary and sufficient for Wg/Wnt ligand binding, strongly suggesting that the fz domain is a Wg/Wnt interacting domain. XX XX case KW Disulfide bond end case FT From: PS50038 FT DOMAIN from..to FT /note="FZ #" FT DISULFID 6..67 FT Tag: disulf; Condition: C-x*-C FT DISULFID 14..60 FT Tag: disulf; Condition: C-x*-C FT DISULFID 51..89 FT Tag: disulf; Condition: C-x*-C FT DISULFID 78..119 FT Tag: disulf; Condition: C-x*-C FT DISULFID 82..106 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 76-190; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: P97299; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00091; DC Domain; TR PROSITE; PS50178; ZF_FYVE; 1; level=0 XX Names: Zinc finger FYVE/FYVE-related type Function: The FYVE domain target signal-transducing proteins to cell membranes through binding to the membrane lipid phosphatidylinositol-3-phosphate (PtdIns(3)P) with high specificity. XX case ( and and and ) and ( and and and ) KW Zinc KW Metal-binding end case KW Zinc-finger XX FT From: PS50178 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="FYVE-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="FYVE-type #; atypical" else FT ZN_FING from..to FT /note="FYVE-type #; degenerate" end case FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 43-83; Related: None; Repeats: 1-2; Topology: Undefined; Example: P40343; Scope: Eukaryota Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00092; DC Domain; TR PROSITE; PS50174; G_PATCH; 1; level=0 XX Names: G-patch Function: Undefined XX FT From: PS50174 FT DOMAIN from..to FT /note="G-patch #" XX Chop: Nter=0; Cter=0; Size: 45-50; Related: None; Repeats: 1; Topology: Undefined; Example: O95872; Scope: Eukaryota Viruses; Retroviridae Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00093; DC Domain; TR PROSITE; PS50180; GAE; 1; level=0 XX Names: GAE Function: Undefined XX FT From: PS50180 FT DOMAIN from..to FT /note="GAE #" XX Chop: Nter=0; Cter=0; Size: 113-122; Related: None; Repeats: 1; Topology: Undefined; Example: Q10410; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00094; DC Domain; TR PROSITE; PS50114; GATA_ZN_FINGER_2; 1; level=0 XX Names: Zinc finger GATA-type Function: Undefined XX DR PROSITE; PS00344; GATA_ZN_FINGER_1; 1; trigger=no XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50114 case and and and FT ZN_FING 7..31 FT /note="GATA-type #" else case and and and FT ZN_FING 7..31 FT /note="GATA-type #; atypical" else FT ZN_FING 7..31 FT /note="GATA-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 25-55; Related: None; Repeats: 1-2; Topology: Undefined; Example: P15976; Scope: Eukaryota Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00095; DC Domain; TR PROSITE; PS50887; GGDEF; 1; level=0 XX Names: GGDEF Function: Undefined XX FT From: PS50887 FT DOMAIN from..to FT /note="GGDEF #" XX Chop: Nter=0; Cter=0; Size: 123-138; Related: None; Repeats: 1-2; Topology: Undefined; Example: P23842; Scope: Bacteria Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00096; DC Domain; TR PROSITE; PS50866; GOLD; 1; level=0 XX Names: GOLD Function: Undefined XX FT From: PS50866 FT DOMAIN from..to FT /note="GOLD #" XX Chop: Nter=0; Cter=0; Size: 82-159; Related: None; Repeats: 1; Topology: Undefined; Example: P27869; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00097; DC Domain; TR PROSITE; PS50877; GOLOCO; 1; level=0 XX Names: GoLoco Function: Undefined XX FT From: PS50877 FT DOMAIN from..to FT /note="GoLoco #" XX Chop: Nter=0; Cter=0; Size: 17-23; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q8IVA1; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00098; DC Domain; TR PROSITE; PS50221; GPS; 1; level=0 XX Names: GPS domain Function: Undefined XX XX GO GO:0016020; C:membrane XX KW Glycoprotein KW Membrane KW Transmembrane XX FT From: PS50221 FT DOMAIN from..to FT /note="GPS #" XX Chop: Nter=0; Cter=0; Size: 47-59; Related: None; Repeats: 1; Topology: Undefined; Example: Q8IZF7; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.10 2022/09/29 // AC PRU00099; DC Domain; TR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1; level=0 XX Names: Guanylate cyclase domain Function: Undefined XX CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase CC family. DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1; trigger=no case GO GO:0000287; F:magnesium ion binding KW Magnesium KW Metal-binding end case FT From: PS50125 FT DOMAIN from..to FT /note="Guanylate cyclase #" FT BINDING 6 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Group: 1; Condition: D FT BINDING 6 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Group: 1; Condition: D FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Group: 1; Condition: I FT BINDING 50 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Group: 1; Condition: D FT BINDING 50 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 108-134; Related: None; Repeats: 1; Topology: Undefined; Example: P32870; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.16 2022/11/19 // AC PRU00100; DC Domain; TR PROSITE; PS50052; GUANYLATE_KINASE_2; 1; level=0 XX Names: Guanylate kinase-like domain GK-like domain Function: Undefined XX DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1; trigger=no XX GO GO:0005524; F:ATP binding GO GO:0016301; F:kinase activity GO GO:0000166; F:nucleotide binding GO GO:0016740; F:transferase activity KW Transferase KW Kinase KW ATP-binding KW Nucleotide-binding XX FT From: PS50052 FT DOMAIN from..to FT /note="Guanylate kinase-like #" FT BINDING 8..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 101-205; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BXL7; Scope: Bacteria Eukaryota Viruses; Vaccinia virus Comments: None XX # Revision 1.11 2022/11/19 // AC PRU00101; DC Domain; TR PROSITE; PS50829; GYF; 1; level=0 XX Names: GYF Function: Undefined XX FT From: PS50829 FT DOMAIN from..to FT /note="GYF #" XX Chop: Nter=0; Cter=0; Size: 49-59; Related: None; Repeats: 1; Topology: Undefined; Example: P34520; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00102; DC Domain; TR PROSITE; PS50885; HAMP; 1; level=0 XX Names: HAMP Function: Undefined XX FT From: PS50885 FT DOMAIN from..to FT /note="HAMP #" XX Chop: Nter=0; Cter=0; Size: 48-57; Related: None; Repeats: 1-2; Topology: Undefined; Example: P59963; Scope: Eukaryota; Porphyra Bacteria Archaea; Halobacteriaceae Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00103; DC Domain; TR PROSITE; PS50077; HEAT_REPEAT; 1; level=0 XX Names: HEAT_repeat Function: It has been noted that many HEAT repeat-containing proteins are involved in intracellular transport processes. XX FT From: PS50077 FT REPEAT from..to FT /note="HEAT #" XX Chop: Nter=0; Cter=0; Size: 20-45; Related: RRU00005!!; Repeats: 1-20; Topology: Undefined; Example: Q09543; Scope: Eukaryota Comments: None XX # Revision 1.10 2019/11/20 // AC PRU00104; DC Domain; TR PROSITE; PS50237; HECT; 1; level=0 XX Names: HECT domain Function: Undefined XX KW Ubl conjugation pathway XX FT From: PS50237 FT DOMAIN from..to FT /note="HECT #" FT ACT_SITE 304 FT /note="Glycyl thioester intermediate" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 100-460; Related: None; Repeats: 1; Topology: Undefined; Example: Q5RBF2; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00105; DC Domain; TR PROSITE; PS50910; HEPN; 1; level=0 XX Names: HEPN Function: Undefined XX FT From: PS50910 FT DOMAIN from..to FT /note="HEPN #" XX Chop: Nter=0; Cter=0; Size: 117-121; Related: None; Repeats: 1; Topology: Undefined; Example: Q58700; Scope: Eukaryota; Eutheria Archaea; Methanocaldococcus Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00106; DC Domain; TR PROSITE; PS50834; HIN_200; 1; level=0 XX Names: HIN-200 domain Function: Undefined XX XX FT From: PS50834 FT DOMAIN from..to FT /note="HIN-200 #" XX Chop: Nter=0; Cter=0; Size: 198-201; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q16666; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00107; DC Domain; TR PROSITE; PS50109; HIS_KIN; 1; level=0 XX Names: Histidine kinase core domain Function: Autophosphorylates at a histidine residue, creating a high-energy phosphoryl group that is subsequently transferred to a phosphoacceptor. XX GO GO:0016740; F:transferase activity GO GO:0016301; F:kinase activity KW Transferase KW Kinase case KW Phosphoprotein end case FT From: PS50109 FT DOMAIN from..to FT /note="Histidine kinase #" FT MOD_RES 4 FT /note="Phosphohistidine; by autocatalysis" FT Condition: H XX Chop: Nter=0; Cter=0; Size: 157-356; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P59963; Scope: Eukaryota Bacteria Archaea Viruses Plastid Mitochondrion Comments: Mitochondrial pyruvate dehydrogenase kinases (PDKs) (EC 2.7.1.99) contain an histidine kinase domain which possess a serine/threonine kinase activity. XX # Revision 1.12 2019/11/20 // AC PRU00108; DC Domain; TR PROSITE; PS50071; HOMEOBOX_2; 1; level=0 XX Names: Homeobox DNA-binding domain Function: The homeobox domain binds DNA through a helix-turn-helix type of structure. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS00027; HOMEOBOX_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW DNA-binding KW Homeobox KW Nucleus XX FT From: PS50071 case FT DNA_BIND from+1..to+1 FT /note="Homeobox; TALE-type #" else FT DNA_BIND from+2..to+1 FT /note="Homeobox #" end case XX Chop: Nter=0; Cter=0; Size: 54-82; Related: None; Repeats: 1-4; Topology: Undefined; Example: P56915; Scope: Eukaryota Comments: None XX # Revision 1.15 2019/11/20 // AC PRU00109; DC Domain; TR PROSITE; PS50815; HORMA; 1; level=0 XX Names: HORMA Function: Undefined XX FT From: PS50815 FT DOMAIN from..to FT /note="HORMA #" XX Chop: Nter=0; Cter=0; Size: 184-231; Related: None; Repeats: 1; Topology: Undefined; Example: P20050; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00110; DC Domain; TR PROSITE; PS50894; HPT; 1; level=0 XX Names: HPt domain Histidine-containing Phosphotransfer domain Function: Contains a histidine residue capable of participating in phosphoryl transfer reactions. XX case KW Phosphoprotein end case FT From: PS50894 FT DOMAIN from..to FT /note="HPt #" FT MOD_RES 40 FT /note="Phosphohistidine" FT Condition: H XX Chop: Nter=0; Cter=0; Size: 84-111; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P0AEC5; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.10 2019/11/20 // AC PRU00111; DC Domain; TR PROSITE; PS50932; HTH_LACI_2; 1; level=0 XX Names: LacI-type HTH domain Function: The lacI-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain present in the lacI/galR family of transcriptional regulators involved in metabolic regulation in prokaryotes. XX XX DR PROSITE; PS00356; HTH_LACI_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50932 FT DOMAIN from..to FT /note="HTH lacI-type #" FT DNA_BIND 3..22 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 54-62; Related: None; Repeats: 1; Topology: Undefined; Example: P44329; Scope: Bacteria Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00112; DC Domain; TR PROSITE; PS50930; HTH_LYTTR; 1; level=0 XX Names: LytTR-type HTH domain Function: The LytTR ('litter') HTH domain is a DNA-binding, potential winged helix-turn-helix (wHTH) domain present in bacterial transcriptional regulators of the algR/agrA/lytR family. XX XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50930 FT DOMAIN from..to FT /note="HTH LytTR-type #" XX Chop: Nter=0; Cter=0; Size: 73-106; Related: None; Repeats: 1; Topology: Undefined; Example: P0A0I7; Scope: Bacteria Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00113; DC Domain; TR PROSITE; PS50825; HYR; 1; level=0 XX Names: HYR domain Function: Undefined XX FT From: PS50825 FT DOMAIN from..to FT /note="HYR #" XX Chop: Nter=0; Cter=0; Size: 83-85; Related: None; Repeats: 1-15; Topology: Undefined; Example: P78539; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00114; DC Domain; TR PROSITE; PS50835; IG_LIKE; 1; level=0 XX Names: Ig-like domain Function: Undefined XX KW Immunoglobulin domain case KW Disulfide bond end case XX FT From: PS50835 FT DOMAIN from..to FT /note="Ig-like ??-type #" FT DISULFID 22..75 FT Tag: disulf; Condition: C-x*-C XX Warn: Check the type of the Ig-like domain(s) Chop: Nter=0; Cter=0; Size: 55-135; Related: None; Repeats: 1-7; Topology: Undefined; Example: P61769; Scope: Eukaryota; Metazoa Bacteria Viruses Comments: None XX # Revision 1.16 2019/11/20 // AC PRU00115; DC Domain; TR PROSITE; PS50166; IMPORTIN_B_NT; 1; level=0 XX Names: Importin N-terminal Function: Undefined XX FT From: PS50166 FT DOMAIN from..to FT /note="Importin N-terminal #" XX Chop: Nter=0; Cter=0; Size: 67-89; Related: None; Repeats: 1; Topology: Undefined; Example: P55060; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00116; DC Domain; TR PROSITE; PS50096; IQ; 1; level=0 XX Names: IQ Function: Undefined XX FT From: PS50096 FT DOMAIN from..to FT /note="IQ #" XX Chop: Nter=0; Cter=0; Size: 14-33; Related: None; Repeats: 1-6; Topology: Undefined; Example: P46940; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00117; DC Domain; TR PROSITE; PS50084; KH_TYPE_1; 1; level=0 XX Names: KH domain Function: The KH domain has been shown to bind RNA. XX XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS50084 FT DOMAIN from..to FT /note="KH #" XX Chop: Nter=0; Cter=0; Size: 27-99; Related: None; Repeats: 1-14; Topology: Undefined; Example: Q9K6V8; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00118; DC Domain; TR PROSITE; PS50823; KH_TYPE_2; 1; level=0 XX Names: KH type-2 domain Function: The KH type-2 domain has been shown to bind RNA. XX XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS50823 FT DOMAIN from..to FT /note="KH type-2 #" XX Chop: Nter=0; Cter=0; Size: 44-97; Related: None; Repeats: 1; Topology: Undefined; Example: Q8UGK1; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00119; DC Domain; TR PROSITE; PS50805; KRAB; 1; level=0 XX Names: KRAB Function: Undefined XX XX FT From: PS50805 FT DOMAIN from..to FT /note="KRAB #" XX Chop: Nter=0; Cter=0; Size: 43-97; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q8IVC4; Scope: Eukaryota; Euteleostomi Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00120; DC Domain; TR PROSITE; PS50806; KRAB_RELATED; 1; level=0 XX Names: KRAB-related domain Function: The KRAB-related domain is a weak transcriptional repression domain. XX XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Transcription KW Transcription regulation XX FT From: PS50806 FT DOMAIN from..to FT /note="KRAB-related #" XX Chop: Nter=0; Cter=0; Size: 64-64; Related: None; Repeats: 1; Topology: Undefined; Example: Q16384; Scope: Eukaryota; Homo Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00121; DC Domain; TR PROSITE; PS50070; KRINGLE_2; 1; level=0 XX Names: Kringle domain Function: Kringle domains are thought to play a role in binding mediators, such as membranes, other proteins or phospholipids, and in the regulation of proteolytic activity. XX DR PROSITE; PS00021; KRINGLE_1; 1; trigger=no KW Kringle case KW Disulfide bond end case FT From: PS50070 FT DOMAIN from..to FT /note="Kringle #" FT DISULFID 2..79 FT Tag: disulf; Condition: C-x*-C FT DISULFID 23..62 FT Tag: disulf; Condition: C-x*-C FT DISULFID 51..74 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 73-85; Related: None; Repeats: 1-10; Topology: Undefined; Example: Q14520; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00122; DC Domain; TR PROSITE; PS50025; LAM_G_DOMAIN; 1; level=0 XX Names: Laminin G-like Function: Undefined XX XX case KW Disulfide bond end case FT From: PS50025 FT DOMAIN from..to FT /note="Laminin G-like #" FT DISULFID 147..174 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 126-231; Related: None; Repeats: 1-6; Topology: Undefined; Example: Q24298; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00123; DC Domain; TR PROSITE; PS50820; LCCL; 1; level=0 XX Names: LCCL Function: Undefined XX XX case KW Disulfide bond end case FT From: PS50820 FT DOMAIN from..to FT /note="LCCL #" FT DISULFID 7..25 FT Tag: disulf; Condition: C-x*-C FT DISULFID 29..49 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 94-97; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: O42163; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00124; DC Domain; TR PROSITE; PS50068; LDLRA_2; 1; level=0 XX Names: LDL-receptor class A Function: Undefined XX DR PROSITE; PS01209; LDLRA_1; 1; trigger=no XX case KW Disulfide bond end case FT From: PS50068 FT DOMAIN from..to FT /note="LDL-receptor class A #" FT DISULFID 2..14 FT Tag: disulf; Condition: C-x*-C FT DISULFID 9..27 FT Tag: disulf; Condition: C-x*-C FT DISULFID 21..36 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 28-52; Related: None; Repeats: 1-36; Topology: Not cytoplasmic; Example: Q14114; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00125; DC Domain; TR PROSITE; PS50023; LIM_DOMAIN_2; 1; level=0 XX Names: LIM zinc-binding domain Function: LIM does not bind DNA, rather it seems to act as interface for protein-protein interaction. XX DR PROSITE; PS00478; LIM_DOMAIN_1; 1; trigger=no XX KW LIM domain KW Metal-binding KW Zinc XX FT From: PS50023 FT DOMAIN entry..exit FT /note="LIM zinc-binding #" XX Chop: Nter=0; Cter=0; Size: 30-114; Related: None; Repeats: 1-5; Topology: Undefined; Example: P50479; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00126; DC Domain; TR PROSITE; PS50896; LISH; 1; level=0 XX Names: LisH Function: Undefined XX FT From: PS50896 FT DOMAIN from..to FT /note="LisH #" XX Chop: Nter=0; Cter=0; Size: 33-33; Related: None; Repeats: 1; Topology: Undefined; Example: Q96G75; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00127; DC Domain; TR PROSITE; PS50838; MAGE; 1; level=0 XX Names: MAGE Function: Undefined XX FT From: PS50838 FT DOMAIN from..to FT /note="MAGE #" XX Chop: Nter=0; Cter=0; Size: 123-202; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y5V3; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00128; DC Domain; TR PROSITE; PS50060; MAM_2; 1; level=0 XX Names: MAM Function: Undefined XX DR PROSITE; PS00740; MAM_1; 1; trigger=no FT From: PS50060 FT DOMAIN from..to FT /note="MAM #" XX Chop: Nter=0; Cter=0; Size: 114-171; Related: None; Repeats: 1-6; Topology: Not cytoplasmic; Example: Q9Y493; Scope: Eukaryota; Euteleostomi Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00129; DC Domain; TR PROSITE; PS50144; MATH; 1; level=0 XX Names: MATH Function: Undefined XX FT From: PS50144 FT DOMAIN from..to FT /note="MATH #" XX Chop: Nter=0; Cter=0; Size: 117-162; Related: None; Repeats: 1; Topology: Undefined; Example: O94972; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00130; DC Domain; TR PROSITE; PS50171; ZF_MATRIN; 1; level=0 XX Names: Zinc finger matrin-type Function: Undefined XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW Nucleus KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50171 case and and and FT ZN_FING from..to FT /note="Matrin-type #" else case and and and FT ZN_FING from..to FT /note="Matrin-type #; atypical" else FT ZN_FING from..to FT /note="Matrin-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 31-33; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9ULV3; Scope: Eukaryota Comments: None XX # Revision 1.12 2019/11/20 // AC PRU00131; DC Domain; TR PROSITE; PS50919; MIR; 1; level=0 XX Names: MIR Function: Undefined XX FT From: PS50919 FT DOMAIN from..to FT /note="MIR #" XX Chop: Nter=0; Cter=0; Size: 46-80; Related: None; Repeats: 1-5; Topology: Undefined; Example: Q9Y6A1; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00132; DC Domain; TR PROSITE; PS50202; MSP; 1; level=0 XX Names: MSP Function: Undefined XX FT From: PS50202 FT DOMAIN from..to FT /note="MSP #" XX Chop: Nter=0; Cter=0; Size: 109-128; Related: None; Repeats: 1; Topology: Undefined; Example: Q10484; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00133; DC Domain; TR PROSITE; PS50090; MYB_LIKE; 1; level=0 XX Names: Myb-like domain Myb/SANT domain Myb-like repeat Function: The myb-like domain resembles the myb-type HTH domain, which is a DNA-binding, helix-turn-helix (HTH) domain of ~55 amino acids, typically occurring in a tandem repeat. Myb-like domains can be involved in different functions, such as protein-interactions or DNA-binding. The SANT domain does not bind to DNA, despite its resemblance to myb-like domains, but it is a protein-protein interaction module that can bind to histone-tails (see ). XX XX FT From: PS50090 FT DOMAIN entry..exit FT /note="Myb-like #" XX Chop: Nter=0; Cter=0; Size: 40-120; Related: PRU00625; PRU00624; Repeats: 1-5; Topology: Undefined; Example: O14108; Scope: Eukaryota Viruses; Alpharetrovirus Comments: None XX # Revision 1.11 2019/11/20 // AC PRU00134; DC Domain; TR PROSITE; PS50865; ZF_MYND_2; 1; level=0 XX Names: Zinc finger MYND-type Function: Undefined XX DR PROSITE; PS01360; ZF_MYND_1; 1; trigger=no XX KW Zinc-finger case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case XX FT From: PS50865 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="MYND-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="MYND-type #; atypical" else FT ZN_FING from..to FT /note="MYND-type #; degenerate" end case FT BINDING 1 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 35-47; Related: None; Repeats: 1; Topology: Undefined; Example: Q9P2S6; Scope: Eukaryota Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00135; DC Domain; TR PROSITE; PS50212; RASGEF_NTER; 1; level=0 XX Names: N-terminal Ras-GEF domain Function: Undefined XX KW Guanine-nucleotide releasing factor FT From: PS50212 FT DOMAIN from..to FT /note="N-terminal Ras-GEF #" XX Chop: Nter=0; Cter=0; Size: 114-156; Related: None; Repeats: 1; Topology: Undefined; Example: Q9NZL6; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00136; DC Domain; TR PROSITE; PS50837; NACHT; 1; level=0 XX Names: NACHT-NTPase domain Function: Undefined XX XX GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Nucleotide-binding XX FT From: PS50837 FT DOMAIN from..to FT /note="NACHT #" FT BINDING 7..14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 295-336; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y239; Scope: Eukaryota Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00137; DC Domain; TR PROSITE; PS50177; NTF2_DOMAIN; 1; level=0 XX Names: NTF2 Function: Undefined XX FT From: PS50177 FT DOMAIN from..to FT /note="NTF2 #" XX Chop: Nter=0; Cter=0; Size: 88-188; Related: None; Repeats: 1; Topology: Undefined; Example: P61970; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00138; DC Domain; TR PROSITE; PS50803; OAR; 1; level=0 XX Names: OAR domain Function: Undefined XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0007275; P:multicellular organism development GO GO:0005634; C:nucleus XX KW Developmental protein KW Nucleus XX FT From: PS50803 FT MOTIF from..to FT /note="OAR #" XX Chop: Nter=0; Cter=0; Size: 14-14; Related: None; Repeats: 1; Topology: Undefined; Example: O75364; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.13 2019/11/20 // AC PRU00139; DC Domain; TR PROSITE; PS50802; OTU; 1; level=0 XX Names: OTU Function: Undefined XX FT From: PS50802 FT DOMAIN from..to FT /note="OTU #" XX Chop: Nter=0; Cter=0; Size: 90-172; Related: None; Repeats: 1; Topology: Undefined; Example: Q66431; Scope: Eukaryota Bacteria; Chlamydia Viruses Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00140; DC Domain; TR PROSITE; PS50112; PAS; 1; level=0 XX Names: PAS Function: Undefined XX FT From: PS50112 FT DOMAIN from..to FT /note="PAS #" XX Chop: Nter=0; Cter=0; Size: 24-90; Related: None; Repeats: 1-3; Topology: Undefined; Example: P78714; Scope: Eukaryota Bacteria Archaea; Halobacterium Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00141; DC Domain; TR PROSITE; PS50113; PAC; 1; level=0 XX Names: PAC domain Function: Undefined XX FT From: PS50113 FT DOMAIN from..to FT /note="PAC #" XX Chop: Nter=0; Cter=0; Size: 38-60; Related: None; Repeats: 1-4; Topology: Undefined; Example: P35841; Scope: Eukaryota Bacteria Archaea; Halobacterium Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00142; DC Domain; TR PROSITE; PS50821; PAZ; 1; level=0 XX Names: PAZ Function: Undefined XX FT From: PS50821 FT DOMAIN from..to FT /note="PAZ #" XX Chop: Nter=0; Cter=0; Size: 109-157; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UL18; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00143; DC Domain; TR PROSITE; PS50106; PDZ; 1; level=0 XX Names: PDZ Function: Undefined XX FT From: PS50106 FT DOMAIN from..to FT /note="PDZ #" XX Chop: Nter=0; Cter=0; Size: 46-103; Related: None; Repeats: 1-6; Topology: Undefined; Example: P0AEH1; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00144; DC Domain; TR PROSITE; PS50940; CHIT_BIND_II; 1; level=0 XX Names: Chitin-binding type-2 domain Function: Chitin-binding XX XX GO GO:0008061; F:chitin binding XX KW Chitin-binding case KW Disulfide bond end case XX FT From: PS50940 FT DOMAIN entry..exit FT /note="Chitin-binding type-2 #" FT DISULFID 34..47 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 50-84; Related: None; Repeats: 1-6; Topology: Undefined; Example: Q13231; Scope: Eukaryota Viruses; Alphabaculovirus Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00145; DC Domain; TR PROSITE; PS50003; PH_DOMAIN; 1; level=0 XX Names: PH Function: Undefined XX FT From: PS50003 FT DOMAIN from..to FT /note="PH #" XX Chop: Nter=0; Cter=0; Size: 34-344; Related: None; Repeats: 1-4; Topology: Undefined; Example: P39969; Scope: Eukaryota Viruses; Gammaretrovirus Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00146; DC Domain; TR PROSITE; PS50016; ZF_PHD_2; 1; level=0 XX Names: Zinc finger PHD-type Function: Undefined XX DR PROSITE; PS01359; ZF_PHD_1; 1; trigger=no XX KW Zinc-finger case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case XX FT From: PS50016 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="PHD-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="PHD-type #; atypical" else FT ZN_FING from..to FT /note="PHD-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 34-89; Related: None; Repeats: 1-6; Topology: Undefined; Example: P55197; Scope: Eukaryota Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00147; DC Domain; TR PROSITE; PS50195; PX; 1; level=0 XX Names: PX Function: Undefined XX FT From: PS50195 FT DOMAIN from..to FT /note="PX #" XX Chop: Nter=0; Cter=0; Size: 109-180; Related: None; Repeats: 1; Topology: Undefined; Example: Q13596; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00148; DC Domain; TR PROSITE; PS01179; PID; 1; level=0 XX Names: PID Function: Undefined XX FT From: PS01179 FT DOMAIN from..to FT /note="PID #" XX Chop: Nter=0; Cter=0; Size: 113-188; Related: None; Repeats: 1-2; Topology: Undefined; Example: P49757; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00149; DC Domain; TR PROSITE; PS50256; PIR_REPEAT_2; 1; level=0 XX Names: PIR1/2/3 repeat Function: Undefined XX DR PROSITE; PS00929; PIR_REPEAT_1; 1; trigger=no FT From: PS50256 FT REPEAT from..to FT /note="PIR1/2/3 #" XX Chop: Nter=0; Cter=0; Size: 13-24; Related: None; Repeats: 1-11; Topology: Undefined; Example: P46999; Scope: Eukaryota; Saccharomyces Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00150; DC Domain; TR PROSITE; PS50822; PIWI; 1; level=0 XX Names: Piwi Function: Undefined XX FT From: PS50822 FT DOMAIN from..to FT /note="Piwi #" XX Chop: Nter=0; Cter=0; Size: 274-328; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UL18; Scope: Eukaryota Archaea Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00151; DC Domain; TR PROSITE; PS50093; PKD; 1; level=0 XX Names: PKD Function: Undefined XX FT From: PS50093 FT DOMAIN from..to FT /note="PKD #" XX Chop: Nter=0; Cter=0; Size: 35-101; Related: None; Repeats: 1-16; Topology: Undefined; Example: P43154; Scope: Eukaryota; Euteleostomi Bacteria Archaea; Methanocaldococcus Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00152; DC Domain; TR PROSITE; PS50095; PLAT; 1; level=0 XX Names: PLAT Function: It has been proposed that the PLAT domain may be involved in protein-protein and protein-lipid interaction. XX XX case KW Disulfide bond end case FT From: PS50095 FT DOMAIN from..to FT /note="PLAT #" FT DISULFID 99..115 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 111-141; Related: None; Repeats: 1; Topology: Undefined; Example: Q09624; Scope: Eukaryota Bacteria; Clostridium Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00153; DC Domain; TR PROSITE; PS50035; PLD; 1; level=0 XX Names: PLD phosphodiesterase Function: Undefined XX FT From: PS50035 FT DOMAIN from..to FT /note="PLD phosphodiesterase #" FT ACT_SITE 6 FT Group: 1; Condition: H FT ACT_SITE 8 FT Group: 1; Condition: K FT ACT_SITE 13 FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 25-41; Related: None; Repeats: 1-2; Topology: Undefined; Example: P58766; Scope: Eukaryota Bacteria Viruses; Chordopoxvirinae Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00154; DC Domain; TR PROSITE; PS50078; POLO_BOX; 1; level=0 XX Names: POLO box Function: Point mutations in the POLO box of the budding yeast CDC5 protein abolish the ability of overexpressed CDC5 to interact with the spindle poles and to organize cytokinetic structures. XX XX FT From: PS50078 FT DOMAIN from..to FT /note="POLO box #" XX Chop: Nter=0; Cter=0; Size: 50-95; Related: None; Repeats: 2; Topology: Undefined; Example: P32562; Scope: Eukaryota Comments: None XX # Revision 1.7 2022/10/17 // AC PRU00155; DC Domain; TR PROSITE; PS50868; POST_SET; 1; level=0 XX Names: Post-SET Function: Undefined XX XX case and GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS50868 FT DOMAIN from..to FT /note="Post-SET #" case FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 1; Condition: C FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 1; Condition: C FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 1; Condition: C end case XX Chop: Nter=0; Cter=0; Size: 17-17; Related: None; Repeats: 1; Topology: Undefined; Example: Q8X225; Scope: Eukaryota Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00156; DC Domain; TR PROSITE; PS50072; CSA_PPIASE_2; 1; level=0 XX Names: PPIase cyclophilin-type domain Function: Undefined XX DR PROSITE; PS00170; CSA_PPIASE_1; 1; trigger=no XX GO GO:0016853; F:isomerase activity XX KW Isomerase KW Rotamase XX FT From: PS50072 FT DOMAIN from..to FT /note="PPIase cyclophilin-type #" XX Chop: Nter=0; Cter=0; Size: 147-197; Related: None; Repeats: 1; Topology: Undefined; Example: P23284; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00157; DC Domain; TR PROSITE; PS50867; PRE_SET; 1; level=0 XX Names: Pre-SET Function: Undefined XX XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS50867 FT DOMAIN from..to FT /note="Pre-SET #" FT BINDING 3 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 3 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 1; Condition: C FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 1; Condition: C FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 17 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 1; Condition: C FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 1; Condition: C FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 1; Condition: C FT BINDING 49 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 1; Condition: C FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 1; Condition: C FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 51-96; Related: None; Repeats: 1; Topology: Undefined; Example: Q9H9B1; Scope: Eukaryota Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00158; DC Domain; TR PROSITE; PS50904; PRELI_MSF1; 1; level=0 XX Names: PRELI/MSF1 Function: Undefined XX FT From: PS50904 FT DOMAIN from..to FT /note="PRELI/MSF1 #" XX Chop: Nter=0; Cter=0; Size: 172-175; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y3B1; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00159; DC Domain; TR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1; level=0 XX Names: Protein kinase domain Function: Undefined XX case DE + AltName: EC=2.7.11.-; else case DE + AltName: EC=2.7.10.-; else case DE + AltName: EC=2.7.-.-; end case case not CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically CC inactive. end case case CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. else case and CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. Ephrin receptor subfamily. else case CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. end case XX case DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1; trigger=no else case DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1; trigger=yes end case case DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1; trigger=no else case DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1; trigger=no end case XX case GO GO:0016301; F:kinase activity GO GO:0016740; F:transferase activity GO GO:0004674; F:protein serine/threonine kinase activity KW Kinase KW Transferase KW Serine/threonine-protein kinase else case GO GO:0016301; F:kinase activity GO GO:0016740; F:transferase activity GO GO:0004713; F:protein tyrosine kinase activity KW Kinase KW Transferase KW Tyrosine-protein kinase end case case GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding KW ATP-binding KW Nucleotide-binding end case FT From: PS50011 FT DOMAIN from..to FT /note="Protein kinase #" case or FT BINDING 7..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Tag: ATP end case case FT BINDING 30 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" end case case FT ACT_SITE 124 FT /note="Proton acceptor" FT Tag: active; Condition: D end case XX Chop: Nter=0; Cter=0; Size: 205-549; Related: None; Repeats: 1-2; Topology: Undefined; Example: O54967; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.47 2022/11/19 // AC PRU00160; DC Domain; TR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1; level=0 TR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1; level=0 XX Names: Protein-tyrosine phosphatase domain Function: Tyrosine specific protein phosphatases (EC 3.1.3.48) (PTPase) are enzymes that catalyze the removal of a phosphate group attached to a tyrosine residue. XX case DE + RecName: EC=3.1.3.-; XX DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1; trigger=no end case DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1; trigger=no XX case GO GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity GO GO:0004725; F:protein tyrosine phosphatase activity GO GO:0016787; F:hydrolase activity XX KW Protein phosphatase KW Hydrolase end case XX FT From: any case FT DOMAIN from..to FT /note="Tyrosine-protein phosphatase #" FT ACT_SITE 89 FT /note="Phosphocysteine intermediate" FT Tag: act_site; Condition: C else case FT DOMAIN from..to FT /note="Tyrosine-protein phosphatase #" FT ACT_SITE 196 FT /note="Phosphocysteine intermediate" FT Tag: act_site; Condition: C end case XX Chop: Nter=0; Cter=0; Size: 63-419; Related: None; Repeats: 1-2; Topology: Undefined; Example: P23469; Q6NKR2; Scope: Eukaryota Comments: None XX # Revision 1.13 2020/05/07 // AC PRU00161; DC Domain; TR PROSITE; PS50890; PUA; 1; level=0 XX Names: PUA Function: Undefined XX FT From: PS50890 FT DOMAIN from..to FT /note="PUA #" XX Chop: Nter=0; Cter=0; Size: 75-92; Related: None; Repeats: 1; Topology: Undefined; Example: Q58428; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00162; DC Domain; TR PROSITE; PS50812; PWWP; 1; level=0 XX Names: PWWP Function: Undefined XX FT From: PS50812 FT DOMAIN from..to FT /note="PWWP #" XX Chop: Nter=0; Cter=0; Size: 51-84; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9ULU4; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00163; DC Domain; TR PROSITE; PS50086; TBC_RABGAP; 1; level=0 XX Names: Rab-GAP TBC Function: Undefined XX FT From: PS50086 FT DOMAIN from..to FT /note="Rab-GAP TBC #" XX Chop: Nter=0; Cter=0; Size: 171-284; Related: None; Repeats: 1; Topology: Undefined; Example: P26448; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00164; DC Domain; TR PROSITE; PS50196; RANBD1; 1; level=0 XX Names: RanBD1 Function: Undefined XX FT From: PS50196 FT DOMAIN from..to FT /note="RanBD1 #" XX Chop: Nter=0; Cter=0; Size: 134-141; Related: None; Repeats: 1-4; Topology: Undefined; Example: P32499; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00165; DC Domain; TR PROSITE; PS50085; RAPGAP; 1; level=0 XX Names: Rap-GAP domain Function: Undefined XX XX GO GO:0005096; F:GTPase activator activity XX KW GTPase activation XX FT From: PS50085 FT DOMAIN from..to FT /note="Rap-GAP #" XX Chop: Nter=0; Cter=0; Size: 217-235; Related: None; Repeats: 1; Topology: Undefined; Example: P47736; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00166; DC Domain; TR PROSITE; PS50200; RA; 1; level=0 XX Names: Ras-associating Function: Undefined XX FT From: PS50200 FT DOMAIN from..to FT /note="Ras-associating #" XX Chop: Nter=0; Cter=0; Size: 80-103; Related: None; Repeats: 1-2; Topology: Undefined; Example: P55196; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00167; DC Domain; TR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1; level=0 XX Names: Ras-GAP Function: Undefined XX DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1; trigger=no FT From: PS50018 FT DOMAIN from..to FT /note="Ras-GAP #" XX Chop: Nter=0; Cter=0; Size: 190-234; Related: None; Repeats: 1; Topology: Undefined; Example: P21359; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00168; DC Domain; TR PROSITE; PS50009; RASGEF_CAT; 1; level=0 XX Names: Ras guanine-nucleotide exchange factors catalytic domain Function: Undefined XX XX DR PROSITE; PS00720; RASGEF; 1; trigger=no XX KW Guanine-nucleotide releasing factor XX FT From: PS50009 FT DOMAIN from..to FT /note="Ras-GEF #" XX Chop: Nter=0; Cter=0; Size: 220-271; Related: None; Repeats: 1; Topology: Undefined; Example: Q9NZL6; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00169; DC Domain; TR PROSITE; PS50110; RESPONSE_REGULATORY; 1; level=0 XX Names: Response regulatory domain Function: Undefined XX XX case KW Phosphoprotein end case XX FT From: PS50110 FT DOMAIN from..to FT /note="Response regulatory #" FT MOD_RES 50 FT /note="4-aspartylphosphate" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 87-143; Related: None; Repeats: 1-3; Topology: Undefined; Example: P0AEC5; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None XX # Revision 1.12 2019/11/20 // AC PRU00170; DC Domain; TR PROSITE; PS50845; RETICULON; 1; level=0 XX Names: Reticulon Function: Undefined XX FT From: PS50845 FT DOMAIN from..to FT /note="Reticulon #" XX Chop: Nter=0; Cter=0; Size: 182-201; Related: None; Repeats: 1; Topology: Undefined; Example: P53694; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00171; DC Domain; TR PROSITE; PS50132; RGS; 1; level=0 XX Names: RGS Function: Undefined XX FT From: PS50132 FT DOMAIN from..to FT /note="RGS #" XX Chop: Nter=0; Cter=0; Size: 99-270; Related: None; Repeats: 1-2; Topology: Undefined; Example: O15169; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00172; DC Domain; TR PROSITE; PS50238; RHOGAP; 1; level=0 XX Names: Rho GTPase-activating proteins domain Function: Undefined XX XX GO GO:0005096; F:GTPase activator activity XX KW GTPase activation XX FT From: PS50238 FT DOMAIN from..to FT /note="Rho-GAP #" XX Chop: Nter=0; Cter=0; Size: 173-260; Related: None; Repeats: 1; Topology: Undefined; Example: Q3KRB8; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00173; DC Domain; TR PROSITE; PS50206; RHODANESE_3; 1; level=0 XX Names: Rhodanese Function: Undefined XX case =2> DR PROSITE; PS00380; RHODANESE_1; 1; trigger=no DR PROSITE; PS00683; RHODANESE_2; 1; trigger=no else DR PROSITE; PS00380; RHODANESE_1; 0-1; trigger=no DR PROSITE; PS00683; RHODANESE_2; 0-1; trigger=no end case FT From: PS50206 FT DOMAIN from..to FT /note="Rhodanese #" case FT ACT_SITE 78 FT /note="S-selanylcysteine intermediate" else case FT ACT_SITE 78 FT /note="Cysteine persulfide intermediate" end case XX Chop: Nter=0; Cter=0; Size: 75-141; Related: None; Repeats: 1-3; Topology: Undefined; Example: P96888; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.14 2019/11/20 // AC PRU00174; DC Domain; TR PROSITE; PS50231; RICIN_B_LECTIN; 1; level=0 XX Names: Ricin B-type lectin Function: The ricin B lectin domain can be present in one or more copies and has been shown in some instance to bind simple sugars, such as galactose or lactose. XX XX GO GO:0030246; F:carbohydrate binding XX KW Lectin case KW Disulfide bond end case XX FT From: PS50231 FT DOMAIN from..to FT /note="Ricin B-type lectin #" FT DISULFID 14..31 FT Tag: disulf; Condition: C-x*-C FT DISULFID 57..74 FT Tag: disulf; Condition: C-x*-C FT DISULFID 100..118 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 50-151; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q95ZJ1; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00175; DC Domain; TR PROSITE; PS50089; ZF_RING_2; 1; level=0 XX Names: Zinc finger RING-type Function: It has been shown that several RING fingers act as E3 enzymes in the ubiquitination process. XX **CC -!- PATHWAY: Ubiquitin conjugation; third step. **CC -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2 **CC ubiquitin-conjugating enzyme. DR PROSITE; PS00518; ZF_RING_1; 1; trigger=no XX KW Zinc-finger **KW Ubl conjugation pathway case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case XX FT From: PS50089 case and and and and and and and FT ZN_FING from..to FT /note="RING-type #" else case and and and and and and and FT ZN_FING from..to FT /note="RING-type #; atypical" else FT ZN_FING from..to FT /note="RING-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 10-70; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9M0R4; Scope: Eukaryota Viruses Comments: None XX # Revision 1.14 2019/11/20 // AC PRU00176; DC Domain; TR PROSITE; PS50102; RRM; 1; level=0 XX Names: RNA recognition motif (RRM) domain Function: binding RNA XX XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS50102 FT DOMAIN from..to FT /note="RRM #" XX Chop: Nter=0; Cter=0; Size: 52-151; Related: None; Repeats: 1-6; Topology: Undefined; Example: P52298; Scope: Eukaryota Bacteria; Synechocystis Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00177; DC Domain; TR PROSITE; PS50142; RNASE_3_2; 1; level=0 XX Names: RNase III Function: Undefined XX DR PROSITE; PS00517; RNASE_3_1; 1; trigger=no FT From: PS50142 FT DOMAIN from..to FT /note="RNase III #" XX Chop: Nter=0; Cter=0; Size: 67-209; Related: None; Repeats: 1-2; Topology: Undefined; Example: P47607; Scope: Eukaryota Bacteria Viruses; Chlorovirus Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00178; DC Domain; TR PROSITE; PS50826; RUN; 1; level=0 XX Names: RUN Function: Undefined XX FT From: PS50826 FT DOMAIN from..to FT /note="RUN #" XX Chop: Nter=0; Cter=0; Size: 142-142; Related: None; Repeats: 1; Topology: Undefined; Example: Q92622; Scope: Eukaryota; Homo Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00179; DC Domain; TR PROSITE; PS50908; RWD; 1; level=0 XX Names: RWD Function: Undefined XX FT From: PS50908 FT DOMAIN from..to FT /note="RWD #" XX Chop: Nter=0; Cter=0; Size: 59-151; Related: None; Repeats: 1; Topology: Undefined; Example: P57060; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00180; DC Domain; TR PROSITE; PS50126; S1; 1; level=0 XX Names: S1 motif Function: Undefined XX FT From: PS50126 FT DOMAIN from..to FT /note="S1 motif #" XX Chop: Nter=0; Cter=0; Size: 33-101; Related: None; Repeats: 1-12; Topology: Undefined; Example: P05198; Scope: Eukaryota Bacteria Archaea Viruses; Orthopoxvirus Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00181; DC Domain; TR PROSITE; PS50832; S1_IF1_TYPE; 1; level=0 XX Names: S1-like domain Function: Undefined XX XX GO GO:0006412; P:translation GO GO:0003743; F:translation initiation factor activity XX KW Initiation factor KW Protein biosynthesis XX FT From: PS50832 FT DOMAIN from..to FT /note="S1-like #" XX Chop: Nter=0; Cter=0; Size: 57-76; Related: None; Repeats: 1; Topology: Undefined; Example: P47813; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/20 // AC PRU00182; DC Domain; TR PROSITE; PS50889; S4; 1; level=0 XX Names: S4 RNA-binding Function: Undefined XX XX DR PROSITE; PS00528; RIBOSOMAL_S4E; 0-1; trigger=no DR PROSITE; PS00632; RIBOSOMAL_S4; 0-1; trigger=no XX KW RNA-binding case or KW rRNA-binding end case XX FT From: PS50889 FT DOMAIN from..to FT /note="S4 RNA-binding #" XX Chop: Nter=0; Cter=0; Size: 53-87; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q44264; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00183; DC Domain; TR PROSITE; PS50275; SAC; 1; level=0 XX Names: SAC Function: Undefined XX FT From: PS50275 FT DOMAIN from..to FT /note="SAC #" XX Chop: Nter=0; Cter=0; Size: 301-394; Related: None; Repeats: 1; Topology: Undefined; Example: P32368; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00184; DC Domain; TR PROSITE; PS50105; SAM_DOMAIN; 1; level=0 XX Names: SAM Function: Undefined XX FT From: PS50105 FT DOMAIN from..to FT /note="SAM #" XX Chop: Nter=0; Cter=0; Size: 39-80; Related: None; Repeats: 1-2; Topology: Undefined; Example: P39969; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00185; DC Domain; TR PROSITE; PS50864; SAND; 1; level=0 XX Names: SAND domain Function: The SAND domain has been proposed to mediate the DNA binding activity. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus XX FT From: PS50864 FT DOMAIN from..to FT /note="SAND #" XX Chop: Nter=0; Cter=0; Size: 81-101; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y692; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.11 2019/11/20 // AC PRU00186; DC Domain; TR PROSITE; PS50800; SAP; 1; level=0 XX Names: SAP Function: Undefined XX FT From: PS50800 FT DOMAIN from..to FT /note="SAP #" XX Chop: Nter=0; Cter=0; Size: 35-35; Related: None; Repeats: 1-2; Topology: Undefined; Example: P45951; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00187; DC Domain; TR PROSITE; PS50804; SCAN_BOX; 1; level=0 XX Names: SCAN box Function: Undefined XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX KW Nucleus XX GO GO:0005634; C:nucleus XX FT From: PS50804 FT DOMAIN from..to FT /note="SCAN box #" XX Chop: Nter=0; Cter=0; Size: 59-95; Related: None; Repeats: 1; Topology: Undefined; Example: P17028; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.14 2019/11/20 // AC PRU00188; DC Domain; TR PROSITE; PS50024; SEA; 1; level=0 XX Names: SEA domain Function: The SEA domain has around 120 residues and its function is not known. XX case KW Autocatalytic cleavage end case KW Glycoprotein XX FT From: PS50024 FT DOMAIN from..to FT /note="SEA #" c? FT SITE 65..66 FT /note="Cleavage; by autolysis" XX Chop: Nter=0; Cter=0; Size: 111-125; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: Q29435; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.9 2019/11/20 // AC PRU00189; DC Domain; TR PROSITE; PS50190; SEC7; 1; level=0 XX Names: SEC7 Function: Undefined XX FT From: PS50190 FT DOMAIN from..to FT /note="SEC7 #" XX Chop: Nter=0; Cter=0; Size: 84-206; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UIA0; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00190; DC Domain; TR PROSITE; PS50280; SET; 1; level=0 XX Names: SET Function: Lysine N-methyltransferase XX case DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. end case XX case KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase end case XX FT From: PS50280 FT DOMAIN from..to FT /note="SET #" case FT BINDING 96 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 1; Condition: C end case FT BINDING 129 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: 116-469; Related: None; Repeats: 1; Topology: Undefined; Example: P42124; Scope: Eukaryota Comments: None XX # Revision 1.15 2022/11/19 // AC PRU00191; DC Domain; TR PROSITE; PS50001; SH2; 1; level=0 XX Names: SH2 domain Function: SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine- containing target peptides in a sequence-specific and strictly phosphorylation-dependent manner. XX KW SH2 domain FT From: PS50001 FT DOMAIN from..to FT /note="SH2 #" XX Chop: Nter=0; Cter=0; Size: 65-129; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q13239; Scope: Eukaryota Viruses; Retroviridae Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00192; DC Domain; TR PROSITE; PS50002; SH3; 1; level=0 XX Names: Src homology 3 (SH3) domain Function: The function of the SH3 domain is not well understood. The current opinion is that they mediate assembly of specific protein complexes via binding to proline-rich peptides. XX XX KW SH3 domain XX FT From: PS50002 FT DOMAIN from..to FT /note="SH3 #" XX Chop: Nter=0; Cter=0; Size: 21-94; Related: None; Repeats: 1-6; Topology: Undefined; Example: P39969; Scope: Eukaryota Viruses; Retroviridae Comments: None XX # Revision 1.8 2019/11/20 // AC PRU00193; DC Domain; TR PROSITE; PS50045; SIGMA54_INTERACT_4; 1; level=0 XX Names: Sigma-54 factor interaction domain Function: Undefined XX DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1; trigger=no DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1; trigger=no DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1; trigger=no XX GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW ATP-binding KW Nucleotide-binding KW Transcription KW Transcription regulation XX FT From: PS50045 FT DOMAIN from..to FT /note="Sigma-54 factor interaction #" FT BINDING 29..36 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 92..101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 200-270; Related: None; Repeats: 1; Topology: Undefined; Example: P41789; Scope: Bacteria Comments: None XX # Revision 1.14 2022/11/19 // AC PRU00194; DC Domain; TR PROSITE; PS50225; SOCS; 1; level=0 XX Names: SOCS box Function: Undefined XX FT From: PS50225 FT DOMAIN from..to FT /note="SOCS box #" XX Chop: Nter=0; Cter=0; Size: 47-64; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y576; Scope: Eukaryota; Euteleostomi Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00195; DC Domain; TR PROSITE; PS50831; SOHO; 1; level=0 XX Names: SoHo domain Function: Undefined XX FT From: PS50831 FT DOMAIN from..to FT /note="SoHo #" XX Chop: Nter=0; Cter=0; Size: 46-73; Related: None; Repeats: 1; Topology: Undefined; Example: P28220; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.4 2019/11/20 // AC PRU00196; DC Domain; TR PROSITE; PS50287; SRCR_2; 1; level=0 XX Names: SRCR domain Scavenger receptor cysteine-rich domain Function: Cysteine-rich domains that are likely to mediate protein-protein interactions and ligand binding. XX DR PROSITE; PS00420; SRCR_1; 1; trigger=no XX case KW Disulfide bond end case FT From: PS50287 FT DOMAIN from..to FT /note="SRCR #" FT DISULFID 26..90 FT Tag: disulf; Condition: C-x*-C FT DISULFID 39..100 FT Tag: disulf; Condition: C-x*-C FT DISULFID 70..80 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=28; Size: 90-130; Related: None; Repeats: 1-11; Topology: Undefined; Example: Q08380; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.7 2019/11/20 // AC PRU00197; DC Domain; TR PROSITE; PS50848; START; 1; level=0 XX Names: START Function: Undefined XX FT From: PS50848 FT DOMAIN from..to FT /note="START #" XX Chop: Nter=0; Cter=0; Size: 202-240; Related: None; Repeats: 1; Topology: Undefined; Example: P46607; Scope: Eukaryota Bacteria; Pseudomonas Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00198; DC Domain; TR PROSITE; PS50801; STAS; 1; level=0 XX Names: STAS Function: Undefined XX FT From: PS50801 FT DOMAIN from..to FT /note="STAS #" XX Chop: Nter=0; Cter=0; Size: 90-213; Related: None; Repeats: 1; Topology: Undefined; Example: P58743; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00199; DC Domain; TR PROSITE; PS50156; SSD; 1; level=0 XX Names: SSD Function: Undefined XX FT From: PS50156 FT DOMAIN from..to FT /note="SSD #" XX Chop: Nter=0; Cter=0; Size: 156-182; Related: None; Repeats: 1; Topology: Undefined; Example: Q13635; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/20 // AC PRU00200; DC Domain; TR PROSITE; PS50296; SUI1; 1; level=0 XX Names: SUI1 Function: Undefined XX FT From: PS50296 FT DOMAIN from..to FT /note="SUI1 #" XX Chop: Nter=0; Cter=0; Size: 60-74; Related: None; Repeats: 1; Topology: Undefined; Example: O43583; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00201; DC Domain; TR PROSITE; PS50252; TBOX_3; 1; level=0 XX Names: T-box domain Function: It probably binds DNA. XX CC -!- SUBCELLULAR LOCATION: Nucleus. DR PROSITE; PS01283; TBOX_1; 1; trigger=no DR PROSITE; PS01264; TBOX_2; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW Nucleus KW DNA-binding XX FT From: PS50252 FT DNA_BIND 6..180 FT /note="T-box #" XX Chop: Nter=0; Cter=0; Size: 64-257; Related: None; Repeats: 1-2; Topology: Undefined; Example: O15178; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.9 2019/11/21 // AC PRU00202; DC Domain; TR PROSITE; PS50192; T_SNARE; 1; level=0 XX Names: t-SNARE coiled-coil homology domain Function: Undefined XX XX KW Coiled coil XX FT From: PS50192 FT DOMAIN from..to FT /note="t-SNARE coiled-coil homology #" XX Chop: Nter=0; Cter=0; Size: 63-65; Related: None; Repeats: 1-2; Topology: Undefined; Example: O15155; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00203; DC Domain; TR PROSITE; PS50134; ZF_TAZ; 1; level=0 XX Names: Zinc finger TAZ-type Function: Undefined XX XX KW Zinc-finger KW Zinc KW Metal-binding XX FT From: PS50134 FT ZN_FING from..to FT /note="TAZ-type #" XX Chop: Nter=0; Cter=0; Size: 82-107; Related: None; Repeats: 2; Topology: Undefined; Example: Q92793; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00204; DC Domain; TR PROSITE; PS50104; TIR; 1; level=0 XX Names: TIR Function: The TIR domain has been defined as a scaffold that promotes assembly of signaling complexes via protein-protein interactions. However, the scaffolding function may be a a recent adaptation. The primordial function of the TIR domain is a self-association-dependent nicotinamide dinucleotide (NAD(+))-cleaving enzyme (NADase) activity that cleaves NAD(+) into nicotinamide (Nam) and ADP-ribose (ADPR), cyclic ADPR (cADPR) or variant cADPR (v-cADPR), with catalytic cleavage executed by a conserved glutamic acid. XX case and and and and and DE + AltName: Full=Probable NAD(+) hydrolase; DE EC=3.2.2.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity. CC Self-association of TIR domains is required for NADase activity. XX KW NAD KW Hydrolase end case XX FT From: PS50104 FT DOMAIN from..to FT /note="TIR #" FT ACT_SITE 77 FT Condition: E case and and and and FT BINDING 10..11 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT BINDING 41 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: E end case XX Chop: Nter=0; Cter=0; Size: 125-180; Related: None; Repeats: 1; Topology: Undefined; Example: Q6SZW1; Scope: Eukaryota Comments: None XX # Revision 1.11 2022/11/19 // AC PRU00205; DC Domain; TR PROSITE; PS50922; TLC; 1; level=0 XX Names: TLC domain Function: Undefined XX XX GO GO:0016020; C:membrane XX KW Membrane KW Transmembrane XX FT From: PS50922 FT DOMAIN from..to FT /note="TLC #" XX Chop: Nter=0; Cter=0; Size: 185-217; Related: None; Repeats: 1; Topology: Undefined; Example: P27544; Scope: Eukaryota Comments: None XX # Revision 1.7 2022/09/29 // AC PRU00206; DC Domain; TR PROSITE; PS50050; TNFR_NGFR_2; 1; level=0 XX Names: TNFR-Cys Function: Undefined XX DR PROSITE; PS00652; TNFR_NGFR_1; 1; trigger=no XX case KW Disulfide bond end case FT From: PS50050 FT REPEAT from..to FT /note="TNFR-Cys #" FT DISULFID 2..17 FT Tag: disulf; Condition: C-x*-C FT DISULFID 20..33 FT Tag: disulf; Condition: C-x*-C FT DISULFID 23..41 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 18-61; Related: None; Repeats: 1-6; Topology: Not cytoplasmic; Example: P68637; Scope: Eukaryota Viruses; Chordopoxvirinae Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00207; DC Domain; TR PROSITE; PS50145; ZF_TRAF; 1; level=0 XX Names: Zinc finger TRAF-type Function: Undefined XX XX KW Zinc-finger KW Zinc KW Metal-binding XX FT From: PS50145 FT ZN_FING from..to FT /note="TRAF-type #" XX Chop: Nter=0; Cter=0; Size: 53-59; Related: None; Repeats: 1-3; Topology: Undefined; Example: P11467; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00208; DC Domain; TR PROSITE; PS50926; TRAM; 1; level=0 XX Names: TRAM domain Function: The TRAM domain is predicted to bind tRNA. XX FT From: PS50926 FT DOMAIN from..to FT /note="TRAM #" XX Chop: Nter=0; Cter=0; Size: 55-81; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q96SZ6; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00209; DC Domain; TR PROSITE; PS50886; TRBD; 1; level=0 XX Names: tRNA-binding domain Function: Undefined XX XX GO GO:0003723; F:RNA binding GO GO:0000049; F:tRNA binding XX KW RNA-binding KW tRNA-binding XX FT From: PS50886 FT DOMAIN from..to FT /note="tRNA-binding #" XX Chop: Nter=0; Cter=0; Size: 93-123; Related: None; Repeats: 1; Topology: Undefined; Example: Q12904; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00210; DC Domain; TR PROSITE; PS50092; TSP1; 1; level=0 XX Names: TSP type-1 Function: Undefined XX XX case KW Disulfide bond end case FT From: PS50092 FT DOMAIN from..to FT /note="TSP type-1 #" FT DISULFID 12..47 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 16..52 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 26..37 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 2..37 FT Tag: disulf; Group: 2; Condition: C-x*-C FT DISULFID 12..16 FT Tag: disulf; Group: 2; Condition: C-x*-C FT DISULFID 47..52 FT Tag: disulf; Group: 2; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 41-84; Related: None; Repeats: 1-15; Topology: Undefined; Example: Q18206; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00211; DC Domain; TR PROSITE; PS50304; TUDOR; 1; level=0 XX Names: Tudor Function: Undefined XX FT From: PS50304 FT DOMAIN from..to FT /note="Tudor #" XX Chop: Nter=0; Cter=0; Size: 56-64; Related: None; Repeats: 1-9; Topology: Undefined; Example: Q15047; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00212; DC Domain; TR PROSITE; PS50030; UBA; 1; level=0 XX Names: UBA Function: Undefined XX FT From: PS50030 FT DOMAIN from..to FT /note="UBA #" XX Chop: Nter=0; Cter=0; Size: 39-51; Related: None; Repeats: 1-3; Topology: Undefined; Example: P45974; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00213; DC Domain; TR PROSITE; PS50330; UIM; 1; level=0 XX Names: UIM Function: Undefined XX FT From: PS50330 FT DOMAIN from..to FT /note="UIM #" XX Chop: Nter=0; Cter=0; Size: 17-20; Related: None; Repeats: 1-3; Topology: Undefined; Example: P40343; Scope: Eukaryota; Euteleostomi Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00214; DC Domain; TR PROSITE; PS50053; UBIQUITIN_2; 1; level=0 TR PROSITE; PS51943; COV_NSP3A_UBL; 1; level=0 TR PROSITE; PS51944; COV_NSP3D_UBL; 1; level=0 XX Names: Ubiquitin-like Function: Undefined XX case DR PROSITE; PS00299; UBIQUITIN_1; 1; trigger=no end case XX FT From: any FT DOMAIN from..to FT /note="Ubiquitin-like #" case FT CROSSLNK 76 FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with FT K-? in acceptor proteins)" FT Condition: G end case XX Chop: Nter=0; Cter=0; Size: 39-87; Related: None; Repeats: 1-2; Topology: Undefined; Example: P63165; Scope: Eukaryota Comments: None XX # Revision 1.8 2020/10/02 // AC PRU00215; DC Domain; TR PROSITE; PS50033; UBX; 1; level=0 XX Names: UBX Function: Undefined XX FT From: PS50033 FT DOMAIN from..to FT /note="UBX #" XX Chop: Nter=0; Cter=0; Size: 77-145; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BZV1; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00216; DC Domain; TR PROSITE; PS50173; UMUC; 1; level=0 XX Names: umuC domain Function: Undefined XX XX case GO GO:0000287; F:magnesium ion binding XX KW Magnesium KW Metal-binding end case XX FT From: PS50173 FT DOMAIN from..to FT /note="UmuC #" FT ACT_SITE 102 FT Condition: E FT BINDING 5 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: D FT BINDING 101 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: D FT SITE 10 FT /note="Substrate discrimination" XX Chop: Nter=0; Cter=0; Size: 177-257; Related: None; Repeats: 1; Topology: Undefined; Example: Q4JB80; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00217; DC Domain; TR PROSITE; PS50151; UVR; 1; level=0 XX Names: UVR Function: Undefined XX FT From: PS50151 FT DOMAIN from..to FT /note="UVR #" XX Chop: Nter=0; Cter=0; Size: 35-36; Related: None; Repeats: 1; Topology: Undefined; Example: P46523; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00218; DC Domain; TR PROSITE; PS50179; VHS; 1; level=0 XX Names: VHS domain Function: The VHS domain of Hrs makes both intra- and intermolecular interactions with FYVE domains and it has been proposed that it might as well interact with other domains. XX FT From: PS50179 FT DOMAIN from..to FT /note="VHS #" XX Chop: Nter=0; Cter=0; Size: 131-137; Related: PRU00243; Repeats: 1; Topology: Cytoplasmic; Example: P40343; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00219; DC Domain; TR PROSITE; PS50234; VWFA; 1; level=0 XX Names: VWFA Function: Undefined XX FT From: PS50234 FT DOMAIN from..to FT /note="VWFA #" XX Chop: Nter=0; Cter=0; Size: 123-237; Related: None; Repeats: 1-12; Topology: Undefined; Example: Q9H6X2; Scope: Eukaryota Bacteria Archaea; Methanocaldococcus Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00220; DC Domain; TR PROSITE; PS50184; VWFC_2; 1; level=0 XX Names: VWFC Function: Undefined XX DR PROSITE; PS01208; VWFC_1; 1; trigger=no FT From: PS50184 FT DOMAIN from..to FT /note="VWFC #" XX Chop: Nter=0; Cter=0; Size: 46-82; Related: None; Repeats: 1-5; Topology: Undefined; Example: P02452; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00221; DC Domain; TR PROSITE; PS50082; WD_REPEATS_2; 1; level=0 TR PROSITE; PS50294; WD_REPEATS_REGION; 1; level=0 XX Names: WD repeat Function: Undefined XX DR PROSITE; PS00678; WD_REPEATS_1; 1; trigger=no XX KW WD repeat XX FT From: PS50082 FT REPEAT from..to FT /note="WD #" XX Chop: Nter=0; Cter=0; Size: 23-83; Related: RRU00004!!; Repeats: 1-16; Topology: Undefined; Example: O14576; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00222; DC Domain; TR PROSITE; PS50814; WIF; 1; level=0 XX Names: WIF domain Function: The WIF domain is an around 140-amino acid module which presents an independent folding unit in receptor molecules that bind to palmitoylated signaling proteins. XX XX case KW Disulfide bond end case XX FT From: PS50814 FT DOMAIN from..to FT /note="WIF #" FT DISULFID 97..133 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 129-139; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9Y5W5; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00223; DC Domain; TR PROSITE; PS50811; WRKY; 1; level=0 XX Names: WRKY DNA-binding domain Function: The WRKY domain binds specifically to the DNA sequence motif (T)(T)TGAC[CT], which is known as the W box. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS50811 FT DNA_BIND from..to FT /note="WRKY #" XX Chop: Nter=0; Cter=0; Size: 65-71; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9SI37; Scope: Eukaryota; Arabidopsis Comments: None XX # Revision 1.14 2022/06/27 // AC PRU00224; DC Domain; TR PROSITE; PS50020; WW_DOMAIN_2; 1; level=0 XX Names: WW/rsp5/WWP domain Function: It has been shown to bind proteins with particular proline- motifs, [AP]-P-P-[AP]-Y. XX DR PROSITE; PS01159; WW_DOMAIN_1; 1; trigger=no FT From: PS50020 FT DOMAIN from..to FT /note="WW #" XX Chop: Nter=0; Cter=0; Size: 26-35; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q9H4B6; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00225; DC Domain; TR PROSITE; PS50882; YTH; 1; level=0 XX Names: YTH Function: Undefined XX FT From: PS50882 FT DOMAIN from..to FT /note="YTH #" XX Chop: Nter=0; Cter=0; Size: 135-138; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BYJ9; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00226; DC Domain; TR PROSITE; PS50081; ZF_DAG_PE_2; 1; level=0 XX Names: Zinc finger phorbol-ester/DAG-type Function: It is essential for DAG/PE-binding. XX DR PROSITE; PS00479; ZF_DAG_PE_1; 1; trigger=no XX GO GO:0019992; F:diacylglycerol binding XX KW Metal-binding KW Zinc KW Zinc-finger XX FT From: PS50081 FT ZN_FING from..to FT /note="Phorbol-ester/DAG-type #" XX Chop: Nter=0; Cter=0; Size: 43-59; Related: None; Repeats: 1-3; Topology: Undefined; Example: P23743; Scope: Eukaryota Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00227; DC Domain; TR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1; level=0 XX Names: Fungal Zn(2)-Cys(6) binuclear cluster domain Function: It binds DNA in a zinc-dependent fashion. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Metal-binding KW Nucleus KW Transcription KW Transcription regulation KW Zinc XX FT From: PS50048 FT DNA_BIND 2..29 FT /note="Zn(2)-C6 fungal-type #" XX Chop: Nter=0; Cter=0; Size: 27-38; Related: None; Repeats: 1; Topology: Undefined; Example: P87000; Scope: Eukaryota; Fungi Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00228; DC Domain; TR PROSITE; PS50135; ZF_ZZ_2; 1; level=0 XX Names: Zinc finger ZZ-type Function: Undefined XX DR PROSITE; PS01357; ZF_ZZ_1; 1; trigger=no XX KW Zinc-finger case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case XX FT From: PS50135 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="ZZ-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="ZZ-type #; atypical" else FT ZN_FING from..to FT /note="ZZ-type #; degenerate" end case FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 30 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 42-48; Related: None; Repeats: 1; Topology: Undefined; Example: Q92793; Scope: Eukaryota Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00229; DC Domain; TR PROSITE; PS50914; BON; 1; level=0 XX Names: BON domain Function: The BON domain is likely to be a phospholipid-binding domain. XX FT From: PS50914 FT DOMAIN from..to FT /note="BON #" XX Chop: Nter=0; Cter=0; Size: 67-71; Related: None; Repeats: 1-2; Topology: Undefined; Example: P55702; Scope: Bacteria Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00230; DC Domain; TR PROSITE; PS50933; CHRD; 1; level=0 XX Names: CHRD domain Function: Undefined XX XX GO GO:0007275; P:multicellular organism development XX KW Developmental protein XX FT From: PS50933 FT DOMAIN from..to FT /note="CHRD #" XX Chop: Nter=0; Cter=0; Size: 110-141; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q9H2X0; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00231; DC Domain; TR PROSITE; PS50859; LONGIN; 1; level=0 XX Names: Longin domain Function: It has been proposed that the longin domain might be involved in the regulation of membrane fusion. XX XX KW Coiled coil XX FT From: PS50859 FT DOMAIN from..to FT /note="Longin #" XX Chop: Nter=0; Cter=0; Size: 104-128; Related: None; Repeats: 1; Topology: Undefined; Example: Q94AU2; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00232; DC Domain; TR PROSITE; PS50906; NIT; 1; level=0 XX Names: Nitrate and nitrite sensing (NIT) domain Function: Undefined XX FT From: PS50906 FT DOMAIN from..to FT /note="NIT #" XX Chop: Nter=0; Cter=0; Size: 248-248; Related: None; Repeats: 1; Topology: Undefined; Example: Q48468; Scope: Bacteria; Klebsiella Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00233; DC Domain; TR PROSITE; PS50900; PLAC; 1; level=0 XX Names: PLAC domain Function: Undefined XX XX FT From: PS50900 FT DOMAIN from..to FT /note="PLAC #" XX Chop: Nter=0; Cter=0; Size: 38-45; Related: None; Repeats: 1; Topology: Undefined; Example: P29122; Scope: Eukaryota; Eutheria Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00234; DC Domain; TR PROSITE; PS50916; RABBD; 1; level=0 XX Names: Rab-binding domain Function: Undefined XX FT From: PS50916 FT DOMAIN from..to FT /note="RabBD #" XX Chop: Nter=0; Cter=0; Size: 42-184; Related: None; Repeats: 1; Topology: Undefined; Example: Q86UR5; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00235; DC Domain; TR PROSITE; PS50012; RCC1_3; 1; level=0 XX Names: RCC1 repeat Function: Undefined XX XX DR PROSITE; PS00625; RCC1_1; 1; trigger=no DR PROSITE; PS00626; RCC1_2; 1; trigger=no XX FT From: PS50012 FT REPEAT from..to FT /note="RCC1 #" XX Chop: Nter=0; Cter=0; Size: 39-94; Related: RRU00003!!; Repeats: 2-7; Topology: Undefined; Example: O74381; Scope: Eukaryota Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00236; DC Domain; TR PROSITE; PS50305; SIRTUIN; 1; level=0 XX Names: Sirtuin catalytic domain Sir2 domain Function: Sirtuins are responsible for a newly classified chemical reaction, NAD- dependent protein deacetylation. XX case DE + RecName: EC=2.3.1.286; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl- CC ADP-D-ribose + L-lysyl-[protein] + nicotinamide; CC Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; CC EC=2.3.1.286; XX GO GO:0016407; F:acetyltransferase activity XX KW NAD KW Transferase end case case KW Metal-binding KW Zinc end case XX FT From: PS50305 FT DOMAIN from..to FT /note="Deacetylase sirtuin-type #" case FT ACT_SITE 129 FT /note="Proton acceptor" FT Tag: act_site; Condition: H end case FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 140 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 161 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: [CH] FT BINDING 164 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 207-331; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P06700; Scope: Eukaryota Archaea Bacteria Comments: None XX # Revision 1.14 2022/11/19 // AC PRU00237; DC Domain; TR PROSITE; PS50061; ETS_DOMAIN_3; 1; level=0 XX Names: ETS domain Function: Involved in DNA-binding. It seems to recognize purine-rich sequences. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS00345; ETS_DOMAIN_1; 1; trigger=no DR PROSITE; PS00346; ETS_DOMAIN_2; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS50061 FT DNA_BIND from..to FT /note="ETS #" XX Chop: Nter=0; Cter=0; Size: 80-83; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P14921; Scope: Eukaryota Viruses Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00238; DC Domain; TR PROSITE; PS01033; GLOBIN; 1; level=0 XX Names: Globin domain Function: Globins are heme-containing proteins involved in binding and/or transporting oxygen. XX case not CC -!- SIMILARITY: Belongs to the globin family. end case XX case or GO GO:0006810; P:transport end case case GO GO:0015671; P:oxygen transport XX KW Oxygen transport end case case or KW Heme KW Iron KW Metal-binding KW Transport end case XX FT From: PS01033 FT DOMAIN from..to FT /note="Globin #" case FT BINDING 61 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT Group: 1; Condition: H FT BINDING 93 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="proximal binding residue" FT Group: 1; Condition: H else FT BINDING 61 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="distal binding residue" FT Group: 2; Condition: [HQ] FT BINDING 93 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="proximal binding residue" FT Group: 2; Condition: H end case XX Chop: Nter=0; Cter=0; Size: 108-151; Related: None; Repeats: 1-9; Topology: Not cytoplasmic; Example: Q8WWM9; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.16 2024/01/10 // AC PRU00239; DC Domain; TR PROSITE; PS50203; CALPAIN_CAT; 1; level=0 XX Names: Cysteine proteinase, calpain-type, catalytic domain Function: Calpains are a family of cytosolic cysteine proteinases XX case DE + RecName: EC=3.4.22.-; end case XX XX case GO GO:0008234; F:cysteine-type peptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS50203 FT DOMAIN from..to FT /note="Calpain catalytic #" FT ACT_SITE 61 FT Group: 1; Condition: C FT ACT_SITE 222 FT Group: 1; Condition: H FT ACT_SITE 243 FT Group: 1; Condition: N XX Chop: Nter=0; Cter=0; Size: 291-344; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9HC96; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.9 2019/11/21 // AC PRU00240; DC Domain; TR PROSITE; PS50141; A_DEAMIN_EDITASE; 1; level=0 XX Names: Adenosine to inosine editase domain Function: Enzymes that catalyze the site-selective deamination of adenosine residue into inosine within double stranded regions of mRNA. XX case and DE + RecName: EC=3.5.4.-; end case XX XX case and GO GO:0016787; F:hydrolase activity XX KW Hydrolase end case case KW Metal-binding KW Zinc end case XX FT From: PS50141 FT DOMAIN from..to FT /note="A to I editase #" FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H FT ACT_SITE 27 FT /note="Proton donor" FT Condition: E FT BINDING 81 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 149 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 325-367; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q99MU3; Scope: Eukaryota Comments: None XX # Revision 1.13 2022/11/19 // AC PRU00241; DC Domain; TR PROSITE; PS50903; RUBREDOXIN_LIKE; 1; level=0 XX Names: Rubredoxin-like domain Function: It is involved in electron transfer processes. XX DR PROSITE; PS00202; RUBREDOXIN; 0-1; trigger=no case GO GO:0009055; F:electron transfer activity GO GO:0006810; P:transport GO GO:0005506; F:iron ion binding GO GO:0046872; F:metal ion binding XX KW Transport KW Electron transport KW Metal-binding KW Iron end case XX FT From: PS50903 FT DOMAIN from..to FT /note="Rubredoxin-like #" FT BINDING 6 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 9 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 38 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 41 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="#1" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 34-54; Related: None; Repeats: 2; Topology: Cytoplasmic; Example: P19500; Scope: Bacteria Archaea Comments: None XX # Revision 1.13 2022/11/19 // AC PRU00242; DC Domain; TR PROSITE; PS50939; CYTOCHROME_B561; 1; level=0 XX Names: Cytochrome b561 domain Function: Cytochromes b561 are di-heme transmembrane electron transport proteins. XX XX GO GO:0016020; C:membrane GO GO:0006810; P:transport case GO GO:0005506; F:iron ion binding GO GO:0046872; F:metal ion binding end case XX KW Electron transport KW Membrane KW Transmembrane KW Transport case KW Heme KW Iron KW Metal-binding end case XX FT From: PS50939 FT DOMAIN from..to FT /note="Cytochrome b561 #" FT BINDING 37 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 73 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 95 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_note="substrate" FT Group: 1; Condition: H FT BINDING 107 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 146 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 198-214; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: P49447; Scope: Eukaryota Comments: None XX # Revision 1.14 2022/11/19 // AC PRU00243; DC Domain; TR PROSITE; PS50942; ENTH; 1; level=0 XX Names: ENTH domain Epsin NH2-terminal homology domain Epsin N-terminal homology domain Function: The ENTH domain has been shown to bind to phosphoinositides, as well as to interact with proteins. XX XX DR General; Transmembrane; -; 6; trigger=yes XX FT From: PS50942 FT DOMAIN from..to FT /note="ENTH #" XX Chop: Nter=0; Cter=0; Size: 126-134; Related: PRU00218; Repeats: 1; Topology: Cytoplasmic; Example: O60641; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00244; DC Domain; TR PROSITE; PS50924; MHYT; 1; level=0 XX Names: MHYT domain Function: A predicted transmembrane domain that could serve as a sensor domain toward oxygen, CO or NO. XX XX DR General; Transmembrane; -; 6-7; trigger=yes XX GO GO:0016020; C:membrane XX KW Membrane KW Transmembrane XX FT From: PS50924 FT DOMAIN from..to FT /note="MHYT #" XX Chop: Nter=0; Cter=0; Size: 188-195; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9ABX9; Scope: Bacteria Comments: None XX # Revision 1.14 2022/09/29 // AC PRU00245; DC Domain; TR PROSITE; PS50807; GCM; 1; level=0 XX Names: GCM domain Function: The GCM motif has been shown to be a DNA binding domain that recognizes preferentially the nonpalindromic octamer 5'-ATGCGGGT-3'. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0007275; P:multicellular organism development GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription case GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding end case XX KW Developmental protein KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation case KW Metal-binding KW Zinc end case XX FT From: PS50807 FT DNA_BIND from..to FT /note="GCM #" XX FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 105 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 156-160; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9NP62; Scope: Eukaryota Comments: None XX # Revision 1.16 2022/11/19 // AC PRU00246; DC Domain; TR PROSITE; PS50836; DOMON; 1; level=0 XX Names: DOMON domain Function: The architectures of the DOMON domain proteins strongly suggest a function in extracellular adhesion. XX XX FT From: PS50836 FT DOMAIN from..to FT /note="DOMON #" XX Chop: Nter=0; Cter=0; Size: 117-117; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P09172; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00247; DC Domain; TR PROSITE; PS50934; SWIRM; 1; level=0 XX Names: SWIRM domain Function: The SWIRM domain is predicted to mediate specific protein-protein interactions in the assembly of chromatin-protein complexes. XX XX FT From: PS50934 FT DOMAIN from..to FT /note="SWIRM #" XX Chop: Nter=0; Cter=0; Size: 86-102; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9XWP6; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00248; DC Domain; TR PROSITE; PS50918; WWE; 1; level=0 XX Names: WWE domain Function: The WWE domain could function in specific interactions with other proteins and help in targeting the different kinds of E3-like and ADP-ribosylation activities to proteins participating in various signaling cascades. XX XX FT From: PS50918 FT DOMAIN from..to FT /note="WWE #" XX Chop: Nter=0; Cter=0; Size: 77-91; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: Q7Z6Z7; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00249; DC Domain; TR PROSITE; PS50917; SPOC; 1; level=0 XX Names: SPOC domain Function: The SPOC domain could mediate interaction with corepressors. XX XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Transcription KW Transcription regulation XX FT From: PS50917 FT DOMAIN from..to FT /note="SPOC #" XX Chop: Nter=0; Cter=0; Size: 167-180; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q8SX83; Scope: Eukaryota Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00250; DC Domain; TR PROSITE; PS50913; GRIP; 1; level=0 XX Names: GRIP domain Function: The GRIP domain mediates binding to Golgi membranes. XX XX KW Golgi apparatus XX FT From: PS50913 FT DOMAIN from..to FT /note="GRIP #" XX Chop: Nter=0; Cter=0; Size: 48-52; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q96CN9; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00251; DC Domain; TR PROSITE; PS50066; MADS_BOX_2; 1; level=0 XX Names: MADS-box domain Function: The MADS-box domain is a DNA-binding domain found in transcriptional factors. XX CC -!- SUBCELLULAR LOCATION: Nucleus. DR PROSITE; PS00350; MADS_BOX_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS50066 FT DOMAIN from..to FT /note="MADS-box #" XX Chop: Nter=0; Cter=0; Size: 55-61; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q8RVL4; Scope: Eukaryota Comments: None XX # Revision 1.12 2022/06/27 // AC PRU00252; DC Domain; TR PROSITE; PS50935; SSB; 1; level=0 XX Names: SSB domain Function: The SSB domain is involved in binding to ssDNA. XX XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS50935 FT DOMAIN from..to FT /note="SSB #" XX Chop: Nter=0; Cter=0; Size: 97-113; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: P18022; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00253; DC Domain; TR PROSITE; PS50931; HTH_LYSR; 1; level=0 XX Names: LysR-type HTH domain Function: The lysR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain present in lysR-type transcriptional regulators. XX XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50931 FT DOMAIN from..to FT /note="HTH lysR-type #" FT DNA_BIND 18..37 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 44-61; Related: None; Repeats: 1; Topology: Undefined; Example: P45600; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00254; DC Domain; TR PROSITE; PS50937; HTH_MERR_2; 1; level=0 XX Names: MerR-type HTH domain Function: The merR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain present in the merR family of transcriptional regulators. XX DR PROSITE; PS00552; HTH_MERR_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50937 FT DOMAIN from..to FT /note="HTH merR-type #" FT DNA_BIND 4..23 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 27-75; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P0A2Q8; Scope: Bacteria Archaea Comments: None XX # Revision 1.10 2022/06/27 // AC PRU00255; DC Domain; TR PROSITE; PS50869; BRICHOS; 1; level=0 XX Names: BRICHOS domain Function: Unknown XX FT From: PS50869 FT DOMAIN from..to FT /note="BRICHOS #" XX Chop: Nter=0; Cter=0; Size: 83-104; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y287; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00256; DC Domain; TR PROSITE; PS50816; NAF; 1; level=0 XX Names: NAF domain Function: The NAF domain represents a minimum protein interaction module that is both necessary and sufficient to mediate the interaction with the CBL calcium sensor proteins. XX FT From: PS50816 FT DOMAIN from..to FT /note="NAF #" XX Chop: Nter=0; Cter=0; Size: 25-26; Related: None; Repeats: 1; Topology: Undefined; Example: Q8RWC9; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00257; DC Domain; TR PROSITE; PS50943; HTH_CROC1; 1; level=0 XX Names: Cro/C1-type HTH domain Function: The cro/C1-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain in transcriptional regulators. XX XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50943 FT DOMAIN from..to FT /note="HTH cro/C1-type #" FT DNA_BIND 12..31 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 53-62; Related: None; Repeats: 1; Topology: Undefined; Example: P14819; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.9 2022/06/27 // AC PRU00258; DC Domain; TR PROSITE; PS50075; CARRIER; 1; level=0 XX Names: Carrier protein (CP) domain and phosphopantetheine attachment site Function: Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of carrier proteins (CP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. XX case CC -!- COFACTOR: CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; XX DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1; trigger=no XX KW Phosphopantetheine end case XX FT From: PS50075 FT DOMAIN from..to FT /note="Carrier #" FT MOD_RES 36 FT /note="O-(pantetheine 4'-phosphoryl)serine" FT Condition: S XX Chop: Nter=0; Cter=0; Size: 41-79; Related: None; Repeats: 1-5; Topology: Cytoplasmic; Example: P19787; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.12 2022/04/05 // AC PRU00259; DC Domain; TR PROSITE; PS50176; ARM_REPEAT; 1; level=0 XX Names: Armadillo/plakoglobin ARM repeat Function: Interact with diverse binding partners. XX FT From: PS50176 FT REPEAT from..to FT /note="ARM #" XX Chop: Nter=0; Cter=0; Size: 28-45; Related: RRU00001!!; Repeats: 1-9; Topology: Undefined; Example: P14923; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00260; DC Domain; TR PROSITE; PS50228; SUEL_LECTIN; 1; level=0 XX Names: SUEL-type lectin domain Function: L-rhamnose and D-galactose binding. XX XX GO GO:0030246; F:carbohydrate binding XX KW Lectin XX FT From: PS50228 FT DOMAIN from..to FT /note="SUEL-type lectin #" XX Chop: Nter=0; Cter=0; Size: 87-93; Related: None; Repeats: 1; Topology: Undefined; Example: P58658; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00261; DC Domain; TR PROSITE; PS50941; CHIT_BIND_I_2; 1; level=0 XX Names: Chitin-binding type-1 domain Function: Bind chitin. XX DR PROSITE; PS00026; CHIT_BIND_I_1; 1; trigger=no XX GO GO:0008061; F:chitin binding XX KW Chitin-binding case KW Disulfide bond end case XX FT From: PS50941 FT DOMAIN from..to FT /note="Chitin-binding type-1 #" FT DISULFID 4..19 FT Tag: disulf; Condition: C-x*-C FT DISULFID 13..25 FT Tag: disulf; Condition: C-x*-C FT DISULFID 18..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 36..40 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 36-57; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q9S8M0; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00262; DC Domain; TR PROSITE; PS50898; RBD; 1; level=0 XX Names: Ras-binding domain Function: Ras-binding. XX FT From: PS50898 FT DOMAIN from..to FT /note="RBD #" XX Chop: Nter=0; Cter=0; Size: 68-77; Related: None; Repeats: 1-2; Topology: Undefined; Example: O43566; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00263; DC Domain; TR PROSITE; PS50128; SURP; 1; level=0 XX Names: SURP motif repeat Function: Unknown XX XX GO GO:0006397; P:mRNA processing XX KW mRNA processing KW mRNA splicing XX FT From: PS50128 FT REPEAT from..to FT /note="SURP motif #" XX Chop: Nter=0; Cter=0; Size: 39-44; Related: None; Repeats: 2; Topology: Undefined; Example: Q8IWZ8; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00264; DC Domain; TR PROSITE; PS50064; ZF_PARP_2; 1; level=0 XX Names: Zinc finger poly(ADP-ribose) polymerase (PARP)-type Function: Bind specifically to single-stranded DNA XX DR PROSITE; PS00347; ZF_PARP_1; 1; trigger=no XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW Nucleus KW DNA-binding KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50064 case and and and FT ZN_FING from..to FT /note="PARP-type #" else case and and and FT ZN_FING from..to FT /note="PARP-type #; atypical" else FT ZN_FING from..to FT /note="PARP-type #; degenerate" end case FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 83-93; Related: None; Repeats: 1-2; Topology: Undefined; Example: P35875; Scope: Eukaryota Comments: None XX # Revision 1.14 2022/11/19 // AC PRU00265; DC Domain; TR PROSITE; PS50254; REL_2; 1; level=0 XX Names: NF-kappa-B/Rel/dorsal domain Function: Unknown XX DR PROSITE; PS01204; REL_1; 1; trigger=no FT From: PS50254 FT DOMAIN from..to FT /note="RHD #" XX Chop: Nter=0; Cter=0; Size: 274-313; Related: None; Repeats: 1; Topology: Undefined; Example: Q94527; Scope: Eukaryota Viruses Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00266; DC Domain; TR PROSITE; PS50137; DS_RBD; 1; level=0 XX Names: Double stranded RNA-binding domain Function: Recognize double-stranded RNAs XX XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS50137 FT DOMAIN from..to FT /note="DRBM #" XX Chop: Nter=0; Cter=0; Size: 69-91; Related: None; Repeats: 1-5; Topology: Undefined; Example: P0A7Y0; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00267; DC Domain; TR PROSITE; PS50118; HMG_BOX_2; 1; level=0 XX Names: HMG boxes A and B DNA-binding domains Function: Bind preferentially to distorted DNAs XX c? not CC -!- SUBCELLULAR LOCATION: Nucleus. DR PROSITE; PS00353; HMG_BOX_1; 0-1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW Nucleus KW DNA-binding XX FT From: PS50118 FT DNA_BIND from..to FT /note="HMG box #" XX case Warn: If the entry belongs to the HMG1/HMG2 protein family, it should contain DR PROSITE; PS00353; HMG_BOX_1; end case Chop: Nter=0; Cter=0; Size: 44-81; Related: None; Repeats: 1-6; Topology: Undefined; Example: Q24537; Scope: Eukaryota Viruses Comments: None XX # Revision 1.14 2019/11/21 // AC PRU00268; DC Domain; TR PROSITE; PS50881; S5_DSRBD; 1; level=0 XX Names: S5 double stranded RNA-binding domain Function: Interacts with the 16S RNA XX DR PROSITE; PS00585; RIBOSOMAL_S5; 1; trigger=no XX GO GO:1990904; C:ribonucleoprotein complex GO GO:0003735; F:structural constituent of ribosome XX KW Ribonucleoprotein KW Ribosomal protein XX FT From: PS50881 FT DOMAIN from..to FT /note="S5 DRBM #" XX Chop: Nter=0; Cter=0; Size: 60-70; Related: None; Repeats: 1; Topology: Undefined; Example: P0A7W1; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.9 2019/11/21 // AC PRU00269; DC Domain; TR PROSITE; PS50290; PI3_4_KINASE_3; 1; level=0 XX Names: PI3K/PI4K catalytic domain Function: Phosphorylates phosphoinositides on the 3-hydroxyl group of the inositol ring. XX XX DR PROSITE; PS00915; PI3_4_KINASE_1; 1; trigger=no DR PROSITE; PS00916; PI3_4_KINASE_2; 1; trigger=no XX GO GO:0016740; F:transferase activity GO GO:0016301; F:kinase activity XX KW Transferase KW Kinase XX FT From: PS50290 FT DOMAIN from..to FT /note="PI3K/PI4K catalytic #" FT REGION 7..13 FT /note="G-loop #" FT REGION 144..152 FT /note="Catalytic loop #" FT REGION 164..188 FT /note="Activation loop #" XX Chop: Nter=0; Cter=0; Size: 240-390; Related: None; Repeats: 1; Topology: Undefined; Example: P22543; Scope: Eukaryota Comments: None XX # Revision 1.9 2021/10/26 // AC PRU00270; DC Domain; TR PROSITE; PS50007; PIPLC_X_DOMAIN; 1; level=0 XX Names: Phosphatidylinositol-specific phospholipase C X domain Function: Important for the catalytic activity XX XX case GO GO:0016787; F:hydrolase activity GO GO:0016042; P:lipid catabolic process GO GO:0007165; P:signal transduction XX KW Hydrolase KW Lipid degradation KW Lipid metabolism KW Transducer end case XX FT From: PS50007 FT DOMAIN from..to FT /note="PI-PLC X-box #" FT ACT_SITE 16 FT Group: 1; Condition: H FT ACT_SITE 61 FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 100-174; Related: None; Repeats: 1; Topology: Undefined; Example: Q9NQ66; Scope: Eukaryota Comments: None XX # Revision 1.9 2019/11/21 // AC PRU00271; DC Domain; TR PROSITE; PS50008; PIPLC_Y_DOMAIN; 1; level=0 XX Names: Phosphatidylinositol-specific phospholipase C Y domain Function: Important for the catalytic activity. XX XX GO GO:0016787; F:hydrolase activity GO GO:0007165; P:signal transduction GO GO:0016042; P:lipid catabolic process XX KW Transducer KW Hydrolase KW Lipid degradation KW Lipid metabolism XX FT From: PS50008 FT DOMAIN from..to FT /note="PI-PLC Y-box #" XX Chop: Nter=0; Cter=0; Size: 60-120; Related: None; Repeats: 1; Topology: Undefined; Example: Q9NQ66; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00272; DC Domain; TR PROSITE; PS50830; TNASE_3; 1; level=0 XX Names: Thermonuclease domain Function: catalyzes the hydrolysis of both DNA and RNA at the 5' position of the phosphodiester bond yielding 3'-mononucleotides and dinucleotides XX case ( or ) and CC -!- SIMILARITY: Belongs to the thermonuclease family. end case DR PROSITE; PS01123; TNASE_1; 1; trigger=no DR PROSITE; PS01284; TNASE_2; 1; trigger=no XX case GO GO:0005509; F:calcium ion binding end case case GO GO:0016787; F:hydrolase activity end case XX case KW Calcium KW Metal-binding end case case KW Hydrolase KW Nuclease KW Endonuclease end case XX FT From: PS50830 FT DOMAIN from..to FT /note="TNase-like #" FT BINDING 14 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 1; Condition: D FT BINDING 33 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 1; Condition: D FT BINDING 34 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 1; Condition: T FT ACT_SITE 28 FT Group: 2; Condition: R FT ACT_SITE 36 FT Group: 2; Condition: E FT ACT_SITE 79 FT Group: 2; Condition: R XX Chop: Nter=0; Cter=0; Size: 119-209; Related: None; Repeats: 1; Topology: Undefined; Example: P22997; Q7KZF4; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.15 2022/11/19 // AC PRU00273; DC Domain; TR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1; level=0 XX Names: Intein DOD homing endonuclease Function: Homing endonucleases are rare-cutting enzymes encoded by inteins and introns. XX FT From: PS50819 FT DOMAIN from..to FT /note="DOD-type homing endonuclease #" XX Chop: Nter=0; Cter=0; Size: 80-178; Related: None; Repeats: 1-2; Topology: Undefined; Example: P21505; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00274; DC Domain; TR PROSITE; PS50240; TRYPSIN_DOM; 1; level=0 XX Names: Serine proteases, trypsin domain Function: Cleaves preferentially: Arg-|-Xaa, Lys-|-Xaa XX case DE + RecName: EC=3.4.21.-; end case XX CC -!- SIMILARITY: Belongs to the peptidase S1 family. case DR PROSITE; PS00134; TRYPSIN_HIS; 1; trigger=no DR PROSITE; PS00135; TRYPSIN_SER; 1; trigger=no else DR PROSITE; PS00134; TRYPSIN_HIS; 0-1; trigger=no DR PROSITE; PS00135; TRYPSIN_SER; 0-1; trigger=no end case case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0004252; F:serine-type endopeptidase activity XX KW Hydrolase KW Protease KW Serine protease end case case KW Disulfide bond end case FT From: PS50240 FT DOMAIN from..to FT /note="Peptidase S1 #" FT ACT_SITE 42 FT /note="Charge relay system" FT Group: 1; Condition: H FT ACT_SITE 91 FT /note="Charge relay system" FT Group: 1; Condition: D FT ACT_SITE 186 FT /note="Charge relay system" FT Group: 1; Condition: S FT DISULFID 27..43 FT Tag: disulf; Condition: C-x*-C FT DISULFID 125..192 FT Tag: disulf; Condition: C-x*-C FT DISULFID 156..171 FT Tag: disulf; Condition: C-x*-C FT DISULFID 182..210 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 150-286; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9BYE2; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.19 2019/11/21 // AC PRU00275; DC Domain; TR PROSITE; PS50175; ASP_PROT_RETROV; 1; level=0 XX Names: Eukaryotic and viral aspartyl proteases Function: Belongs to peptidase family A2 XX case and DE + RecName: EC=3.4.23.16; else case and DE + RecName: EC=3.4.23.47; else case DE + RecName: EC=3.4.23.-; end case XX case CC -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag CC and Gag-Pol polyproteins during or shortly after the release of the CC virion from the plasma membrane. Cleavages take place as an ordered, CC step-wise cascade to yield mature proteins. This process is called CC maturation. Displays maximal activity during the budding process just CC prior to particle release from the cell. Also cleaves Nef and Vif, CC probably concomitantly with viral structural proteins on maturation of CC virus particles. else case CC -!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of Gag CC and Gag-Pol polyproteins during or shortly after the release of the CC virion from the plasma membrane. Cleavages take place as an ordered, CC step-wise cascade to yield mature proteins. This process is called CC maturation. Displays maximal activity during the budding process just CC prior to particle release from the cell. end case case and CC -!- CATALYTIC ACTIVITY: CC Reaction=Specific for a P1 residue that is hydrophobic, and P1' CC variable, but often Pro.; EC=3.4.23.16; else case and CC -!- CATALYTIC ACTIVITY: CC Reaction=Endopeptidase for which the P1 residue is preferably CC hydrophobic.; EC=3.4.23.47; end case XX DR PROSITE; PS00141; ASP_PROTEASE; 1; trigger=no XX case GO GO:0004190; F:aspartic-type endopeptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Aspartyl protease KW Hydrolase KW Protease end case XX FT From: PS50175 FT DOMAIN from..to FT /note="Peptidase A2 #" case FT ACT_SITE 6 FT /note="Protease; shared with dimeric partner" FT Tag: act_site; Condition: D else FT ACT_SITE 6 FT /note="@TARGET_ACTIVITY_VISIBILITY|For protease activity@" FT Tag: act_site; Condition: D end case XX Chop: Nter=0; Cter=0; Size: 40-82; Related: None; Repeats: 1; Topology: Undefined; Example: P51518; Scope: Eukaryota Viruses Comments: None XX # Revision 1.20 2019/11/21 // AC PRU00276; DC Domain; TR PROSITE; PS50215; ADAM_MEPRO; 1; level=0 XX Names: ADAM type metalloprotease domain Function: Belongs to peptidase family M12B XX case KW Metal-binding KW Zinc end case case KW Disulfide bond end case FT From: PS50215 FT DOMAIN from..to FT /note="Peptidase M12B #" FT BINDING 137 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT ACT_SITE 138 FT Condition: E FT BINDING 141 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT DISULFID 112..192 FT Tag: disulf; Condition: C-x*-C FT DISULFID 152..176 FT Tag: disulf; Condition: C-x*-C FT DISULFID 154..159 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 150-252; Related: None; Repeats: 1; Topology: Undefined; Example: P83255; Scope: Eukaryota Comments: None XX # Revision 1.13 2022/11/19 // AC PRU00277; DC Domain; TR PROSITE; PS50059; FKBP_PPIASE; 1; level=0 XX Names: PPIase FKBP-type domain Function: Peptidyl-prolyl cis-trans isomerase activity (EC 5.2.1.8) XX DE + RecName: EC=5.2.1.8; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-peptidylproline (omega=180) = [protein]- CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA- CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, CC ChEBI:CHEBI:83834; EC=5.2.1.8; XX GO GO:0016853; F:isomerase activity XX KW Isomerase KW Rotamase XX FT From: PS50059 FT DOMAIN from..to FT /note="PPIase FKBP-type #" XX Chop: Nter=0; Cter=0; Size: 72-130; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q02790; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.12 2019/11/21 // AC PRU00278; DC Domain; TR PROSITE; PS50198; PPIC_PPIASE_2; 1; level=0 XX Names: PpiC domain Function: Accelerates protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides XX DR PROSITE; PS01096; PPIC_PPIASE_1; 1; trigger=no XX GO GO:0016853; F:isomerase activity XX KW Isomerase KW Rotamase XX FT From: PS50198 FT DOMAIN from..to FT /note="PpiC #" XX Chop: Nter=0; Cter=0; Size: 72-128; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q13526; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00279; DC Domain; TR PROSITE; PS50255; CYTOCHROME_B5_2; 1; level=0 XX Names: Cytochrome b5 family, heme-binding domain Function: A membrane-bound hemoprotein which acts as an electron carrier for several membrane-bound oxygenases XX DR PROSITE; PS00191; CYTOCHROME_B5_1; 1; trigger=no XX case KW Heme KW Iron KW Metal-binding end case XX FT From: PS50255 FT DOMAIN from..to FT /note="Cytochrome b5 heme-binding #" FT BINDING 36 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 60 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 76-85; Related: None; Repeats: 1-2; Topology: Undefined; Example: P00171; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00280; DC Domain; TR PROSITE; PS50846; HMA_2; 1; level=0 XX Names: Heavy-metal-associated domain Function: Found in proteins that transport or detoxify heavy metals. This domain contains two conserved cysteines that could be involved in the binding of these metals. XX case DR PROSITE; PS01047; HMA_1; 1; trigger=no XX KW Metal-binding end case XX FT From: PS50846 FT DOMAIN from..to FT /note="HMA #" FT BINDING 12 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 15 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#1" FT Group: 1; Condition: C XX Warn: Replace "Metal cation" by the corresponding metal if it is known. Chop: Nter=0; Cter=0; Size: 54-75; Related: None; Repeats: 1-6; Topology: Undefined; Example: Q47840; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00282; DC Domain; TR PROSITE; PS50920; SOLCAR; 1; level=0 XX Names: Solute carrier (Solcar) repeat Function: Found in substrate carrier proteins involved in energy transfer XX XX GO GO:0016020; C:membrane XX KW Membrane KW Transmembrane XX FT From: PS50920 FT REPEAT from..to FT /note="Solcar #" XX Chop: Nter=0; Cter=0; Size: 74-143; Related: None; Repeats: 1-3; Topology: Undefined; Example: O43772; Scope: Eukaryota Mitochondrion Comments: None XX # Revision 1.7 2022/09/29 // AC PRU00283; DC Domain; TR PROSITE; PS50067; KINESIN_MOTOR_2; 1; level=0 XX Names: Kinesin motor domain Function: A large globular N-terminal domain which is responsible for the motor activity of kinesin XX CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Kinesin family. DR PROSITE; PS00411; KINESIN_MOTOR_1; 1; trigger=no XX case GO GO:0005524; F:ATP binding GO GO:0003774; F:cytoskeletal motor activity GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Motor protein KW Nucleotide-binding end case XX FT From: PS50067 FT DOMAIN from..to FT /note="Kinesin motor #" FT BINDING 90..97 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Tag: ATP; Condition: [AG]-x(4)-G-K-[ST] XX Chop: Nter=0; Cter=0; Size: 160-376; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BVG8; Scope: Eukaryota Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00284; DC Domain; TR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1; level=0 XX Names: Methyl-accepting transducer domain Function: Respond to changes in the concentration of attractants and repellents in the environment, and transduce a signal from the outside to the inside of the cell XX DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1; trigger=no XX KW Transducer XX FT From: PS50111 FT DOMAIN from..to FT /note="Methyl-accepting transducer #" XX Chop: Nter=0; Cter=0; Size: 221-265; Related: None; Repeats: 1; Topology: Undefined; Example: P02942; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00285; DC Domain; TR PROSITE; PS01031; SHSP; 1; level=0 XX Names: Small heat shock protein (sHSP) domain Function: Seems to act as chaperones that can protect other proteins against heat-induced denaturation and aggregation XX CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) family. XX FT From: PS01031 FT DOMAIN from..to FT /note="sHSP #" XX Chop: Nter=0; Cter=0; Size: 58-158; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q16082; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00286; DC Domain; TR PROSITE; PS50076; DNAJ_2; 1; level=0 XX Names: dnaJ domain Function: Interacts with the chaperone hsp70-like dnaK protein. XX DR PROSITE; PS00636; DNAJ_1; 1; trigger=no FT From: PS50076 FT DOMAIN from..to FT /note="J #" XX Chop: Nter=0; Cter=0; Size: 53-88; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Z9E9; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00288; DC Domain; TR PROSITE; PS50115; ARFGAP; 1; level=0 XX Names: ARF GTPase-activating proteins domain Function: GTPase-activating XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50115 FT DOMAIN from..to FT /note="Arf-GAP #" case and and and FT ZN_FING 16..39 FT /note="C4-type #" else case and and and FT ZN_FING 16..39 FT /note="C4-type #; atypical" else FT ZN_FING 16..39 FT /note="C4-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 110-144; Related: None; Repeats: 1; Topology: Undefined; Example: Q8N6T3; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00289; DC Domain; TR PROSITE; PS50901; FTSK; 1; level=0 XX Names: FtsK domain Function: thought to be involved in DNA translocation by coupling ATP hydrolysis to movement relative to the long axis of DNA XX XX GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Nucleotide-binding XX FT From: PS50901 FT DOMAIN from..to FT /note="FtsK #" FT BINDING 18..25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 154-200; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: P46889; Scope: Bacteria Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00290; DC Domain; TR PROSITE; PS50892; V_SNARE; 1; level=0 XX Names: v-SNARE coiled-coil homology domain Function: binds t-SNARE XX XX KW Coiled coil XX FT From: PS50892 FT DOMAIN from..to FT /note="v-SNARE coiled-coil homology #" XX Chop: Nter=0; Cter=0; Size: 57-70; Related: None; Repeats: 1; Topology: Undefined; Example: P23763; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00291; DC Domain; TR PROSITE; PS50891; LOB; 1; level=0 XX Names: LOB domain Function: Unknown XX FT From: PS50891 FT DOMAIN from..to FT /note="LOB #" XX Chop: Nter=0; Cter=0; Size: 101-107; Related: None; Repeats: 1; Topology: Undefined; Example: O64836; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00292; DC Domain; TR PROSITE; PS50945; I_LWEQ; 1; level=0 XX Names: I/LWEQ domain Function: The I/LWEQ domain has been shown to bind to F-actin and to bundle actin filaments. XX FT From: PS50945 FT DOMAIN from..to FT /note="I/LWEQ #" XX Chop: Nter=0; Cter=0; Size: 193-199; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9Y490; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00293; DC Site; TR PROSITE; PS00016; RGD; 1; level=1 XX Names: Cell attachment sequence Function: The 'RGD' tripeptide has been shown to play a role in cell adhesion. XX GO GO:0007155; P:cell adhesion XX KW Cell adhesion XX FT From: PS00016 FT MOTIF from..to FT /note="Cell attachment site" XX Chop: Nter=0; Cter=0; Size: 3; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P83041; Scope: Eukaryota Viruses Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00294; DC Domain; TR PROSITE; PS50870; AH; 1; level=1 XX Names: Arfaptin homology (AH) domain Function: The AH domain of arfaptin has been shown to dimerize and to bind Arf and Rho family GTPases. XX FT From: PS50870 FT DOMAIN from..to FT /note="AH #" XX Chop: Nter=0; Cter=0; Size: 200-220; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P53367; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00295; DC Domain; TR PROSITE; PS50189; NTR; 1; level=1 XX Names: NTR domain Function: The NTR domain is implicated in inhibition of zinc metalloproteinases of the metzincin family. XX XX case KW Disulfide bond end case FT From: PS50189 FT DOMAIN from..to FT /note="NTR #" FT DISULFID 1..76 FT Tag: disulf; Group: 1; Condition: C-x*-C case FT DISULFID 5..78 FT Tag: disulf; Condition: C-x*-C FT DISULFID 5..107 FT Tag: disulf; Condition: C-x*-C end case FT DISULFID 19..134 FT Tag: disulf; Group: 1; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 110-200; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P97299; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00296; DC Domain; TR PROSITE; PS50944; HTH_DTXR; 1; level=0 XX Names: DtxR-type HTH domain Function: The dtxR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain present in metalloregulators of the dtxR/mntR family. XX XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50944 FT DOMAIN from..to FT /note="HTH dtxR-type #" XX Chop: Nter=0; Cter=0; Size: 60-65; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P0A9F1; Scope: Bacteria Archaea Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00298; DC Domain; TR PROSITE; PS50292; PEROXIDASE_3; 1; level=0 XX Names: Animal heme peroxidase Function: Removal of H(2)O(2) XX case and and CC -!- CATALYTIC ACTIVITY: CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:17499; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per heterodimer.; CC -!- COFACTOR: CC Name=heme b; Xref=ChEBI:CHEBI:60344; CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per CC heterodimer.; end case CC -!- SIMILARITY: Belongs to the peroxidase family. XX case DR PROSITE; PS00435; PEROXIDASE_1; 1; trigger=no DR PROSITE; PS00436; PEROXIDASE_2; 1; trigger=no end case XX case and and GO GO:0016491; F:oxidoreductase activity GO GO:0004601; F:peroxidase activity KW Oxidoreductase KW Peroxidase end case case KW Iron KW Heme end case case KW Calcium end case case or KW Metal-binding end case case KW Disulfide bond end case XX FT From: PS50292 case and FT CHAIN 2..108 FT /note=" light chain" FT CHAIN 109..Cter FT /note=" heavy chain" ** From PMID: 1320128; PMID: 11705390 end case FT BINDING 95 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /note="covalent" FT Group: 1; Condition: D FT BINDING 238 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /note="covalent" FT Group: 1; Condition: E FT ACT_SITE 96 FT /note="Proton acceptor" FT Group: 2; Condition: H FT SITE 235 FT /note="Transition state stabilizer" FT Group: 2; Condition: R FT BINDING 97 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 3; Condition: D FT BINDING 164 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 3; Condition: [ST] FT BINDING 166 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 3; Condition: [FY] FT BINDING 168 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 3; Condition: D FT BINDING 170 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 3; Condition: [ST] FT BINDING 332 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT DISULFID 4..17 FT Tag: disulf; Condition: C-x*-C FT DISULFID 111..121 FT Tag: disulf; Condition: C-x*-C FT DISULFID 115..139 FT Tag: disulf; Condition: C-x*-C FT DISULFID 217..228 FT Tag: disulf; Condition: C-x*-C FT DISULFID 435..491 FT Tag: disulf; Condition: C-x*-C FT DISULFID 534..560 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 510-750; Related: None; Repeats: 1-6; Topology: Undefined; Example: P11247; Scope: Eukaryota Comments: None XX # Revision 1.22 2022/11/19 // AC PRU00300; DC Domain; TR Metamotif; -; PS50021~7,91~PS50021 XX Names: Actin-binding region Function: Each single actin-binding region, comprising two CH domains, is able to bind one actin monomer in the filament. XX XX DR PROSITE; PS50021; CH; 2; trigger=yes DR PROSITE; PS00019; ACTININ_1; 1-2; trigger=no DR PROSITE; PS00020; ACTININ_2; 1-2; trigger=no XX GO GO:0003779; F:actin binding KW Actin-binding XX FT From: any FT REGION from..to FT /note="Actin-binding #" XX Chop: Nter=0; Cter=0; Size: 225-325; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: O97592; Scope: Eukaryota Comments: None XX # Revision 1.13 2019/11/21 // AC PRU00302; DC Domain; TR PROSITE; PS50923; SUSHI; 1; level=0 XX Names: Sushi domain Function: involved in many recognition processes, including the binding of several complement factors to fragments C3b and C4b. XX KW Sushi case KW Disulfide bond end case FT From: PS50923 FT DOMAIN from..to FT /note="Sushi #" FT DISULFID 3..46 FT Tag: disulf; Condition: C-x*-C FT DISULFID 32..59 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 13-77; Related: None; Repeats: 1-20; Topology: Not cytoplasmic; Example: P20851; Scope: Eukaryota; Metazoa Viruses Comments: None XX # Revision 1.11 2019/11/21 // AC PRU00303; DC Domain; c? or or TR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1; level=0 XX Names: Prokaryotic membrane lipoprotein lipid attachment site Function: site of signal peptide cleavage and attachment of glyceride-fatty acid lipids that anchor proteins in the membrane XX DE + Flags: Precursor; case not CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. GO GO:0005886; C:plasma membrane end case XX case not KW Membrane end case KW Palmitate KW Signal KW Lipoprotein XX FT From: PS51257 FT SIGNAL 1..34 FT LIPID 35 FT /note="N-palmitoyl cysteine" FT LIPID 35 FT /note="S-diacylglycerol cysteine" FT CHAIN 35..Cter FT /note="" XX Chop: Nter=0; Cter=0; Size: 14-35; Related: ANA00006; ANA00002; Repeats: 1; Topology: Not cytoplasmic; Example: P23898; Scope: Bacteria Archaea Viruses Comments: None XX # Revision 1.19 2019/11/21 // AC PRU00304; DC Domain; TR PROSITE; PS50211; DENN; 1; level=0 XX Names: DENN domain Function: The tripartite DENN domain is composed of three distinct modules which are always associated due to functional and/or structural constraints: upstream DENN or uDENN, the better conserved central or core or cDENN, and downstream or dDENN regions. The function of DENN domain remains to date unclear, although it appears to represent a good candidate for a GTP/GDP exchange activity. XX FT From: PS50211 FT DOMAIN from..162 FT /note="uDENN #" FT DOMAIN 185..321 FT /note="cDENN #" FT DOMAIN 323..to FT /note="dDENN #" XX Chop: Nter=0; Cter=0; Size: 180-230; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: O02626; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00307; DC Domain; TR PROSITE; PS50949; HTH_GNTR; 1; level=0 XX Names: GntR-type HTH domain Function: The gntR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 60-70 residues present in transcriptional regulators of the gntR family. XX XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50949 FT DOMAIN from..to FT /note="HTH gntR-type #" FT DNA_BIND 29..48 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 50-75; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9S470; Scope: Bacteria Comments: None XX # Revision 1.9 2022/06/27 // AC PRU00308; DC Domain; TR PROSITE; PS50921; ANTAR; 1; level=0 XX Names: ANTAR domain Function: The ANTAR domain is supposed to be an RNA-binding motif. XX XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Transcription KW Transcription antitermination KW Transcription regulation XX FT From: PS50921 FT DOMAIN from..to FT /note="ANTAR #" XX Chop: Nter=0; Cter=0; Size: 60-70; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P10932; Scope: Bacteria Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00309; DC Domain; TR PROSITE; PS50950; THAP; 1; level=0 XX Names: Zinc finger THAP-type Function: The THAP-type zinc finger is supposed to be a DNA-binding domain. XX XX GO GO:0003677; F:DNA binding case and and and GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding end case XX KW Zinc-finger KW DNA-binding case and and and KW Zinc KW Metal-binding end case XX FT From: PS50950 case and and and FT ZN_FING 5..58 FT /note="THAP-type #" else case and and and FT ZN_FING 5..58 FT /note="THAP-type #; atypical" else FT ZN_FING 5..58 FT /note="THAP-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 70-100; Related: None; Repeats: 1-27; Topology: Cytoplasmic; Example: Q9NVV9; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00310; DC Domain; TR PROSITE; PS50951; SARAH; 1; level=0 XX Names: SARAH domain Function: The SARAH domain could be a trimerization domain. XX XX FT From: PS50951 FT DOMAIN from..to FT /note="SARAH #" XX Chop: Nter=0; Cter=0; Size: 45-50; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9H4B6; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00311; DC Domain; TR PROSITE; PS50952; KIX; 1; level=0 XX Names: KIX domain Function: The KIX domain appears to be a common docking site on CBP for many transcriptional activators. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Activator KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS50952 FT DOMAIN from..to FT /note="KIX #" XX Chop: Nter=0; Cter=0; Size: 75-85; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: Q92793; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.12 2022/07/05 // AC PRU00312; DC Domain; TR PROSITE; PS50953; KID; 1; level=0 XX Names: KID domain Function: Ser-133 phosphorylation of CREB within the KID domain promotes target gene activation via complex formation with the KIX domain of the CBP and P300 coactivators, whereas concurrent phosphorylation of the CREB KID domain at Ser-142 inhibits transcriptional induction. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus case or KW Phosphoprotein end case KW Transcription KW Transcription regulation XX FT From: PS50953 FT DOMAIN from..to FT /note="KID #" FT MOD_RES 33 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 42 FT /note="Phosphoserine" FT Condition: S XX Chop: Nter=0; Cter=0; Size: 55-65; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P16220; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.13 2022/06/27 // AC PRU00313; DC Domain; TR PROSITE; PS50954; LEM; 1; level=0 XX Names: LEM domain Function: The LEM domain has been shown to be mediate binding to BAF (barrier- to-autointegration factor) and BAF-DNA complexes. XX XX FT From: PS50954 FT DOMAIN from..to FT /note="LEM #" XX Chop: Nter=0; Cter=0; Size: 30-50; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P50402; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00314; DC Domain; TR PROSITE; PS50955; LEM_LIKE; 1; level=0 XX Names: LEM-like domain Function: The LEM-like domain has been shown to bind directly to DNA. XX XX FT From: PS50955 FT DOMAIN from..to FT /note="LEM-like #" XX Chop: Nter=0; Cter=0; Size: 40-50; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P42166; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00315; DC Domain; TR PROSITE; PS50948; PAN; 1; level=0 XX Names: PAN/Apple domain Function: The PAN/Apple domain has been shown to bind directly to kininogen, factor XIIa, platelets,factor IX and heparin. XX case not and not DR PROSITE; PS00495; APPLE; 1; trigger=no end case XX case KW Disulfide bond end case XX FT From: PS50948 case or FT DOMAIN from..to FT /note="PAN #" else FT DOMAIN from..to FT /note="Apple #" end case FT DISULFID 1..78 FT Tag: disulf; Condition: C-x*-C FT DISULFID 30..52 FT Tag: disulf; Condition: C-x*-C FT DISULFID 34..40 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 72-95; Related: None; Repeats: 4; Topology: Not cytoplasmic; Example: P03951; P14210; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.19 2019/11/21 // AC PRU00316; DC Domain; TR PROSITE; PS50853; FN3; 1; level=0 XX Names: FN3 domain Function: The FN3 domain has been shown to be involved in binding substrate. XX DR PROSITE; PS00016; RGD; 1; trigger=yes XX FT From: PS50853 FT DOMAIN from..to FT /note="Fibronectin type-III #" XX Chop: Nter=0; Cter=0; Size: 78-135; Related: None; Repeats: 33; Topology: Not cytoplasmic; Example: P23352; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2020/11/11 // AC PRU00317; DC Domain; TR PROSITE; PS50302; PUM; 1; level=0 XX Names: Pumilio repeat Function: Pumilio repeats have been shown to bind specific RNA sequences mainly found in the 3' UTR of mRNA and repress their translation. XX XX FT From: PS50302 FT REPEAT from..to FT /note="Pumilio #" XX Chop: Nter=0; Cter=0; Size: 30-50; Related: None; Repeats: 9; Topology: Not cytoplasmic; Example: P25822; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00318; DC Domain; TR PROSITE; PS50303; PUM_HD; 1; level=0 XX Names: Pumilio homology domain Function: Pumilio homology domain has been shown to bind specific RNA sequences mainly found in the 3' UTR of mRNA and repress their translation. XX XX FT From: PS50303 FT DOMAIN from..to FT /note="PUM-HD #" XX Chop: Nter=0; Cter=0; Size: 300-450; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P25822; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00319; DC Domain; TR PROSITE; PS50956; HTH_ASNC_2; 1; level=0 XX Names: AsnC-type HTH domain Function: The asnC-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 60 amino acids present in transcription regulators of the asnC/lrp family. XX XX DR PROSITE; PS00519; HTH_ASNC_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50956 FT DOMAIN from..to FT /note="HTH asnC-type #" FT DNA_BIND 20..39 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 40-100; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P0ACJ4; Scope: Bacteria Archaea Comments: None XX # Revision 1.13 2022/06/27 // AC PRU00320; DC Domain; TR PROSITE; PS50960; HTH_PSQ; 1; level=0 XX Names: Psq-type HTH domain Function: The psq-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50 amino acids present in eukaryotic proteins of the Pipsqueak family. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus XX FT From: PS50960 FT DOMAIN entry..exit FT /note="HTH psq-type #" FT DNA_BIND 29..49 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 45-60; Related: None; Repeats: 1-4; Topology: Not cytoplasmic; Example: P07199; Scope: Eukaryota Comments: None XX # Revision 1.13 2019/11/21 // AC PRU00321; DC Domain; TR PROSITE; PS50828; SMR; 1; level=0 XX Names: Smr domain Function: It has been proposed that the Smr domain acts as a nicking endonuclease. XX FT From: PS50828 FT DOMAIN from..to FT /note="Smr #" XX Chop: Nter=0; Cter=0; Size: 70-100; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P76053; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00322; DC Domain; TR PROSITE; PS50199; ZF_RANBP2_2; 1; level=0 XX Names: Zinc finger RanBP2-type Function: It has been shown that RanBP2-type zinc fingers bind RanGDP (but not RanGTP) and the exportin-1 protein (a receptor of the export pathway). XX DR PROSITE; PS01358; ZF_RANBP2_1; 1; trigger=no KW Zinc-finger case and and and KW Zinc KW Metal-binding end case FT From: PS50199 case and and and FT ZN_FING from..to FT /note="RanBP2-type #" else case and and and FT ZN_FING from..to FT /note="RanBP2-type #; atypical" else FT ZN_FING from..to FT /note="RanBP2-type #; degenerate" end case FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 30-35; Related: None; Repeats: 8; Topology: Cytoplasmic; Example: P49792; Scope: Eukaryota Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00323; DC Domain; TR PROSITE; PS50963; LINK_2; 1; level=0 XX Names: Link domain Function: Link domains are hyaluronan(HA)-binding domains found in proteins involved in in the assembly of extracellular matrix, cell adhesion, and migration. XX DR PROSITE; PS01241; LINK_1; 1; trigger=no XX case KW Disulfide bond end case FT From: PS50963 FT DOMAIN from..to FT /note="Link #" FT DISULFID 23..92 FT Tag: disulf; Condition: C-x*-C FT DISULFID 47..68 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 80-105; Related: None; Repeats: 1-4; Topology: Not cytoplasmic; Example: P98066; Scope: Eukaryota; Metazoa; Craniata Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00325; DC Domain; TR PROSITE; PS50966; ZF_SWIM; 1; level=0 XX Names: Zinc finger SWIM-type Function: Undefined XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50966 case and and and FT ZN_FING from..to FT /note="SWIM-type #" else case and and and FT ZN_FING from..to FT /note="SWIM-type #; atypical" else FT ZN_FING from..to FT /note="SWIM-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 25-45; Related: None; Repeats: 1-2; Topology: Undefined; Example: P33353; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00326; DC Domain; TR PROSITE; PS50863; B3; 1; level=0 XX Names: B3 domain Function: DNA binding domain. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS50863 FT DNA_BIND from..to FT /note="TF-B3 #" XX Chop: Nter=0; Cter=0; Size: 95-110; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q8L7G0; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.10 2022/06/27 // AC PRU00327; DC Domain; TR PROSITE; PS50965; NERD; 1; level=0 XX Names: NERD domain Function: The NERD domain is predicted to be connected to DNA processing and genomic context and distant homology analysis suggest a nuclease function. XX FT From: PS50965 FT DOMAIN from..to FT /note="NERD #" XX Chop: Nter=0; Cter=0; Size: 108-128; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q8KYT4; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00328; DC Domain; TR PROSITE; PS50967; HRDC; 1; level=0 XX Names: HRDC domain Function: The HRDC domain is involved in the binding of DNA to specific DNA structures (e.g. long-forked duplexes and Holliday junctions) that are formed during replication, recombination or transcription. XX FT From: PS50967 FT DOMAIN from..to FT /note="HRDC #" XX Chop: Nter=0; Cter=0; Size: 70-87; Related: None; Repeats: 1-3; Topology: Cytoplasmic; Example: Q14191; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00330; DC Domain; TR PROSITE; PS50069; CULLIN_2; 1; level=0 XX Names: Cullin Function: Undefined XX CC -!- SIMILARITY: Belongs to the cullin family. DR PROSITE; PS01256; CULLIN_1; 1; trigger=no XX Chop: Nter=0; Cter=0; Size: 150-250; Related: None; Repeats: 1; Topology: Undefined; Example: Q13616; Scope: Eukaryota Comments: Essential component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex XX # Revision 1.2 2004/05/06 // AC PRU00331; DC Domain; TR PROSITE; PS50957; JOSEPHIN; 1; level=0 XX Names: Josephin domain Function: The Josephin domain is believed to be a mainly alpha helical cysteine-protease domain predicted to be active against ubiquitin chains or related substrates. XX case GO GO:0016787; F:hydrolase activity KW Hydrolase end case FT From: PS50957 FT DOMAIN from..to FT /note="Josephin #" FT ACT_SITE 14 FT Group: 1; Condition: C FT ACT_SITE 117 FT Group: 1; Condition: H FT ACT_SITE 132 FT Group: 1; Condition: [DN] XX Chop: Nter=0; Cter=0; Size: 165-195; Related: None; Repeats: 1; Topology: Undefined; Example: Q15040; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00332; DC Domain; TR PROSITE; PS50961; HTH_LA; 1; level=0 XX Names: La-type HTH domain Function: The La-type HTH domain is an RNA-binding, winged helix-turn-helix (wHTH) domain of about 90 residues present in La proteins and other eukaryotic RNA-binding proteins. XX XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS50961 FT DOMAIN from..to FT /note="HTH La-type RNA-binding #" XX Chop: Nter=0; Cter=0; Size: 80-110; Related: None; Repeats: 1; Topology: Undefined; Example: P05455; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00333; DC Domain; TR PROSITE; PS50970; HCY; 1; level=0 XX Names: Homocysteine-binding domain Function: The homocysteine- (Hcy-)binding domain utilizes a Zn(Cys)3 cluster to bind and activate Hcy. XX case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case case GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity KW Zinc KW Metal-binding KW Transferase KW Methyltransferase end case FT From: PS50970 FT DOMAIN from..to FT /note="Hcy-binding #" FT BINDING 215 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 281 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 282 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 295-330; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9SDL7; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00334; DC Domain; TR PROSITE; PS50972; PTERIN_BINDING; 1; level=0 XX Names: Pterin-binding domain Function: The pterin-binding domain is folded into a (beta/alpha)8 barrel which forms a cup for pterin binding. XX FT From: PS50972 FT DOMAIN from..to FT /note="Pterin-binding #" XX Chop: Nter=0; Cter=0; Size: 240-320; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P0AC13; Scope: Eukaryota Archaea Bacteria Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00335; DC Domain; TR PROSITE; PS50977; HTH_TETR_2; 1; level=0 XX Names: TetR-type HTH domain Function: The tetR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 60 residues present in the tetR family of prokaryotic transcription regulators. XX XX DR PROSITE; PS01081; HTH_TETR_1; 1; trigger=no XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS50977 FT DOMAIN from..to FT /note="HTH tetR-type #" FT DNA_BIND 24..43 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 54-67; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: P0ACT4; Scope: Bacteria Archaea Comments: None XX # Revision 1.11 2019/11/21 // AC PRU00336; DC Domain; TR PROSITE; PS50969; FCP1; 1; level=0 XX Names: FCP1 homology domain Function: The FCP1 homology domain contains a DxDx(T/v) motif preceded by four hydrophobic residues characteristic of a large family of metal-dependent phosphohydrolases and phosphotransferases. XX case and GO GO:0016787; F:hydrolase activity KW Hydrolase end case FT From: PS50969 FT DOMAIN from..to FT /note="FCP1 homology #" XX Chop: Nter=0; Cter=0; Size: 150-200; Related: None; Repeats: 1; Topology: Undefined; Example: Q03254; Scope: Eukaryota Viruses Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00337; DC Domain; TR PROSITE; PS50978; NEAT; 1; level=0 XX Names: NEAT domain Function: Given its predicted extracellular location and its close association with the components of an iron transport system, one possible function of the NEAT domain is to be a receptor of the siderophore-iron complex. XX FT From: PS50978 FT DOMAIN from..to FT /note="NEAT #" XX Chop: Nter=0; Cter=0; Size: 115-135; Related: None; Repeats: 1-7; Topology: Undefined; Example: Q99TD3; Scope: Bacteria Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00338; DC Domain; TR PROSITE; PS50982; MBD; 1; level=0 XX Names: Methyl-CpG-binding domain (MBD) Function: Some MBDs have been shown to mediate binding to DNA and others protein-protein interactions. XX FT From: PS50982 FT DOMAIN from..to FT /note="MBD #" XX Chop: Nter=0; Cter=0; Size: 65-80; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q15047; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00339; DC Domain; TR PROSITE; PS50005; TPR; 1; level=0 XX Names: TPR repeat Function: TPR repeats mediate protein-protein interactions and the assembly of multiprotein complexes. XX XX DR PROSITE; PS50293; TPR_REGION; 1; trigger=no XX KW TPR repeat XX FT From: PS50005 FT REPEAT from..to FT /note="TPR #" XX Chop: Nter=0; Cter=0; Size: 30-40; Related: RRU00002!!; Repeats: 1-12; Topology: Undefined; Example: O15294; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00340; DC Domain; TR PROSITE; PS50987; HTH_ARSR_2; 1; level=0 XX Names: ArsR-type HTH domain Function: The arsR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain present in transcription regulators of the arsR/smtB family, involved in stress-response to heavy metal ions. In this domain two distinct sites for metal-binding have been identified, one in helix alpha 3 and another in helix alpha 5, and other sites occur. XX XX DR PROSITE; PS00846; HTH_ARSR_1; 1; trigger=no XX GO GO:0003677; F:DNA binding case GO GO:0046872; F:metal ion binding end case GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding case or KW Metal-binding end case case KW Metal-thiolate cluster end case KW Transcription KW Transcription regulation XX FT From: PS50987 FT DOMAIN from..to FT /note="HTH arsR-type #" FT DNA_BIND 35..58 FT /note="H-T-H motif" FT BINDING 34 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 36 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 77 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#2" FT Group: 2; Condition: D FT BINDING 79 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 90 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 93 FT /ligand="a metal cation" FT /ligand_id="ChEBI:CHEBI:25213" FT /ligand_label="#2" FT Group: 2; Condition: [EH] XX Warn: Replace "Metal cation" by the corresponding metal if it is known. Chop: Nter=0; Cter=0; Size: 68-110; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P30340; Scope: Bacteria Archaea Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00341; DC Domain; TR PROSITE; PS50986; MANSC; 1; level=0 XX Names: MANSC domain Function: It has been proposed that the MANSC domain in HAI-1 might function through binding with hepatocyte growth factor activator and matriptase. XX FT From: PS50986 FT DOMAIN from..to FT /note="MANSC #" XX Chop: Nter=0; Cter=0; Size: 80-90; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9H8J5; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00342; DC Domain; TR PROSITE; PS50984; TRUD; 1; level=0 XX Names: TRUD domain Function: The TRUD domain is likely to be involved in substrate recognition and may represent a RNA binding module. XX FT From: PS50984 FT DOMAIN from..to FT /note="TRUD #" XX Chop: Nter=0; Cter=0; Size: 120-250; Related: None; Repeats: 1; Topology: Undefined; Example: Q57261; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00343; DC Domain; TR PROSITE; PS50988; TROVE; 1; level=0 XX Names: TROVE domain Function: The TROVE domain may be involved in binding the RNA components of the three RNPs, which are telomerase RNA, Y RNA and vault RNA. XX GO GO:1990904; C:ribonucleoprotein complex XX KW Ribonucleoprotein XX FT From: PS50988 FT DOMAIN from..to FT /note="TROVE #" XX Chop: Nter=0; Cter=0; Size: 330-490; Related: None; Repeats: 1; Topology: Undefined; Example: P10155; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00344; DC Domain; TR PROSITE; PS50983; FE_B12_PBP; 1; level=0 XX Names: Iron siderophore/cobalamin periplasmic-binding domain Function: The iron siderophore/cobalamin periplasmic-binding domain delivers the ligand to the extracellular gate of the transmembrane domains. XX XX GO GO:0006810; P:transport case GO GO:0016020; C:membrane end case KW Transport KW Signal case KW Membrane KW Lipoprotein else KW Periplasm end case XX FT From: PS50983 FT DOMAIN from..to FT /note="Fe/B12 periplasmic-binding #" XX Chop: Nter=0; Cter=0; Size: 240-285; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P37028; P11460; Scope: Bacteria Archaea Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00345; DC Domain; TR PROSITE; PS50995; HTH_MARR_2; 1; level=0 XX Names: MarR-type HTH domain Function: The marR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 135 amino acids present in transcription regulators of the marR/slyA family, involved in the development of antibiotic resistance. XX XX DR PROSITE; PS01117; HTH_MARR_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50995 FT DOMAIN from..to FT /note="HTH marR-type #" FT DNA_BIND 47..70 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 120-160; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q93CC3; Scope: Bacteria Archaea Comments: None XX # Revision 1.10 2022/06/27 // AC PRU00346; DC Domain; TR PROSITE; PS50974; ADOMET_ACTIVATION; 1; level=0 XX Names: AdoMet activation domain Function: The AdoMet domain is found in prokaryotic and eukaryotic methione synthase (MetH). It binds S-adenosylmethionine and is required for reductive activation. XX GO GO:0016740; F:transferase activity KW Transferase KW Methyltransferase FT From: PS50974 FT DOMAIN from..to FT /note="AdoMet activation #" XX Chop: Nter=0; Cter=0; Size: 295-350; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P13009; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00347; DC Domain; TR PROSITE; PS50856; AMOP; 1; level=0 XX Names: AMOP domain Function: The presence of the AMOP domain in cell adhesion molecules could be indicative of a role for this domain in adhesion. XX FT From: PS50856 FT DOMAIN from..to FT /note="AMOP #" XX Chop: Nter=0; Cter=0; Size: 155-185; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q20762; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00348; DC Domain; TR PROSITE; PS50993; NIDOGEN_G2; 1; level=0 XX Names: Nidogen G2 beta-barrel domain Function: The nidogen G2 beta-barrel domain contains a large surface patch that is involved in the binding of perlecan, and possibly also of collagen IV. XX GO GO:0031012; C:extracellular matrix GO GO:0005604; C:basement membrane XX KW Extracellular matrix KW Basement membrane XX FT From: PS50993 FT DOMAIN from..to FT /note="Nidogen G2 beta-barrel #" XX Chop: Nter=0; Cter=0; Size: 230-240; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: O88322; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00349; DC Domain; TR PROSITE; PS51000; HTH_DEOR_2; 1; level=0 XX Names: DeoR-type HTH domain Function: The deoR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 amino acids present in transcription regulators of the deoR family, involved in sugar catabolism. XX XX DR PROSITE; PS00894; HTH_DEOR_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS51000 FT DOMAIN from..to FT /note="HTH deoR-type #" FT DNA_BIND 18..37 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 45-70; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P0ACK5; Scope: Bacteria Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00350; DC Domain; TR PROSITE; PS50958; SMB_2; 1; level=0 XX Names: Somatomedin B (SMB) domain Function: The SMB domain of vitronectin has been demonstrated to interact with both the urokinase receptor and the plasminogen activator inhibitor-1 (PAI-1) and the conserved cysteines of the NPP1 somatomedin B-like domain have been shown to mediate homodimerization. XX XX DR PROSITE; PS00524; SMB_1; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS50958 FT DOMAIN from..to FT /note="SMB #" FT DISULFID 5..9 FT /note="Alternate" FT Tag: disulf; Condition: C-x*-C FT DISULFID 5..21 FT /note="Alternate" FT Tag: disulf; Condition: C-x*-C FT DISULFID 9..39 FT /note="Alternate" FT Tag: disulf; Condition: C-x*-C FT DISULFID 19..21 FT /note="Alternate" FT Tag: disulf; Condition: C-x*-C FT DISULFID 19..32 FT /note="Alternate" FT Tag: disulf; Condition: C-x*-C FT DISULFID 25..31 FT Tag: disulf; Condition: C-x*-C FT DISULFID 32..39 FT /note="Alternate" FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 35-55; Related: None; Repeats: 2; Topology: Not cytoplasmic; Example: Q9GZM7; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.9 2019/11/21 // AC PRU00351; DC Domain; TR PROSITE; PS51013; PANNEXIN; 1; level=0 XX Names: Pannexin family Function: The pannexin family combines invertebrate gap junction proteins (innexins) and their vertebrate and viral homologs. XX CC -!- SIMILARITY: Belongs to the pannexin family. XX DR General; Transmembrane; -; 4; trigger=yes XX GO GO:0005921; C:gap junction GO GO:0016020; C:membrane XX KW Gap junction KW Membrane KW Transmembrane XX Chop: Nter=0; Cter=0; Size: 340-405; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q96RD7; Scope: Eukaryota; Metazoa Viruses; Polydnaviriformidae Comments: None XX # Revision 1.8 2022/09/29 // AC PRU00352; DC Domain; TR PROSITE; PS51004; SEMA; 1; level=0 XX Names: Sema domain Function: The 500 amino acid Sema domain is a receptor recognition and binding module. XX XX case KW Disulfide bond end case FT From: PS51004 FT DOMAIN from..to FT /note="Sema #" FT DISULFID 74..85 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 103..112 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 234..344 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 258..304 FT Tag: disulf; Group: 1; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 400-520; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9H2E6; Scope: Eukaryota; Metazoa Viruses Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00353; DC Domain; TR PROSITE; PS51005; NAC; 1; level=0 XX Names: NAC domain Function: The NAC domain has been shown to be a DNA-binding domain (DBD) and a dimerization domain. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: The NAC domain includes a DNA binding domain and a dimerization CC domain. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51005 FT DOMAIN from..to FT /note="NAC #" FT DNA_BIND 102..to+6 XX Chop: Nter=0; Cter=0; Size: 145-175; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: Q9ZNU2; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00354; DC Domain; TR PROSITE; PS51006; PABS_2; 1; level=0 XX Names: Polyamine biosynthesis (PABS) domain Function: The catalytic PABS domain is found in polyamine biosynthetic enzymes. XX XX DR PROSITE; PS01330; PABS_1; 1; trigger=no XX GO GO:0006596; P:polyamine biosynthetic process GO GO:0016740; F:transferase activity XX KW Polyamine biosynthesis KW Transferase XX FT From: PS51006 FT DOMAIN from..to FT /note="PABS #" FT ACT_SITE 156 FT /note="Proton acceptor" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 240-305; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P09158; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00355; DC Domain; TR PROSITE; PS51011; ARID; 1; level=0 XX Names: ARID domain Function: The AT-rich interaction domain (ARID) is an ~100-amino acid DNA- binding module found in a large number of eukaryotic transcription factors that regulate cell proliferation, differentiation and development. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation FT From: PS51011 FT DOMAIN from..to FT /note="ARID #" XX Chop: Nter=0; Cter=0; Size: 88-95; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q24573; Scope: Eukaryota Comments: None XX # Revision 1.10 2022/06/27 // AC PRU00356; DC Domain; TR PROSITE; PS51014; COBK_CBIJ; 1; level=0 XX Names: Precorrin-6x reductase domain Function: The precorrin-6x reductase domain catalyzes the NADPH-dependent reduction of precorrin-6x to a dihydro derivative named precorrin-6y. XX CC -!- SIMILARITY: Belongs to the precorrin-6x reductase family. XX GO GO:0009236; P:cobalamin biosynthetic process GO GO:0016491; F:oxidoreductase activity KW Cobalamin biosynthesis KW NADP KW Oxidoreductase XX Chop: Nter=0; Cter=0; Size: 240-260; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q10680; Q57972; Scope: Bacteria Archaea Comments: None XX # Revision 1.2 2017/01/07 // AC PRU00357; DC Domain; TR PROSITE; PS51017; CCT; 1; level=0 XX Names: CCT domain Function: The CCT domain is a plant module that has been shown to be involved in nuclear localization and probably also has a role in protein-protein interaction. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS51017 FT DOMAIN from..to FT /note="CCT #" XX Chop: Nter=0; Cter=0; Size: 40-45; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9LKL2; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00358; DC Domain; TR PROSITE; PS51015; YDG; 1; level=0 XX Names: MyTH4 domain Function: The YDG domain is necessary to direct to the chromatin a number of heterogeneous proteins with associated enzymatic activities. XX case CC -!- SUBCELLULAR LOCATION: Nucleus. end case XX case GO GO:0005634; C:nucleus end case XX case KW Nucleus end case XX FT From: PS51015 FT DOMAIN from..to FT /note="YDG #" XX Chop: Nter=0; Cter=0; Size: 135-155; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9FF80; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00359; DC Domain; TR PROSITE; PS51016; MYTH4; 1; level=0 XX Names: MyTH4 domain Function: The function of the MyTH4 domain is presently unknown, although its presence in several different putative motor proteins raises the possibility that different motor proteins might share similar mechanisms for targeting or regulation. XX FT From: PS51016 FT DOMAIN from..to FT /note="MyTH4 #" XX Chop: Nter=0; Cter=0; Size: 140-240; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: Q9W5D0; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00361; DC Domain; TR PROSITE; PS51021; BAR; 1; level=0 XX Names: BAR domain Function: BAR domain containing proteins are a unique class of adaptor proteins characterized by a common N-terminal fold termed the BAR domain. XX KW Coiled coil FT From: PS51021 FT DOMAIN from..to FT /note="BAR" XX Chop: Nter=0; Cter=0; Size: 222; Related: None; Repeats: 1; Topology: Undefined; Example: P49418; Scope: Eukaryota Scope: Bacteria Archaea Comments: Recent papers, based on sequence and structural similarities have shown that a conserved region in more divergent families, like oligophrenin, centaurin beta, sorting nexin, ICA69, pick1 or arfaptins, is related to the BAR domain. These families are however too divergent to be detected by the profile. XX # Revision 1.6 2019/11/21 // AC PRU00362; DC Domain; TR PROSITE; PS50990; PEPTIDASE_C39; 1; level=0 XX Names: Peptidase family C39 domain Function: This domain is a thiol peptidase found in ABC transporters, and belongs to the C39 peptidase family. XX case ( and ) DE + RecName: EC=3.4.22.-; end case XX DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1; trigger=no DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1; trigger=yes DR PROSITE; PS50990; PEPTIDASE_C39; 1; trigger=no DR PROSITE; PS50929; ABC_TM1F; 1; trigger=no XX case or KW Transport end case case ( or ) and defined and KW Membrane KW Cell inner membrane end case case or KW Transmembrane KW ATP-binding KW Nucleotide-binding end case case ( and ) KW Thiol protease KW Hydrolase KW Protease end case FT From: PS00017 FT BINDING from..to FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="#" FT From: PS50990 FT DOMAIN from..to FT /note="Peptidase C39 #" case FT ACT_SITE 7 else case FT ACT_SITE 81 end case XX Chop: Nter=0; Cter=0; Size: 121; Related: PRU01700; Repeats: 1; Topology: Undefined; Example: P08716; Scope: Bacteria Archaea Comments: A number of the proteins are classified as non-peptidase homologues as they either have been found experimentally to be without peptidase activity, or to lack amino acid residues that are believed to be essential for the catalytic activity. XX # Revision 1.20 2022/11/19 // AC PRU00363; DC Domain; TR PROSITE; PS51019; REELIN; 1; level=0 XX Names: Reelin domain Function: The function of the reelin domain is not yet known. XX GO GO:0031012; C:extracellular matrix XX KW Extracellular matrix XX FT From: PS51019 FT DOMAIN from..to FT /note="Reelin #" XX Chop: Nter=0; Cter=0; Size: 160-170; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9HCB6; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00364; DC Domain; TR PROSITE; PS51020; SPONDIN; 1; level=0 XX Names: Spondin domain Function: The function of the spondin domain is not known but it might interact with other factors. XX GO GO:0031012; C:extracellular matrix XX KW Extracellular matrix XX FT From: PS51020 FT DOMAIN from..to FT /note="Spondin #" XX Chop: Nter=0; Cter=0; Size: 190-200; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9HCB6; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00365; DC Domain; TR PROSITE; PS51022; L27; 1; level=0 XX Names: L27 domain Function: The L27 domain is a specific protein-protein interaction module capable of forming heteromeric complexes that can integrate multiple scaffold proteins into supramolecular assemblies required for establishment and maintenance of cell polarity. XX FT From: PS51022 FT DOMAIN from..to FT /note="L27 #" XX Chop: Nter=0; Cter=0; Size: 45-70; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: Q9NUP9; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00366; DC Domain; TR PROSITE; PS51032; AP2_ERF; 1; level=0 XX Names: AP2/ERF DNA-binding domain Function: AP2/ERF is a plant DNA binding domain. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51032 FT DNA_BIND from..to FT /note="AP2/ERF #" XX Chop: Nter=0; Cter=0; Size: 63-67; Related: None; Repeats: 1-2; Topology: Undefined; Example: O82132; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.13 2022/06/27 // AC PRU00367; DC Domain; TR PROSITE; PS51024; ZF_FCS; 1; level=0 XX Names: Zinc finger FCS-type Function: This domain can bind RNA in a non-sequence-specific manner. XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS51024 case and and and FT ZN_FING from..to FT /note="FCS-type #" else case and and and FT ZN_FING from..to FT /note="FCS-type #; atypical" else FT ZN_FING from..to FT /note="FCS-type #; degenerate" end case FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 30 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 30-50; Related: None; Repeats: 1; Topology: Undefined; Example: P39769; Scope: Eukaryota Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00368; DC Domain; TR PROSITE; PS50871; C1Q; 1; level=0 XX Names: C1q domain Function: The C-terminal globular domain of the C1q subcomponents and collagen types VIII and X is important both for the correct folding and alignment of the triple helix and for protein-protein recognition events. For collagen type X it has been suggested that the domain is important for initiation and maintenance of the correct assembly of the protein. XX FT From: PS50871 FT DOMAIN from..to FT /note="C1q #" XX Chop: Nter=0; Cter=0; Size: 125-155; Related: None; Repeats: 1-2; Topology: Undefined; Example: P02745; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00369; DC Domain; TR PROSITE; PS51035; BAG; 1; level=0 XX Names: BAG domain Function: BAG domain can interact with Hsc70/Hsp70 and can modulate either positively or negatively these chaperone proteins. XX XX DR PROSITE; PS51035; BAG; 1; trigger=no XX FT From: PS51035 FT DOMAIN from..to FT /note="BAG #" XX Chop: Nter=0; Cter=0; Size: 74-95; Related: none; Repeats: 1; Topology: Undefined; Example: O95816; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00370; DC Domain; TR PROSITE; PS51038; BAH; 1; level=0 XX Names: BAH domain Function: The BAH domain appears to act as a protein-protein interaction module specialized in gene silencing. XX XX DR PROSITE; PS51038; BAH; 1; trigger=no XX FT From: PS51038 FT DOMAIN from..to FT /note="BAH #" XX Chop: Nter=0; Cter=0; Size: 119; Related: none; Repeats: 1-2; Topology: Undefined; Example: P53236; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00371; DC Domain; TR PROSITE; PS51031; BESS; 1; level=0 XX Names: BESS domain Function: The BESS domain directs a variety of protein-protein interactions, including interactions with itself, with Dorsal, and with a TBP-associated factor. XX CC -!- SUBCELLULAR LOCATION: Nucleus. GO GO:0005634; C:nucleus KW Nucleus FT From: PS51031 FT DOMAIN from..to FT /note="BESS #" XX Chop: Nter=0; Cter=0; Size: 35-45; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P05552; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.9 2019/11/21 // AC PRU00372; DC Domain; TR PROSITE; PS51029; MADF; 1; level=0 XX Names: MADF domain Function: The myb/SANT-like domain in Adf-1 (MADF) is a ~80-amino-acid module that directs sequence specific DNA binding to a site consisting of multiple trinucleotide repeats. XX case not CC -!- SUBCELLULAR LOCATION: Nucleus. end case GO GO:0003677; F:DNA binding case not GO GO:0005634; C:nucleus end case GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding case not KW Nucleus end case KW Transcription KW Transcription regulation FT From: PS51029 FT DNA_BIND from..to FT /note="MADF #" XX Chop: Nter=0; Cter=0; Size: 75-85; Related: None; Repeats: 1-3; Topology: Not cytoplasmic; Example: P05552; Scope: Eukaryota; Metazoa Viruses Comments: None XX # Revision 1.14 2022/06/27 // AC PRU00373; DC Domain; TR PROSITE; PS50909; GAT; 1; level=0 XX Names: GAT domain Function: The GAT domain of GGAs serves as a molecular anchor of GGA to trans- Golgi network (TGN) membranes via its interaction with the GTP-bound form of a member of the ARF family of small GTPases and can bind specifically to the Rab GTPase effector rabaptin5 and to ubiquitin. XX GO GO:0016020; C:membrane GO GO:0015031; P:protein transport GO GO:0006810; P:transport KW Membrane KW Protein transport KW Transport FT From: PS50909 FT DOMAIN entry..exit FT /note="GAT #" XX Chop: Nter=0; Cter=0; Size: 85-130; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9UJY5; O60784; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00374; DC Domain; TR PROSITE; PS51042; CUT; 1; level=0 XX Names: CUT domain Function: The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS51042; CUT; 1; trigger=no XX GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus XX FT From: PS51042 FT DNA_BIND from..to FT /note="CUT #" XX Chop: Nter=0; Cter=0; Size: 88; Related: none; Repeats: 1-3; Topology: Undefined; Example: P39880; Scope: Eukaryota Comments: None XX # Revision 1.12 2019/11/21 // AC PRU00375; DC Domain; TR PROSITE; PS51034; ZP_2; 1; level=0 XX Names: ZP domain Function: The zona pellucida (ZP) domain is a protein polymerization module of ~260 amino acid module, which is found at the C-terminus of many secreted eukaryotic glycoproteins that play fundamental roles in development, hearing, immunity, and cancer. XX XX DR PROSITE; PS00682; ZP_1; 1; trigger=no XX FT From: PS51034 FT DOMAIN from..to FT /note="ZP #" XX Chop: Nter=0; Cter=0; Size: 245-280; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P60852; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00376; DC Domain; TR PROSITE; PS51037; YEATS; 1; level=0 XX Names: YEATS domain Function: The YEATS domain (Yaf9, ENL, AF9, Taf14, and Sas5) is a reader module that selectively recognizes histone lysine acylation, including acetylation, propionylation, butyrylation, crotonylation, 2-hydroxyisobutyrylation, and succinylation. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus KW Nucleus XX FT From: PS51037 FT DOMAIN from..to FT /note="YEATS #" XX Chop: Nter=0; Cter=0; Size: 130-270; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q99314; Scope: Eukaryota Comments: None XX # Revision 1.8 2020/08/27 // AC PRU00377; DC Domain; TR PROSITE; PS51051; DSL; 1; level=0 XX Names: DSL domain Function: The DSL domain may mediates oligomerization of DSL proteins to form an active ligand and mediates interaction with the extracellular domain of Lin-12/Notch proteins. XX XX DR PROSITE; PS51051; DSL; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51051 FT DOMAIN from..to FT /note="DSL #" FT DISULFID 3..12 FT Tag: disulf; Condition: C-x*-C FT DISULFID 16..28 FT Tag: disulf; Condition: C-x*-C FT DISULFID 36..45 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 45; Related: none; Repeats: 1; Topology: Undefined; Example: P45442; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00378; DC Domain; TR PROSITE; PS51043; DDHD; 1; level=0 XX Names: DDHD domain Function: The DDHD domain function is not currently known but it may be implicated in phospholipid metabolism, membrane turnover, or intracellular trafficking. XX XX DR PROSITE; PS51043; DDHD; 1; trigger=no XX FT From: PS51043 FT DOMAIN from..to FT /note="DDHD #" XX Chop: Nter=0; Cter=0; Size: 202; Related: none; Repeats: 1; Topology: Undefined; Example: Q8NEL9; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00379; DC Domain; c? TR PROSITE; PS51055; ITAM_1; 0-1; level=0 c? TR PROSITE; PS51056; ITAM_2; 0-1; level=0 XX Names: ITAM motif Function: The ITAM is an immunoreceptor tyrosine-based activation motif. Phosphorylation of the two ITAM tyrosines is a critical event in signal transduction. This phosphorylation was found to reflect activation of the src family kinase Lyn and Syk. XX XX case DR PROSITE; PS51055; ITAM_1; 1; trigger=no end case case DR PROSITE; PS51056; ITAM_2; 1; trigger=no end case XX FT From: PS51055 FT DOMAIN from..to FT /note="ITAM #" FT MOD_RES 12 FT /note="Phosphotyrosine" FT Condition: Y FT MOD_RES 23 FT /note="Phosphotyrosine" FT Condition: Y FT From: PS51056 FT DOMAIN from..to FT /note="ITAM #" FT MOD_RES 5 FT /note="Phosphotyrosine" FT Condition: Y FT MOD_RES 18 FT /note="Phosphotyrosine" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: 24-26; Related: none; Repeats: 1-3; Topology: Undefined; Example: P04234; P28728; Scope: Eukaryota Viruses Comments: None XX # Revision 1.13 2019/11/21 // AC PRU00380; DC Domain; TR PROSITE; PS51054; ORANGE; 1; level=0 XX Names: Orange domain Function: The Orange domain is a ~35 residue domain of unknown function, present in eukaryotic DNA-binding transcription repressors which regulate cell differentiation, embryonic patterning and other biological processes in both vertebrates and invertebrates. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51054 FT DOMAIN from..to FT /note="Orange #" XX Chop: Nter=0; Cter=0; Size: 20-45; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: O14503; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.10 2022/06/27 // AC PRU00381; DC Domain; TR PROSITE; PS51057; PAIRED_2; 1; level=0 XX Names: Paired DNA-binding domain Function: The paired domain is a ~126 amino acid DNA-binding domain, which is found in eukaryotic transcription regulatory proteins involved in embryogenesis. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS00034; PAIRED_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Paired box KW Transcription KW Transcription regulation XX FT From: PS51057 FT DNA_BIND from..to FT /note="Paired #" FT REGION 4..60 FT /note="PAI subdomain #" FT REGION 79..to FT /note="RED subdomain #" XX Chop: Nter=0; Cter=0; Size: 120-140; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P63016; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.12 2022/06/27 // AC PRU00382; DC Domain; TR PROSITE; PS51061; R3H; 1; level=0 XX Names: R3H motif Function: The R3H domain is a conserved sequence motif, which might be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. XX XX GO GO:0003676; F:nucleic acid binding XX FT From: PS51061 FT DOMAIN from..to FT /note="R3H #" XX Chop: Nter=0; Cter=0; Size: 65; Related: none; Repeats: 1; Topology: Undefined; Example: P38935; Q01620; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00383; DC Domain; TR PROSITE; PS51046; GON; 1; level=0 XX Names: GON domain Function: The GON domain is a ~200-residue module, whose presence is a hallmark of a subfamily of structurally and evolutionarily related ADAMTSs, called GON-ADAMTSs. XX XX FT From: PS51046 FT DOMAIN from..to FT /note="GON #" XX Chop: Nter=0; Cter=0; Size: 195-205; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9P2N4; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00384; DC Domain; TR PROSITE; PS51041; EMI; 1; level=0 XX Names: EMI domain Function: It has been suggested that the EMI domain could be a protein-protein interaction module, as the EMI domain of EMILIN-1 was found to interact with the C1q domain of EMILIN-2. XX XX case KW Disulfide bond end case XX FT From: PS51041 FT DOMAIN from..to FT /note="EMI #" FT DISULFID 5..76 FT Tag: disulf; Condition: C-x*-C FT DISULFID 34..46 FT Tag: disulf; Condition: C-x*-C FT DISULFID 75..90 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 50-85; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9Y6C2; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00385; DC Domain; TR PROSITE; PS51049; KASH; 1; level=0 XX Names: KASH domain Function: The KASH or KLS domain is a highly hydrophobic nuclear envelope localization domain of ~60 amino acids comprising an ~20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. XX XX DR General; Transmembrane; -; 1; trigger=no XX GO GO:0016020; C:membrane XX KW Membrane KW Transmembrane XX FT From: PS51049 FT TOPO_DOM Nter..9 FT /note="Cytoplasmic" FT TRANSMEM 10..30 FT /note="Helical; Anchor for type IV membrane protein" FT TOPO_DOM 31..Cter FT /note="Perinuclear space" FT DOMAIN from..to FT /note="KASH #" XX Chop: Nter=0; Cter=0; Size: 55-65; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q8NF91; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.12 2022/09/29 // AC PRU00386; DC Domain; TR PROSITE; PS51048; SGS; 1; level=0 XX Names: SGS domain Function: The SGS domain has been shown to bind to proteins of the S100 family, which are thought to function as sensors of calcium ion concentration in the cell. XX XX FT From: PS51048 FT DOMAIN from..to FT /note="SGS #" XX Chop: Nter=0; Cter=0; Size: 75-95; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q08446; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00387; DC Domain; TR PROSITE; PS51063; HTH_CRP_2; 1; level=0 XX Names: Crp-type HTH domain Function: The crp-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 70-75 amino acids present in transcription regulators of the crp-fnr family, involved in the control of virulence factors, enzymes of aromatic ring degradation, nitrogen fixation, photosynthesis, and various types of respiration. XX XX DR PROSITE; PS00042; HTH_CRP_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS51063 FT DOMAIN from..to FT /note="HTH crp-type #" FT DNA_BIND 43..62 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 40-90; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P27369; Scope: Bacteria Plastid Comments: None XX # Revision 1.9 2022/06/27 // AC PRU00388; DC Domain; TR PROSITE; PS50127; UBC_2; 1; level=0 XX Names: Ubiquitin-conjugating (UBC) core domain Function: Catalyzes the covalent attachment of ubiquitin to target proteins. XX case DE + RecName: EC= 2.3.2.-; end case CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. XX case DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1; trigger=no XX GO GO:0016874; F:ligase activity KW Transferase KW Ubl conjugation pathway end case XX FT From: PS50127 FT DOMAIN from..to FT /note="UBC core #" FT ACT_SITE 85 FT /note="Glycyl thioester intermediate" FT Tag: act_site; Condition: C XX Chop: Nter=0; Cter=0; Size: 100-170; Related: None; Repeats: 1; Topology: Undefined; Example: P52484; Scope: Eukaryota Comments: None XX # Revision 1.14 2020/04/15 // AC PRU00389; DC Domain; TR PROSITE; PS51064; IRS_PTB; 1; level=0 XX Names: IRS-type PTB domain Function: IRS-type PTB domain has an average length of about 100 amino acids. It binds to the insulin receptor through the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins. XX XX DR PROSITE; PS51064; IRS_PTB; 1; trigger=no XX FT From: PS51064 FT DOMAIN from..to FT /note="IRS-type PTB #" XX Chop: Nter=0; Cter=0; Size: 105; Related: none; Repeats: 1; Topology: Undefined; Example: Q99704; P35568; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00390; DC Domain; TR PROSITE; PS51071; HTH_RPIR; 1; level=0 XX Names: RpiR-type HTH domain Function: The rpiR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 75-80 amino acids present in prokaryotic regulators of transcription. XX XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS51071 FT DOMAIN from..to FT /note="HTH rpiR-type #" FT DNA_BIND 37..56 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 70-90; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P0ACS7; Scope: Bacteria Comments: None XX # Revision 1.9 2022/06/27 // AC PRU00391; DC Domain; TR PROSITE; PS51066; ZF_FPG_2; 1; level=0 XX Names: Zinc finger FPG-type Function: Zinc finger specific to Formamidopyrimidine-DNA glycosylase and Endonuclease VIII. It binds DNA. XX case and and and CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case DR PROSITE; PS01242; ZF_FPG_1; 1; trigger=no XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS51066 case and and and FT ZN_FING from..to FT /note="FPG-type #" else case and and and FT ZN_FING from..to FT /note="FPG-type #; atypical" else FT ZN_FING from..to FT /note="FPG-type #; degenerate" FT ACT_SITE 25 FT /note="Proton donor (in delta-elimination)" FT Condition: R end case XX Chop: Nter=0; Cter=0; Size: 25-50; Related: None; Repeats: 1; Topology: Undefined; Example: P64159; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.12 2019/11/21 // AC PRU00392; DC Domain; TR PROSITE; PS51068; FPG_CAT; 1; level=0 XX Names: Formamidopyrimidine-DNA glycosylase catalytic domain Function: DNA glycosylase XX case DE + AltName: EC=3.2.2.-; DE EC=4.2.99.18; XX CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation CC or by mutagenic agents. Acts as DNA glycosylase that recognizes and CC removes damaged bases. CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'- CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3- CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'- CC deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA- CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, CC ChEBI:CHEBI:167181; EC=4.2.99.18; CC -!- SIMILARITY: Belongs to the FPG family. end case XX case GO GO:0006974; P:DNA damage response GO GO:0006281; P:DNA repair GO GO:0003677; F:DNA binding GO GO:0016798; F:hydrolase activity, acting on glycosyl bonds GO GO:0016787; F:hydrolase activity GO GO:0016829; F:lyase activity GO GO:0003824; F:catalytic activity KW DNA damage KW DNA repair KW DNA-binding KW Glycosidase KW Hydrolase KW Lyase KW Multifunctional enzyme end case XX FT From: PS51068 FT ACT_SITE 1 FT /note="Schiff-base intermediate with DNA" FT Group: 1; Condition: P FT ACT_SITE 2 FT /note="Proton donor" FT Group: 1; Condition: E FT ACT_SITE 57 FT /note="Proton donor (in beta-elimination)" FT Group: 1; Condition: K XX Chop: Nter=0; Cter=0; Size: 70-150; Related: None; Repeats: 1; Topology: Undefined; Example: P05523; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.17 2024/01/11 // AC PRU00393; DC Domain; TR PROSITE; PS51077; HTH_ICLR; 1; level=0 XX Names: IclR-type HTH domain Function: The iclR-type HTH domain is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 60 amino acids present in transcription regulators of the iclR family, involved in carbon metabolism in eubacteria and archaea. XX XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS51077 FT DOMAIN from..to FT /note="HTH iclR-type #" FT DNA_BIND 23..42 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 50-75; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: P37728; Scope: Bacteria Archaea Viruses Comments: None XX # Revision 1.10 2022/06/27 // AC PRU00394; DC Domain; TR PROSITE; PS51078; ICLR_ED; 1; level=0 XX Names: IclR effector binding domain Function: The iclR effector binding domain is a ~170 residues C-terminal regulatory domain, present in transcription regulators of the iclR family, involved in carbon metabolism in eubacteria and archaea. XX XX FT From: PS51078 FT DOMAIN 15..to FT /note="IclR-ED #" XX Chop: Nter=0; Cter=0; Size: 170-190; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: P16528; Scope: Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00395; DC Domain; TR PROSITE; PS51052; CYCLOTIDE; 1; level=0 XX Names: Cyclotides Function: Cyclotides (cyclo peptides) are plant peptides of ~30 amino acids with a head-to-tail cyclic backbone and six cysteine residues involved in three disulfide bonds. They are most likely present as defense molecules. XX CC -!- FUNCTION: Probably participates in a plant defense mechanism. CC -!- PTM: This is a cyclic peptide. case and not CC -!- SIMILARITY: Belongs to the cyclotide family. Bracelet subfamily. else case and not CC -!- SIMILARITY: Belongs to the cyclotide family. Moebius subfamily. else CC -!- SIMILARITY: Belongs to the cyclotide family. end case CC -!- CAUTION: This peptide is cyclic. The start position was chosen by CC similarity to Oak1 (kalata B1) for which the DNA sequence is known. DR PROSITE; PS60008; CYCLOTIDE_BRACELET; 0-1; trigger=no DR PROSITE; PS60009; CYCLOTIDE_MOEBIUS; 0-3; trigger=no KW Plant defense case KW Disulfide bond end case XX FT From: PS51052 FT PEPTIDE from..to FT /note="" FT DISULFID 5..19 FT Tag: disulf; Condition: C-x*-C FT DISULFID 9..21 FT Tag: disulf; Condition: C-x*-C FT DISULFID 14..26 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 20-35; Related: None; Repeats: 1-3; Topology: Not cytoplasmic; Example: P58433; P56254; Scope: Eukaryota; Viridiplantae; Embryophyta Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00396; DC Domain; TR PROSITE; PS51053; SERTA; 1; level=0 XX Names: SERTA domain Function: The cyclin-dependent kinase CDK4-interacting segment of TRIP-Br1 includes most of the SERTA domain. XX XX FT From: PS51053 FT DOMAIN from..to FT /note="SERTA #" XX Chop: Nter=0; Cter=0; Size: 45-50; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UHV2; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00397; DC Domain; TR PROSITE; PS51059; PARP_CATALYTIC; 1; level=0 XX Names: PARP catalytic domain Function: Poly(ADP-ribose) polymerase (PARP) transfers the ADP-ribose moiety from its substrate, nicotinamide adenine dinucleotide (NAD), to carboxylate groups of aspartic and glutamic residues. XX GO GO:0016740; F:transferase activity GO GO:0016757; F:glycosyltransferase activity XX KW Glycosyltransferase KW NAD KW Transferase XX FT From: PS51059 FT DOMAIN from..to FT /note="PARP catalytic #" XX Chop: Nter=0; Cter=0; Size: 185-235; Related: None; Repeats: 1; Topology: Undefined; Example: P35875; Scope: Eukaryota Comments: None XX # Revision 1.8 2021/06/03 // AC PRU00398; DC Domain; TR PROSITE; PS51060; PARP_ALPHA_HD; 1; level=0 XX Names: PARP alpha-helical domain Function: The poly(ADP-ribose) polymerase (PARP) alpha-helical domain is thought to relay the activation signal issued on binding to damaged DNA. XX XX FT From: PS51060 FT DOMAIN from..to FT /note="PARP alpha-helical #" XX Chop: Nter=0; Cter=0; Size: 115-140; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P09874; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00399; DC Domain; TR PROSITE; PS51062; RUNT; 1; level=0 XX Names: Runt domain Function: The Runt domain confers DNA binding ability to the consensus core PyGPyGGT and mediates the interaction of mammalian RUNX proteins with the beta-subunit, designated core-binding factor beta (CBFbeta), which increases the DNA binding affinity of the heterodimer. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription case or KW Chloride end case KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51062 FT DOMAIN from..to FT /note="Runt #" FT REGION 31..35 FT /note="Interaction with DNA" FT REGION 86..94 FT /note="Interaction with DNA" FT REGION 119..128 FT /note="Interaction with DNA" FT BINDING 63 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#1" FT Group: 1; Condition: N FT BINDING 67 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 90 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#2" FT Group: 2; Condition: R FT BINDING 121 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#2" FT Group: 2; Condition: V XX Chop: Nter=0; Cter=0; Size: 125-135; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q01196; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.11 2022/11/19 // AC PRU00400; DC Domain; TR PROSITE; PS51065; NHR; 1; level=0 XX Names: Neuralized homology repeat (NHR) domain Function: It has been suggested that the NHR domain is required for the localization of neuralized to the plasma membrane and that it might possess a microtubule-binding function. XX XX FT From: PS51065 FT DOMAIN from..to FT /note="NHR #" XX Chop: Nter=0; Cter=0; Size: 150-225; Related: None; Repeats: 1-6; Topology: Undefined; Example: P29503; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00401; DC Domain; TR PROSITE; PS51073; RPEL; 1; level=0 XX Names: RPEL repeat Function: RPEL (RPxxxEL) repeats have been shown to be required for unpolymerized actin binding and proteins containing RPEL repeats are able to modify cell shape and/or are important in the regulation of gene expression by the actin cytoskeleton. XX XX FT From: PS51073 FT REPEAT from..to FT /note="RPEL #" XX Chop: Nter=0; Cter=0; Size: 20-30; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q8IZQ8; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00402; DC Domain; TR PROSITE; PS51069; GBP; 1; level=0 XX Names: GBP repeat Function: The GBP repeats have been shown to bind to the erythrocyte receptor glycophorin. XX FT From: PS51069 FT REPEAT entry..exit FT /note="GBP #" XX Chop: Nter=0; Cter=0; Size: 40-55; Related: None; Repeats: 8-12; Topology: Undefined; Example: Q8I6U8; Scope: Eukaryota; Alveolata; Plasmodium Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00403; DC Domain; TR PROSITE; PS51070; SHD; 1; level=0 XX Names: Stonin homology domain (SHD) Function: The ~140 amino-acid SHD domain may be unique to members of the stonin family, which are supposed to be endocytotic proteins involved in clathrin-mediated endocytosis at synapses. Its function is not yet known. XX XX GO GO:0006897; P:endocytosis GO GO:0016020; C:membrane GO GO:0045202; C:synapse KW Endocytosis KW Membrane KW Synapse XX FT From: PS51070 FT DOMAIN from..to FT /note="SHD #" XX Chop: Nter=0; Cter=0; Size: 130-180; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q24212; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00404; DC Domain; TR PROSITE; PS51072; MHD; 1; level=0 XX Names: Mu homology domain (MHD) Function: The MHD domain is found in endocytotic proteins involved in clathrin-mediated endocytosis and has been shown to bind to the C2B domain of members of the synaptotagmin family. XX XX GO GO:0006886; P:intracellular protein transport GO GO:0030131; C:clathrin adaptor complex XX KW Protein transport KW Transport XX FT From: PS51072 FT DOMAIN from..to FT /note="MHD #" XX Chop: Nter=0; Cter=0; Size: 240-345; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P38153; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00405; DC Domain; TR PROSITE; PS50878; RT_POL; 1; level=0 XX Names: Reverse transcriptase (RT) catalytic domain Function: The RT domain exhibits two enzymatic activities: RNA-dependent DNA polymerase and DNA-dependent DNA polymerase. XX case DE + RecName: EC=2.7.7.49; DE EC=2.7.7.7; end case case and CC -!- FUNCTION: RT is a multifunctional enzyme that converts the viral CC dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus CC entry into the cell. This enzyme displays a DNA polymerase activity CC that can copy either DNA or RNA templates, and a ribonuclease H (RNAse CC H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a CC partially processive 3' to 5' endonucleasic mode. Conversion of viral CC genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the CC primer-binding site (PBS) situated at the 5' end of the viral RNA. RT CC uses the 3' end of the tRNA primer to perfom a short round of RNA- CC dependent minus-strand DNA synthesis. The reading proceeds through the CC U5 region and ends after the repeated (R) region which is present at CC both ends of viral RNA. The portion of the RNA-DNA heteroduplex is CC digested by the RNase H, resulting in a ssDNA product attached to the CC tRNA primer. This ssDNA/tRNA hybridizes with the identical R region CC situated at the 3' end of viral RNA. This template exchange, known as CC minus-strand DNA strong stop transfer, can be either intra- or CC intermolecular. RT uses the 3' end of this newly synthetized short CC ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the CC whole template. RNase H digests the RNA template except for two CC polypurine tracts (PPTs) situated at the 5' end and near the center of CC the genome. It is not clear if both polymerase and RNase H activities CC are simultaneous. RNase H probably can proceed both in a polymerase- CC dependent (RNA cut into small fragments by the same RT performing DNA CC synthesis) and a polymerase-independent mode (cleavage of remaining RNA CC fragments by free RTs). Secondly, RT performs DNA-directed plus-strand CC DNA synthesis using the PPTs that have not been removed by RNase H as CC primers. PPTs and tRNA primers are then removed by RNAse H. The 3' and CC 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. CC Strand displacement synthesis by RT to the PBS and PPT ends produces a CC blunt ended, linear dsDNA copy of the viral genome that includes long CC terminal repeats (LTRs) at both ends. else case and CC -!- FUNCTION: RT is a multifunctional enzyme that converts the viral CC dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus CC entry into the cell. This enzyme displays a DNA polymerase activity CC that can copy either DNA or RNA templates, and a ribonuclease H (RNAse CC H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a CC partially processive 3' to 5' endonucleasic mode. Conversion of viral CC genomic RNA into dsDNA requires many steps. A tRNA-Trp binds to the CC primer-binding site (PBS) situated at the 5' end of the viral RNA. RT CC uses the 3' end of the tRNA primer to perfom a short round of RNA- CC dependent minus-strand DNA synthesis. The reading proceeds through the CC U5 region and ends after the repeated (R) region which is present at CC both ends of viral RNA. The portion of the RNA-DNA heteroduplex is CC digested by the RNase H, resulting in a ssDNA product attached to the CC tRNA primer. This ssDNA/tRNA hybridizes with the identical R region CC situated at the 3' end of viral RNA. This template exchange, known as CC minus-strand DNA strong stop transfer, can be either intra- or CC intermolecular. RT uses the 3' end of this newly synthetized short CC ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the CC whole template. RNase H digests the RNA template except for a CC polypurine tract (PPT) situated at the 5' end of the genome. It is not CC clear if both polymerase and RNase H activities are simultaneous. RNase CC H probably can proceed both in a polymerase-dependent (RNA cut into CC small fragments by the same RT performing DNA synthesis) and a CC polymerase-independent mode (cleavage of remaining RNA fragments by CC free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis CC using the PPT that has not been removed by RNase H as primers. PPT and CC tRNA primers are then removed by RNAse H. The 3' and 5' ssDNA PBS CC regions hybridize to form a circular dsDNA intermediate. Strand CC displacement synthesis by RT to the PBS and PPT ends produces a blunt CC ended, linear dsDNA copy of the viral genome that includes long CC terminal repeats (LTRs) at both ends. else case or or or and CC -!- FUNCTION: RT is a multifunctional enzyme that converts the viral CC dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus CC entry into the cell. This enzyme displays a DNA polymerase activity CC that can copy either DNA or RNA templates, and a ribonuclease H (RNAse CC H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a CC partially processive 3' to 5' endonucleasic mode. Conversion of viral CC genomic RNA into dsDNA requires many steps. A tRNA binds to the primer- CC binding site (PBS) situated at the 5' end of the viral RNA. RT uses the CC 3' end of the tRNA primer to perfom a short round of RNA-dependent CC minus-strand DNA synthesis. The reading proceeds through the U5 region CC and ends after the repeated (R) region which is present at both ends of CC viral RNA. The portion of the RNA-DNA heteroduplex is digested by the CC RNase H, resulting in a ssDNA product attached to the tRNA primer. This CC ssDNA/tRNA hybridizes with the identical R region situated at the 3' CC end of viral RNA. This template exchange, known as minus-strand DNA CC strong stop transfer, can be either intra- or intermolecular. RT uses CC the 3' end of this newly synthetized short ssDNA to perfom the RNA- CC dependent minus-strand DNA synthesis of the whole template. RNase H CC digests the RNA template except for a polypurine tract (PPT) situated CC at the 5' end of the genome. It is not clear if both polymerase and CC RNase H activities are simultaneous. RNase H probably can proceed both CC in a polymerase-dependent (RNA cut into small fragments by the same RT CC performing DNA synthesis) and a polymerase-independent mode (cleavage CC of remaining RNA fragments by free RTs). Secondly, RT performs DNA- CC directed plus-strand DNA synthesis using the PPT that has not been CC removed by RNase H as primers. PPT and tRNA primers are then removed by CC RNAse H. The 3' and 5' ssDNA PBS regions hybridize to form a circular CC dsDNA intermediate. Strand displacement synthesis by RT to the PBS and CC PPT ends produces a blunt ended, linear dsDNA copy of the viral genome CC that includes long terminal repeats (LTRs) at both ends. else case and CC -!- FUNCTION: RT is a multifunctional enzyme that converts the viral CC dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus CC entry into the cell. This enzyme displays a DNA polymerase activity CC that can copy either DNA or RNA templates, and a ribonuclease H (RNAse CC H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a CC partially processive 3' to 5' endonucleasic mode. Conversion of viral CC genomic RNA into dsDNA requires many steps. A tRNA-Pro binds to the CC primer-binding site (PBS) situated at the 5' end of the viral RNA. RT CC uses the 3' end of the tRNA primer to perfom a short round of RNA- CC dependent minus-strand DNA synthesis. The reading proceeds through the CC U5 region and ends after the repeated (R) region which is present at CC both ends of viral RNA. The portion of the RNA-DNA heteroduplex is CC digested by the RNase H, resulting in a ssDNA product attached to the CC tRNA primer. This ssDNA/tRNA hybridizes with the identical R region CC situated at the 3' end of viral RNA. This template exchange, known as CC minus-strand DNA strong stop transfer, can be either intra- or CC intermolecular. RT uses the 3' end of this newly synthetized short CC ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the CC whole template. RNase H digests the RNA template except for a CC polypurine tract (PPT) situated at the 5' end of the genome. It is not CC clear if both polymerase and RNase H activities are simultaneous. RNase CC H probably can proceed both in a polymerase-dependent (RNA cut into CC small fragments by the same RT performing DNA synthesis) and a CC polymerase-independent mode (cleavage of remaining RNA fragments by CC free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis CC using the PPT that has not been removed by RNase H as primers. PPT and CC tRNA primers are then removed by RNAse H. The 3' and 5' ssDNA PBS CC regions hybridize to form a circular dsDNA intermediate. Strand CC displacement synthesis by RT to the PBS and PPT ends produces a blunt CC ended, linear dsDNA copy of the viral genome that includes long CC terminal repeats (LTRs) at both ends. end case XX case CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:173112; EC=2.7.7.49; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:173112; EC=2.7.7.7; end case XX case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=The RT polymerase active site binds 2 magnesium ions.; end case XX case CC -!- SUBUNIT: The reverse transcriptase is a heterodimer of p66 RT and p51 CC RT (RT p66/p51). Heterodimerization of RT is essential for DNA CC polymerase activity. Despite the sequence identities, p66 RT and p51 RT CC have distinct folding. else case CC -!- SUBUNIT: The reverse transcriptase forms a heterodimer of alpha and CC beta subunits. else case CC -!- SUBUNIT: The reverse transcriptase is a monomer. end case XX case CC -!- DOMAIN: The p66 RT is structured in five subdomains: finger, palm, CC thumb, connection and RNase H. Within the palm subdomain, the 'primer CC grip' region is thought to be involved in the positioning of the primer CC terminus for accomodating the incoming nucleotide. The RNase H domain CC stabilizes the association of RT with primer-template. end case XX case CC -!- PTM: Specific enzymatic cleavages by the viral protease yield mature CC proteins. The protease is released by autocatalytic cleavage. The CC polyprotein is cleaved during and after budding, this process is termed CC maturation. Proteolytic cleavage of p66 RT removes the RNase H domain CC to yield the p51 RT subunit. end case XX case CC -!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme that CC lacks a proof-reading function. High mutations rate is a direct CC consequence of this characteristic. RT also displays frequent template CC swiching leading to high recombination rate. Recombination mostly CC occurs between homologous regions of the two copackaged RNA genomes. If CC these two RNA molecules derive from different viral strains, reverse CC transcription will give rise to highly recombinated proviral DNAs. end case XX XX GO GO:0016740; F:transferase activity GO GO:0016779; F:nucleotidyltransferase activity GO GO:0003964; F:RNA-directed DNA polymerase activity GO GO:0003887; F:DNA-directed DNA polymerase activity XX KW Transferase KW Nucleotidyltransferase KW RNA-directed DNA polymerase KW DNA-directed DNA polymerase KW Multifunctional enzyme KW DNA-binding KW RNA-binding KW DNA recombination KW Metal-binding KW Magnesium XX FT From: PS50878 FT DOMAIN from..to FT /note="Reverse transcriptase #" FT BINDING 66 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Group: 1; Condition: D FT BINDING 130 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Group: 1; Condition: D FT BINDING 131 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 140-285; Related: None; Repeats: 1; Topology: Undefined; Example: O14746; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.23 2022/11/19 // AC PRU00406; DC Domain; TR PROSITE; PS51082; WH2; 1; level=0 XX Names: WH2 domain WASP-Homology 2 Wiskott-Aldrich homology 2 Function: The WH2 (WASP-Homology 2, or Wiskott-Aldrich homology 2) domain is an ~18 amino acids actin-binding motif. XX XX GO GO:0003779; F:actin binding KW Actin-binding FT From: PS51082 FT DOMAIN from..to FT /note="WH2 #" XX Chop: Nter=0; Cter=0; Size: 10-30; Related: None; Repeats: 1-4; Topology: Cytoplasmic; Example: O00401; Scope: Eukaryota Viruses Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00407; DC Domain; TR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1; level=0 XX Names: Nuclear hormone receptors DNA-binding domain Function: Nuclear hormone receptors are ligand-activated transcription factors that regulate gene expression by interacting with specific DNA sequences upstream of their target genes. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription GO GO:0005634; C:nucleus case and and and or and and and GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding end case XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation KW Zinc-finger case and and and or and and and KW Zinc KW Metal-binding end case XX FT From: PS51030 FT DNA_BIND from..to FT /note="Nuclear receptor #" case and and and FT ZN_FING 4..24 FT /note="NR C4-type" else case and and and FT ZN_FING 4..24 FT /note="NR C4-type; atypical" else FT ZN_FING 4..24 FT /note="NR C4-type; degenerate" end case case and and and FT ZN_FING 40..59 FT /note="NR C4-type" else case and and and FT ZN_FING 40..59 FT /note="NR C4-type; atypical" else FT ZN_FING 40..59 FT /note="NR C4-type; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 30-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q9W539; Scope: Eukaryota Viruses Comments: None XX # Revision 1.17 2022/06/27 // AC PRU00408; DC Domain; TR PROSITE; PS50879; RNASE_H_1; 1; level=0 XX Names: Ribonuclease H type-1 domain Function: Ribonuclease H (RNase H) (EC 3.1.26.4) recognizes and cleaves the RNA strand of RNA-DNA heteroduplexes. XX DE + RecName: EC=3.1.26.4; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; XX GO GO:0004519; F:endonuclease activity GO GO:0016787; F:hydrolase activity GO GO:0004518; F:nuclease activity case GO GO:0000287; F:magnesium ion binding end case XX KW Endonuclease KW Hydrolase KW Nuclease case KW Magnesium KW Metal-binding end case XX FT From: PS50879 FT DOMAIN from..to FT /note="RNase H type-1" case not and not FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#2" FT Group: 1; Condition: D FT BINDING 50 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 72 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 136 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#2" FT Group: 1; Condition: D end case XX Chop: Nter=0; Cter=0; Size: 101-205; Related: None; Repeats: 1; Topology: Undefined; Example: Q08885; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.19 2022/11/19 // AC PRU00409; DC Domain; TR PROSITE; PS50975; ATP_GRASP; 1; level=0 XX Names: ATP-grasp domain Function: The ATP-grasp superfamily currently includes 17 groups of enzymes, catalyzing ATP-dependent ligation of a carboxylate containing molecule to an amino or thiol group-containing molecule. XX case or CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds #(Mg(2+)~Mn(2+),ion) per subunit.; end case XX GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding case or GO GO:0000287; F:magnesium ion binding GO GO:0030145; F:manganese ion binding end case XX KW ATP-binding KW Nucleotide-binding case or KW Magnesium KW Manganese KW Metal-binding end case XX FT From: PS50975 FT DOMAIN from..to FT /note="ATP-grasp #" case not FT BINDING 27..84 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" end case FT BINDING 152 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#1" FT Group: 1; Condition: [QDE] FT BINDING 152 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#1" FT Group: 1; Condition: [QDE] FT BINDING 165 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 165 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#2" FT Group: 2; Condition: E FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#2" FT Group: 2; Condition: E FT BINDING 167 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#2" FT Group: 2; Condition: N FT BINDING 167 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#2" FT Group: 2; Condition: N XX case not or not Warn: one magnesium or manganese binding site was not detected! end case Chop: Nter=0; Cter=0; Size: 140-255; Related: None; Repeats: 1; Topology: Undefined; Example: Q75D66; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.28 2022/11/19 // AC PRU00410; DC Domain; TR PROSITE; PS50229; WH1; 1; level=0 XX Names: WH1 domain WASP-Homology 1 Wiskott-Aldrich homology 1 EVH1 Ena/VASP homology 1 Enabled/Vasodilator-stimulated phosphoprotein homology 1 Function: The WH1 (WASP-Homology 1, or Wiskott-Aldrich homology 1) or EVH1 (Ena/VASP homology 1, or Enabled/Vasodilator-stimulated phosphoprotein homology 1) domain is an ~110 amino acids protein-protein interaction module. XX XX FT From: PS50229 FT DOMAIN from..to FT /note="WH1 #" XX Chop: Nter=0; Cter=0; Size: 100-130; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: P42768; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00411; DC Domain; TR PROSITE; PS50043; HTH_LUXR_2; 1; level=0 XX Names: LuxR-type HTH domain Function: The luxR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 65 amino acids, present in transcription regulators of the LuxR/FixJ family of response regulators. XX XX DR PROSITE; PS00622; HTH_LUXR_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS50043 FT DOMAIN from..to FT /note="HTH luxR-type #" FT DNA_BIND 24..43 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 50-75; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P31802; Scope: Bacteria Plastid Comments: None XX # Revision 1.9 2022/06/27 // AC PRU00412; DC Domain; TR PROSITE; PS51087; APAG; 1; level=0 XX Names: ApaG domain Function: The apaG domain is a ~125 amino acids domain present in bacterial apaG proteins and in eukaryotic F-box proteins. XX XX FT From: PS51087 FT DOMAIN from..to FT /note="ApaG #" XX Chop: Nter=0; Cter=0; Size: 110-140; Related: None; Repeats: 1; Topology: Undefined; Example: Q56017; Scope: Bacteria Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00413; DC Domain; TR PROSITE; PS51090; CORTACTIN; 1; level=0 XX Names: Cortactin repeat HS1 repeat Function: The cortactin or HS1 repeat is a tandem repeat of 37-amino acid actin-binding domains. XX XX GO GO:0003779; F:actin binding KW Actin-binding FT From: PS51090 FT REPEAT entry..exit FT /note="Cortactin #" XX Chop: Nter=0; Cter=0; Size: 30-50; Related: None; Repeats: 1-7; Topology: Cytoplasmic; Example: Q14247; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00414; DC Domain; TR PROSITE; PS51110; SAP_A; 1; level=0 XX Names: Saposin A-type domain Function: The saposin A-type domain is a ~40 amino acid domain present in the saposin precursor, prosaposin, in the propeptides that are cleaved off in the activation reaction. XX FT From: PS51110 FT DOMAIN from..to FT /note="Saposin A-type #" XX Chop: Nter=0; Cter=0; Size: 30-50; Related: None; Repeats: 1-2; Topology: Undefined; Example: P07602; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00415; DC Domain; TR PROSITE; PS50015; SAP_B; 1; level=0 XX Names: Saposin B-type domain Function: The saposin B-type domain is a ~80 amino acid domain present in saposins and related proteins that interact with lipids. In plant aspartic proteinases the two subdomains that are connected by disulfide bridges occur in inversed order, these "swapped" halves are called a "swaposin" domain. XX XX case KW Glycoprotein end case case KW Disulfide bond end case XX FT From: PS50015 FT DOMAIN entry..exit FT /note="Saposin B-type #" FT DISULFID 5..79 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 8..73 FT Tag: disulf; Group: 2; Condition: C-x*-C FT DISULFID 36..48 FT Tag: disulf; Group: 3; Condition: C-x*-C FT CARBOHYD 22 FT /note="N-linked (GlcNAc...) asparagine" FT Condition: N XX case not and not and not Warn: In plant aspartic proteinases two half SAP_B subdomains occur in inversed order. Correct the boundaries and check the three disulfide bonds in these "swaposins". end case Chop: Nter=0; Cter=0; Size: 35-160; Related: None; Repeats: 1-8; Topology: Undefined; Example: P07602; Scope: Eukaryota Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00416; DC Domain; TR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1; level=0 XX Names: PTS EIIA type-1 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and CC -!- DOMAIN: The PTS EIIA type-1 domain is phosphorylated by phospho-HPr on CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS CC EIIB type-1 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphotransferase system KW Transferase end case FT From: PS51093 FT DOMAIN from..to FT /note="PTS EIIA type-1 #" FT ACT_SITE 53 FT /note="Tele-phosphohistidine intermediate; for EIIA FT activity" FT Condition: H XX Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl donor. Check DE, KW and CC DOMAIN. Chop: Nter=0; Cter=0; Size: 105; Related: none; Repeats: 1; Topology: Undefined; Example: P09323; Scope: Bacteria Archaea Comments: None XX # Revision 1.18 2019/11/21 // AC PRU00417; DC Domain; TR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1; level=0 XX Names: PTS EIIA type-2 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS CC EIIB type-2 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphoprotein KW Phosphotransferase system KW Transferase end case XX FT From: PS51094 FT DOMAIN from..to FT /note="PTS EIIA type-2 #" case or FT ACT_SITE 61 FT /note="Tele-phosphohistidine intermediate; for EIIA FT activity" FT Condition: H else FT ACT_SITE 61 FT /note="Tele-phosphohistidine intermediate" FT Condition: H end case XX Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW , FT and CC DOMAIN. Chop: Nter=0; Cter=0; Size: 142; Related: none; Repeats: 1; Topology: Undefined; Example: P44715; Scope: Bacteria Archaea Comments: None XX # Revision 1.16 2019/11/21 // AC PRU00418; DC Domain; TR PROSITE; PS51095; PTS_EIIA_TYPE_3; 1; level=0 XX Names: PTS EIIA type-3 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and CC -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS CC EIIB type-3 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphoprotein KW Phosphotransferase system KW Transferase end case FT From: PS51095 FT DOMAIN from..to FT /note="PTS EIIA type-3 #" FT MOD_RES 75 FT /note="Phosphohistidine; by HPr" FT Condition: H XX Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW, FT and CC DOMAIN. Chop: Nter=0; Cter=0; Size: 99; Related: none; Repeats: 1; Topology: Undefined; Example: Q45402; Scope: Bacteria Archaea Comments: None XX # Revision 1.18 2019/11/21 // AC PRU00419; DC Domain; TR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1; level=0 XX Names: PTS EIIA type-4 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and CC -!- DOMAIN: The EIIA type-4 domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the EIIB CC type-4 domain. end case XX case ( or ) and GO GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system GO GO:0016740; F:transferase activity XX KW Phosphotransferase system KW Transferase end case FT From: PS51096 FT DOMAIN from..to FT /note="PTS EIIA type-4 #" case or FT ACT_SITE 9 FT /note="Tele-phosphohistidine intermediate; for EIIA FT activity" FT Condition: H else FT ACT_SITE 9 FT /note="Tele-phosphohistidine intermediate" FT Condition: H end case XX Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW, FT and CC DOMAIN. Chop: Nter=0; Cter=0; Size: 125; Related: none; Repeats: 1; Topology: Undefined; Example: P26379; Scope: Bacteria Archaea Comments: None XX # Revision 1.17 2019/11/21 // AC PRU00420; DC Domain; TR PROSITE; PS51097; PTS_EIIA_TYPE_5; 1; level=0 XX Names: PTS EIIA type-5 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and CC -!- DOMAIN: The EIIA type-5 domain is phosphorylated by phospho-HPr on a CC histidyl residue. Then, it transfers the phosphoryl group to the EIIB CC type-5 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphoprotein KW Phosphotransferase system KW Transferase end case FT From: PS51097 FT DOMAIN from..to FT /note="PTS EIIA type-5 #" FT MOD_RES 41 FT /note="Phosphohistidine; by HPr" FT Condition: H XX Chop: Nter=0; Cter=0; Size: 114; Related: none; Repeats: 1; Topology: Undefined; Example: P05706; Scope: Bacteria Archaea Comments: None XX # Revision 1.17 2019/11/21 // AC PRU00421; DC Domain; TR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1; level=0 XX Names: PTS EIIB type-1 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and DE + RecName: EC=2.7.1.-; XX CC -!- DOMAIN: The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on CC a cysteinyl residue. Then, it transfers the phosphoryl group to the CC sugar substrate concomitantly with the sugar uptake processed by the CC PTS EIIC type-1 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphotransferase system KW Transferase end case FT From: PS51098 FT DOMAIN from..to FT /note="PTS EIIB type-1 #" FT ACT_SITE 23 FT /note="Phosphocysteine intermediate; for EIIB activity" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 82; Related: none; Repeats: 1-2; Topology: Undefined; Example: P69789; Scope: Bacteria Archaea Comments: None XX # Revision 1.22 2019/11/21 // AC PRU00422; DC Domain; TR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1; level=0 XX Names: PTS EIIB type-2 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and DE + RecName: EC=2.7.1.-; XX CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on CC a cysteinyl residue. Then, it transfers the phosphoryl group to the CC sugar substrate concomitantly with the sugar uptake processed by the CC PTS EIIC type-2 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphoprotein KW Phosphotransferase system KW Transferase end case FT From: PS51099 FT DOMAIN from..to FT /note="PTS EIIB type-2 #" FT MOD_RES 8 FT /note="Phosphocysteine; by EIIA" FT Condition: C XX Warn: This domain can be found in other kind of proteins, mainly transcriptional regulators, in these cases it may serve as a regulatory function, through its phosphorylation activity, or as a simple phosphoryl. Check DE, KW, CC, FT DOMAIN AND CC CATALYTIC ACTIVITY. Chop: Nter=0; Cter=0; Size: 98; Related: none; Repeats: 1-2; Topology: Undefined; Example: P20966; Scope: Bacteria Archaea Comments: None XX # Revision 1.17 2019/11/21 // AC PRU00423; DC Domain; TR PROSITE; PS51100; PTS_EIIB_TYPE_3; 1; level=0 XX Names: PTS EIIB type-3 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and DE + RecName: EC=2.7.1.-; XX CC -!- DOMAIN: The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on CC a cysteinyl residue. Then, it transfers the phosphoryl group to the CC sugar substrate concomitantly with the sugar uptake processed by the CC PTS EIIC type-3 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphoprotein KW Phosphotransferase system KW Transferase end case FT From: PS51100 FT DOMAIN from..to FT /note="PTS EIIB type-3 #" FT MOD_RES 8 FT /note="Phosphocysteine; by EIIA" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 106; Related: none; Repeats: 1; Topology: Undefined; Example: P55901; Scope: Bacteria Archaea Comments: None XX # Revision 1.18 2019/11/21 // AC PRU00424; DC Domain; TR PROSITE; PS51101; PTS_EIIB_TYPE_4; 1; level=0 XX Names: PTS EIIB type-4 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and DE + RecName: EC=2.7.1.-; XX CC -!- DOMAIN: The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on CC a histidyl residue. Then, it transfers the phosphoryl group to the CC sugar substrate concomitantly with the sugar uptake processed by the CC PTS EIIC type-4 domain. end case XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphoprotein KW Phosphotransferase system KW Transferase end case FT From: PS51101 FT DOMAIN from..to FT /note="PTS EIIB type-4 #" FT MOD_RES 16 FT /note="Phosphohistidine; by EIIA" FT Condition: H XX Chop: Nter=0; Cter=0; Size: 166; Related: none; Repeats: 1; Topology: Undefined; Example: P26380; Scope: Bacteria Archaea Comments: None XX # Revision 1.18 2019/11/21 // AC PRU00425; DC Domain; TR PROSITE; PS51102; PTS_EIIB_TYPE_5; 1; level=0 XX Names: PTS_EIIB type-5 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case ( or ) and DE + RecName: EC=2.7.1.-; XX CC -!- DOMAIN: The PTS EIIB type-5 domain is phosphorylated by phospho-EIIA on CC a cysteinyl residue. Then, it transfers the phosphoryl group to the CC sugar substrate concomitantly with the sugar uptake processed by the CC PTS EIIC type-5 domain. end case XX DR PROSITE; PS51102; PTS_EIIB_TYPE_5; 1; trigger=no XX case ( or ) and GO GO:0016740; F:transferase activity XX KW Phosphoprotein KW Phosphotransferase system KW Transferase end case FT From: PS51102 FT DOMAIN from..to FT /note="PTS EIIB type-5 #" FT MOD_RES 72 FT /note="Phosphocysteine; by EIIA" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 192; Related: none; Repeats: 1; Topology: Undefined; Example: O32333; Scope: Bacteria Archaea Comments: None XX # Revision 1.20 2019/11/21 // AC PRU00426; DC Domain; TR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1; level=0 XX Names: PTS EIIC type-1 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case or CC -!- DOMAIN: The EIIC domain type-1 forms the PTS system translocation CC channel and contains the specific substrate-binding site. end case case and defined and CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case and defined and CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else case and defined CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. end case XX DR General; Transmembrane; -; 6-10; trigger=yes XX GO GO:0051119; F:sugar transmembrane transporter activity case and defined and GO GO:0005886; C:plasma membrane else case and defined and GO GO:0005886; C:plasma membrane else case and defined GO GO:0005886; C:plasma membrane else GO GO:0016020; C:membrane end case XX case or KW Phosphotransferase system KW Transport KW Sugar transport KW Transmembrane KW Membrane end case case ( or ) and defined and KW Cell inner membrane end case FT From: PS51103 FT DOMAIN from..to FT /note="PTS EIIC type-1 #" XX Chop: Nter=0; Cter=0; Size: 369-380; Related: none; Repeats: 1; Topology: Undefined; Example: P09323; Scope: Bacteria Archaea Comments: None XX # Revision 1.21 2019/11/21 // AC PRU00427; DC Domain; TR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1; level=0 XX Names: PTS EIIC type-2 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case or CC -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation CC channel and contains the specific substrate-binding site. end case case and defined and CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case and defined and CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else case and defined CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. end case XX DR General; Transmembrane; -; 6-8; trigger=yes XX GO GO:0051119; F:sugar transmembrane transporter activity case and defined and GO GO:0005886; C:plasma membrane else case and defined and GO GO:0005886; C:plasma membrane else case and defined GO GO:0005886; C:plasma membrane else GO GO:0016020; C:membrane end case XX case or KW Transport KW Sugar transport KW Phosphotransferase system KW Transmembrane KW Membrane end case case ( or ) and defined and KW Cell inner membrane end case FT From: PS51104 FT DOMAIN from..to FT /note="PTS EIIC type-2 #" XX Chop: Nter=0; Cter=0; Size: 352; Related: none; Repeats: 1; Topology: Undefined; Example: P42956; Scope: Bacteria Archaea Comments: None XX # Revision 1.22 2019/11/21 // AC PRU00428; DC Domain; TR PROSITE; PS51105; PTS_EIIC_TYPE_3; 1; level=0 XX Names: PTS EIIC type-3 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case or CC -!- DOMAIN: The EIIC type-3 domain forms the PTS system translocation CC channel and contains the specific substrate-binding site. end case case and defined and CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case and defined and CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else case and defined CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. end case XX DR General; Transmembrane; -; 6-8; trigger=yes XX GO GO:0051119; F:sugar transmembrane transporter activity case and defined and GO GO:0005886; C:plasma membrane else case and defined and GO GO:0005886; C:plasma membrane else case and defined GO GO:0005886; C:plasma membrane else GO GO:0016020; C:membrane end case XX case or KW Transport KW Sugar transport KW Phosphotransferase system KW Transmembrane KW Membrane end case case ( or ) and defined and KW Cell inner membrane end case FT From: PS51105 FT DOMAIN from..to FT /note="PTS EIIC type-3 #" XX Warn: This domain can be found in association with EAL domain, in these cases it may have an other function. Check DE and CC DOMAIN. Chop: Nter=0; Cter=0; Size: 407; Related: none; Repeats: 1; Topology: Undefined; Example: Q45400; Scope: Bacteria Archaea Comments: None XX # Revision 1.23 2019/11/21 // AC PRU00429; DC Domain; TR PROSITE; PS51106; PTS_EIIC_TYPE_4; 1; level=0 XX Names: PTS EIIC type-4 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case or CC -!- DOMAIN: The EIIC type-4 domain forms the PTS system translocation CC channel and contains the specific substrate-binding site. end case case and defined and CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case and defined and CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else case and defined CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. end case XX DR General; Transmembrane; -; 6-8; trigger=yes XX GO GO:0051119; F:sugar transmembrane transporter activity case and defined and GO GO:0005886; C:plasma membrane else case and defined and GO GO:0005886; C:plasma membrane else case and defined GO GO:0005886; C:plasma membrane else GO GO:0016020; C:membrane end case XX case or KW Transport KW Sugar transport KW Phosphotransferase system KW Transmembrane KW Membrane end case case ( or ) and defined and KW Cell inner membrane end case FT From: PS51106 FT DOMAIN from..to FT /note="PTS EIIC type-4 #" XX Chop: Nter=0; Cter=0; Size: 234; Related: none; Repeats: 1; Topology: Undefined; Example: P26381; Scope: Bacteria Archaea Comments: None XX # Revision 1.21 2019/11/21 // AC PRU00430; DC Domain; TR PROSITE; PS51107; PTS_EIIC_TYPE_5; 1; level=0 XX Names: PTS EIIC type-5 domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case or CC -!- DOMAIN: The EIIC domain type-5 forms the PTS system translocation CC channel and contains the specific substrate-binding site. end case case and defined and CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case and defined and or and defined CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. end case XX DR General; Transmembrane; -; 6-8; trigger=yes XX GO GO:0051119; F:sugar transmembrane transporter activity case ( or ) and defined GO GO:0005886; C:plasma membrane else GO GO:0016020; C:membrane end case XX case or KW Transport KW Sugar transport KW Phosphotransferase system KW Transmembrane KW Membrane end case case ( or ) and defined and KW Cell inner membrane end case FT From: PS51107 FT DOMAIN from..to FT /note="PTS EIIC type-5 #" XX Chop: Nter=0; Cter=0; Size: 187; Related: none; Repeats: 1; Topology: Undefined; Example: O32332; Scope: Bacteria Archaea Comments: None XX # Revision 1.25 2019/11/21 // AC PRU00431; DC Domain; TR PROSITE; PS51108; PTS_EIID; 1; level=0 XX Names: PTS EIID domain Function: Phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system. XX case or CC -!- DOMAIN: The EIID domain, with its homologous EIIC domain, forms the PTS CC system translocation channel and contains part of its specific CC substrate-binding site. end case case and defined and CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein. else case and defined and CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else case and defined CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. else CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. end case XX DR PROSITE; PS51108; PTS_EIID; 1; trigger=no DR General; Transmembrane; -; 2-6; trigger=yes XX GO GO:0051119; F:sugar transmembrane transporter activity case and defined and GO GO:0005886; C:plasma membrane else case and defined and GO GO:0005886; C:plasma membrane else case and defined GO GO:0005886; C:plasma membrane else GO GO:0016020; C:membrane end case XX case or KW Phosphotransferase system KW Transport KW Sugar transport KW Transmembrane KW Membrane end case case ( or ) and defined and KW Cell inner membrane end case FT From: PS51108 FT DOMAIN from..to FT /note="PTS EIID #" XX Chop: Nter=0; Cter=0; Size: 265; Related: none; Repeats: 1; Topology: Undefined; Example: P26382; Scope: Bacteria Archaea Comments: None XX # Revision 1.22 2019/11/21 // AC PRU00432; DC Domain; TR PROSITE; PS51113; ZF_BTK; 1; level=0 XX Names: Zinc finger Btk-type Btk Motif (BM) Function: The Btk-type zinc finger is a domain of ~37 amino acids present in eukaryotic signalling proteins. XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS51113 case and and and FT ZN_FING from..to FT /note="Btk-type #" else case and and and FT ZN_FING from..to FT /note="Btk-type #; atypical" else FT ZN_FING from..to FT /note="Btk-type #; degenerate" end case FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 30-45; Related: None; Repeats: 1; Topology: Undefined; Example: O95294; Scope: Eukaryota Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00433; DC Domain; TR PROSITE; PS51007; CYTC; 1; level=0 XX Names: Cytochrome c domain Function: Cytochromes c typically function in electron transfer, but c-type cytochrome centers are also found in the active sites of many enzymes, XX XX KW Heme KW Iron KW Metal-binding XX FT From: PS51007 FT DOMAIN from..to FT /note="Cytochrome c #" FT BINDING 18 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="#1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Condition: H FT BINDING 14 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="#1" FT /note="covalent" FT Group: 1; Condition: C FT BINDING 17 FT /ligand="heme c" FT /ligand_id="ChEBI:CHEBI:61717" FT /ligand_label="#1" FT /note="covalent" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 60-120; Related: None; Repeats: 3; Topology: Undefined; Example: P0A389; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.13 2022/11/19 // AC PRU00434; DC Domain; TR PROSITE; PS50893; ABC_TRANSPORTER_2; 1-2; level=0 XX Names: ABC transporter family domain ATP binding cassette domain Function: Uses the hydrolysis of ATP to energize diverse biological systems XX XX DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1; trigger=no XX case not GO GO:0043190; C:ATP-binding cassette (ABC) transporter complex GO GO:0006810; P:transport end case GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding XX case not KW Transport end case KW ATP-binding KW Nucleotide-binding case ( or ) and defined and and not KW Cell inner membrane KW Cell membrane KW Membrane end case case not KW Membrane end case XX FT From: PS50893 FT DOMAIN from..to FT /note="ABC transporter #" FT BINDING 33..40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [AG]-x(4)-G-K-[ST] XX Chop: Nter=0; Cter=0; Size: 200-2438; Related: none; Repeats: 1-2; Topology: Not cytoplasmic; Example: P02915; P60752; P13569; Scope: Eukaryota Bacteria Archaea Plastid Viruses; Spbetavirus Comments: Contains ABC cassette but lost transport capability in UvrA subfamily. XX # Revision 1.26 2022/11/19 // AC PRU00435; DC Domain; TR PROSITE; PS51118; HTH_HXLR; 1; level=0 XX Names: HxlR-type HTH domain Function: The hxlR-type HTH domain is a domain of ~90-100 amino acids present in putative transcription regulators with a winged helix-turn-helix (wHTH) structure. XX XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Transcription KW Transcription regulation XX FT From: PS51118 FT DOMAIN from..to FT /note="HTH hxlR-type #" XX Chop: Nter=0; Cter=0; Size: 85-110; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: P42406; Scope: Bacteria Archaea Comments: None XX # Revision 1.6 2022/06/27 // AC PRU00436; DC Domain; TR PROSITE; PS51080; CTF_NFI_2; 1; level=0 XX Names: CTF/NF-I DNA-binding domain Function: The CTF/NF-I DNA-binding domain contains four conserved Cys residues, which are required for its DNA-binding activity. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the CTF/NF-I family. XX DR PROSITE; PS00349; CTF_NFI_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006260; P:DNA replication GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Activator KW DNA-binding KW DNA replication KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51080 FT DNA_BIND from..to FT /note="CTF/NF-I #" XX Chop: Nter=0; Cter=0; Size: 190-195; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q12857; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.7 2022/06/27 // AC PRU00437; DC Domain; TR PROSITE; PS51109; G5; 1; level=0 XX Names: G5 domain Function: The G5 domain may confer localization or substrate specificity on the proteins in which it is found. XX XX FT From: PS51109 FT DOMAIN from..to FT /note="G5 #" XX Chop: Nter=0; Cter=0; Size: 75-90; Related: None; Repeats: 1-7; Topology: Cytoplasmic; Example: P37546; Scope: Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00438; DC Domain; TR PROSITE; PS51075; MH1; 1; level=0 XX Names: MAD homology domain 1 (MH1) Function: The MH1 domain has a role in DNA binding and negatively regulates the functions of MH2 domain. XX XX FT From: PS51075 FT DOMAIN from..to FT /note="MH1 #" XX Chop: Nter=0; Cter=0; Size: 120-170; Related: None; Repeats: 1; Topology: Undefined; Example: Q99717; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00439; DC Domain; TR PROSITE; PS51076; MH2; 1; level=0 XX Names: MAD homology domain 2 (MH2) Function: The MH2 domain is responsible for transactivation and mediates phosphorylation-triggered heteromeric assembly between Smad4 and R-Smad. XX XX case KW Phosphoprotein end case FT From: PS51076 FT DOMAIN from..to FT /note="MH2 #" case FT MOD_RES 193 FT /note="Phosphoserine" FT MOD_RES 195 FT /note="Phosphoserine" end case XX Chop: Nter=0; Cter=0; Size: 160-235; Related: None; Repeats: 1; Topology: Undefined; Example: Q99717; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00440; DC Domain; TR PROSITE; PS51119; TAFH; 1; level=0 XX Names: TAFH/NHR1 domain TAF homology Nervy homology region 1 domain I TAF110 domain Function: The TAF homology (TAFH) or Nervy homology region 1 (NHR1) domain is a domain of 95-100 amino acids present in eukaryotic proteins of the MTG/ETO family and whereof the core ~75-80 residues occur in TAF proteins. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51119 FT DOMAIN from..to FT /note="TAFH #" XX Chop: Nter=0; Cter=0; Size: 90-110; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q06455; Scope: Eukaryota Comments: None XX # Revision 1.12 2022/06/27 // AC PRU00441; DC Domain; TR PROSITE; PS50928; ABC_TM1; 0-1; level=0 TR PROSITE; PS50929; ABC_TM1F; 0-1; level=0 XX Names: ABC transporter integral membrane type-1 domain ATP binding cassette superfamily Function: ABC transporter integral membrane type-1 domain profile XX XX DR General; Transmembrane; -; 4-7; trigger=yes XX GO GO:0043190; C:ATP-binding cassette (ABC) transporter complex GO GO:0016020; C:membrane GO GO:0006810; P:transport XX KW Transmembrane case ( or ) and defined and KW Cell inner membrane KW Membrane end case XX FT From: any FT DOMAIN from..to FT /note="ABC transmembrane type-1 #" XX Chop: Nter=0; Cter=0; Size: 200-2438; Related: none; Repeats: 1-2; Topology: Not cytoplasmic; Example: P68183; P02915; P60752; P13569; Scope: Bacteria Archaea Plastid Viruses Comments: The domain associated with the profile PS50929 TM1F is always found fused to the ABC transporter domain. XX # Revision 1.11 2022/09/30 // AC PRU00442; DC Domain; TR PROSITE; PS51012; ABC_TM2; 1; level=0 XX Names: ABC transporter integral membrane type-2 family domain ATP binding cassette superfamily Function: ABC transporter integral membrane type-2 domain profile XX XX GO GO:0043190; C:ATP-binding cassette (ABC) transporter complex GO GO:0016020; C:membrane GO GO:0006810; P:transport XX KW Transmembrane case ( or ) and defined and KW Cell inner membrane KW Membrane end case XX FT From: PS51012 FT DOMAIN from..to FT /note="ABC transmembrane type-2 #" XX Chop: Nter=0; Cter=0; Size: 200-400; Related: none; Repeats: 1-2; Topology: Not cytoplasmic; Example: O52619; Scope: Bacteria Archaea Plastid Comments: None. XX # Revision 1.13 2022/09/30 // AC PRU00443; DC Domain; TR PROSITE; PS51121; NTA; 1; level=0 XX Names: NtA (N-terminal agrin) domain Function: The NtA domain is a region of 135 amino acids required for the localization of agrin to synaptic basal lamina and other basement membranes. XX case KW Disulfide bond end case XX FT From: PS51121 FT DOMAIN from..to FT /note="NtA #" FT DISULFID 1..73 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 120-150; Related: None; Repeats: 1; Topology: Undefined; Example: O00468; Scope: Eukaryota Comments: None XX # Revision 1.7 2023/11/16 // AC PRU00444; DC Domain; TR PROSITE; PS51124; PEPTIDASE_C16; 1-2; level=0 XX Names: Peptidase family C16 domain Function: Peptidase family C16 contains polyprotein processing endopeptidases from coronaviruses. XX case DE + RecName: EC=3.4.22.-; end case XX case KW Thiol protease KW Hydrolase KW Protease end case KW Zinc-finger case KW Zinc KW Metal-binding end case FT From: PS51124 FT DOMAIN from..to FT /note="Peptidase C16 #" FT ACT_SITE 39 FT /note="For PL#1-PRO activity" FT Group: 1; Condition: C FT ACT_SITE 198 FT /note="For PL#1-PRO activity" FT Group: 1; Condition: H FT ACT_SITE 211 FT /note="For PL#1-PRO activity" FT Group: 1; Condition: D case and and and FT ZN_FING 117..150 FT /note="C4-type #" else case and and and FT ZN_FING 117..150 FT /note="C4-type #; atypical" else FT ZN_FING 117..150 FT /note="C4-type #; degenerate" end case FT BINDING 117 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] FT BINDING 150 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 250-260; Related: none; Repeats: 1-2; Topology: Undefined; Example: P16342; Scope: Viruses Comments: None XX # Revision 1.16 2022/11/19 // AC PRU00445; DC Domain; TR PROSITE; PS51127; BIG1; 1; level=0 XX Names: Big-1 (Bacterial Ig-like domain 1) domain Function: The bacterial immunoglobulin-like (Ig) domain 1 or Big-1 domain is a domain of ~95 amino acids present in bacterial adhesion molecules of the intimin/invasin family, involved in pathogenicity. XX XX FT From: PS51127 FT DOMAIN from..to FT /note="Big-1 #" XX Chop: Nter=0; Cter=0; Size: 80-110; Related: None; Repeats: 1-50; Topology: Undefined; Example: P19809; Scope: Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00446; DC Domain; TR PROSITE; PS51132; OLF; 1; level=0 XX Names: olfactomedin-like domain OLF domain Function: The olfactomedin-like domain is a module of ~260 residues present in metazoan secreted glycoproteins with a characteristic tissue-specific expression. XX XX case KW Disulfide bond end case XX FT From: PS51132 FT DOMAIN from..to FT /note="Olfactomedin-like #" FT DISULFID 2..184 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 240-280; Related: None; Repeats: 1; Topology: Undefined; Example: Q866N2; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00447; DC Domain; TR PROSITE; PS51135; CIDE_N; 1; level=0 XX Names: CIDE-N domain CIDE domain CAD domain N-terminal domain (NTD) Function: The CIDE-N domain is a ~78 amino acid protein-protein interaction domain in the N-terminal part of Cell death-Inducing DFF45-like Effector (CIDE) proteins, involved in apoptosis. XX XX GO GO:0006915; P:apoptotic process KW Apoptosis XX FT From: PS51135 FT DOMAIN from..to FT /note="CIDE-N #" XX Chop: Nter=0; Cter=0; Size: 70-90; Related: None; Repeats: 1; Topology: Undefined; Example: O76075; Scope: Eukaryota; Metazoa Viruses; Baculoviridae Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00448; DC Domain; TR PROSITE; PS50222; EF_HAND_2; 1; level=0 XX Names: EF-hand Function: Undefined XX DR PROSITE; PS00018; EF_HAND_1; 0-1; trigger=no XX case KW Calcium KW Metal-binding end case XX FT From: PS50222 FT DOMAIN from..to FT /note="EF-hand #" case FT BINDING 14 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 16 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 18 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 20 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 25 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] end case XX Chop: Nter=0; Cter=0; Size: 20-45; Related: None; Repeats: 1-8; Topology: Undefined; Example: P62157; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.15 2022/11/19 // AC PRU00449; DC Domain; TR PROSITE; PS51039; ZF_AN1; 1; level=0 XX Names: AN1-type Function: Undefined XX KW Zinc-finger case ( and and and ) or ( and and and ) KW Metal-binding KW Zinc end case XX FT From: PS51039 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="AN1-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="AN1-type #; atypical" else FT ZN_FING from..to FT /note="AN1-type #; degenerate" end case FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 42 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 42-45; Related: None; Repeats: 1; Topology: Undefined; Example: P53899; Scope: Eukaryota Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00450; DC Domain; TR PROSITE; PS50876; ZF_INTEGRASE; 1; level=0 XX Names: Zinc finger integrase-type Function: required for integration activity and enhances tetramerization in the context of the full-length integrase. XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS50876 case and and and FT ZN_FING from..to FT /note="Integrase-type #" else case and and and FT ZN_FING from..to FT /note="Integrase-type #; atypical" else FT ZN_FING from..to FT /note="Integrase-type #; degenerate" end case FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 30-54; Related: None; Repeats: 1-3; Topology: Undefined; Example: P51517; Scope: Eukaryota Viruses Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00451; DC Domain; TR PROSITE; PS51036; ZF_A20; 1; level=0 XX Names: Zinc finger A20-type Function: Functions as a ubiquitin ligase by polyubiquitinating RIP with Lys- 48-linked ubiquitin chains. XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS51036 case and and and FT ZN_FING from..to FT /note="A20-type #" else case and and and FT ZN_FING from..to FT /note="A20-type #. atypical" else FT ZN_FING from..to FT /note="A20-type #; degenerate" end case FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 11 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 32-34; Related: None; Repeats: 1-7; Topology: Undefined; Example: P21580; Scope: Eukaryota; Mammalia Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00452; DC Domain; TR PROSITE; PS51044; ZF_SP_RING; 1; level=0 XX Names: Zinc finger SP-RING-type Function: Like classical RING fingers SP-RINGs function as an E3 enzyme but specific for sumoylation. XX XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS51044 case and and and FT ZN_FING from..to FT /note="SP-RING-type #" else case and and and FT ZN_FING from..to FT /note="SP-RING-type #; atypical" else FT ZN_FING from..to FT /note="SP-RING-type #; degenerate" end case FT BINDING 32 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 58 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 60-85; Related: None; Repeats: 1; Topology: Undefined; Example: O54714; Scope: Eukaryota Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00453; DC Domain; TR PROSITE; PS51083; ZF_HIT; 1; level=0 XX Names: Zinc finger HIT-type Function: Undefined XX GO GO:0008270; F:zinc ion binding XX KW Zinc-finger case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case XX FT From: PS51083 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="HIT-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="HIT-type #; atypical" else FT ZN_FING from..to FT /note="HIT-type #; degenerate" end case FT BINDING 1 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 26-40; Related: None; Repeats: 1; Topology: Undefined; Example: P38772; Scope: Eukaryota Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00454; DC Domain; TR PROSITE; PS51050; ZF_CW; 1; level=0 XX Names: Zinc finger CW-type Function: Undefined XX XX case and and and XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51050 case and and and FT ZN_FING from..to FT /note="CW-type #" else case and and and FT ZN_FING from..to FT /note="CW-type #; atypical" else FT ZN_FING from..to FT /note="CW-type #; degenerate" end case FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 35 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 39-56; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TE76; Scope: Eukaryota; Mammalia Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00455; DC Domain; TR PROSITE; PS51081; ZF_SIAH; 1; level=0 XX Names: Zinc finger SIAH-type Function: substrate- and cofactor-interaction domain XX KW Zinc-finger case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case FT From: PS51081 case and and and and and and and FT ZN_FING from..to FT /note="SIAH-type #" else case and and and and and and and FT ZN_FING from..to FT /note="SIAH-type #; atypical" else FT ZN_FING from..to FT /note="SIAH-type #; degenerate" end case FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 50-70; Related: None; Repeats: 1; Topology: Undefined; Example: Q8R4T2; Scope: Eukaryota Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00456; DC Domain; TR PROSITE; PS51074; DPH_MB; 1; level=0 XX Names: DPH-type metal-binding (MB) domain CSL-type MB domain Function: The DHP-type or CSL-type MB domain contains a Cys-X-Cys...Cys-X2-Cys motif which tetrahedrically coordinates either Fe or Zn, but Zn is much more tightly bound. XX case CC -!- DOMAIN: The DPH-type metal-binding (MB) domain can bind either zinc or CC iron ions. XX KW Metal-binding KW Iron KW Zinc end case XX FT From: PS51074 FT DOMAIN from..to FT /note="DPH-type MB #" FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 50-75; Related: None; Repeats: 1; Topology: Undefined; Example: Q6VUC1; Scope: Eukaryota Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00457; DC Domain; TR PROSITE; PS50994; INTEGRASE; 1; level=0 XX Names: Integrase catalytic domain Function: The integrase catalytic domain catalyzes a series of reactions to integrate the viral genome into a host chromosome. XX case KW Hydrolase KW Nuclease KW Endonuclease KW DNA integration KW DNA recombination end case XX case GO GO:0004518; F:nuclease activity GO GO:0004519; F:endonuclease activity GO GO:0016787; F:hydrolase activity GO GO:0006310; F:DNA recombination GO GO:0006313; F:DNA transposition end case XX FT From: PS50994 FT DOMAIN from..to FT /note="Integrase catalytic #" FT BINDING 12 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Group: 1; Condition: D FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT Group: 1; Condition: D **FT ACT_SITE 107 107 Integrase. **FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 43-217; Related: None; Repeats: 1; Topology: Undefined; Example: O92956; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.12 2023/03/27 // AC PRU00458; DC Domain; TR PROSITE; PS51115; LAMININ_IVA; 1; level=0 XX Names: Laminin IV type A domain Function: Undefined XX FT From: PS51115 FT DOMAIN from..to FT /note="Laminin IV type A #" XX Chop: Nter=0; Cter=0; Size: 167-202; Related: None; Repeats: 1-3; Topology: Undefined; Example: P15215; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00459; DC Domain; TR PROSITE; PS51079; MBT; 1; level=0 XX Names: MBT domain Function: Undefined XX FT From: PS51079 FT REPEAT from..to FT /note="MBT #" XX Chop: Nter=0; Cter=0; Size: 94-105; Related: None; Repeats: 2-4; Topology: Undefined; Example: Q9UHJ3; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00460; DC Domain; TR PROSITE; PS50027; EGF_LAM_2; 1; level=0 XX Names: Laminin EGF-like domain Function: binding basement membranes proteins XX KW Laminin EGF-like domain case KW Disulfide bond end case FT From: PS50027 FT DOMAIN from..to FT /note="Laminin EGF-like #" FT DISULFID 1..13 FT Tag: disulf; Condition: C-x*-C FT DISULFID 3..20 FT Tag: disulf; Condition: C-x*-C FT DISULFID 22..31 FT Tag: disulf; Condition: C-x*-C FT DISULFID 34..48 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 3-91; Related: None; Repeats: 1-23; Topology: Undefined; Example: Q9R1A3; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00461; DC Domain; TR PROSITE; PS51120; LDLRB; 1; level=0 XX Names: LDL-receptor class B repeat Function: important for ligand release and recycling of the receptor XX FT From: PS51120 FT REPEAT from..to FT /note="LDL-receptor class B #" XX Chop: Nter=0; Cter=0; Size: 36-56; Related: None; Repeats: 4-37; Topology: Undefined; Example: P01133; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00462; DC Domain; TR PROSITE; PS51116; LAMININ_IVB; 1; level=0 XX Names: Laminin IV type B Function: Undefined XX FT From: PS51116 FT DOMAIN from..to FT /note="Laminin IV type B #" XX Chop: Nter=0; Cter=0; Size: 200-225; Related: None; Repeats: 1; Topology: Undefined; Example: Q61292; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00463; DC Domain; TR PROSITE; PS50998; GLA_2; 1; level=0 XX Names: Gla domain Function: a membrane binding motif which, in the presence of calcium ions, interacts with phospholipid membranes that include phosphatidylserine XX case or CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent CC carboxylation. These residues are essential for the binding of calcium. end case DR PROSITE; PS00011; GLA_1; 1; trigger=no XX case or GO GO:0005509; F:calcium ion binding end case XX case or KW Calcium KW Gamma-carboxyglutamic acid end case case KW Disulfide bond end case XX FT From: PS50998 FT DOMAIN from..to FT /note="Gla #" FT MOD_RES 21 FT /note="4-carboxyglutamate" FT Group: 1; Condition: E FT MOD_RES 24 FT /note="4-carboxyglutamate" FT Group: 2; Condition: E FT DISULFID 18..23 FT Tag: disulf; Condition: C-x*-C FT DISULFID 23..29 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 17-45; Related: None; Repeats: 1; Topology: Undefined; Example: P84349; Scope: Eukaryota; Gnathostomata Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00464; DC Domain; TR PROSITE; PS51084; HIT_2; 1; level=0 XX Names: HIT Function: The HIT domain is related to GalT nucleotide-binding proteins. XX FT From: PS51084 FT DOMAIN from..to FT /note="HIT #" FT MOTIF 93..97 FT /note="Histidine triad motif #" FT Condition: H-x-H-x-H XX Chop: Nter=0; Cter=0; Size: 26-132; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BGQ0; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00465; DC Domain; TR PROSITE; PS51085; 2FE2S_FER_2; 1; level=0 XX Names: 2Fe-2S ferredoxin-type domain Function: Undefined XX case CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Note=Binds #([2Fe-2S], cluster) end case XX DR PROSITE; PS00197; 2FE2S_FER_1; 0-1; trigger=no XX case GO GO:0051537; F:2 iron, 2 sulfur cluster binding GO GO:0005506; F:iron ion binding XX KW 2Fe-2S KW Iron KW Iron-sulfur KW Metal-binding end case XX FT From: PS51085 FT DOMAIN from..to FT /note="2Fe-2S ferredoxin-type #" FT BINDING 37 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 42 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 45 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 72 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT /ligand_label="#1" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 25-116; Related: None; Repeats: 1; Topology: Undefined; Example: P81372; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.14 2022/11/19 // AC PRU00466; DC Domain; TR PROSITE; PS51117; LAMININ_NTER; 1; level=0 XX Names: Laminin N-terminal domain Function: Undefined XX FT From: PS51117 FT DOMAIN from..to FT /note="Laminin N-terminal #" XX Chop: Nter=0; Cter=0; Size: 200-225; Related: None; Repeats: 1; Topology: Undefined; Example: Q61292; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00467; DC Domain; TR PROSITE; PS51112; AMMECR1; 1; level=0 XX Names: AMMECR1 domain Function: The high level of conservation of the AMMECR1 domain points to a basic cellular function, potentially in either the transcription, replication, repair or translation machinery. XX XX FT From: PS51112 FT DOMAIN from..to FT /note="AMMECR1 #" XX Chop: Nter=0; Cter=0; Size: 170-230; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y4X0; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00468; DC Domain; TR PROSITE; PS51140; CUE; 1; level=0 XX Names: CUE domain Function: The Coupling of Ubiquitin conjugation to ER degradation or CUE domain can bind monoubiquitin and can be required for ubiquitination of the protein in which it is found. XX XX KW Ubl conjugation pathway XX FT From: PS51140 FT DOMAIN from..to FT /note="CUE #" XX Chop: Nter=0; Cter=0; Size: 35-50; Related: None; Repeats: 1-2; Topology: Undefined; Example: P54787; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00469; DC Domain; TR PROSITE; PS51134; ZF_TFIIB; 1; level=0 XX Names: Zinc finger TFIIB-type Function: The zinc finger contacts the rbp1 subunit of Pol II through its dock domain XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS51134 case and and and FT ZN_FING from..to FT /note="TFIIB-type #" else case and and and FT ZN_FING from..to FT /note="TFIIB-type #; atypical" else FT ZN_FING from..to FT /note="TFIIB-type #; degenerate" end case FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 18-33; Related: None; Repeats: 1; Topology: Undefined; Example: Q00403; Scope: Eukaryota Archaea Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00470; DC Domain; TR PROSITE; PS51141; ZF_SBP; 1; level=0 XX Names: Zinc finger SBP-type Function: DNA-binding XX KW Zinc-finger case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case XX FT From: PS51141 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="SBP-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="SBP-type #; atypical" else FT ZN_FING from..to FT /note="SBP-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 76-77; Related: None; Repeats: 1; Topology: Undefined; Example: Q8LFW6; Scope: Eukaryota; Embryophyta Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00471; DC Domain; TR PROSITE; PS51131; ZN_HOOK; 1; level=0 XX Names: Zinc-hook domain Function: dimerization domain XX XX case GO GO:0046872; F:metal ion binding KW Zinc KW Metal-binding end case XX FT From: PS51131 FT DOMAIN from..to FT /note="Zinc-hook #" FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 95-107; Related: None; Repeats: 1; Topology: Undefined; Example: P12753; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00472; DC Domain; TR PROSITE; PS51133; ZF_TFIIS_2; 1; level=0 XX Names: Zinc finger TFIIS-type Function: involved in RNA cleavages when pol II is blocked by backtracking XX DR PROSITE; PS00466; ZF_TFIIS_1; 1; trigger=no XX case and and and GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51133 case and and and FT ZN_FING from..to FT /note="TFIIS-type #" else case and and and FT ZN_FING from..to FT /note="TFIIS-type #; atypical" else FT ZN_FING from..to FT /note="TFIIS-type #; degenerate" end case FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 39-42; Related: None; Repeats: 1; Topology: Undefined; Example: P07273; Scope: Eukaryota Viruses Archaea Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00473; DC Domain; TR PROSITE; PS51123; OMPA_2; 1; level=0 XX Names: OmpA-like domain Function: The OmpA-like domain is thought to be responsible for non-covalent interactions with peptidoglycan. XX XX DR PROSITE; PS01068; OMPA_1; 1; trigger=no XX GO GO:0016020; C:membrane XX KW Membrane XX FT From: PS51123 FT DOMAIN from..to FT /note="OmpA-like #" XX Chop: Nter=0; Cter=0; Size: 105-140; Related: None; Repeats: 1; Topology: Undefined; Example: P0A910; Scope: Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00474; DC Domain; TR PROSITE; PS51122; CALPONIN_2; 1; level=0 XX Names: Calponin-like repeat Function: The calponin-like repeat is a short actin-binding module. XX XX DR PROSITE; PS01052; CALPONIN_1; 1; trigger=no XX GO GO:0003779; F:actin binding XX KW Actin-binding XX FT From: PS51122 FT REPEAT from..to FT /note="Calponin-like #" XX Chop: Nter=0; Cter=0; Size: 25-29; Related: None; Repeats: 3-7; Topology: Cytoplasmic; Example: P51911; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00475; DC Domain; TR PROSITE; PS51136; WAC; 1; level=0 XX Names: WAC domain Function: The DNA-binding region of Acf1 includes the WAC domain, which is necessary for the efficient binding of ACF complex to DNA. It seems probable that the WAC domain will be involved in DNA binding in other related factors. XX CC -!- SUBCELLULAR LOCATION: Nucleus. GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS51136 FT DOMAIN from..to FT /note="WAC #" XX Chop: Nter=0; Cter=0; Size: 105-110; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P53125; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00476; DC Domain; TR PROSITE; PS51138; ENT; 1; level=0 XX Names: EMSY N-terminal (ENT) domain Function: The ENT domain is a ~90-residue module, which is unique in the human proteome, although multiple copies are found in Arabidopsis proteins. XX XX FT From: PS51138 FT DOMAIN from..to FT /note="ENT #" XX Chop: Nter=0; Cter=0; Size: 80-100; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q7Z589; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00477; DC Domain; TR PROSITE; PS50847; GRAM_POS_ANCHORING; 1; level=0 XX Names: LPXTG sorting signal motif Function: The LPXTG motif is part of the C-terminal sorting signal found in surface proteins from Gram-positive cocci. XX CC -!- SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. XX DR General; Transmembrane; -; 1; trigger=no XX GO GO:0005618; C:cell wall XX KW Cell wall KW Peptidoglycan-anchor KW Secreted XX FT From: PS50847 FT PROPEP 5..Cter FT /note="Removed by sortase" FT MOTIF from..5 FT /note="LPXTG sorting signal" FT MOD_RES 4 FT /note="Pentaglycyl murein peptidoglycan amidated threonine" FT Condition: T FT MOD_RES 4 FT /note="Pentaglycyl murein peptidoglycan amidated alanine" FT Condition: A XX Chop: Nter=0; Cter=0; Size: 30-40; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P13050; Scope: Bacteria Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00478; DC Domain; TR PROSITE; PS51091; FN1_2; 1; level=0 XX Names: FN1 domain Function: In human tissue plasminogen activator chain A, the FN1 domain together with the following EGF-like domain are involved in fibrin-binding XX XX case KW Disulfide bond end case XX FT From: PS51091 FT DOMAIN from..to FT /note="Fibronectin type-I #" FT DISULFID 3..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 30..42 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 30-60; Related: None; Repeats: 12; Topology: Not cytoplasmic; Example: P00748; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00479; DC Domain; TR PROSITE; PS51092; FN2_2; 1; level=0 XX Names: FN2 domain Function: The FN2 domain is important for collagen binding. XX XX case KW Disulfide bond end case XX FT From: PS51092 FT DOMAIN from..to FT /note="Fibronectin type-II #" FT DISULFID 6..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 20..47 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 30-60; Related: None; Repeats: 3; Topology: Not cytoplasmic; Example: P00748; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00480; DC Domain; TR PROSITE; PS51130; PDXT_SNO_2; 1; level=0 XX Names: PdxT/SNO family Function: PdxS/SNZ and pdxT/SNO proteins form a complex which serves as a glutamine amidotransferase to supply ammonia as a source of the ring nitrogen of vitamin B6. PdxT/SNO appear to encode the glutaminase subunit, which produces ammonia from glutamine. XX case DE AltName: Full=Probable glutamine amidotransferase; DE EC=2.6.-.-; end case XX CC -!- SIMILARITY: Belongs to the glutamine amidotransferase pdxT/SNO family. XX DR PROSITE; PS01236; PDXT_SNO_1; 1; trigger=no XX case GO GO:0006541; P:glutamine metabolic process GO GO:0016740; F:transferase activity end case case and GO GO:0008615; P:pyridoxine biosynthetic process end case XX case KW Glutamine amidotransferase KW Transferase end case case or KW Pyridoxal phosphate end case case KW Pyridoxine biosynthesis end case XX FT From: PS51130 FT ACT_SITE 79 FT /note="Nucleophile" FT Condition: C case FT ACT_SITE 176 FT Condition: H FT ACT_SITE 178 FT Condition: E end case FT BINDING 111 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT Condition: R XX Chop: Nter=0; Cter=0; Size: 170-215; Related: PRU00605; PRU00606; Repeats: 1; Topology: Undefined; Example: Q03144; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.11 2022/11/19 // AC PRU00481; DC Domain; TR PROSITE; PS51129; PDXS_SNZ_2; 1; level=0 XX Names: PdxS/SNZ family Function: PdxS/SNZ and pdxT/SNO proteins form a complex which serves as a glutamine amidotransferase to supply ammonia as a source of the ring nitrogen of vitamin B6. PdxS/SNZ appear to encode the synthase subunit which combines ammonia with five- and three-carbon phosphosugars to form vitamin B6. XX CC -!- SIMILARITY: Belongs to the PdxS/SNZ family. XX DR PROSITE; PS01235; PDXS_SNZ_1; 1; trigger=no XX Chop: Nter=0; Cter=0; Size: 275-325; Related: None; Repeats: 1; Topology: Undefined; Example: Q03148; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.2 2017/06/28 // AC PRU00482; DC Domain; TR PROSITE; PS51114; FBA; 1; level=0 XX Names: F-box-associated (FBA) domain Function: The FBA domain is likely to be a glycoprotein-binding module. XX XX FT From: PS51114 FT DOMAIN from..to FT /note="FBA #" XX Chop: Nter=0; Cter=0; Size: 150-185; Related: None; Repeats: 1; Topology: Undefined; Example: Q80UW2; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00483; DC Domain; TR PROSITE; PS51137; VM; 1; level=0 XX Names: VM domain Function: The VM domain is a 38-amino acid module found in Drosophila melanogaster vitelline membrane (VM) proteins. XX XX FT From: PS51137 FT DOMAIN from..to FT /note="VM #" XX Chop: Nter=0; Cter=0; Size: 35-40; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P11449; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00484; DC Domain; TR PROSITE; PS51139; GTF2I; 1; level=0 XX Names: GTF2I-like repeat Function: The GTF2I-like repeats are specific to the TFII-I family of transcription factors and are likely to be involved in DNA binding. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the TFII-I family. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51139 FT REPEAT from..to FT /note="GTF2I-like #" XX Chop: Nter=0; Cter=0; Size: 90-100; Related: None; Repeats: 1-6; Topology: Undefined; Example: Q9UHL9; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00485; DC Domain; TR PROSITE; PS51145; ZU5; 1; level=0 XX Names: ZU5 domain ZU-5 domain Function: The ZU5 domain is a versatile protein-protein interaction module with more than one interaction surface that acts indifferent modes to interact with a variety of partners. XX case KW Autocatalytic cleavage end case XX FT From: PS51145 FT DOMAIN from..to FT /note="ZU5 #" case FT ACT_SITE 130 FT ACT_SITE 132 FT SITE 131..132 FT /note="Cleavage; by autolysis" FT REGION 111..138 FT /note="Peptidase S68" end case XX Chop: Nter=0; Cter=0; Size: 85-130; Related: None; Repeats: 1; Topology: Undefined; Example: Q26261; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00487; DC Domain; TR PROSITE; PS51146; KAIC; 1; level=0 XX Names: KaiC domain Function: The kaiC domain is a ~240 residue domain of the cyanobacterial circadian (daily) clock protein kaiC and related prokaryotic proteins. XX XX case GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding KW ATP-binding KW Nucleotide-binding end case XX FT From: PS51146 FT DOMAIN from..to FT /note="KaiC #" XX FT From: PS00017 FT BINDING from..to FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="#" XX Chop: Nter=0; Cter=0; Size: 220-260; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q79PF4; Scope: Bacteria Archaea Comments: None XX # Revision 1.6 2022/11/19 // AC PRU00488; DC Domain; TR PROSITE; PS51147; PFTA; 1; level=0 XX Names: Protein prenyltransferases alpha subunit repeat Function: Protein prenyltransferases catalyze the transfer of an isoprenyl moiety to a cysteine at or near the C-terminus of several eukaryotic proteins. XX DE + RecName: EC=2.5.1.-; XX XX GO GO:0004659; F:prenyltransferase activity GO GO:0016740; F:transferase activity XX KW Prenyltransferase KW Transferase XX FT From: PS51147 FT REPEAT entry..exit FT /note="PFTA #" XX Chop: Nter=0; Cter=0; Size: 25-40; Related: None; Repeats: 2-6; Topology: Undefined; Example: O24304; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00489; DC Domain; TR PROSITE; PS51143; MT_A70; 1; level=0 XX Names: MT-A70-like family Function: The MT-A70-like family comprises four subfamilies with varying degrees of interrelatedness. One subfamily is a small group of bacterial DNA: m6A MTases. The other three are paralogous eukaryotic lineages, two of which have not been associated with MTase activity but include proteins that regulate mRNA levels via unknown mechanisms apparently not involving methylation. XX CC -!- SIMILARITY: Belongs to the MT-A70-like family. XX Chop: Nter=0; Cter=0; Size: 215-245; Related: None; Repeats: 1; Topology: Undefined; Example: Q86U44; P25583; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.1 2005/10/20 // AC PRU00490; DC Domain; TR PROSITE; PS51154; MACRO; 1; level=0 TR PROSITE; PS51940; SARS_NSP3C_N; 1; level=0 TR PROSITE; PS51941; BCOV_NSP3C_M; 1; level=0 XX Names: Macro domain A1pp domain ADRP domain X domain Nsp3c-N SUD-N Nsp3c-M SUD-M Function: The Macro domain is a module of ~180 amino acids which can bind ADP-ribose, an NAD metabolite or related ligands. XX XX FT From: any FT DOMAIN entry..exit FT /note="Macro #" XX Chop: Nter=13; Cter=0; Size: 140-210; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q8IXQ6; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.8 2020/09/24 // AC PRU00491; DC Domain; TR PROSITE; PS51159; CBM21; 1; level=0 XX Names: CBM21 (carbohydrate binding type-21) domain Carbohydrate-Binding Module (CBM) family 21 Starch-binding domain (SBD) Function: The CBM21 domain is a 90-130 amino acid carbohydrate binding domain, present in several eukaryotic proteins implicated in glycogen metabolism. XX FT From: PS51159 FT DOMAIN from..to FT /note="CBM21 #" XX Chop: Nter=0; Cter=0; Size: 85-140; Related: None; Repeats: 1-2; Topology: Undefined; Example: O95685; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00492; DC Domain; TR PROSITE; PS51161; ATP_CONE; 1; level=0 XX Names: ATP-cone domain Function: The ATP-cone domain is an ATP-binding module. XX XX GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Nucleotide-binding XX FT From: PS51161 FT DOMAIN from..to FT /note="ATP-cone #" XX Chop: Nter=0; Cter=0; Size: 75-105; Related: None; Repeats: 1-3; Topology: Cytoplasmic; Example: P23921; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00493; DC Domain; TR PROSITE; PS51149; GLY_RADICAL_2; 1; level=0 XX Names: Glycine radical domain Function: The glycine radical domain is a conserved region centered around the glycine which, in pfl, is known to bear the free radical. XX XX DR PROSITE; PS00850; GLY_RADICAL_1; 1; trigger=no XX case KW Organic radical end case XX FT From: PS51149 FT DOMAIN from..to FT /note="Glycine radical #" FT MOD_RES 97 FT /note="Glycine radical" FT Condition: G XX Chop: Nter=0; Cter=0; Size: 115-135; Related: None; Repeats: 1; Topology: Undefined; Example: P68066; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00494; DC Domain; TR PROSITE; PS51150; AGOUTI_2; 1; level=0 XX Names: Agouti domain Function: The agouti domain is a Cys-rich C-terminal module, which is responsible for melanocortin receptor binding activity in vitro. XX XX DR PROSITE; PS60024; AGOUTI_1; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51150 FT DOMAIN from..to FT /note="Agouti #" FT DISULFID 1..16 FT Tag: disulf; Condition: C-x*-C FT DISULFID 8..22 FT Tag: disulf; Condition: C-x*-C FT DISULFID 15..33 FT Tag: disulf; Condition: C-x*-C FT DISULFID 19..40 FT Tag: disulf; Condition: C-x*-C FT DISULFID 24..31 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 35-45; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: O00253; Scope: Eukaryota; Metazoa; Craniata Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00495; DC Domain; TR PROSITE; PS51153; RPW8; 1; level=0 XX Names: RPW8 domain Function: The RPW8 domain is an ~150 amino acid module forming the N-terminus of a group of plant disease resistance proteins, which have a nucleotide- binding site (NBS) and leucine-rich repeats (LRRs). XX XX GO GO:0009626; P:plant-type hypersensitive response GO GO:0006952; P:defense response XX KW Hypersensitive response KW Plant defense XX FT From: PS51153 FT DOMAIN from..to FT /note="RPW8 #" XX Chop: Nter=0; Cter=0; Size: 145-155; Related: None; Repeats: 1; Topology: Undefined; Example: Q9FW44; Scope: Eukaryota; Viridiplantae; Embryophyta Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00496; DC Domain; TR PROSITE; PS51148; AXH; 1; level=0 XX Names: AXH domain Function: The AXH (ataxin-1 and HMG-box protein 1) domain is a module of ~130 amino acids, which has been suggested to be a molecular scaffold domain engaged in multiple protein-protein interactions and in RNA binding. XX XX FT From: PS51148 FT DOMAIN from..to FT /note="AXH #" XX Chop: Nter=0; Cter=0; Size: 130-145; Related: None; Repeats: 1; Topology: Undefined; Example: P54253; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00497; DC Domain; TR PROSITE; PS51155; CHIT_BIND_RR_2; 1; level=0 XX Names: Chitin-binding type R&R domain Function: The chitin-binding type R&R domain is found in arthropod cuticular proteins. XX XX DR PROSITE; PS00233; CHIT_BIND_RR_1; 1; trigger=no XX GO GO:0042302; F:structural constituent of cuticle XX KW Cuticle XX FT From: PS51155 FT DOMAIN from..to FT /note="Chitin-binding type R&R #" XX Chop: Nter=0; Cter=0; Size: 60-80; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: P02839; Scope: Eukaryota; Metazoa; Arthropoda Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00498; DC Site; TR PROSITE; PS00001; ASN_GLYCOSYLATION; 1; level=0 XX Names: N-glycosylation site Function: Unknown XX KW Glycoprotein FT From: PS00001 FT CARBOHYD 1 FT /note="N-linked (GlcNAc...) asparagine" FT Condition: N XX Chop: Nter=0; Cter=0; Size: 1; Related: None; Repeats: unlimited; Topology: Not cytoplasmic; Example: P02724; Scope: Eukaryota Viruses Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00499; DC Domain; TR PROSITE; PS00017; ATP_GTP_A; 1; level=0 XX Names: ATP/GTP-binding site motif A (P-loop) Function: This loop interacts with one of the phosphate groups of the nucleotide. XX GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Nucleotide-binding XX FT From: PS00017 FT BINDING from..to FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 8; Related: None; Repeats: unlimited; Topology: Undefined; Example: P19483; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00500; DC Domain; TR PROSITE; PS51162; THYROGLOBULIN_1_2; 1; level=0 XX Names: thyroglobulin type-1 domain Tg type-I repeat Function: the Tg type-1 repeat is a module of about 70 amino acids present 11x in thyroglobulin (Tg) and as a single or repeated sequence in cysteine proteinase inhibitors and other proteins. XX XX case KW Disulfide bond end case XX FT From: PS51162 FT DOMAIN entry..exit FT /note="Thyroglobulin type-1 #" FT DISULFID 4..23 FT Tag: disulf; Condition: C-x*-C FT DISULFID 34..41 FT Tag: disulf; Condition: C-x*-C FT DISULFID 43..63 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 40-210; Related: None; Repeats: 1-11; Topology: Undefined; Example: P24592; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00501; DC Domain; TR PROSITE; PS51158; ALPHA_KINASE; 1; level=0 XX Names: Alpha-type protein kinase Function: phosphorylate amino acids located within alpha-helices XX FT From: PS51158 FT DOMAIN from..to FT /note="Alpha-type protein kinase #" XX Chop: Nter=0; Cter=0; Size: 191-277; Related: None; Repeats: 1; Topology: Undefined; Example: O01991; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00502; DC Domain; TR PROSITE; PS50271; ZF_UBP; 1; level=0 XX Names: UBP-type zinc finger Function: ubiquitin binding domain XX case ( and and and ) or ( and and and ) or ( and and and ) GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS50271 case ( and and and ) and ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="UBP-type #" else case ( and and and ) and ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="UBP-type #; atypical" else FT ZN_FING from..to FT /note="UBP-type #; degenerate" end case FT BINDING 3 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 76 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 59-76; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q5DU02; Scope: Eukaryota Comments: None XX # Revision 1.6 2022/11/19 // AC PRU00503; DC Domain; TR PROSITE; PS51126; DILUTE; 1; level=0 XX Names: dilute domain Function: anchors myosin V to cargoes via attachments to organelle-specific receptors XX FT From: PS51126 FT DOMAIN from..to FT /note="Dilute #" XX Chop: Nter=0; Cter=0; Size: 213-300; Related: None; Repeats: 1; Topology: Undefined; Example: Q69Z89; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00504; DC Domain; TR PROSITE; PS51125; NHL; 1; level=0 XX Names: NHL repeat Function: could be involved in protein-protein interaction XX FT From: PS51125 FT REPEAT from..to FT /note="NHL #" XX Chop: Nter=0; Cter=0; Size: 39-52; Related: None; Repeats: 4-6; Topology: Undefined; Example: Q8CH72; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00505; DC Domain; TR PROSITE; PS51088; TEA_2; 1; level=0 XX Names: TEA DNA-binding domain Function: DNA binding XX DR PROSITE; PS00554; TEA_1; 1; trigger=no FT From: PS51088 FT DNA_BIND from..to FT /note="TEA #" XX Chop: Nter=0; Cter=0; Size: 64-66; Related: None; Repeats: 1; Topology: Undefined; Example: P30052; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00506; DC Domain; TR PROSITE; PS51027; INTEGRASE_DBD; 1; level=0 XX Names: integrase-type DNA-binding domain Function: DNA-binding XX FT From: PS51027 FT DNA_BIND from..to FT /note="Integrase-type #" XX Chop: Nter=0; Cter=0; Size: 45-54; Related: None; Repeats: 1; Topology: Undefined; Example: Q04095; Scope: Eukaryota Viruses Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00507; DC Domain; TR PROSITE; PS51151; NAC_AB; 1; level=0 XX Names: NAC-A/B (NAC-alpha/beta) domain Function: Undefined XX FT From: PS51151 FT DOMAIN from..to FT /note="NAC-A/B #" XX Chop: Nter=0; Cter=0; Size: 30-68; Related: None; Repeats: 1; Topology: Undefined; Example: P70670; Scope: Eukaryota Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00508; DC Domain; TR PROSITE; PS51157; ZF_UBR; 1; level=0 XX Names: UBR-type zinc finger Function: it binds specifically to proteins bearing N-terminal residues that are destabilizing according to the N-end rule XX FT From: PS51157 FT ZN_FING from..to FT /note="UBR-type #" XX Chop: Nter=0; Cter=0; Size: 67-75; Related: None; Repeats: 1; Topology: Undefined; Example: O60014; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00509; DC Domain; TR PROSITE; PS51058; ZF_CXXC; 1; level=0 XX Names: CXXC-type zinc finger Function: it binds specifically to non-methylated CpG XX case ( and and and ) or ( and and and ) GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51058 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="CXXC-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="CXXC-type #; atypical" else FT ZN_FING from..to FT /note="CXXC-type #; degenerate" end case FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 11 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 42 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 6-48; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q6PCT2; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2022/11/19 // AC PRU00510; DC Domain; TR PROSITE; PS51128; ZF_DKSA_2; 1; level=0 XX Names: dksA C4-type zinc finger Function: it binds the RNA polymerase XX FT From: PS51128 FT ZN_FING 44..68 FT /note="dksA C4-type #" XX Chop: Nter=0; Cter=0; Size: 19-33; Related: None; Repeats: 1; Topology: Undefined; Example: P41059; Scope: Bacteria Viruses Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00511; DC Domain; TR PROSITE; PS51111; REJ; 1; level=0 XX Names: REJ domain Function: The REJ domain is an extracellular module of ~1000 amino acids, which might function in ion transport homeostasis. XX XX FT From: PS51111 FT DOMAIN from..to FT /note="REJ #" XX Chop: Nter=0; Cter=0; Size: 680-900; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q8TDX9; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00512; DC Domain; TR PROSITE; PS51156; ELM2; 1; level=0 XX Names: ELM2 domain Function: The ELM2 (EGL-27 and MTA1 homology) domain has been shown to function as a transcriptional repression domain through recruitment of HDAC activity. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Nucleus KW Repressor KW Transcription KW Transcription regulation XX FT From: PS51156 FT DOMAIN from..to FT /note="ELM2 #" XX Chop: Nter=0; Cter=0; Size: 85-115; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9P2K3; Scope: Eukaryota Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00513; DC Domain; TR PROSITE; PS51172; CBM3; 1-3; level=0 XX Names: CBM3 (carbohydrate binding type-3) domain Function: Involved in the binding to crystalline cellulose. XX XX DR PROSITE; PS51172; CBM3; 1-3; trigger=no XX FT From: PS51172 FT DOMAIN from..to FT /note="CBM3 #" XX Chop: Nter=0; Cter=0; Size: 150-160; Related: none; Repeats: 1-3; Topology: Undefined; Example: Q06851; P04955; P28622; Scope: Bacteria Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00514; DC Domain; TR PROSITE; PS51167; CHORISMATE_MUT_1; 1; level=0 XX Names: chorismate mutase aroH-type domain CM domain Function: Chorismate mutase is a regulatory enzyme required for biosynthesis of the aromatic amino acids phenylalanine and tyrosine. XX DE + RecName: EC=5.4.99.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; XX GO GO:0009073; P:aromatic amino acid family biosynthetic process GO GO:0008652; P:amino acid biosynthetic process GO GO:0016853; F:isomerase activity XX KW Aromatic amino acid biosynthesis KW Amino-acid biosynthesis KW Isomerase XX FT From: PS51167 FT DOMAIN from..to FT /note="Chorismate mutase aroH-type #" XX Chop: Nter=0; Cter=0; Size: 105-130; Related: None; Repeats: 1; Topology: Undefined; Example: P19080; Scope: Bacteria Comments: None XX # Revision 1.9 2022/09/30 // AC PRU00515; DC Domain; TR PROSITE; PS51168; CHORISMATE_MUT_2; 1; level=0 XX Names: chorismate mutase domain CM domain Function: Chorismate mutase is a regulatory enzyme required for biosynthesis of the aromatic amino acids phenylalanine and tyrosine. XX DE + RecName: EC=5.4.99.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; XX GO GO:0009073; P:aromatic amino acid family biosynthetic process GO GO:0008652; P:amino acid biosynthetic process GO GO:0016853; F:isomerase activity XX KW Aromatic amino acid biosynthesis KW Amino-acid biosynthesis KW Isomerase XX FT From: PS51168 FT DOMAIN from..to FT /note="Chorismate mutase #" XX Chop: Nter=0; Cter=0; Size: 70-110; Related: None; Repeats: 1; Topology: Undefined; Example: Q02287; Scope: Bacteria Archaea Eukaryota; Chromadorea Comments: None XX # Revision 1.11 2022/09/30 // AC PRU00516; DC Domain; TR PROSITE; PS51169; CHORISMATE_MUT_3; 1; level=0 XX Names: chorismate mutase domain CM domain Function: Chorismate mutase is a regulatory enzyme required for biosynthesis of the aromatic amino acids phenylalanine and tyrosine. XX DE + RecName: EC=5.4.99.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=chorismate = prephenate; Xref=Rhea:RHEA:13897, CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29934; EC=5.4.99.5; XX GO GO:0003824; F:catalytic activity GO GO:0009073; P:aromatic amino acid family biosynthetic process GO GO:0008652; P:amino acid biosynthetic process GO GO:0016853; F:isomerase activity XX KW Allosteric enzyme KW Aromatic amino acid biosynthesis KW Amino-acid biosynthesis KW Isomerase XX FT From: PS51169 FT DOMAIN from..to FT /note="Chorismate mutase #" XX Chop: Nter=0; Cter=0; Size: 240-270; Related: None; Repeats: 1; Topology: Undefined; Example: O13739; Scope: Eukaryota; Fungi Eukaryota; Viridiplantae Comments: None XX # Revision 1.10 2022/09/30 // AC PRU00517; DC Domain; TR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1; level=0 XX Names: prephenate dehydratase domain PDT domain Function: Prephenate dehydratase (EC 4.2.1.51) catalyzes the decarboxylation of prephenate into phenylpyruvate. XX DE + RecName: EC=4.2.1.51; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + prephenate = 3-phenylpyruvate + CO2 + H2O; CC Xref=Rhea:RHEA:21648, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18005, ChEBI:CHEBI:29934; EC=4.2.1.51; XX GO GO:0009094; P:L-phenylalanine biosynthetic process GO GO:0009073; P:aromatic amino acid family biosynthetic process GO GO:0008652; P:amino acid biosynthetic process GO GO:0016829; F:lyase activity XX KW Phenylalanine biosynthesis KW Aromatic amino acid biosynthesis KW Amino-acid biosynthesis KW Lyase XX FT From: PS51171 FT DOMAIN from..to FT /note="Prephenate dehydratase #" XX Chop: Nter=5; Cter=0; Size: 170-230; Related: None; Repeats: 1; Topology: Undefined; Example: P32452; Scope: Bacteria Archaea Eukaryota; Fungi Eukaryota; Viridiplantae Comments: None XX # Revision 1.9 2022/09/30 // AC PRU00518; DC Domain; TR PROSITE; PS51163; YRDC; 1; level=0 XX Names: YrdC-like domain Function: The yrdC-like domain is an ~185-residue module which can be found in stand-alone form, or in association with other domains such as the acylphosphatase-like domain, the sua5-like domain, the hypF-like domain or the hypF-type zinc finger. XX XX FT From: PS51163 FT DOMAIN from..to FT /note="YrdC-like #" XX Chop: Nter=0; Cter=0; Size: 160-205; Related: None; Repeats: 1; Topology: Undefined; Example: P30131; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00519; DC Domain; TR PROSITE; PS50040; EF1G_C; 1; level=0 XX Names: Elongation factor 1 (EF-1) gamma C-terminal domain Function: The eukaryotic elongation factor 1 (EF-1) gamma chain is a protein of about 410 to 440 residues, which consists of two independent domains, a glutathione S-transferase (GST) homologous N-terminal region responsible for the interaction with EF-1 alpha and a highly conserved exceptionally protease resistant ~160 residue C-terminal domain. XX XX GO GO:0006412; P:translation GO GO:0003746; F:translation elongation factor activity XX KW Elongation factor KW Protein biosynthesis XX FT From: PS50040 FT DOMAIN from..to FT /note="EF-1-gamma C-terminal #" XX Chop: Nter=0; Cter=0; Size: 155-165; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P26641; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00520; DC Domain; TR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1; level=0 XX Names: Acylphosphatase-like domain Function: Acylphosphatase (EC 3.6.1.7) [1,2] catalyzes the hydrolysis of various acyl phosphate carboxyl-phosphate bonds such as carbamyl phosphate, succinyl phosphate, 1,3-diphosphoglycerate, etc. XX case DE + RecName: EC=3.6.1.7; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate; CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7; end case XX DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1; trigger=no DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1; trigger=no case XX GO GO:0016787; F:hydrolase activity XX KW Hydrolase XX end case FT From: PS51160 FT DOMAIN from..to FT /note="Acylphosphatase-like #" FT ACT_SITE 16 FT Group: 1; Condition: R FT ACT_SITE 34 FT Group: 1; Condition: N XX Chop: Nter=0; Cter=0; Size: 65-100; Related: None; Repeats: 1; Topology: Undefined; Example: P0AB65; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.11 2019/11/21 // AC PRU00521; DC Domain; TR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1; level=0 XX Names: G-protein coupled receptors family 1 Function: transduces extracellular signals by interaction with guanine nucleotide-binding (G) proteins. XX CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. XX DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1; trigger=no XX GO GO:0004930; F:G protein-coupled receptor activity GO GO:0007186; F:G protein-coupled receptor signaling pathway GO GO:0007165; P:signal transduction XX KW G-protein coupled receptor KW Membrane KW Receptor KW Transducer case KW Disulfide bond end case XX FT From: PS50262 FT DISULFID 57..136 FT Tag: disulf; Condition: C-x*-C FT DISULFID 129..135 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 200-400; Related: None; Repeats: 1; Topology: Undefined; Example: Q9N298; Scope: Eukaryota Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00522; DC Domain; TR PROSITE; PS51176; PDH_ADH; 1; level=0 XX Names: Prephenate/arogenate dehydrogenase domain PDH domain Function: Prephenate dehydrogenase (EC 1.3.1.12) (PDH), arogenate dehydrogenase (EC 1.3.1.43) (ADH) and cyclohexadienyl dehydrogenase (which can accept both prephenate and arogenate as substrate) are dehydrogenases of different intermediates for the biosynthesis of tyrosine. XX DE + RecName: EC=1.3.1.-; XX XX GO GO:0009073; P:aromatic amino acid family biosynthetic process GO GO:0008652; P:amino acid biosynthetic process GO GO:0006571; P:tyrosine biosynthetic process GO GO:0016491; F:oxidoreductase activity XX KW Aromatic amino acid biosynthesis KW Amino-acid biosynthesis KW Tyrosine biosynthesis KW Oxidoreductase XX FT From: PS51176 FT DOMAIN from..to FT /note="Prephenate/arogenate dehydrogenase #" XX Chop: Nter=0; Cter=10; Size: 250-300; Related: None; Repeats: 1-2; Topology: Undefined; Example: P20692; Scope: Bacteria Archaea Eukaryota; Fungi Eukaryota; Viridiplantae Comments: None XX # Revision 1.7 2022/09/30 // AC PRU00523; DC Domain; TR PROSITE; PS51175; CBM6; 1-3; level=0 XX Names: CBM6 (carbohydrate binding type-6) domain Function: Involved in the binding to amorphous cellulose, xylan, mixed beta-(1,3)(1,4)glucan and beta-1,3-glucan, and is also present in a alpha-1,6-mannanase and several alpha-agarases. XX XX DR PROSITE; PS51175; CBM6; 1-3; trigger=no XX FT From: PS51175 FT DOMAIN from..to FT /note="CBM6 #" XX Chop: Nter=0; Cter=0; Size: 110-140; Related: none; Repeats: 1-3; Topology: Undefined; Example: P10478; P55296; P55297; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00524; DC Domain; TR PROSITE; PS51177; LUMAZINE_BIND; 1; level=0 XX Names: Riboflavin synthase alpha chain lumazine-binding repeat Lum-binding domain Function: Riboflavin synthase, catalyzing the biosynthesis of riboflavin (vitamin B2) by dismutation of 6,7-dimethyl-8-(1'-D-ribityl)lumazine (Lum) (EC 2.5.1.9), and antenna proteins involved in bioluminescence of marine bacteria seem to have evolved from the duplication of a domain of about 100 residues, the lumazine-binding repeat. XX XX FT From: PS51177 FT REPEAT entry..exit FT /note="Lumazine-binding #" XX Chop: Nter=0; Cter=0; Size: 80-110; Related: None; Repeats: 2; Topology: Undefined; Example: P0AFU8; Scope: Bacteria Eukaryota; Fungi Eukaryota; Viridiplantae Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00525; DC Domain; TR PROSITE; PS50258; LNR; 1-3; level=0 XX Names: Lin-12/Notch (LNR) repeat Function: The LNR is supposed to negatively regulates the Lin-12/Notch proteins activity, and participates in maintaining the receptor in its resting conformation prior to ligand binding. XX XX DR PROSITE; PS50258; LNR; 1-3; trigger=no XX GO GO:0005509; F:calcium ion binding GO GO:0007219; P:Notch signaling pathway XX case KW Calcium KW Metal-binding end case case KW Disulfide bond end case XX FT From: PS50258 FT REPEAT entry..exit FT /note="LNR #" FT DISULFID 1..25 FT Tag: disulf; Condition: C-x*-C FT DISULFID 7..20 FT Tag: disulf; Condition: C-x*-C FT DISULFID 16..32 FT Tag: disulf; Condition: C-x*-C FT BINDING 13 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 1; Condition: [DN] FT BINDING 28 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 1; Condition: D FT BINDING 31 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 1; Condition: [DE] XX Chop: Nter=0; Cter=0; Size: 35-45; Related: none; Repeats: 1-3; Topology: Undefined; Example: Q3T906; Scope: Eukaryota Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00526; DC Domain; TR PROSITE; PS51180; BRO1; 1; level=0 XX Names: BRO1 domain Function: The BRO1 domain of fungal and mammalian proteins is involved in protein targeting to the lysosome or vacuole by binding multivesicular body components (ESCRT-III proteins) like Snf7 and can thus function to target BRO1 domain-containing proteins to endosomes. XX XX FT From: PS51180 FT DOMAIN entry..exit FT /note="BRO1 #" XX Chop: Nter=0; Cter=0; Size: 280-465; Related: None; Repeats: 1; Topology: Undefined; Example: Q6PB44; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00527; DC Domain; TR PROSITE; PS51174; BARWIN_3; 1; level=0 XX Names: Barwin domain Function: A domain found in plant proteins that could be involved in a defense mechanism. XX XX DR PROSITE; PS00771; BARWIN_1; 1; trigger=no DR PROSITE; PS00772; BARWIN_2; 1; trigger=no FT From: PS51174 FT DOMAIN from..to FT /note="Barwin #" XX Chop: Nter=0; Cter=0; Size: 115-130; Related: None; Repeats: 1; Topology: Undefined; Example: P28814; Scope: Eukaryota; Viridiplantae; Embryophyta Viruses Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00528; DC Domain; TR PROSITE; PS51178; PASTA; 1; level=0 XX Names: PASTA domain Function: The PASTA domain (for penicillin-binding protein and serine/threonine kinase associated domain) is an extracellular module of ~70 residues that is found in the C-termini of eukaryotic-like serine/threonine kinases (PSTKs) and high molecular weight penicilin-binding proteins (PBPs). XX XX FT From: PS51178 FT DOMAIN from..to FT /note="PASTA #" XX Chop: Nter=0; Cter=0; Size: 55-75; Related: None; Repeats: 1-5; Topology: Not cytoplasmic; Example: Q9S2C0; Scope: Bacteria Archaea Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00529; DC Domain; TR PROSITE; PS51165; THUMP; 1; level=0 XX Names: THUMP domain Function: The THUMP (after thiouridine synthases, RNA methylases and pseudouridine synthases) domain is a module of 100-110 amino acid residues which is involved RNA metabolism. THUMP is an ancient domain with predicted RNA-binding capacity that probably functions by delivering a variety of RNA modification enzymes to their targets. XX XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS51165 FT DOMAIN from..to FT /note="THUMP #" XX Chop: Nter=0; Cter=0; Size: 90-120; Related: None; Repeats: 1; Topology: Undefined; Example: P53072; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00530; DC Domain; TR PROSITE; PS51179; POU_3; 1; level=0 XX Names: POU-specific (POUs) domain Function: The POUs domain is always found in association with a POU- homeodomain, and both are required for high affinity and sequence-specific DNA binding. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS00035; POU_1; 1; trigger=no DR PROSITE; PS00465; POU_2; 1; trigger=no case XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX end case FT From: PS51179 FT DOMAIN from..to FT /note="POU-specific #" XX Chop: Nter=0; Cter=0; Size: 70-115; Related: None; Repeats: 1; Topology: Undefined; Example: P24350; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.11 2022/06/27 // AC PRU00531; DC Domain; TR PROSITE; PS51185; WHEP_TRS_2; 1-6; level=0 XX Names: WHEP-TRS domain Function: This domain may play a role in the association of tRNA-synthetases into multienzyme complexes. XX XX DR PROSITE; PS51185; WHEP_TRS_2; 1-6; trigger=no XX FT From: PS51185 FT DOMAIN from..to FT /note="WHEP-TRS #" XX Chop: Nter=0; Cter=0; Size: 40-60; Related: none; Repeats: 1-6; Topology: Undefined; Example: P07814; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00532; DC Domain; TR PROSITE; PS51186; GNAT; 0-1; level=0 TR PROSITE; PS51729; GNAT_YJDJ; 0-1; level=0 TR PROSITE; PS51730; GNAT_ATAT; 0-1; level=0 TR PROSITE; PS51731; GNAT_NAGS; 0-1; level=0 XX Names: Gcn5-related N-acetyltransferase (GNAT) domain Function: The GNAT domain catalyzes the transfer of an acetyl group from the CoA donor to a primary amine of the acceptor, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodeling. XX DE + RecName: EC=2.3.1.-; XX XX GO GO:0016407; F:acetyltransferase activity GO GO:0016740; F:transferase activity XX KW Acyltransferase KW Transferase XX FT From: any FT DOMAIN entry..exit FT /note="N-acetyltransferase #" XX Chop: Nter=0; Cter=0; Size: 80-210; Related: PRU00533; PRU00536; Repeats: 1-3; Topology: Undefined; Example: Q92831; Scope: Bacteria Eukaryota Archaea Viruses Comments: None XX # Revision 1.12 2019/11/21 // AC PRU00533; DC Domain; TR PROSITE; PS51187; AUTOINDUCER_SYNTH_2; 1; level=0 XX Names: Autoinducer synthase family Function: Autoinducers are hormone-like molecules produced by bacterial synthases as signals to sense cell density and activate adaptations, by a process termed quorum sensing. XX CC -!- SIMILARITY: Belongs to the autoinducer synthase family. XX GO GO:0009372; P:quorum sensing XX KW Autoinducer synthesis KW Quorum sensing XX Chop: Nter=0; Cter=0; Size: 170-200; Related: PRU00532; Repeats: 1; Topology: Undefined; Example: P33883; Scope: Bacteria; Pseudomonadota Comments: None XX # Revision 1.3 2023/01/26 // AC PRU00534; DC Domain; TR PROSITE; PS51189; FAT; 1; level=0 XX Names: FAT domain Function: The PI-kinase domain of members of the PIK-related family is wedged between the ~550-amino acid-long FAT (FRAP, ATM, TRRAP) domain and the ~35 residue C-terminal FATC domain. XX XX DR PROSITE; PS51190; FATC; 1; trigger=no XX FT From: PS51189 FT DOMAIN from..to FT /note="FAT #" XX Chop: Nter=0; Cter=0; Size: 540-720; Related: None; Repeats: 1; Topology: Undefined; Example: P38110; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00535; DC Domain; TR PROSITE; PS51190; FATC; 1; level=0 XX Names: FATC domain Function: The PI-kinase domain of members of the PIK-related family is wedged between the ~550-amino acid-long FAT (FRAP, ATM, TRRAP) domain and the ~35 residue C-terminal FATC domain. XX XX DR PROSITE; PS51189; FAT; 1; trigger=no XX FT From: PS51190 FT DOMAIN from..to FT /note="FATC #" XX Chop: Nter=0; Cter=0; Size: 30-35; Related: None; Repeats: 1; Topology: Undefined; Example: P38110; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00537; DC Domain; TR PROSITE; PS51183; JMJN; 1; level=0 XX Names: JmjN domain Function: The JmjN domain is found in the jumonji family of transcription factors and always co-occurs with the JmjC domain. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51183 FT DOMAIN from..to FT /note="JmjN #" XX Chop: Nter=0; Cter=0; Size: 40-45; Related: None; Repeats: 1; Topology: Undefined; Example: P29375; Scope: Eukaryota Comments: None XX # Revision 1.7 2022/06/27 // AC PRU00538; DC Domain; TR PROSITE; PS51184; JMJC; 1; level=0 XX Names: JmjC domain Function: the JmjC domain is found in organisms from bacteria to human and has been shown to function in a histone demethylation mechanism that is conserved from yeast to human. XX case GO GO:0046872; F:metal ion binding KW Iron KW Metal-binding end case XX FT From: PS51184 FT DOMAIN from..to FT /note="JmjC #" FT BINDING 47 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 49 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: [DE] FT BINDING 129 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: [HY] XX Chop: Nter=0; Cter=0; Size: 120-230; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y4C1; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.7 2022/11/19 // AC PRU00539; DC Domain; TR PROSITE; PS50507; RDRP_SSRNA_POS; 0-1; level=0 TR PROSITE; PS50522; RDRP_PHAGE; 0-1; level=0 TR PROSITE; PS50523; RDRP_DSRNA_REO; 0-1; level=0 TR PROSITE; PS50524; RDRP_DSRNA_BIR; 0-1; level=0 TR PROSITE; PS50525; RDRP_SSRNA_NEG_SEG; 0-1; level=0 TR PROSITE; PS50526; RDRP_SSRNA_NEG_NONSEG; 0-1; level=0 XX Names: RdRp Function: RNA-directed RNA polymerase. XX DE + AltName: Full=RNA-directed RNA polymerase; DE EC=2.7.7.48; XX CC -!- FUNCTION: RNA-directed RNA polymerase. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; XX GO GO:0000166; F:nucleotide binding GO GO:0016779; F:nucleotidyltransferase activity GO GO:0003968; F:RNA-dependent RNA polymerase activity GO GO:0003723; F:RNA binding GO GO:0016740; F:transferase activity XX KW Nucleotide-binding KW Nucleotidyltransferase KW Viral RNA replication KW RNA-directed RNA polymerase KW Transferase XX FT From: any FT DOMAIN from..to FT /note="RdRp catalytic #" XX Chop: Nter=0; Cter=0; Size: 90-230; Related: None; Repeats: 1; Topology: Undefined; Example: P24658; Scope: Viruses Comments: None XX # Revision 1.11 2022/09/30 // AC PRU00540; DC Domain; TR PROSITE; PS51197; HTH_RRF2_2; 1; level=0 XX Names: Rrf2-type HTH domain Function: The rrf2-type HTH domain is a putative DNA-binding, winged helix-turn-helix (wHTH) domain of about 130 residues present in transcription regulators of the rrf2 family, involved in nitrite or iron metabolism. The C-terminal part of the domain contains 3 conserved cysteine residues that may bind an Fe-S cluster. XX XX DR PROSITE; PS01332; HTH_RRF2_1; 1; trigger=no XX GO GO:0003677; F:DNA binding case GO GO:0046872; F:metal ion binding end case GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding case KW Metal-binding end case KW Transcription KW Transcription regulation XX FT From: PS51197 FT DOMAIN from..to FT /note="HTH rrf2-type #" FT DNA_BIND 26..49 FT /note="H-T-H motif" FT BINDING 90 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: C FT BINDING 96 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: C FT BINDING 102 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 120-150; Related: PRU00393; PRU00307; Repeats: 1; Topology: Undefined; Example: P0AGK8; Scope: Bacteria Comments: None XX # Revision 1.15 2022/11/19 // AC PRU00541; DC Domain; TR PROSITE; PS51192; HELICASE_ATP_BIND_1; 0-1; level=0 TR PROSITE; PS51193; HELICASE_ATP_BIND_2; 0-1; level=0 XX Names: Helicase ATP-binding domain Function: Helicase ATP-binding domain in association with helicase C-terminal domain catalyze the separation of double-stranded nucleic acids XX XX DR PROSITE; PS00039; DEAD_ATP_HELICASE; 0-1; trigger=no DR PROSITE; PS00690; DEAH_ATP_HELICASE; 0-1; trigger=no XX GO GO:0004386; F:helicase activity GO GO:0005524; F:ATP binding GO GO:0016787; F:hydrolase activity GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Helicase KW Hydrolase KW Nucleotide-binding XX FT From: any FT DOMAIN from..to FT /note="Helicase ATP-binding #" case =1> FT BINDING 14..21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" end case case =1> FT BINDING 36..43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" end case case FT MOTIF 118..121 FT /note="DEAD box" end case case FT MOTIF 118..121 FT /note="DEAH box" end case case FT MOTIF 231..234 FT /note="DEAD box" end case case FT MOTIF 231..234 FT /note="DEAH box" end case XX Chop: Nter=0; Cter=0; Size: 120-350; Related: None; Repeats: 2; Topology: Undefined; Example: Q14240; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00542; DC Domain; TR PROSITE; PS51194; HELICASE_CTER; 1; level=0 XX Names: Helicase C-terminal domain Function: Helicase C-terminal domain in association with helicase ATP-binding domain catalyze the separation of double-stranded nucleic acids XX XX FT From: PS51194 FT DOMAIN from..to FT /note="Helicase C-terminal #" XX Chop: Nter=0; Cter=0; Size: 95-208; Related: None; Repeats: 2; Topology: Undefined; Example: Q14240; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00543; DC Domain; TR PROSITE; PS51201; RCK_N; 1-2; level=0 XX Names: RCK N-terminal domain Function: Largely involved in redox-linked regulation of potassium channels, the N-terminal part of the regulators of K+ conductance (RCK) domain is predicted to be an active dehydrogenase at least in some cases. Certain bind nicotinamide adenine dinucleotide (NAD) through a glycine motif, but for many RCK domains the ligand is unknown. XX XX DR PROSITE; PS51201; RCK_N; 1-2; trigger=no XX FT From: PS51201 FT DOMAIN from..to FT /note="RCK N-terminal #" XX Chop: Nter=0; Cter=0; Size: 100-150; Related: none; Repeats: 1-2; Topology: Undefined; Example: P0AGI8; Scope: Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00544; DC Domain; TR PROSITE; PS51202; RCK_C; 1-4; level=0 XX Names: RCK C-terminal domain Function: The C-terminal part of the regulators of K+ conductance (RCK) domain is less conserved among RCK domains, being absent in some. It is predicted to bind unidentified ligands and to regulate sulfate, sodium and other transporters. It forms an extention of the dimer interface and further stabilizes the RCK homodimer. XX XX DR PROSITE; PS51202; RCK_C; 1-4; trigger=no XX GO GO:0043266; P:regulation of potassium ion transport GO GO:0015459; F:potassium channel regulator activity XX FT From: PS51202 FT DOMAIN from..to FT /note="RCK C-terminal #" XX Chop: Nter=0; Cter=0; Size: 75-100; Related: none; Repeats: 1-4; Topology: Undefined; Example: P0AGI8; Scope: Bacteria Archaea Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00545; DC Domain; TR PROSITE; PS51200; SHORT_SCORPION_CHLORIDE; 1; level=0 XX Names: Scorpion short toxin chloride channel inhibitor subfamily Function: Short scorpion toxin chloride channel inhibitors are short-chain neurotoxins (SCNs), which block small-conductance chloride channels. They are 30-40-residue long and contain four intramolecular disulfide bridges, which have been assigned as C1-C4, C2-C6, C3-C7 and C5-C8. XX CC -!- FUNCTION: Probable chloride channel ligand, which blocks small- CC conductance chloride channels. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Chloride CC channel inhibitor family. XX GO GO:0019869; F:chloride channel inhibitor activity GO GO:0008200; F:ion channel inhibitor activity XX KW Secreted KW Voltage-gated chloride channel impairing toxin KW Chloride channel impairing toxin KW Ion channel impairing toxin KW Neurotoxin KW Toxin case KW Disulfide bond end case XX FT From: PS51200 FT DISULFID 1..18 FT Tag: disulf; Condition: C-x*-C FT DISULFID 4..25 FT Tag: disulf; Condition: C-x*-C FT DISULFID 15..30 FT Tag: disulf; Condition: C-x*-C FT DISULFID 19..32 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 20-35; Related: None; Repeats: 1; Topology: Undefined; Example: P15229; Scope: Eukaryota; Metazoa; Arachnida; Scorpiones Comments: None XX # Revision 1.10 2021/06/03 // AC PRU00546; DC Domain; TR PROSITE; PS51188; ZF_CR; 1; level=0 XX Names: CR-type zinc finger Function: important for the autonomous, dnaK-independent chaperone activity, but also necessary for the interaction site dnaK XX XX KW Metal-binding KW Zinc KW Zinc-finger XX FT From: PS51188 FT ZN_FING from..to FT /note="CR-type #" XX Chop: Nter=0; Cter=0; Size: 73-93; Related: None; Repeats: 1; Topology: Undefined; Example: Q5XAD7; Scope: Eukaryota Bacteria Viruses Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00547; DC Domain; TR PROSITE; PS51203; CS; 1; level=0 XX Names: CS domain Function: The bipartite CS domain, which was named after CHORD-containing proteins and SGT1, is a ~100-residue protein-protein interaction module. XX XX FT From: PS51203 FT DOMAIN from..to FT /note="CS #" XX Chop: Nter=0; Cter=0; Size: 80-105; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q08446; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00548; DC Domain; TR PROSITE; PS50188; B302_SPRY; 1; level=0 XX Names: B30.2/SPRY domain Function: The B30.2/SPRY domain in these proteins is likely to function through protein-protein interaction. XX XX FT From: PS50188 FT DOMAIN from..to FT /note="B30.2/SPRY #" XX Chop: Nter=0; Cter=0; Size: 105-255; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q13410; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00549; DC Domain; TR PROSITE; PS51204; HSA; 1; level=0 XX Names: HSA domain Function: The helicase/SANT-associated (HSA) domain is a predicted DNA-binding domain of ~75 amino acids, which is found in the eukaryotic SRCAP/p400/DOM and SNF2/brahma families. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus XX FT From: PS51204 FT DOMAIN from..to FT /note="HSA #" XX Chop: Nter=0; Cter=0; Size: 70-85; Related: None; Repeats: 1; Topology: Undefined; Example: Q8CHI8; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00550; DC Domain; TR PROSITE; PS51205; VPS9; 1; level=0 XX Names: VPS9 domain Function: The VPS9 domain is a GDP-GTP exchange factor (GEF) domain that catalyzes nucleotide exchange on Rab5, which activates this Rab GTPase. XX XX GO GO:0005096; F:GTPase activator activity KW GTPase activation XX FT From: PS51205 FT DOMAIN from..to FT /note="VPS9 #" XX Chop: Nter=0; Cter=0; Size: 130-170; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TB24; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00551; DC Domain; TR PROSITE; PS51206; SF3_HELICASE_1; 0-1; level=0 TR PROSITE; PS51218; SF3_HELICASE_2; 0-1; level=0 XX Names: Superfamily 3 helicase domain SF3 helicase domain Function: Helicases encoded mainly by small RNA and DNA viruses and some large nucleocytoplasmic DNA viruses. XX XX DR PROSITE; PS00017; ATP_GTP_A; 1; trigger=yes XX GO GO:0004386; F:helicase activity XX KW Helicase XX FT From: any FT DOMAIN from..to FT /note="SF3 helicase #" XX Chop: Nter=0; Cter=0; Size: 128-198; Related: None; Repeats: 1; Topology: Undefined; Example: P50762; Scope: Viruses Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00552; DC Domain; TR PROSITE; PS51195; Q_MOTIF; 1; level=0 XX Names: Q motif Function: The Q motif is characteristic of and unique to DEAD box family of helicases. It is supposed to control ATP binding and hydrolysis. XX XX FT From: PS51195 FT MOTIF from..to FT /note="Q motif" XX Chop: Nter=0; Cter=0; Size: 20-35; Related: None; Repeats: 1; Topology: Undefined; Example: Q14240; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.2 2019/11/21 // AC PRU00553; DC Domain; TR PROSITE; PS51207; PXA; 1; level=0 XX Names: PXA domain Function: The PX-associated (PXA) domain is a ~200-amino acid module of unknown function. Perhaps it is required for protein-protein interaction and/ or filament formation. XX XX FT From: PS51207 FT DOMAIN from..to FT /note="PXA #" XX Chop: Nter=0; Cter=0; Size: 170-190; Related: None; Repeats: 1; Topology: Undefined; Example: Q01846; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00555; DC Domain; TR PROSITE; PS51210; PLA2C; 1; level=0 XX Names: PLA2c domain Function: The PLA2c domain is the catalytic lipase domain in cytosolic phospholipase A2 (cPLA2) (EC 3.1.1.4) and lysophospholipase or phospholipase B (PLB) (EC 3.1.1.5) of vertebrates and fungi. XX DE + RecName: EC=3.1.1.-; XX XX GO GO:0016787; F:hydrolase activity GO GO:0016042; P:lipid catabolic process XX KW Hydrolase KW Lipid degradation KW Lipid metabolism XX FT From: PS51210 FT DOMAIN from..to FT /note="PLA2c #" XX Chop: Nter=0; Cter=0; Size: 520-610; Related: None; Repeats: 1; Topology: Undefined; Example: Q9P8P2; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00556; DC Domain; TR PROSITE; PS51208; AUTOTRANSPORTER; 1; level=0 XX Names: Autotransporter Function: Undefined XX XX KW Cell membrane KW Cell outer membrane XX FT From: any FT DOMAIN from..to FT /note="Autotransporter #" XX Chop: Nter=0; Cter=0; Size: 230-318; Related: None; Repeats: 1; Topology: Undefined; Example: Q9PL46; Scope: Bacteria Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00557; DC Domain; TR PROSITE; PS51211; VITELLOGENIN; 1; level=0 XX Names: Vitellogenin domain Function: The vitellogenin (VTG) protein, a major lipoprotein in many oviparous animals, is a precursor of a lipid-binding product found in the yolk of egg-laying animals, and involved in lipid and metal storage. At the N-terminal, it contains a sequence of about 670 amino acids (LV1n chain), which is also conserved in other large lipoproteins, such as microsomal triglyceride transfer protein (MTP) and apolipoprotein B-100 (apoB) XX XX DR PROSITE; PS51211; VITELLOGENIN; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51211 FT DOMAIN from..to FT /note="Vitellogenin #" FT DISULFID 139..165 FT Tag: disulf; Condition: C-x*-C FT DISULFID 181..184 FT Tag: disulf; Condition: C-x*-C FT DISULFID 409..414 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 600-660; Related: none; Repeats: 1; Topology: Undefined; Example: Q91062; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00558; DC Domain; TR PROSITE; PS51212; WSC; 1; level=0 XX Names: WSC domain Function: The WSC domain is a putative carbohydrate binding domain of about 90 amino acids. XX XX FT From: PS51212 FT DOMAIN entry..exit FT /note="WSC #" XX Chop: Nter=5; Cter=5; Size: 80-110; Related: None; Repeats: 1-5; Topology: Undefined; Example: Q7KVA1; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00559; DC Domain; TR PROSITE; PS51213; ELK; 1; level=0 XX Names: ELK domain Function: The ELK domain could function as a nuclear localization signal. It also is considered to act as a protein-protein interaction domain, but the precise role of this domain has not been determined. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the TALE/KNOX homeobox family. XX GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS51213 FT DOMAIN from..to FT /note="ELK #" XX Chop: Nter=0; Cter=0; Size: 20-25; Related: None; Repeats: 1; Topology: Undefined; Example: P24345; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00560; DC Domain; TR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 0-1; level=0 XX Names: UvrD helicase ATP-binding domain Function: UvrD helicase unwind DNA with a 3'-5' polarity XX XX GO GO:0004386; F:helicase activity GO GO:0005524; F:ATP binding GO GO:0016787; F:hydrolase activity GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Helicase KW Hydrolase KW Nucleotide-binding XX FT From: PS51198 FT DOMAIN from..to FT /note="UvrD-like helicase ATP-binding #" FT BINDING 22..29 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 200-600; Related: None; Repeats: 2; Topology: Undefined; Example: P64319; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00561; DC Domain; TR PROSITE; PS51214; IBB; 1; level=0 XX Names: IBB domain Function: The IBB domain is a highly basic amino-terminal region of roughly 40 amino-acid residues, which is responsible for importin-beta binding. XX XX GO GO:0006810; P:transport XX KW Transport XX FT From: PS51214 FT DOMAIN from..to FT /note="IBB #" XX Chop: Nter=0; Cter=0; Size: 50-70; Related: None; Repeats: 1-2; Topology: Undefined; Example: P52294; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00562; DC Domain; TR PROSITE; PS51215; AWS; 1; level=0 XX Names: AWS domain Function: In a subset of SET and post-SET containing proteins, a so-called associated with SET (AWS) domain is found instead of the pre-SET domain. XX XX FT From: PS51215 FT DOMAIN from..to FT /note="AWS #" XX Chop: Nter=0; Cter=0; Size: 40-60; Related: None; Repeats: 1; Topology: Undefined; Example: P46995; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00563; DC Domain; TR PROSITE; PS51216; NEBULIN; 1; level=0 XX Names: Nebulin repeat Nebulin-like motif Function: The nebulin repeat is a tandemly repeated actin-binding module of about 35 amino acids. XX XX GO GO:0003779; F:actin binding KW Actin-binding XX FT From: PS51216 FT REPEAT entry..exit FT /note="Nebulin #" XX Chop: Nter=3; Cter=3; Size: 10-45; Related: None; Repeats: 2-187; Topology: Undefined; Example: O76041; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00564; DC Domain; TR PROSITE; PS51219; DPCK; 1; level=0 XX Names: Dephospho-CoA kinase (DPCK) domain Function: Dephospho-coenzyme A kinase (DPCK) (EC 2.7.1.24) catalyzes the final step in coenzyme A (CoA) biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a phosphate donor. XX DE AltName: Full=Dephospho-CoA kinase; DE EC=2.7.1.24; DE AltName: Full=Dephosphocoenzyme A kinase; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-dephospho-CoA + ATP = ADP + CoA + H(+); CC Xref=Rhea:RHEA:18245, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57328, ChEBI:CHEBI:456216; CC EC=2.7.1.24; XX DR PROSITE; PS00017; ATP_GTP_A; 1; trigger=yes XX GO GO:0015937; P:coenzyme A biosynthetic process GO GO:0016301; F:kinase activity GO GO:0016740; F:transferase activity XX KW Coenzyme A biosynthesis KW Kinase KW Transferase XX FT From: PS51219 FT DOMAIN from..to FT /note="DPCK #" XX Chop: Nter=0; Cter=0; Size: 175-235; Related: None; Repeats: 1; Topology: Undefined; Example: P0A6I9; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00565; DC Domain; TR PROSITE; PS50032; KA1; 1; level=0 XX Names: KA1 (kinase-associated) domain Function: Undefined XX FT From: PS50032 FT DOMAIN from..to FT /note="KA1 #" XX Chop: Nter=0; Cter=0; Size: 47-48; Related: None; Repeats: 1; Topology: Undefined; Example: Q38997; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00567; DC Domain; TR PROSITE; PS51223; MAP; 1; level=0 XX Names: MAP repeat Function: Undefined XX FT From: PS51223 FT REPEAT from..to FT /note="MAP #" XX Chop: Nter=0; Cter=0; Size: 29-108; Related: None; Repeats: 3-6; Topology: Undefined; Example: Q53599; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00568; DC Domain; TR PROSITE; PS51221; TTL; 1; level=0 XX Names: TTL domain Function: The TTL (tubulin tyrosine ligase) domain is a ~350 amino acid module present in a family of eukaryotic proteins that could catalyze ligations of diverse amino acids to tubulins or other substrates. XX DE + RecName: EC=6.-.-.-; XX XX GO GO:0016874; F:ligase activity XX KW Ligase XX FT From: PS51221 FT DOMAIN from..to FT /note="TTL #" XX Chop: Nter=0; Cter=0; Size: 330-400; Related: None; Repeats: 1; Topology: Undefined; Example: Q8NG68; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00569; DC Domain; TR PROSITE; PS51222; DCD; 1; level=0 XX Names: DCD domain Function: The DCD domain is found in plant proteins involved in development and cell death. XX XX FT From: PS51222 FT DOMAIN from..to FT /note="DCD #" XX Chop: Nter=0; Cter=0; Size: 130-135; Related: None; Repeats: 1-2; Topology: Undefined; Example: P37707; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00570; DC Domain; TR PROSITE; PS51220; NIDO; 1; level=0 XX Names: NIDO domain Function: The ~180-residue NIDO domain is an extracellular domain of unknown function, found in nidogen (entactin) and hypothetical proteins. XX XX FT From: PS51220 FT DOMAIN from..to FT /note="NIDO #" XX Chop: Nter=0; Cter=0; Size: 135-170; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: P14543; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00571; DC Domain; TR PROSITE; PS51224; MVP; 1; level=0 XX Names: MVP repeat MVP domain vault repeat Function: The MVP repeat is a ~53 amino acid module of major vault protein (MVP) which forms a structural part of the wall of vaults, which are large ribonucleoprotein particles that are found in all higher eukaryotes. XX CC -!- SUBCELLULAR LOCATION: Cytoplasm. XX GO GO:1990904; C:ribonucleoprotein complex GO GO:0005737; C:cytoplasm XX KW Cytoplasm KW Ribonucleoprotein XX FT From: PS51224 FT REPEAT from..to FT /note="MVP #" XX Chop: Nter=0; Cter=0; Size: 35-80; Related: None; Repeats: 6-9; Topology: Undefined; Example: Q14764; Scope: Eukaryota Comments: None XX # Revision 1.10 2019/11/21 // AC PRU00572; DC Domain; TR PROSITE; PS51227; SPR; 1; level=0 XX Names: Sprouty (SPR) domain profile Function: The SPR domain is conserved, C-terminal cystein-rich region, related to Sprouty and Spred proteins family. This domain has been defined as a novel translocation domain (SpryTD). XX XX DR PROSITE; PS51227; SPR; 1; trigger=no XX FT From: PS51227 FT DOMAIN from..to FT /note="SPR #" XX Chop: Nter=0; Cter=0; Size: 90-120; Related: none; Repeats: 1; Topology: Undefined; Example: Q7Z699; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00573; DC Domain; TR PROSITE; PS51228; ACB_2; 1; level=0 XX Names: Acyl-CoA-binding (ACB) domain Function: The ACB domain consists of four alpha-helices arranged in a bowl shape with a highly exposed acyl-CoA-binding site. XX XX DR PROSITE; PS00880; ACB_1; 1; trigger=no XX FT From: PS51228 FT DOMAIN from..to FT /note="ACB #" XX Chop: Nter=0; Cter=0; Size: 80-95; Related: None; Repeats: 1-2; Topology: Undefined; Example: P07108; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00574; DC Domain; TR PROSITE; PS51229; DCUN1; 1; level=0 XX Names: DCUN1 domain Function: The DCUN1 domain is an ~190-residue module of unknown function which is found in the eukaryotic defective in cullin neddylation (DCN) protein family. XX XX FT From: PS51229 FT DOMAIN from..to FT /note="DCUN1 #" XX Chop: Nter=0; Cter=0; Size: 185-245; Related: None; Repeats: 1; Topology: Undefined; Example: Q12395; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00575; DC Domain; TR PROSITE; PS51226; TEP1_N; 1; level=0 XX Names: TEP1 N-terminal repeat Function: The TEP1 N-terminal repeat is a 30 residue module whereof 4 tandemly arranged copies form the N-terminus of telomerase protein component 1 (TP1) or TEP1, which is a protein component of two ribonucleoprotein (RNP) complexes: vaults and telomerase. XX GO GO:0005694; C:chromosome GO GO:1990904; C:ribonucleoprotein complex GO GO:0007004; C:telomere maintenance via telomerase GO GO:0000781; C:chromosome, telomeric region XX KW Chromosome KW Ribonucleoprotein KW Telomere XX FT From: PS51226 FT REPEAT entry..exit FT /note="TEP1 N-terminal #" XX Chop: Nter=0; Cter=0; Size: 25-35; Related: None; Repeats: 4; Topology: Undefined; Example: Q99973; Scope: Eukaryota; Craniata Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00576; DC Domain; TR PROSITE; PS51230; EB1_C; 1; level=0 XX Names: EB1-like C-terminal (EB1-C) Function: Microtubule-associated proteins of the EB1 (end-binding protein 1) family have a bipartite composition: the N-terminal CH domain mediates microtubule plus end localization and a C-terminal cargo binding domain (EB1-C) that captures cell polarity determinants. XX XX KW Microtubule XX FT From: PS51230 FT DOMAIN from..to FT /note="EB1 C-terminal #" XX Chop: Nter=0; Cter=0; Size: 70-95; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q15691; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00577; DC Domain; TR PROSITE; PS51231; DAD; 1; level=0 XX Names: Diaphanous autoregulatory domain (DAD) DRF autoregulatory domain Diaphanous autoinhibitory domain Function: The DAD domain is a ~32 amino acid autoinhibitory domain in diaphanous-related formins (DRF), which inhibits the activity of the DRF catalytical formin homology 2 (FH2) domain to nucleate and elongate nonbranched actin filaments. XX XX FT From: PS51231 FT DOMAIN from..to FT /note="DAD #" XX Chop: Nter=0; Cter=0; Size: 20-40; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Z207; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00579; DC Domain; TR PROSITE; PS51232; GBD_FH3; 1; level=0 XX Names: Rho GTPase-binding/formin homology 3 (GBD/FH3) domain Function: The GBD/FH3 domain is approximately 380 residues in length. Its role appears to be twofold. On one hand the N-terminal region of formins is involved in subcellular localization through interaction with diverse targets. On the other hand the GBD/FH3 domain is involved in regulation of activation by releasing of an intramolecular interaction between the DAD and the N-terminus. XX FT From: PS51232 FT DOMAIN from..to FT /note="GBD/FH3 #" XX Chop: Nter=0; Cter=0; Size: 360-525; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9Y4D1; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00580; DC Domain; TR PROSITE; PS51233; VWFD; 1-6; level=0 XX Names: VWFD domain profile Function: Von Willebrand factor (VWF) is a large, multimeric blood glycoprotein synthesized in endothelial cells and megakaryocytes, that is required for normal hemostasis. The type D domain (VWFD) is not only required for blood clotting factor VIII binding but also for normal multimerization of VWF. XX XX DR PROSITE; PS51233; VWFD; 1-6; trigger=no XX case KW Disulfide bond end case XX FT From: PS51233 FT DOMAIN from..to FT /note="VWFD #" FT DISULFID 3..139 FT Tag: disulf; Condition: C-x*-C FT DISULFID 25..175 FT Tag: disulf; Condition: C-x*-C FT DISULFID 34..136 FT Tag: disulf; Condition: C-x*-C FT DISULFID 49..57 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 200-230; Related: none; Repeats: 1-6; Topology: Undefined; Example: P04275; Scope: Eukaryota Comments: None XX # Revision 1.7 2021/04/13 // AC PRU00581; DC Domain; TR PROSITE; PS51225; MARVEL; 1; level=0 XX Names: MARVEL domain Function: The ~130-residue MAL and related proteins for vesicle trafficking and membrane link (MARVEL) domain is a module with a four transmembrane-helix architecture that has been identified in proteins of the myelin and lymphocyte (MAL), physins, gyrins and occludin families. XX XX DR General; Transmembrane; -; 4; trigger=no XX GO GO:0016020; C:membrane XX KW Membrane KW Transmembrane XX FT From: PS51225 FT DOMAIN from..to FT /note="MARVEL #" XX Chop: Nter=0; Cter=0; Size: 115-215; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: Q8IZ96; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.6 2022/09/30 // AC PRU00582; DC Domain; TR PROSITE; PS51252; ANTISTASIN; 1; level=0 XX Names: Antistasin-like domain Function: Antistatin is a small, disulphide cross-linked serine protease inhibitor isolated from the salivary glands of the Mexican leech. Many metazoan proteins share sequence homology with this antistasin-like domain. XX XX FT From: PS51252 FT DOMAIN from..to FT /note="Antistasin-like #" XX Chop: Nter=0; Cter=0; Size: 25-35; Related: None; Repeats: 1-6; Topology: Not cytoplasmic; Example: P15358; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00583; DC Domain; TR PROSITE; PS51253; HTH_CENPB; 1; level=0 XX Names: CENPB-type HTH domain Function: The CENPB-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 70-75 amino acids, present in eukaryotic centromere proteins and transposases. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus XX FT From: PS51253 FT DOMAIN from..to FT /note="HTH CENPB-type #" FT DNA_BIND 34..64 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 60-85; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: P07199; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00584; DC Domain; TR PROSITE; PS51255; ADPK; 1; level=0 XX Names: ADP-dependent kinase (ADPK) domain Function: Archeal ADP-dependent glucokinases (ADPGKs) and phosphofructokinases (ADPPKKs) form an ADP-dependent kinase (ADPK) family, which was tentatively named the PFKC family. A ~460-residue ADPK domain is also found in a bifunctional ADP-dependent gluco/phosphofructo-kinase (ADP-GK/PFK) from Methanococcus jannaschii as well as in homologous hypothetical proteins present in several eukaryotes. XX DE + RecName: EC=2.7.1.-; XX case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 Mg(2+) ion per subunit.; end case CC -!- PATHWAY: Carbohydrate degradation; glycolysis. XX GO GO:0006096; P:glycolytic process GO GO:0016301; F:kinase activity case GO GO:0000287; F:magnesium ion binding end case GO GO:0016740; F:transferase activity XX KW Glycolysis KW Kinase case KW Magnesium KW Metal-binding end case KW Transferase XX FT From: PS51255 FT DOMAIN from..to FT /note="ADPK #" FT ACT_SITE 446 FT /note="Proton acceptor" FT Condition: D FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: E FT BINDING 297 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: E FT BINDING 446 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 440-485; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BRR6; Scope: Eukaryota Archaea Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00585; DC Domain; TR PROSITE; PS51256; GS; 1; level=0 XX Names: GS domain Function: The GS domain is a short (~30 residues), highly conserved regulatory sequence which is found N-terminal to the kinase domain on the cytoplasmic side of members of the type I TGF-beta receptor (TbetaR-I) family. At least three, and perhaps four to five of the serines and threonines in the GS domain, must be phosphorylated to fully activate TbetaR-1. XX CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. TGFB receptor CC subfamily. XX KW Phosphoprotein XX FT From: PS51256 FT DOMAIN from..to FT /note="GS #" XX Chop: Nter=0; Cter=0; Size: 25-35; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: P36896; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00586; DC Domain; TR PROSITE; PS51262; COS; 1; level=0 XX Names: COS domain Function: The COS domain is an ~60-residue module found in N-terminal RING finger/B-box/coiled coil (RBCC) or tripartite motif (TRIM) proteins and in a distantly related non-RBCC microtubule-binding protein, GLFND. XX XX FT From: PS51262 FT DOMAIN from..to FT /note="COS #" XX Chop: Nter=0; Cter=0; Size: 55-65; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q9UJV3; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00587; DC Domain; TR PROSITE; PS51258; MHD1; 1; level=0 XX Names: Munc13-homology domain 1 (MHD1) Function: The MHD1 domain is present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. XX XX FT From: PS51258 FT DOMAIN from..to FT /note="MHD1 #" XX Chop: Nter=0; Cter=0; Size: 115-190; Related: None; Repeats: 1-2; Topology: Undefined; Example: P27715; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00588; DC Domain; TR PROSITE; PS51259; MHD2; 1; level=0 XX Names: Munc13-homology domain 2 (MHD2) Function: The MHD2 domain is present in a wide variety of proteins from Arabidopsis thaliana, C. elegans, Drosophila melanogaster, mouse, rat and human, some of which may function in a Munc13-like manner to regulate membrane trafficking. XX XX FT From: PS51259 FT DOMAIN from..to FT /note="MHD2 #" XX Chop: Nter=0; Cter=0; Size: 105-170; Related: None; Repeats: 1; Topology: Undefined; Example: P27715; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00589; DC Domain; TR PROSITE; PS51182; C2_TENSIN; 1; level=0 XX Names: C2 tensin-type domain Function: Binds phopholipid membranes in a Ca2+ independent manner. XX FT From: any FT DOMAIN from..to FT /note="C2 tensin-type #" XX Chop: Nter=0; Cter=0; Size: 110-232; Related: None; Repeats: 1; Topology: Undefined; Example: P60483; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00590; DC Domain; TR PROSITE; PS51181; PPASE_TENSIN; 1; level=0 XX Names: phosphatase tensin-type domain Function: lipid phosphatase domain. XX XX GO GO:0016787; F:hydrolase activity GO GO:0004721; F:phosphoprotein phosphatase activity XX KW Hydrolase KW Protein phosphatase XX FT From: PS51181 FT DOMAIN from..to FT /note="Phosphatase tensin-type #" FT ACT_SITE 112 FT /note="Phosphocysteine intermediate" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 137-221; Related: None; Repeats: 1; Topology: Undefined; Example: O75061; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00591; DC Domain; TR PROSITE; PS51170; CW; 1; level=0 XX Names: cell wall-binding repeat Function: sugar binding domain. XX FT From: PS51170 FT REPEAT from..to FT /note="Cell wall-binding #" XX Chop: Nter=0; Cter=0; Size: 13-22; Related: None; Repeats: 6-32; Topology: Undefined; Example: P18177; Scope: Bacteria Viruses Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00592; DC Domain; TR PROSITE; PS50058; G_PROTEIN_GAMMA; 1; level=0 XX Names: G protein gamma domain Function: It acts as intermediaries in the transduction of signals generated by transmembrane receptors. XX FT From: PS50058 FT DOMAIN from..to FT /note="G protein gamma #" XX Chop: Nter=0; Cter=0; Size: 60-68; Related: None; Repeats: 1; Topology: Undefined; Example: P49809; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00593; DC Domain; TR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1; level=0 XX Names: araC/xylS-type HTH domain Function: The araC/xylS-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 100 amino acids, present in bacterial transcription regulators of genes involved in resistance to antibiotics, organic solvents and heavy metals. XX XX DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Transcription KW Transcription regulation XX FT From: PS01124 FT DOMAIN from..to FT /note="HTH araC/xylS-type #" FT DNA_BIND 18..39 FT /note="H-T-H motif" FT DNA_BIND 66..89 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 80-120; Related: None; Repeats: 1; Topology: Undefined; Example: P0ACH5; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2022/06/27 // AC PRU00594; DC Domain; TR PROSITE; PS51166; CBM20; 1; level=0 XX Names: CBM20 (carbohydrate binding type-20) domain Function: has been shown to bind granular starch. XX FT From: any FT DOMAIN from..to FT /note="CBM20 #" XX Chop: Nter=0; Cter=0; Size: 98-122; Related: None; Repeats: 1; Topology: Undefined; Example: P26827; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00595; DC Domain; TR PROSITE; PS51089; HP; 1; level=0 XX Names: HP (headpiece) domain Function: F-actin-binding domain XX XX GO GO:0003779; F:actin binding XX KW Actin-binding XX FT From: PS51089 FT DOMAIN from..to FT /note="HP #" XX Chop: Nter=0; Cter=0; Size: 62-67; Related: None; Repeats: 1; Topology: Undefined; Example: O75366; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00596; DC Domain; TR PROSITE; PS51199; SF4_HELICASE; 1; level=0 XX Names: SF4 helicase domain Function: Undefined XX XX GO GO:0005524; F:ATP binding GO GO:0006260; P:DNA replication GO GO:0003677; F:DNA binding GO GO:0004386; F:helicase activity GO GO:0016787; F:hydrolase activity GO GO:0000166; F:nucleotide binding GO GO:0006269; C:DNA replication, synthesis of RNA primer GO GO:0005658; C:alpha DNA polymerase:primase complex XX KW ATP-binding KW DNA replication KW DNA-binding KW Helicase KW Hydrolase KW Nucleotide-binding KW Primosome XX FT From: PS51199 FT DOMAIN from..to FT /note="SF4 helicase #" FT BINDING 32..39 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 250-298; Related: None; Repeats: 1-2; Topology: Undefined; Example: P57611; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.6 2022/11/19 // AC PRU00597; DC Domain; TR PROSITE; PS51164; CBM1_2; 1; level=0 XX Names: CBM1 (fungal-type carbohydrate-binding) domain Function: carbohydrate-binding module. XX FT From: PS51164 FT DOMAIN from..to FT /note="CBM1 #" XX Chop: Nter=0; Cter=0; Size: 26-43; Related: None; Repeats: 1-4; Topology: Undefined; Example: O14405; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00599; DC Domain; TR PROSITE; PS51263; ADF_H; 1; level=0 XX Names: ADF-H domain Function: The actin-depolymerizing factor homology (ADF-H) domain is an ~150- amino acid motif present in three phylogenetically distinct classes of eukaryotic actin-binding proteins that all appear to use the ADF-H domain for their interactions with actin. XX XX GO GO:0003779; F:actin binding XX KW Actin-binding XX FT From: PS51263 FT DOMAIN from..to FT /note="ADF-H #" XX Chop: Nter=0; Cter=0; Size: 125-160; Related: None; Repeats: 1-3; Topology: Undefined; Example: P23528; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00600; DC Domain; TR PROSITE; PS51265; ZF_DBF4; 1; level=0 XX Names: DBF4-type zinc finger Function: involved in the initiation of DNA replication XX case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51265 case and and and FT ZN_FING from..to FT /note="DBF4-type #" else case and and and FT ZN_FING from..to FT /note="DBF4-type #; atypical" else FT ZN_FING from..to FT /note="DBF4-type #; degenerate" end case FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 11 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 49-69; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UBU7; Scope: Eukaryota Comments: None XX # Revision 1.7 2022/11/19 // AC PRU00601; DC Domain; TR PROSITE; PS51266; ZF_CHY; 1; level=0 XX Names: Zinc finger CHY-type Function: Fill in XX XX case ( and and and ) or ( and and and ) or ( and and and ) GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51266 case and and and and and and and and and and and FT ZN_FING from..to FT /note="CHY-type #" else case and and and and and and and and and and and FT ZN_FING from..to FT /note="CHY-type #; atypical" else FT ZN_FING from..to FT /note="CHY-type #; degenerate" end case FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 32 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 58-95; Related: None; Repeats: 1; Topology: Undefined; Example: O14033; Scope: Eukaryota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU00602; DC Domain; TR PROSITE; PS51269; COMM; 1; level=0 XX Names: COMM domain Function: The proteins designated as COMMD or COMM domain containing 1-10 are extensively conserved in multicellular eukaryotic organisms. The protein family is defined by the presence of a C-terminal motif termed COMM domain, which functions as an interface for protein-protein interactions. XX XX FT From: PS51269 FT DOMAIN from..to FT /note="COMM #" XX Chop: Nter=0; Cter=0; Size: 60-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q8N668; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00603; DC Domain; TR PROSITE; PS51271; WAPL; 1; level=0 XX Names: WAPL domain Function: The WINGS APART-LIKE (WAPL) protein of Drosophila melanogaster regulates heterochromatin structure. Although the high-sequence conservation is limited to a third of the protein sequence, a WAPL homologue has been identified in mammals. XX XX FT From: PS51271 FT DOMAIN from..to FT /note="WAPL #" XX Chop: Nter=0; Cter=0; Size: 505-550; Related: None; Repeats: 1; Topology: Undefined; Example: Q9W517; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00604; DC Domain; TR PROSITE; PS51277; BURP; 1; level=0 XX Names: BURP domain Function: The BURP domain is a ~230-residue module, which is found in the C- terminal part of a number of plant cell wall proteins. It is possible that the BURP domain represents a general motif for localization of proteins within the cell wall matrix. XX XX FT From: PS51277 FT DOMAIN from..to FT /note="BURP #" XX Chop: Nter=0; Cter=0; Size: 190-220; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q08298; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00605; DC Domain; TR PROSITE; PS51273; GATASE_TYPE_1; 1; level=0 XX Names: Glutamine amidotransferase (GATase) type 1 domain trpG-type gatase GATases class-I triad type GATase Function: GATases are enzymes that catalyze the removal of the ammonia group from glutamine and transfer this group to a substrate to form a new carbon-nitrogen group. In the GATase type 1 domain the catalytic cysteine is located in a triad of Cys-His-Glu that forms the active site. XX XX case GO GO:0006541; P:glutamine metabolic process XX KW Glutamine amidotransferase end case XX FT From: PS51273 FT DOMAIN from..to FT /note="Glutamine amidotransferase type-1 #" FT ACT_SITE 77 FT /note="Nucleophile" FT Group: 1; Condition: C FT ACT_SITE 163 FT Group: 1; Condition: H FT ACT_SITE 165 FT Group: 1; Condition: E XX Warn: Proteins with this domain may have different enzymatic activities (EC 2.4.2.-, EC 2.4.2.14, EC 4.1.3.27, EC 4.1.3.-, EC 6.3.4.2, EC 6.3.5.2, EC 6.3.5.5 or EC 6.3.5.3). Chop: Nter=0; Cter=6; Size: 165-300; Related: PRU00480; PRU00606; PRU00607; PRU00608; Repeats: 1-2; Topology: Undefined; Example: P0A6F1; Scope: Bacteria Eukaryota Archaea Viruses Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00606; DC Domain; TR PROSITE; PS51274; GATASE_COBBQ; 1; level=0 XX Names: CobBQ-type glutamine amidotransferase (GATase) domain glutaminase domain GATase class-I of cobyrinic/cobyric acid synthetase Function: GATases are enzymes that catalyze the removal of the ammonia group from glutamine and transfer this group to a substrate to form a new carbon- nitrogen group. The catalytic Cys is located in a Cys-His active site that resembles that of GATases type 1. XX XX GO GO:0006541; P:glutamine metabolic process XX KW Glutamine amidotransferase XX FT From: PS51274 FT DOMAIN from..to FT /note="GATase cobBQ-type #" case FT ACT_SITE 82 FT /note="Nucleophile" FT Condition: C FT ACT_SITE 186 FT Condition: H end case XX Chop: Nter=0; Cter=0; Size: 160-230; Related: PRU00605; PRU00480; Repeats: 1; Topology: Undefined; Example: Q57908; Scope: Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00607; DC Domain; TR PROSITE; PS51275; PEPTIDASE_C26_GGH; 1; level=0 XX Names: Gamma-glutamyl hydrolase domain Peptidase C26 family. GGH subfamily. Function: Gamma-glutamyl hydrolase (GGH) (EC 3.4.19.9) is an enzyme that cleaves gamma-linked glutamyl bonds, and with particular substrate the enzyme acts as an endopeptidase. XX case DE + RecName: EC=3.4.19.9; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = CC (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate; CC Xref=Rhea:RHEA:56784, Rhea:RHEA-COMP:14738, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57453, ChEBI:CHEBI:141005; CC EC=3.4.19.9; XX GO GO:0034722; F:gamma-glutamyl-peptidase activity GO GO:0016787; F:hydrolase activity XX KW Hydrolase end case XX FT From: PS51275 FT DOMAIN from..to FT /note="Gamma-glutamyl hydrolase #" FT ACT_SITE 110 FT /note="Nucleophile" FT Group: 1; Condition: C FT ACT_SITE 222 FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 280-310; Related: PRU00605; Repeats: 1; Topology: Undefined; Example: Q92820; Scope: Eukaryota Comments: None XX # Revision 1.12 2021/10/28 // AC PRU00608; DC Domain; TR PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1; level=0 XX Names: PfpI endopeptidase domain Peptidase C56 family. PfpI endopeptidase subfamily. Function: Pfpi-like intracellular proteases are cysteine peptidases, with a GATase type 1-like active site. XX case DE + RecName: EC=3.2.-.-; XX GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Hydrolase KW Protease end case XX FT From: PS51276 FT DOMAIN entry..exit FT /note="PfpI endopeptidase #" FT ACT_SITE 101 FT /note="Nucleophile" FT Group: 1; Condition: C FT ACT_SITE 102 FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 160-180; Related: PRU00605; Repeats: 1-2; Topology: Undefined; Example: Q51732; Scope: Bacteria Eukaryota Archaea Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00609; DC Domain; TR PROSITE; PS51278; GATASE_TYPE_2; 1; level=0 XX Names: Glutamine amidotransferase (GATase) type 2 domain purF-type gatase GATases class-II N-terminal nucleophile (Ntn) type GATase Function: GATases are enzymes that catalyze the removal of the ammonia group from glutamine and transfer this group to a substrate to form a new carbon-nitrogen group. In the GATase type 2 domain the active site is formed by a cysteine present at the N-terminal extremity. XX case GO GO:0006541; P:glutamine metabolic process XX KW Glutamine amidotransferase end case XX FT From: PS51278 FT DOMAIN from..to FT /note="Glutamine amidotransferase type-2 #" FT ACT_SITE 1 FT /note="Nucleophile" FT Condition: C XX Warn: Proteins with this domain may have different enzymatic activities (EC 2.4.2.14, EC 2.6.1.16, EC 6.3.5.4, EC 1.4.1.13, EC 1.4.7.1 or EC 1.4.1.14). Chop: Nter=0; Cter=3; Size: 175-410; Related: None; Repeats: 1; Topology: Undefined; Example: P0AG16; Scope: Bacteria Eukaryota Archaea Viruses Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00610; DC Domain; TR PROSITE; PS51279; BCNT_C; 1; level=0 XX Names: Bucentaur C-terminal (BCNT-C) domain Function: The h-type BCNT proteins contain a highly conserved 82-amino acid region at the C-terminus (BCNT-C) that is not present in p97BCNT. XX XX FT From: PS51279 FT DOMAIN from..to FT /note="BCNT-C #" XX Chop: Nter=0; Cter=0; Size: 60-85; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UEE9; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00611; DC Domain; TR PROSITE; PS51281; TAP_C; 1; level=0 XX Names: TAP C-terminal (TAP-C) domain Function: Members of the NXF family of shuttling transport receptors for nuclear export of mRNA have a modular structure. Their most C-terminal TAP-C domain is important for binding to FG repeat-containing nuclear pore proteins (FG-nucleoporins) and is sufficient to mediate nuclear shuttling. XX CC -!- FUNCTION: Involved in the export of mRNA from the nucleus to the CC cytoplasm. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localizes at both the CC nuclear and cytoplasmic site of the pores. Shuttles between the nucleus CC and the cytoplasm. XX GO GO:0006397; P:mRNA processing GO GO:0006406; P:mRNA export from nucleus GO GO:0005634; C:nucleus GO GO:0006810; P:transport XX KW Cytoplasm KW mRNA transport KW Nucleus KW Transport XX FT From: PS51281 FT DOMAIN from..to FT /note="TAP-C #" XX Chop: Nter=0; Cter=0; Size: 50-60; Related: None; Repeats: 1; Topology: Undefined; Example: P84149; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00612; DC Domain; TR PROSITE; PS51282; DWNN; 1; level=0 XX Names: DWNN domain Function: The ~75-residue DWNN (Domain With No Name) domain is highly conserved through eukaryotic species but is absent in prokaryotes. The DWNN domain may act as an ubiquitin-like modifier, possibly playing a role in the regulation of the splicing machinery. XX XX FT From: PS51282 FT DOMAIN from..to FT /note="DWNN #" XX Chop: Nter=0; Cter=0; Size: 70-75; Related: None; Repeats: 1; Topology: Undefined; Example: Q7Z6E9; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00613; DC Domain; TR PROSITE; PS51283; DUSP; 1; level=0 XX Names: DUSP domain Domain present in ubiquitin-specific proteases Function: The ~120-residue DUSP domain is located in single or tandem copy both N- and C-terminal of the ubiquitin carboxyl-terminal hydrolase catalytic core domain of deubiquitinating enzymes (DUB). XX XX FT From: PS51283 FT DOMAIN from..to FT /note="DUSP #" XX Chop: Nter=0; Cter=0; Size: 90-220; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q9USM5; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00614; DC Domain; TR PROSITE; PS51284; DOC; 1; level=0 XX Names: DOC domain Domain present in ubiquitin-specific proteases Function: The DOC domain is found in the APC10 subunit of a multi-subunit E3 protein ubiquitin ligase as well as in several hypothetical proteins that may mediate ubiquitination reactions, because they contain combinations of either RING finger, cullin or HECT domains. XX XX FT From: PS51284 FT DOMAIN from..to FT /note="DOC #" XX Chop: Nter=0; Cter=0; Size: 175-190; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UM13; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00615; DC Domain; TR PROSITE; PS50531; HTH_IS21; 1; level=0 XX Names: IS21 transposase-type HTH domain Function: The IS21 transposase-type HTH domain is a putative DNA-binding, helix-turn-helix (HTH) domain of about 60-65 amino acids, present in transposases of IS21-like prokaryotic insertion sequences. XX XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS50531 FT DOMAIN from..to FT /note="HTH IS21-type #" FT DNA_BIND 14..35 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 50-75; Related: None; Repeats: 1; Topology: Undefined; Example: P0A134; Scope: Bacteria Archaea Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00616; DC Domain; TR PROSITE; PS50532; HTH_IS408; 1; level=0 XX Names: IS408/IS1162 transposase-type HTH domain Function: The IS408 transposase-type HTH domain is a putative DNA-binding, helix-turn-helix (HTH) domain of about 80-85 amino acids, present in transposases of IS408/IS1162-like prokaryotic insertion sequences. XX XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS50532 FT DOMAIN from..to FT /note="HTH IS408-type #" FT DNA_BIND 13..34 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 70-90; Related: None; Repeats: 1; Topology: Undefined; Example: Q51761; Scope: Bacteria Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00617; DC Domain; TR PROSITE; PS51217; UVRD_HELICASE_CTER; 1; level=0 XX Names: UvrD-like helicase C-terminal domain Function: UvrD helicase unwind DNA with a 3'-5' polarity XX XX FT From: PS51217 FT DOMAIN from..to FT /note="UvrD-like helicase C-terminal #" XX Chop: Nter=0; Cter=0; Size: 150-380; Related: None; Repeats: 2; Topology: Undefined; Example: P64319; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00618; DC Domain; TR PROSITE; PS51285; AGC_KINASE_CTER; 1; level=0 XX Names: AGC-kinase C-terminal domain Function: AGC kinase proteins are characterized by three conserved phosphorylation sites that critically regulate their function. The first one is located in an activation loop in the center of the kinase domain. The two other phosphorylation sites are located outside the kinase domain in a conserved region on its C-terminal side, the AGC-kinase C-terminal domain. These sites serves as phosphorylation-regulated switches to control both intra- and inter-molecular interactions. Without these priming phosphorylations, the kinases are catalytically inactive. XX case KW Phosphoprotein end case FT From: PS51285 FT DOMAIN from..to FT /note="AGC-kinase C-terminal" FT MOD_RES 42 FT /note="Phosphoserine" FT Tag: phospho; Condition: S FT MOD_RES 42 FT /note="Phosphothreonine" FT Tag: phospho; Condition: T FT MOD_RES 61 FT /note="Phosphoserine" FT Tag: phospho; Condition: S FT MOD_RES 61 FT /note="Phosphothreonine" FT Tag: phospho; Condition: T FT MOD_RES 62 FT /note="Phosphotyrosine" FT Tag: phospho; Condition: Y XX Chop: Nter=0; Cter=0; Size: 40-125; Related: None; Repeats: 1; Topology: Undefined; Example: Q6P0Q8; Scope: Eukaryota Viruses; Murine leukemia virus Comments: None; XX # Revision 1.2 2020/06/08 // AC PRU00619; DC Domain; TR PROSITE; PS51286; RAP; 1; level=0 XX Names: RAP domain RNA-binding domain abundant in Apicomplexans Function: The RAP domain might mediate a range of cellular functions through its potential interactions with RNA. XX XX FT From: PS51286 FT DOMAIN from..to FT /note="RAP #" XX Chop: Nter=0; Cter=0; Size: 55-65; Related: None; Repeats: 1; Topology: Undefined; Example: Q53R41; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00620; DC Domain; TR PROSITE; PS51287; T_AG_OBD; 1; level=0 XX Names: Large T-antigen (T-ag) origin-binding domain (OBD) Function: T-ag is a multidomain protein that contains an N-terminal J domain, a central origin-binding domain (OBD), and a C-terminal superfamily 3 helicase domain. XX XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS51287 FT DNA_BIND from..to FT /note="T-ag OBD #" XX Chop: Nter=0; Cter=0; Size: 110-125; Related: None; Repeats: 1; Topology: Undefined; Example: P03070; Scope: Viruses; Polyomaviridae Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00621; DC Domain; TR PROSITE; PS51290; CRIC; 1; level=0 XX Names: CRIC domain Conserved region in CNK domain Function: The CRIC domain is enriched in leucine residues and functions as a protein-protein interaction domain. XX XX FT From: PS51290 FT DOMAIN from..to FT /note="CRIC #" XX Chop: Nter=0; Cter=0; Size: 85-100; Related: None; Repeats: 1; Topology: Undefined; Example: Q969H4; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00622; DC Domain; TR PROSITE; PS51289; GLG1_C_RICH; 1; level=0 XX Names: Cysteine-rich GLG1 repeat Function: The cysteine-rich GLG1 repeat from Golgi apparatus protein 1 (GLG1) is a ~60-amino acid module that contains 4 Cys residues, which can form intrachain disulfide bridges. XX XX FT From: PS51289 FT REPEAT entry..exit FT /note="Cys-rich GLG1 #" XX Chop: Nter=0; Cter=0; Size: 30-80; Related: None; Repeats: 2-16; Topology: Undefined; Example: Q02391; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00623; DC Domain; TR PROSITE; PS51292; ZF_RING_CH; 1; level=0 XX Names: Zinc finger RING-CH-type Function: The RING-CH-type is an E3 ligase mainly found in proteins associated to membranes. XX CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3 ligase CC activity. XX KW Ligase KW Ubl conjugation pathway KW Zinc-finger case ( and and and ) or ( and and and ) KW Zinc KW Metal-binding end case XX FT From: PS51292 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="RING-CH-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="RING-CH-type #; atypical" else FT ZN_FING from..to FT /note="RING-CH-type #; degenerate" end case FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 50-85; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TCQ1; Scope: Eukaryota Viruses Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00624; DC Domain; TR PROSITE; PS51293; SANT; 1; level=0 XX Names: SANT domain Function: The SANT domain is a protein-protein interaction module, which can bind to histone-tails. Although SANT domains show remarkable sequence and structural similarity to the DNA-binding helix-turn-helix (HTH) domain of the myb-like tandem repeat (see ), their function is not DNA binding. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005515; F:protein binding GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS51293 FT DOMAIN from..to FT /note="SANT #" XX Chop: Nter=0; Cter=0; Size: 30-80; Related: PRU00133; PRU00625; Repeats: 1-2; Topology: Undefined; Example: Q99543; Q08773; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00625; DC Domain; TR PROSITE; PS51294; HTH_MYB; 1; level=0 XX Names: Myb-type HTH DNA-binding domain Myb/SANT repeat Function: The myb-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of ~55 amino acids, typically occurring in a tandem repeat in eukaryotic transcription factors. Some single myb-like domains can be involved in other functions, such as protein-binding, but several single myb-like domains bind DNA (see ). XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51294 case FT DNA_BIND entry..exit FT /note="Myb-like GARP #" else FT DOMAIN entry..exit FT /note="HTH myb-type #" FT DNA_BIND 30..55 FT /note="H-T-H motif" end case XX Chop: Nter=0; Cter=0; Size: 40-80; Related: PRU00133; PRU00624; Repeats: 1-5; Topology: Undefined; Example: P54274; O49397; Scope: Eukaryota Viruses; Alpharetrovirus Comments: None XX # Revision 1.10 2022/06/27 // AC PRU00626; DC Domain; TR PROSITE; PS51295; CRM; 1; level=0 XX Names: CRM domain Chloroplast RNA splicing and ribosome maturation domain Function: The CRM domain is an ~100-amino acid RNA-binding domain. XX XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS51295 FT DOMAIN from..to FT /note="CRM #" XX Chop: Nter=0; Cter=0; Size: 95-105; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q84N49; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00627; DC Domain; TR PROSITE; PS51025; PWI; 1; level=0 XX Names: PWI domain Function: The PWI domain, named after a highly conserved PWI tri-peptide located within its N-terminal region, is a ~80 amino acid RNA/DNA-binding domain that has an equal preference for single- and double-stranded nucleic acids and is likely to have multiple important functions in pre-mRNA processing. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006397; P:mRNA processing XX KW Nucleus KW mRNA processing XX FT From: PS51025 FT DOMAIN from..to FT /note="PWI #" XX Chop: Nter=0; Cter=0; Size: 85-105; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q5ZMJ9; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00628; DC Domain; TR PROSITE; PS51296; RIESKE; 1; level=0 XX Names: Rieske [2Fe-2S] iron-sulfur domain Function: binds 2Fe-2S iron-sulfur XX CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; CC Note=Binds 1 [2Fe-2S] cluster per subunit.; XX XX case KW 2Fe-2S KW Iron KW Iron-sulfur KW Metal-binding end case case KW Disulfide bond end case XX FT From: PS51296 FT DOMAIN from..to FT /note="Rieske #" FT BINDING 41 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: C FT BINDING 43 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: H FT BINDING 61 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: C FT BINDING 64 FT /ligand="[2Fe-2S] cluster" FT /ligand_id="ChEBI:CHEBI:190135" FT Group: 1; Condition: H FT DISULFID 46..63 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 25-136; Related: None; Repeats: 1; Topology: Undefined; Example: Q93SW6; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.13 2022/11/19 // AC PRU00629; DC Domain; TR PROSITE; PS51297; K_BOX; 1; level=0 XX Names: K-box domain Function: The 80-amino acid K-box domain was originally identified as a region with low but significant similarity to a region of keratin, which is part of the coiled-coil sequence constituting the central rod-shaped domain of keratin. XX XX FT From: PS51297 FT DOMAIN from..to FT /note="K-box #" XX Chop: Nter=0; Cter=0; Size: 70-95; Related: None; Repeats: 1; Topology: Undefined; Example: P17839; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00630; DC Domain; TR PROSITE; PS51299; HTH_APSES; 1; level=0 XX Names: APSES-type HTH DNA_binding domain Function: The APSES (ASM-1, Phd1, StuA, EFG1, and Sok2) domain is an ~110- residue sequence-specific DNA-binding domain found in a family of fungal transcription factors that regulate development or cell cycle progression. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51299 FT DOMAIN from..to FT /note="HTH APSES-type #" FT DNA_BIND 35..56 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 105-115; Related: None; Repeats: 1; Topology: Undefined; Example: P36011; Scope: Eukaryota; Fungi Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00631; DC Domain; TR PROSITE; PS51301; KILA_N; 1; level=0 XX Names: KilA-N domain Function: The amino-terminal module of the poxvirus D6R/NIR proteins defines a novel conserved DNA-binding domain (the KilA-N domain) that is found in a wide range of proteins of large bacterial and eukaryotic DNA viruses. The KilA-N domain has been suggested to be homologous to the fungal DNA-binding APSES domain. XX XX FT From: PS51301 FT DOMAIN from..to FT /note="KilA-N #" XX Chop: Nter=0; Cter=0; Size: 70-115; Related: None; Repeats: 1; Topology: Undefined; Example: P19653; Scope: Eukaryota Viruses Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00632; DC Domain; TR PROSITE; PS51302; SIM_C; 1; level=0 XX Names: Single-minded C-terminal domain Function: Undefined XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51302 FT DOMAIN from..to FT /note="Single-minded C-terminal #" XX Chop: Nter=0; Cter=0; Size: 320-435; Related: None; Repeats: 1; Topology: Undefined; Example: P81133; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2022/06/27 // AC PRU00634; DC Domain; TR PROSITE; PS51234; TSP3; 1; level=0 XX Names: Thrombospondin type-3 (TSP3) repeat Function: The calcium-binding TSP3 repeats are a tandem of aspartic acid-rich motifs, which resembles EF hands in the acidic side chains. But unlike EF hands, the calcium-binding loops of the TSP3 repeats are not flanked by secondary structure elements. The individual calcium-binding repeats are linked by disulfide bonds to each other. XX XX GO GO:0005509; F:calcium ion binding XX KW Calcium XX FT From: PS51234 FT REPEAT from..to FT /note="TSP type-3 #" XX Chop: Nter=0; Cter=0; Size: 13-53; Related: None; Repeats: 8; Topology: Undefined; Example: P35442; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00635; DC Domain; TR PROSITE; PS51236; TSP_CTER; 1; level=0 XX Names: Thrombospondin C-terminal domain Function: Thrombospondins are multimeric multidomain glycoproteins that function at cell surfaces and in the extracellular matrix milieu. The function of the C-terminal domain is not yet known. XX XX FT From: PS51236 FT DOMAIN from..to FT /note="TSP C-terminal #" XX Chop: Nter=0; Cter=0; Size: 203-225; Related: None; Repeats: 1; Topology: Undefined; Example: P35445; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00636; DC Domain; TR PROSITE; PS51303; PET; 1; level=0 XX Names: PET domain Function: The PET domain is a ~110 amino acid motif in the N-terminal part of LIM domain proteins, which has been suggested to play a role in protein-protein interactions. XX XX FT From: PS51303 FT DOMAIN from..to FT /note="PET #" XX Chop: Nter=0; Cter=4; Size: 100-115; Related: None; Repeats: 1; Topology: Undefined; Example: Q71QF9; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00637; DC Domain; TR PROSITE; PS51306; ASD1; 1; level=0 XX Names: ASD1 domain Function: ASD1 is required for targeting proteins of the Shroom family to actin. XX XX GO GO:0003779; F:actin binding XX KW Actin-binding XX FT From: PS51306 FT DOMAIN from..to FT /note="ASD1 #" XX Chop: Nter=0; Cter=0; Size: 85-105; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TF72; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00638; DC Domain; TR PROSITE; PS51307; ASD2; 1; level=0 XX Names: ASD2 domain Function: ASD2 is capable of eliciting an actomyosin based constriction event in proteins of the Shroom family. XX XX FT From: PS51307 FT DOMAIN from..to FT /note="ASD2 #" XX Chop: Nter=0; Cter=0; Size: 265-300; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TF72; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00639; DC Domain; TR PROSITE; PS51304; GALECTIN; 1; level=0 XX Names: Galactoside-binding lectin (galectin) domain Function: Galectins (also known as galaptins or S-lectin) are a family of proteins defined by having at least one characteristic carbohydrate recognition domain (CRD) with an affinity for beta-galactosides and sharing certain sequence elements. XX XX GO GO:0030246; F:carbohydrate binding XX KW Lectin XX FT From: PS51304 FT DOMAIN from..to FT /note="Galectin #" XX Chop: Nter=0; Cter=0; Size: 120-145; Related: None; Repeats: 1-3; Topology: Undefined; Example: P09382; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00641; DC Domain; TR PROSITE; PS51309; PABC; 1; level=0 XX Names: Poly(A)-binding protein C-terminal (PABC) domain Function: The ~75-residue poly(A)-binding protein C-terminal domain (PABC) is binds a conserved motif of 12-15 amino acids, termed PABP-interacting motif (PAM)-2. XX XX FT From: PS51309 FT DOMAIN from..to FT /note="PABC #" XX Chop: Nter=0; Cter=0; Size: 75-85; Related: None; Repeats: 1; Topology: Undefined; Example: P11940; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00642; DC Domain; TR PROSITE; PS51310; VPS28_C; 1; level=0 XX Names: VPS28 C-terminal domain Function: The C-terminal domain of VPS28 is characterized by a high-sequence conservation throughout all kingdoms of life. It serves as an adaptor module linked to the ESCRT-I complex that connects its function to other components of the VPS machinery, including ESCRT-III VPS20. XX CC -!- SIMILARITY: Belongs to the VPS28 family. XX GO GO:0015031; P:protein transport GO GO:0006810; P:transport XX KW Protein transport KW Transport XX FT From: PS51310 FT DOMAIN from..to FT /note="VPS28 C-terminal #" XX Chop: Nter=0; Cter=0; Size: 90-100; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UK41; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00644; DC Domain; TR PROSITE; PS51312; SB; 1; level=0 XX Names: Steadiness box (SB) domain Function: The assembly of the ESCRT-I complex is directed by the C-terminal steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C- terminal half of VPS37. XX XX GO GO:0015031; P:protein transport GO GO:0006810; P:transport XX KW Protein transport KW Transport XX FT From: PS51312 FT DOMAIN from..to FT /note="SB #" XX Chop: Nter=0; Cter=0; Size: 60-90; Related: None; Repeats: 1; Topology: Undefined; Example: Q99816; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00645; DC Domain; TR PROSITE; PS51313; VPS28_N; 1; level=0 XX Names: VPS28 N-terminal domain Function: The assembly of the ESCRT-I complex is directed by the C-terminal steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C- terminal half of VPS37. XX CC -!- SIMILARITY: Belongs to the VPS28 family. XX GO GO:0015031; P:protein transport GO GO:0006810; P:transport XX KW Protein transport KW Transport XX FT From: PS51313 FT DOMAIN from..to FT /note="VPS28 N-terminal #" XX Chop: Nter=0; Cter=0; Size: 95-120; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UK41; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00646; DC Domain; TR PROSITE; PS51314; VPS37_C; 1; level=0 XX Names: VPS37 C-terminal domain Function: The assembly of the ESCRT-I complex is directed by the C-terminal steadiness box (SB) of VPS23, the N-terminal half of VPS28, and the C- terminal half of VPS37. XX XX GO GO:0015031; P:protein transport GO GO:0006810; P:transport XX KW Protein transport KW Transport XX FT From: PS51314 FT DOMAIN from..to FT /note="VPS37 C-terminal #" XX Chop: Nter=0; Cter=0; Size: 85-95; Related: None; Repeats: 1; Topology: Undefined; Example: Q8NEZ2; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00647; DC Domain; TR PROSITE; PS51316; ODV; 1; level=0 XX Names: Olduvai (ODV) domain Neuroblastoma breakpoint family (NBPF) domain Function: Proteins of the neuroblastoma breakpoint family (NBPF) contain a highly conserved domain of unknown function, which has been named the Olduvai (ODV) domain. XX XX FT From: PS51316 FT DOMAIN entry..exit FT /note="Olduvai #" XX Chop: Nter=0; Cter=0; Size: 60-120; Related: None; Repeats: 1-10; Topology: Undefined; Example: Q3BBV0; Scope: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia Comments: None XX # Revision 1.5 2020/01/21 // AC PRU00648; DC Domain; TR PROSITE; PS51318; TAT; 1; level=0 XX Names: Signal peptide Function: Signal for Twin arginine translocation (Tat) pathway. XX DE + Flags: Precursor; XX CC -!- PTM: Predicted to be exported by the Tat system. The position of the CC signal peptide cleavage has not been experimentally proven. XX KW Signal XX FT From: PS51318 FT SIGNAL 1..to FT /note="Tat-type signal" FT CHAIN to+1..Cter FT /note="" XX Chop: Nter=0; Cter=0; Size: 22-45; Related: None; Repeats: 1; Topology: Undefined; Example: Q8CVZ3; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00649; DC Domain; TR PROSITE; PS51319; TFIIS_N; 1; level=0 XX Names: TFIIS N-terminal domain Function: The TFIIS N-terminal domain is a compact four-helix bundle, which is also found in other transcription factors and proteins that are predominantly nuclear localized. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS51319 FT DOMAIN from..to FT /note="TFIIS N-terminal #" XX Chop: Nter=0; Cter=0; Size: 70-85; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q96ST2; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00650; DC Domain; TR PROSITE; PS51320; TIFY; 1; level=0 XX Names: Tify domain Function: The tify domain is a 36-amino acid domain only found among Embryophyta (land plants). It has been named after the most conserved amino acid pattern (TIF[F/Y]XG] it contains. Tify domain containing proteins might be involved in developmental processes and some of them have features that are characteristic for transcription factors: a nuclear localization and the presence of a putative DNA-binding domain. XX XX FT From: PS51320 FT DOMAIN from..to FT /note="Tify #" XX Chop: Nter=0; Cter=0; Size: 35-40; Related: None; Repeats: 1; Topology: Undefined; Example: Q8H1G0; Scope: Eukaryota; Viridiplantae; Embryophyta Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00651; DC Domain; TR PROSITE; PS51321; TFIIS_CENTRAL; 1; level=0 XX Names: TFIIS central domain Function: The transcription factor IIS (TFIIS) is a modular factor that comprises an N-terminal domain, a central domain, and a C-terminal TFIIS-type zinc finger. The central domain is conserved in TFIIS homologues and interacts with RNA polymerase II. XX case CC -!- SUBCELLULAR LOCATION: Nucleus. end case XX case GO GO:0005634; C:nucleus XX KW Nucleus end case XX FT From: PS51321 FT DOMAIN from..to FT /note="TFIIS central #" XX Chop: Nter=0; Cter=0; Size: 75-140; Related: None; Repeats: 1; Topology: Undefined; Example: P07273; Scope: Eukaryota Viruses Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00652; DC Domain; TR PROSITE; PS51322; UEV; 1; level=0 XX Names: UEV domain Function: The N-terminal ubiquitin E2 variant (UEV) domain is ~145 amino acid residues in length and shows significant sequence similarity to E2 ubiquitin ligases but is unable to catalyze ubiquitin transfer as it lacks the active site cysteine that forms the transient thioester bond with the C-terminus of ubiquitin (Ub). Nevertheless, at least some UEVs have retained the ability to bind Ub, and appear to act either as cofactors in ubiquitylation reactions, or as ubiquitin sensors. XX XX FT From: PS51322 FT DOMAIN from..to FT /note="UEV #" XX Chop: Nter=0; Cter=0; Size: 134-160; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LHG8; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00653; DC Domain; TR PROSITE; PS51323; IGFBP_N_2; 1; level=0 XX Names: Insulin-like growth factor binding protein N-terminal domain IGFBP N-terminal domain Function: The IGFBP N-terminal domain participates in binding to IGFs. XX DR PROSITE; PS00222; IGFBP_N_1; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51323 FT DOMAIN from..to FT /note="IGFBP N-terminal #" case FT DISULFID 5..29 FT Tag: disulf; Condition: C-x*-C FT DISULFID 8..31 FT Tag: disulf; Condition: C-x*-C FT DISULFID 13..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 20..35 FT Tag: disulf; Condition: C-x*-C FT DISULFID 43..56 FT Tag: disulf; Condition: C-x*-C FT DISULFID 50..76 FT Tag: disulf; Condition: C-x*-C else FT DISULFID 5..8 FT Tag: disulf; Condition: C-x*-C FT DISULFID 13..20 FT Tag: disulf; Condition: C-x*-C FT DISULFID 29..35 FT Tag: disulf; Condition: C-x*-C FT DISULFID 43..56 FT Tag: disulf; Condition: C-x*-C FT DISULFID 50..76 FT Tag: disulf; Condition: C-x*-C end case XX Chop: Nter=0; Cter=0; Size: 60-100; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P48745; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.4 2023/01/23 // AC PRU00654; DC Domain; TR PROSITE; PS51324; ERV_ALR; 1; level=0 XX Names: ERV/ALR sulfhydryl oxidase domain Function: The ~100-residue ERV/ALR sulfhydryl oxidase domain is a versatile module adapted for catalysis of disulfide bond formation in various organelles and biological settings. XX case DE AltName: Full=FAD-linked sulfhydryl oxidase; DE EC=1.8.3.2; XX CC -!- FUNCTION: FAD-dependent sulfhydryl oxidase that catalyzes disulfide CC bond formation. CC -!- CATALYTIC ACTIVITY: CC Reaction=O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'; CC Xref=Rhea:RHEA:17357, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:16520, ChEBI:CHEBI:17412; EC=1.8.3.2; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; XX GO GO:0016491; F:oxidoreductase activity GO GO:0016972; F:thiol oxidase activity XX KW FAD KW Flavoprotein KW Oxidoreductase end case case KW Disulfide bond end case XX FT From: PS51324 FT DOMAIN from..to FT /note="ERV/ALR sulfhydryl oxidase #" FT DISULFID 48..51 FT /note="Redox-active" FT Tag: disulf; Condition: C-x*-C FT DISULFID 78..95 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 84-120; Related: None; Repeats: 1; Topology: Undefined; Example: P55789; Scope: Eukaryota Viruses Comments: None; XX # Revision 1.14 2022/08/19 // AC PRU00655; DC Domain; TR PROSITE; PS51325; ALPHA_BOX; 1; level=0 XX Names: Alpha box DNA-binding domain Function: All ascomycete MAT idiomorphs encode proteins with confirmed or putative DNA-binding motifs, such as an alpha box for MAT1-1 strains and a high mobility group (HMG) DNA-binding domain for MAT1-2 strains. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the MATALPHA1 family. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51325 FT DNA_BIND from..to FT /note="Alpha box #" XX Chop: Nter=0; Cter=0; Size: 55-60; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P01365; Scope: Eukaryota; Fungi; Ascomycota Comments: None XX # Revision 1.6 2022/06/27 // AC PRU00656; DC Domain; TR PROSITE; PS51326; AVIDIN_2; 1; level=0 XX Names: Avidin-like domain Function: Avidin and streptavidin both form homotetrameric complexes of noncovalently associated chains. Each chain forms a very strong and specific non-covalent complex with one molecule of biotin. The dimeric bacterial avidin sub-family members that bind biotin with high affinity exhibit a dimeric (1-4 dimer) rather than a tetrameric structure. The fibropellin avidin-like domain forms a homotetramer incapable of binding biotin. XX case not CC -!- SUBUNIT: Homotetramer. end case CC -!- SUBCELLULAR LOCATION: Secreted. XX DR PROSITE; PS00577; AVIDIN_1; 1; trigger=no XX case or GO GO:0009374; F:biotin binding XX KW Biotin end case KW Secreted case KW Disulfide bond end case XX FT From: PS51326 FT DOMAIN from..to FT /note="Avidin-like #" case and FT BINDING 31 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT Tag: biotin; Condition: Y else case FT BINDING 31 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT Tag: biotin; Group: 1; Condition: Y FT BINDING 45 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT Tag: biotin; Group: 1; Condition: Y FT BINDING 75 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT Tag: biotin; Group: 1; Condition: W FT BINDING 92 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT Tag: biotin; Group: 1; Condition: W FT BINDING 104 FT /ligand="biotin" FT /ligand_id="ChEBI:CHEBI:57586" FT Tag: biotin; Group: 1; Condition: W end case FT DISULFID 3..79 FT Tag: disulf; Condition: C-x*-C FT DISULFID 40..69 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 115-125; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P02701; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2023/06/26 // AC PRU00657; DC Domain; TR PROSITE; PS51327; DICER_DSRBF; 1; level=0 XX Names: Dicer double-stranded RNA-binding fold domain Function: A typical eukaryotic Dicer consists of a helicase domain, a domain of unknown function, and a PAZ domain at the amino (N)-terminus as well as two ribonuclease III domains and a dsRNA-binding domain (dsRBD) at the carboxy (C)-terminus. XX case and CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily. end case XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS51327 FT DOMAIN from..to FT /note="Dicer dsRNA-binding fold #" XX Chop: Nter=0; Cter=0; Size: 90-100; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UPY3; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00658; DC Domain; TR PROSITE; PS51328; L_LECTIN_LIKE; 1; level=0 XX Names: L-type lectin-like (leguminous) domain Function: The L-type lectin-like domain is a carbohydrate recognition domain (CRD) with an overall globular shape composed of a beta-sandwich of two major twisted antiparallel beta-sheet. XX XX GO GO:0030246; F:carbohydrate binding case GO GO:0046872; F:metal ion binding XX KW Calcium KW Metal-binding end case XX KW Lectin case KW Disulfide bond end case XX FT From: PS51328 FT DOMAIN from..to FT /note="L-type lectin-like #" FT DISULFID 146..185 FT Tag: disulf; Condition: C-x*-C FT BINDING 45 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1; Condition: S FT BINDING 78 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1; Condition: D FT BINDING 134 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1; Condition: H FT BINDING 111..113 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1 FT BINDING 206..208 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1 FT BINDING 109 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: D FT BINDING 111 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: Y FT BINDING 113 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: N FT BINDING 137 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: D XX Chop: Nter=0; Cter=0; Size: 215-230; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P49256; Scope: Eukaryota Comments: None XX # Revision 1.13 2022/11/19 // AC PRU00659; DC Domain; TR PROSITE; PS51329; C_CAP_COFACTOR_C; 1; level=0 XX Names: C-CAP/cofactor C-like domain Function: The C-CAP/cofactor C-like domain is a protein interaction domain present in several cytoskeleton-related proteins. XX XX DR PROSITE; PS01088; CAP_1; 0-1; trigger=no DR PROSITE; PS01089; CAP_2; 0-1; trigger=no XX FT From: PS51329 FT DOMAIN from..to FT /note="C-CAP/cofactor C-like #" XX Chop: Nter=0; Cter=0; Size: 130-160; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q01518; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00660; DC Domain; TR PROSITE; PS51330; DHFR_2; 1; level=0 XX Names: Dihydrofolate reductase (DHFR) domain Function: Dihydrofolate reductases (DHFRs) (EC 1.5.1.3) are ubiquitous enzymes which catalyze the NADPH-linked reduction of 7,8-dihydrofolate to 5,6,7,8- tetrahydrofolate. XX DE + RecName: EC=1.5.1.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + CC H(+) + NADPH; Xref=Rhea:RHEA:15009, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57451, ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; EC=1.5.1.3; XX DR PROSITE; PS00075; DHFR_1; 1; trigger=no XX GO GO:0016491; F:oxidoreductase activity GO GO:0004146; F:dihydrofolate reductase activity GO GO:0050661; F:NADP binding XX KW NADP KW Oxidoreductase XX FT From: PS51330 FT DOMAIN from..to FT /note="DHFR #" XX Chop: Nter=0; Cter=0; Size: 145-257; Related: None; Repeats: 1; Topology: Undefined; Example: Q5V3R2; Scope: Bacteria Eukaryota Viruses Archaea Comments: None; XX # Revision 1.7 2021/01/11 // AC PRU00661; DC Domain; TR PROSITE; PS51331; THYX; 1; level=0 XX Names: Flavin-dependent thymidylate synthase (thyX) domain Function: The thyx domain contains FAD and methylates dUMP at position 5 of the pyrimidine ring. XX case not DE AltName: Full=Probable thymidylate synthase; DE Short=TS; DE Short=TSase; DE EC=2.1.1.148; end case XX CC -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'- CC monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while CC utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, CC and NADPH and FADH(2) as the reductant. CC -!- CATALYTIC ACTIVITY: CC Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) + CC NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+); CC Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636, CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, CC ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; synthase) domain XX GO GO:0008168; F:methyltransferase activity GO GO:0016740; F:transferase activity GO GO:0050797; F:thymidylate synthase (FAD) activity GO GO:0006231; P:dTMP biosynthetic process GO GO:0050660; F:flavin adenine dinucleotide binding XX KW FAD KW Flavoprotein KW Methyltransferase KW Nucleotide biosynthesis KW Transferase XX FT From: PS51331 FT DOMAIN from..to FT /note="ThyX #" FT MOTIF 80..90 FT /note="ThyX motif #" FT Condition: R-H-R-x(7,8)-S XX Chop: Nter=0; Cter=0; Size: 183-266; Related: None; Repeats: 1-2; Topology: Undefined; Example: O86840; Scope: Bacteria Archaea Viruses Eukaryota; Dictyostelium Comments: None; XX # Revision 1.14 2019/11/21 // AC PRU00663; DC Domain; TR PROSITE; PS51334; PRONE; 1; level=0 XX Names: PRONE domain Function: The PRONE domain has been shown to be necessary and sufficient to promote nucleotide release from Rop. XX XX GO GO:0005085; F:guanyl-nucleotide exchange factor activity XX KW Guanine-nucleotide releasing factor XX FT From: PS51334 FT DOMAIN from..to FT /note="PRONE #" XX Chop: Nter=0; Cter=0; Size: 380-410; Related: None; Repeats: 1; Topology: Undefined; Example: Q93ZY2; Scope: Eukaryota; Viridiplantae Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00664; DC Domain; TR PROSITE; PS51335; ELMO; 1; level=0 XX Names: ELMO domain Function: The ELMO (for EnguLfment and cell MOtility) domain has been proposed to be a GAP domain for ARL2 and other members of the Arf family. XX XX FT From: PS51335 FT DOMAIN from..to FT /note="ELMO #" XX Chop: Nter=0; Cter=0; Size: 150-185; Related: None; Repeats: 1; Topology: Undefined; Example: Q92556; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00665; DC Domain; TR PROSITE; PS51336; DM10; 1; level=0 XX Names: DM10 domain Function: DM10 domains might act as flagellar NDK regulatory modules or as units specifically involved in axonemal targeting or assembly. XX XX FT From: PS51336 FT DOMAIN from..to FT /note="DM10 #" XX Chop: Nter=0; Cter=0; Size: 85-145; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q5JVL4; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00666; DC Domain; TR PROSITE; PS51332; B12_BINDING; 1; level=0 XX Names: B12-binding domain Function: The B12-binding domain is mainly found in two families of enzymes present in animals and prokaryotes, which use vitamin B12 (cobalamin) as cofactor. XX XX FT From: PS51332 FT DOMAIN from..to FT /note="B12-binding #" XX Chop: Nter=0; Cter=0; Size: 115-145; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q99707; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00667; DC Domain; TR PROSITE; PS51337; B12_BINDING_NTER; 1; level=0 XX Names: B12-binding N-terminal domain Function: In methionine synthase the cobalamin cofactor is sandwiched between the B12-binding domain and an ~90 residues N-terminal domain forming a helical bundle comprising two pairs of antiparallel helices. XX XX FT From: PS51337 FT DOMAIN from..to FT /note="B12-binding N-terminal" XX Chop: Nter=0; Cter=0; Size: 34-112; Related: None; Repeats: 1; Topology: Undefined; Example: Q55786; Scope: Archaea; Methanosarcina Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00668; DC Domain; TR PROSITE; PS51338; IMD; 1; level=0 XX Names: N-terminal IRSp53 and MIM homology domain IMD Function: The IMD domain can bind to and bundle actin filaments, bind to membranes and interact with the small GTPase Rac . XX XX FT From: PS51338 FT DOMAIN from..to FT /note="IMD #" XX Chop: Nter=0; Cter=0; Size: 225-255; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: O43312; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00669; DC Domain; TR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1; level=0 XX Names: Myotubularin phosphatase domain Function: Myotubularins phosphatase domain is a 3-phosphatases specific for membrane-embedded PtdIns3P and PtdIns(3,5)P2, two PIs that function within the endosomal-lysosomal pathway XX XX FT From: PS51339 FT DOMAIN from..to FT /note="Myotubularin phosphatase #" XX Chop: Nter=0; Cter=0; Size: 305-452; Related: None; Repeats: 1; Topology: Undefined; Example: Q13496; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00670; DC Domain; TR PROSITE; PS51340; MOSC; 1; level=0 XX Names: MOSC domain Function: The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters. XX XX FT From: PS51340 FT DOMAIN from..to FT /note="MOSC #" XX Chop: Nter=0; Cter=0; Size: 65-185; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9C5X8; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00671; DC Domain; TR PROSITE; PS51341; ZF_LTAG_D1; 1; level=0 XX Names: Zinc finger large T-antigen (T-ag) D1-type Function: Undefined XX case and and and GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51341 case and and and FT ZN_FING from..to FT /note="T-ag D1-type #" else case and and and FT ZN_FING from..to FT /note="T-ag D1-type #; atypical" else FT ZN_FING from..to FT /note="T-ag D1-type #; degenerate" end case FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 49 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 90-100; Related: None; Repeats: 1; Topology: Undefined; Example: P03070; Scope: Viruses; Polyomaviridae Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00672; DC Site; TR PROSITE; PS00005; PKC_PHOSPHO_SITE; 1; level=1 XX Names: Protein kinase C phosphorylation site Function: In vivo, protein kinase C exhibits a preference for the phosphorylation of serine or threonine residues found close to a C-terminal basic residue. XX KW Phosphoprotein XX FT From: PS00005 FT MOD_RES 1 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 1 FT /note="Phosphothreonine" FT Condition: T XX Chop: Nter=0; Cter=0; Size: 3; Related: None; Repeats: unlimited; no keyword; Topology: Undefined; Example: P03070; Scope: Eukaryota Viruses Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00673; DC Site; TR PROSITE; PS00006; CK2_PHOSPHO_SITE; 1; level=1 XX Names: Casein kinase II phosphorylation site Function: Casein kinase II (CK-2) is a protein serine/threonine kinase whose activity is independent of cyclic nucleotides and calcium. XX KW Phosphoprotein XX FT From: PS00006 FT MOD_RES 1 FT /note="Phosphoserine" FT Condition: S FT MOD_RES 1 FT /note="Phosphothreonine" FT Condition: T XX Chop: Nter=0; Cter=0; Size: 3; Related: None; Repeats: unlimited; no keyword; Topology: Undefined; Example: P03070; Scope: Eukaryota Viruses Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00674; DC Domain; TR PROSITE; PS51342; COLIPASE_2; 1; level=0 XX Names: Colipase family Function: Colipase is a small protein of ~100 amino acids that functions as a cofactor for pancreatic lipase. It also binds to the bile-salt covered triacylglycerol interface thus allowing the enzyme to anchor itself to the water-lipid interface. Colipases contain ten cysteines involved in five disulfide bonds. XX case CC -!- FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the CC lipase to anchor itself to the lipid-water interface. Without colipase CC the enzyme is washed off by bile salts, which have an inhibitory effect CC on the lipase. CC -!- SUBUNIT: Forms a 1:1 stoichiometric complex with pancreatic lipase. CC -!- SUBCELLULAR LOCATION: Secreted. end case CC -!- SIMILARITY: Belongs to the colipase family. XX case DR PROSITE; PS00121; COLIPASE_1; 1; trigger=no XX GO GO:0007586; P:digestion GO GO:0016042; P:lipid catabolic process XX KW Digestion KW Lipid degradation KW Lipid metabolism KW Secreted end case case KW Disulfide bond end case XX FT From: PS51342 FT DISULFID 12..23 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 18..34 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 22..56 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 44..64 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 58..82 FT Tag: disulf; Group: 1; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 80-90; Related: None; Repeats: 1; Topology: Undefined; Example: Q91XL7; Scope: Eukaryota; Metazoa; Vertebrata Comments: None XX # Revision 1.7 2019/11/21 // AC PRU00675; DC Domain; TR PROSITE; PS51343; PII_GLNB_DOM; 1; level=0 XX Names: P-II protein family PII protein P(II) protein Function: P-II family proteins are regulators of nitrogen metabolism. XX case or CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. end case CC -!- SIMILARITY: Belongs to the P(II) protein family. XX case DR PROSITE; PS00496; PII_GLNB_UMP; 1; trigger=no end case DR PROSITE; PS00638; PII_GLNB_CTER; 1; trigger=no XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription case GO GO:0000166; F:nucleotide binding end case case or GO GO:0009507; C:chloroplast end case XX KW Transcription KW Transcription regulation case KW Nucleotide-binding end case case or KW Chloroplast KW Plastid end case XX FT From: PS51343 FT MOD_RES 51 FT /note="O-UMP-tyrosine" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: 100-135; Related: None; Repeats: 1; Topology: Undefined; Example: Q9CJK1; Q9TM37; Scope: Eukaryota; Rhodophyta Eukaryota; Viridiplantae Archaea Bacteria Plastid Comments: None XX # Revision 1.7 2022/06/27 // AC PRU00676; DC Domain; TR PROSITE; PS51344; HTH_TFE_IIE; 1; level=0 XX Names: TFE/IIEalpha-type HTH domain Function: It has been proposed that the TFE/IIEalpha-type HTH domain acts as a bridging factor or adapter between the TATA box-binding protein, the polymerase, and possibly promoter DNA. XX XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Transcription KW Transcription regulation XX FT From: PS51344 FT DOMAIN from..to FT /note="HTH TFE/IIEalpha-type #" XX Chop: Nter=0; Cter=0; Size: 85-110; Related: None; Repeats: 1; Topology: Undefined; Example: P29083; Scope: Eukaryota Archaea Comments: None XX # Revision 1.5 2022/06/27 // AC PRU00677; DC Domain; TR PROSITE; PS51345; MYOTOXINS_2; 1; level=0 XX Names: Myotoxins family Function: Myotoxins are small basic peptides (42 to 45 residues) from the venom of rattlesnakes that cause severe muscle necrosis by a non-enzymatic mechanism. Myotoxins contain six cysteines involved in three disulfide bonds. XX case CC -!- FUNCTION: This toxin specifically modifies voltage-sensitive sodium CC channels, it exhibits analgesic activity and causes severe muscle CC necrosis by a non-enzymatic mechanism. Moreover, it actively interacts CC with lipid membranes. CC -!- SUBCELLULAR LOCATION: Secreted. end case CC -!- SIMILARITY: Belongs to the snake toxin myotoxin family. XX DR PROSITE; PS00459; MYOTOXINS_1; 0-1; trigger=no XX case GO GO:0019870; F:potassium channel inhibitor activity GO GO:0008200; F:ion channel inhibitor activity XX KW Secreted KW Ion channel impairing toxin KW Potassium channel impairing toxin KW Voltage-gated potassium channel impairing toxin KW Myotoxin KW Toxin end case case KW Disulfide bond end case XX FT From: PS51345 FT DISULFID 4..36 FT Tag: disulf; Condition: C-x*-C FT DISULFID 11..30 FT Tag: disulf; Condition: C-x*-C FT DISULFID 18..37 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 35-50; Related: None; Repeats: 1; Topology: Undefined; Example: O73799; Scope: Eukaryota; Metazoa; Squamata; Serpentes Comments: None XX # Revision 1.7 2021/06/03 // AC PRU00678; DC Domain; TR PROSITE; PS51346; PROKAR_ZN_DEPEND_PLPC_2; 1; level=0 XX Names: Prokaryotic zinc-dependent phospholipase C domain Function: Phospholipase C (EC 3.1.4.3) has a ~245 amino-acids domain with the active site (PLC) in a cleft which is also occupied by 3 zinc ions. There are nine conserved residues known to be involved in binding the zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp. XX case and and DE + AltName: Full=phospholipase C; DE EC=3.1.4.3; DE Short=PLC; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl- CC sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 3 Zn(2+) ions per subunit.; CC -!- SUBCELLULAR LOCATION: Secreted. end case CC -!- SIMILARITY: Belongs to the bacterial zinc-metallophospholipase C CC family. XX case and and DR PROSITE; PS00384; PROKAR_ZN_DEPEND_PLPC_1; 1; trigger=no end case XX case or or GO GO:0016787; F:hydrolase activity GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Hydrolase KW Metal-binding KW Zinc end case XX FT From: PS51346 FT DOMAIN 3..to FT /note="Zn-dependent PLC #" FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: W FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: D FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: H FT BINDING 129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: H FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: D FT BINDING 139 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 155 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: E XX Chop: Nter=3; Cter=0; Size: 230-260; Related: None; Repeats: 1; Topology: Undefined; Example: Q46150; Scope: Bacteria Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00679; DC Domain; TR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1; level=0 XX Names: Phosphotriesterase family Function: The enzyme phosphotriesterase (EC 3.1.8.1) (PTE) (also known as parathion hydrolase) belongs to a family of enzymes that possess a binuclear zinc metal center at their active site. The two zinc ions are coordinated by six different residues, four of which being histidines. XX case and CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit.; end case CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Phosphotriesterase family. XX case DR PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1; trigger=no end case XX case or GO GO:0016787; F:hydrolase activity GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Hydrolase KW Metal-binding KW Zinc end case XX FT From: PS51347 FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /note="via carbamate group" FT Group: 1; Condition: [KE] FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /note="via carbamate group" FT Group: 2; Condition: [KE] FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 204 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 263 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: D FT MOD_RES 142 FT /note="N6-carboxylysine" FT Condition: K XX Chop: Nter=0; Cter=0; Size: 280-360; Related: None; Repeats: 1; Topology: Undefined; Example: P0A433; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.9 2022/11/19 // AC PRU00680; DC Domain; TR PROSITE; PS51348; GLYCOSYL_HYDROL_F22_2; 1; level=0 XX Names: Glycosyl hydrolases family 22 (GH22) domain Function: Alpha-lactalbumin, a regulatory protein in milk, and lysozyme (EC 3.2.1.17) C (chicken type), which acts as a bacteriolytic enzyme, belong to a family of proteins with eight conserved cysteines that form four disulfide bonds. Alpha-lactalbumin lacks the enzymatic activity and the corresponding Glu and Asp residues. Alpha-lactalbumin binds a calcium ion, while most lysozyme C do not bind calcium. XX case DE + AltName: Full=lysozyme C; DE EC=3.2.1.17; DE AltName: Full=1,4-beta-N-acetylmuramidase C; XX CC -!- FUNCTION: Lysozymes have primarily a bacteriolytic function; those in CC tissues and body fluids are associated with the monocyte-macrophage CC system and enhance the activity of immunoagents. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and CC between N-acetyl-D-glucosamine residues in chitodextrins.; CC EC=3.2.1.17; end case CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. XX DR PROSITE; PS00128; GLYCOSYL_HYDROL_F22_1; 1; trigger=no XX case GO GO:0003824; F:catalytic activity GO GO:0019835; P:cytolysis GO GO:0042742; P:defense response to bacterium GO GO:0016798; F:hydrolase activity, acting on glycosyl bonds GO GO:0008152; P:metabolic process GO GO:0016787; F:hydrolase activity end case case and GO GO:0005509; F:calcium ion binding end case XX case KW Antimicrobial KW Bacteriolytic enzyme KW Glycosidase KW Hydrolase end case case and KW Calcium end case case KW Disulfide bond end case XX FT From: PS51348 FT DOMAIN from..to FT /note="C-type lysozyme #" FT ACT_SITE 35 FT Group: 1; Condition: E FT ACT_SITE 52 FT Group: 1; Condition: D case and FT BINDING 82 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 85 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 87 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 90 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 91 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] end case FT DISULFID 6..125 FT Tag: disulf; Condition: C-x*-C FT DISULFID 30..114 FT Tag: disulf; Condition: C-x*-C FT DISULFID 64..80 FT Tag: disulf; Condition: C-x*-C FT DISULFID 76..94 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 110-140; Related: None; Repeats: 1; Topology: Undefined; Example: Q659U0; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00681; DC Domain; TR PROSITE; PS51350; PTS_HPR_DOM; 1; level=0 XX Names: PTS HPR domain Function: The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), which transfers metabolic carbohydrates across the cell membrane in many bacterial species. XX XX case DR PROSITE; PS00369; PTS_HPR_HIS; 1; trigger=no end case case DR PROSITE; PS00589; PTS_HPR_SER; 1; trigger=no end case XX GO GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system GO GO:0016740; F:transferase activity GO GO:0016301; F:kinase activity XX KW Kinase case and KW Phosphoprotein end case KW Phosphotransferase system KW Transferase XX FT From: PS51350 FT DOMAIN from..to FT /note="HPr #" case or FT ACT_SITE 15 FT /note="Pros-phosphohistidine intermediate; for HPr FT activity" FT Condition: H else FT ACT_SITE 15 FT /note="Pros-phosphohistidine intermediate" FT Condition: H end case case and FT MOD_RES 46 FT /note="Phosphoserine; by HPrK/P" end case XX Chop: Nter=0; Cter=0; Size: 80-95; Related: None; Repeats: 1-2; Topology: Undefined; Example: P08877; Scope: Bacteria Archaea Comments: None XX # Revision 1.6 2023/01/13 // AC PRU00682; DC Domain; TR PROSITE; PS51351; TFIIE_BETA_C; 1; level=0 XX Names: TFIIE beta central core DNA-binding domain Function: The ~120-residue central core domain of TFIIE beta plays a role in double-stranded DNA binding of TFIIE. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the TFIIE beta subunit family. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51351 FT DNA_BIND from..to FT /note="TFIIE beta #" XX Chop: Nter=0; Cter=0; Size: 70-85; Related: None; Repeats: 1; Topology: Undefined; Example: Q2KJF9; Scope: Eukaryota Comments: None XX # Revision 1.6 2022/06/27 // AC PRU00683; DC Domain; TR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1; level=0 XX Names: FMN-dependent alpha-hydroxy acid dehydrogenase domain Function: These enzymes are oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins with a TIM barrel structure. XX case DE + RecName: EC=1.-.-.-; end case XX CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid CC dehydrogenase family. XX case DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1; trigger=no XX GO GO:0016491; F:oxidoreductase activity end case XX KW Flavoprotein KW FMN case KW Oxidoreductase end case XX FT From: PS51349 FT DOMAIN from..to FT /note="FMN hydroxy acid dehydrogenase #" FT BINDING 309..313 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT BINDING 332..333 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT ACT_SITE 278 FT /note="Proton acceptor" FT Condition: H FT BINDING 27 FT /ligand="a 2-oxocarboxylate" FT /ligand_id="ChEBI:CHEBI:35179" FT Condition: Y FT BINDING 109 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: S FT BINDING 131 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: Q FT BINDING 133 FT /ligand="a 2-oxocarboxylate" FT /ligand_id="ChEBI:CHEBI:35179" FT Condition: Y FT BINDING 159 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: T FT BINDING 168 FT /ligand="a 2-oxocarboxylate" FT /ligand_id="ChEBI:CHEBI:35179" FT Condition: R FT BINDING 254 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT Condition: K FT BINDING 281 FT /ligand="a 2-oxocarboxylate" FT /ligand_id="ChEBI:CHEBI:35179" FT Condition: R XX Chop: Nter=0; Cter=0; Size: 340-390; Related: None; Repeats: 1; Topology: Undefined; Example: Q6FFS1; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00684; DC Domain; TR PROSITE; PS50404; GST_NTER; 1; level=0 XX Names: Soluble glutathione S-transferase N-terminal domain Function: The soluble glutathione S-transferase N-terminal domain participates in binding the glutathione moiety via its thioredoxin-like domain. XX XX FT From: PS50404 FT DOMAIN from..to FT /note="GST N-terminal #" XX Chop: Nter=0; Cter=0; Size: 18-122; Related: None; Repeats: 1; Topology: Undefined; Example: Q6AXY0; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00685; DC Domain; TR PROSITE; PS50405; GST_CTER; 1; level=0 XX Names: Soluble glutathione S-transferase C-terminal domain Function: The soluble glutathione S-transferases C-terminal domain contains several hydrophobic alpha-helices that specifically bind hydrophobic substrates. XX XX FT From: PS50405 FT DOMAIN from..to FT /note="GST C-terminal #" XX Chop: Nter=0; Cter=0; Size: 66-231; Related: None; Repeats: 1; Topology: Undefined; Example: Q6AXY0; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00686; DC Domain; TR PROSITE; PS51354; GLUTAREDOXIN_2; 1; level=0 XX Names: Glutaredoxin domain Function: It functions as an electron carrier. XX XX FT From: PS51354 FT DOMAIN from..to FT /note="Glutaredoxin #" XX Chop: Nter=0; Cter=0; Size: 80-130; Related: None; Repeats: 1-3; Topology: Undefined; Example: P0AC69; Scope: Eukaryota Bacteria Viruses Archaea; Euryarchaeota Comments: None XX # Revision 1.6 2019/11/21 // AC PRU00690; DC Domain; TR PROSITE; PS51358; NOP; 1; level=0 XX Names: Nop domain Function: The ~120-residue Nop domain is present in various pre-RNA processing ribonucleoproteins (RNP). XX XX FT From: PS51358 FT DOMAIN from..to FT /note="Nop #" XX Chop: Nter=0; Cter=0; Size: 105-143; Related: None; Repeats: 1; Topology: Undefined; Example: Q6BIX6; Scope: Eukaryota Archaea; Methanocaldococcus Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00691; DC Domain; TR PROSITE; PS51352; THIOREDOXIN_2; 1; level=0 XX Names: thioredoxin domain Function: The thioredoxin domain participate in various redox reactions via the reversible oxidation of an active center disulfide bond. XX XX GO GO:0045454; P:cell redox homeostasis case KW Disulfide bond end case XX FT From: PS51352 FT DOMAIN from..to FT /note="Thioredoxin #" FT DISULFID 42..45 FT /note="Redox-active" FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 100-200; Related: None; Repeats: 1-4; Topology: Undefined; Example: P0AEG4; Scope: Eukaryota Bacteria Viruses Archaea; Euryarchaeota Comments: None XX # Revision 1.8 2019/11/21 // AC PRU00692; DC Domain; TR PROSITE; PS51359; COX5B_2; 1; level=0 XX Names: Cytochrome c oxidase subunit Vb, zinc binding domain Function: This domain occurs in a subunit which forms a part of the cytochrome c oxidase (EC 1.9.3.1) enzymatic complex. It contains 3 to 4 conserved cysteine residues which bind a zinc atom. XX case and and DE + AltName: Full=cytochrome c oxidase subunit; XX CC -!- FUNCTION: This protein is one of the nuclear-coded polypeptide chains CC of cytochrome c oxidase, the terminal oxidase in mitochondrial electron CC transport. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. end case CC -!- SIMILARITY: Belongs to the cytochrome c oxidase Vb family. XX case and and DR PROSITE; PS00848; COX5B_1; 1; trigger=no XX GO GO:0016020; C:membrane GO GO:0046872; F:metal ion binding GO GO:0005739; C:mitochondrion GO GO:0008270; F:zinc ion binding XX KW Mitochondrion inner membrane KW Membrane KW Metal-binding KW Mitochondrion KW Zinc end case XX FT From: PS51359 FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: C FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: C FT BINDING 84 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: C FT BINDING 87 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 90-110; Related: None; Repeats: 1; Topology: Undefined; Example: Q5S3G4; Scope: Eukaryota Comments: None XX # Revision 1.7 2022/11/19 // AC PRU00693; DC Domain; TR PROSITE; PS51360; PLUS3; 1; level=0 XX Names: Plus3 domain Function: The capacity to bind single-stranded DNA is at least one function of the Plus3 domain. XX XX FT From: PS51360 FT DOMAIN from..to FT /note="Plus3 #" XX Chop: Nter=0; Cter=0; Size: 125-135; Related: None; Repeats: 1; Topology: Undefined; Example: P53064; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00694; DC Domain; TR PROSITE; PS51361; TENEURIN_N; 1; level=0 XX Names: Teneurin N-terminal domain Function: The N-terminal intracellular domain of vertebrate teneurins contains two EF-hand-like calcium-binding motifs and two polyproline regions involved in protein-protein interactions, followed by a single-span transmembrane domain. XX XX FT From: PS51361 FT DOMAIN from..to FT /note="Teneurin N-terminal #" XX Chop: Nter=0; Cter=0; Size: 200-415; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UKZ4; Scope: Eukaryota; Metazoa; Craniata Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00695; DC Domain; TR PROSITE; PS51363; W2; 1; level=0 XX Names: W2 domain Function: The W2 domain (two invariant tryptophans) is a region of ~165 amino acids which is found in the C-terminus of some eukayrotic initiation factors (eIFs). XX XX FT From: PS51363 FT DOMAIN from..to FT /note="W2 #" XX Chop: Nter=0; Cter=0; Size: 60-195; Related: None; Repeats: 1; Topology: Undefined; Example: Q04637; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00697; DC Domain; TR PROSITE; PS51364; TB; 1; level=0 XX Names: TGF-beta binding (TB) domain Function: The TB fold is globular with six beta-strands and two alpha-helices. The pairing of the eight cysteines is 1-3, 2-6, 4-7, and 5-8, creating a fairly rigid structure. XX XX case KW Disulfide bond end case XX FT From: PS51364 FT DOMAIN from..to FT /note="TB #" FT DISULFID 3..25 FT Tag: disulf; Condition: C-x*-C FT DISULFID 12..37 FT Tag: disulf; Condition: C-x*-C FT DISULFID 26..40 FT Tag: disulf; Condition: C-x*-C FT DISULFID 27..52 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 30-72; Related: None; Repeats: 1-9; Topology: Undefined; Example: Q00918; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00698; DC Domain; TR PROSITE; PS51366; MI; 1; level=0 XX Names: MI domain Function: The MI (after MA-3 and eIF4G) domain is a protein-protein interaction module of ~130 amino acids that appears in several translation factors. XX XX FT From: PS51366 FT DOMAIN from..to FT /note="MI #" XX Chop: Nter=0; Cter=0; Size: 110-140; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q04637; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00699; DC Domain; TR PROSITE; PS51367; THAUMATIN_2; 1; level=0 XX Names: Thaumatin family pathogenesis-related group 5 PR5-like PR-5 family osmotin-like Function: Thaumatin, an intensely sweet-tasting protein from Thaumatococcus daniellii plants and several stress-induced proteins with 8 disulfide bonds from plants form this family. XX CC -!- SIMILARITY: Belongs to the thaumatin family. XX DR PROSITE; PS00316; THAUMATIN_1; 1; trigger=no XX case GO GO:0009607; P:response to biotic stimulus GO GO:0006952; P:defense response end case XX case KW Pathogenesis-related protein KW Plant defense end case case KW Disulfide bond end case XX FT From: PS51367 FT DISULFID 10..210 FT Tag: disulf; Condition: C-x*-C FT DISULFID 56..66 FT Tag: disulf; Condition: C-x*-C FT DISULFID 71..77 FT Tag: disulf; Condition: C-x*-C FT DISULFID 124..199 FT Tag: disulf; Condition: C-x*-C FT DISULFID 129..182 FT Tag: disulf; Condition: C-x*-C FT DISULFID 137..147 FT Tag: disulf; Condition: C-x*-C FT DISULFID 151..160 FT Tag: disulf; Condition: C-x*-C FT DISULFID 161..169 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 140-230; Related: None; Repeats: 1; Topology: Undefined; Example: P81295; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00700; DC Domain; TR PROSITE; PS51368; UREASE_3; 1; level=0 XX Names: Urease domain Function: Urease (EC 3.5.1.5) is a nickel-binding enzyme that catalyzes the hydrolysis of urea to carbon dioxide and ammonia. The urease domain forms an (alpha beta)(8) barrel structure that binds two nickel ions and with a histidine that is catalytically involved. XX case and and and not and not DE + AltName: Full=Urease; DE EC=3.5.1.5; DE AltName: Full=Urea amidohydrolase; end case XX case and and CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; end case case or CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Note=Binds #(Ni(2+),ion) per subunit.; end case case CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case case and CC -!- SIMILARITY: In the C-terminal section; belongs to the metallo-dependent CC hydrolases superfamily. Urease alpha subunit family. else CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Urease alpha subunit family. end case XX case and DR PROSITE; PS01120; UREASE_1; 1; trigger=no end case case DR PROSITE; PS00145; UREASE_2; 1; trigger=no end case XX case GO GO:0016787; F:hydrolase activity end case case or GO GO:0046872; F:metal ion binding GO GO:0016151; F:nickel cation binding end case case GO GO:0005737; C:cytoplasm end case XX case KW Cytoplasm end case case KW Hydrolase end case case or KW Metal-binding KW Nickel end case XX FT From: PS51368 FT DOMAIN from..to FT /note="Urease #" FT ACT_SITE 192 FT /note="Proton donor" FT Condition: H FT BINDING 6 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 8 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 89 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="#1" FT /note="via carbamate group" FT Group: 1; Condition: K FT BINDING 89 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="#2" FT /note="via carbamate group" FT Group: 1; Condition: K FT BINDING 118 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 144 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 232 FT /ligand="Ni(2+)" FT /ligand_id="ChEBI:CHEBI:49786" FT /ligand_label="#1" FT Group: 2; Condition: D FT BINDING 91 FT /ligand="substrate" FT Condition: H XX Chop: Nter=0; Cter=0; Size: 420-470; Related: None; Repeats: 1; Topology: Undefined; Example: Q5KCQ6; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.21 2022/11/19 // AC PRU00701; DC Domain; TR PROSITE; PS51369; TCP; 1; level=0 XX Names: TCP domain Function: So far, members of the TCP family have only been found in plants and function in processes related to cell proliferation. The TCP domain is probably involved in DNA-binding and protein-protein interactions. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51369 FT DOMAIN from..to FT /note="TCP #" XX Chop: Nter=0; Cter=0; Size: 50-65; Related: None; Repeats: 1; Topology: Undefined; Example: Q9SPT4; Scope: Eukaryota; Viridiplantae; Embryophyta Comments: None XX # Revision 1.7 2022/06/27 // AC PRU00702; DC Domain; TR PROSITE; PS51370; R; 1; level=0 XX Names: R domain Function: Most members of the CYC/TB1 subfamily have an R domain, predicted to form a coiled coil that may mediate protein-protein interactions. XX XX FT From: PS51370 FT DOMAIN from..to FT /note="R #" XX Chop: Nter=0; Cter=0; Size: 15-25; Related: None; Repeats: 1; Topology: Undefined; Example: Q9SPT4; Scope: Eukaryota; Viridiplantae; Embryophyta Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00703; DC Domain; TR PROSITE; PS51371; CBS; 1; level=0 XX Names: CBS domain Function: CBS domains act as autoinhibitory regulatory units in some proteins and activate or further inhibit protein function upon binding to adenosine nucleotides (AMP, ADP, ATP, S-adenosyl methionine, NAD, diadenosine polyphosphates). XX XX KW CBS domain XX FT From: PS51371 FT DOMAIN from..to FT /note="CBS #" XX Chop: Nter=0; Cter=0; Size: 26-97; Related: None; Repeats: 1-4; Topology: Undefined; Example: A3LQC5; Scope: Eukaryota Bacteria Archaea Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00704; DC Domain; TR PROSITE; PS51372; PRD_2; 1; level=0 XX Names: PRD domain Function: PRDs in transcrptional antiterminators and activators are phosphoenolpyruvate:sugar phosphotransferase system (PTS) PTS regulatory targets that are (de)phosphorylated in response to the availability of carbon sources. XX XX DR PROSITE; PS00654; PRD_1; 1; trigger=no case KW Phosphoprotein end case XX FT From: PS51372 FT DOMAIN from..to FT /note="PRD #" FT MOD_RES 38 FT /note="Phosphohistidine" FT Tag: phospho; Condition: H FT MOD_RES 97 FT /note="Phosphohistidine" FT Tag: phospho; Condition: H XX Chop: Nter=0; Cter=0; Size: 95-123; Related: None; Repeats: 1-2; Topology: Undefined; Example: P46321; Scope: Bacteria Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00705; DC Domain; TR PROSITE; PS51373; HIPIP; 1; level=0 XX Names: High potential iron-sulfur proteins family Function: High potential iron-sulfur proteins (HiPIP) are a specific class of high-redox potential 4Fe-4S ferredoxins that functions in anaerobic electron transport and which occurs commonly in purple photosynthetic bacteria and in other bacteria, such as Paracoccus denitrificans and Thiobacillus ferrooxidans. XX DE AltName: Full=High-potential iron-sulfur protein; DE Short=HiPIP; XX CC -!- FUNCTION: Specific class of high-redox-potential 4Fe-4S ferredoxins. CC Functions in anaerobic electron transport in most purple and in some CC other photosynthetic bacteria and in at least one genus (Paracoccus) of CC halophilic, denitrifying bacteria. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP) CC family. XX GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0005506; F:iron ion binding GO GO:0051536; F:iron-sulfur cluster binding GO GO:0046872; F:metal ion binding GO GO:0006810; P:transport GO GO:0042597; C:periplasmic space XX KW 4Fe-4S KW Electron transport KW Iron KW Iron-sulfur KW Metal-binding KW Periplasm KW Transport XX FT From: PS51373 FT BINDING 36 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Condition: C FT BINDING 39 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Condition: C FT BINDING 53 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Condition: C FT BINDING 67 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Condition: C XX Chop: Nter=0; Cter=0; Size: 55-90; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P59860; Scope: Bacteria Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00706; DC Domain; TR PROSITE; PS51374; NDPK_LIKE; 1; level=0 XX Names: Nucleoside diphosphate kinase (NDK)-like domain Function: All Nme enzymes possess at least one nucleoside diphosphate kinase (NDK)-like domain of ~150 amino acids. XX case and DE + AltName: Full=Nucleoside diphosphate kinase; DE Short=NDK; DE Short=NDP kinase {ECO:0000255|HAMAP-Rule:MF_00451}; DE EC=2.7.4.6; CC -!- CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'- CC diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + CC ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, CC ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CC -!- CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP CC = a ribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:18113, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC -!- COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; end case CC -!- SIMILARITY: Belongs to the NDK family. XX case and DR PROSITE; PS00469; NDPK; 1; trigger=no XX GO GO:0004550; F:nucleoside diphosphate kinase activity GO GO:0006241; P:CTP biosynthetic process GO GO:0005524; F:ATP binding GO GO:0006228; P:UTP biosynthetic process GO GO:0006183; P:GTP biosynthetic process GO GO:0016310; P:phosphorylation GO GO:0046872; F:metal ion binding XX KW Kinase KW Transferase KW Nucleotide-binding KW ATP-binding KW Magnesium KW Metal-binding KW Nucleotide metabolism KW Phosphoprotein end case XX FT From: PS51374 FT DOMAIN from..to FT /note="NDPK-like #" case FT ACT_SITE 114 FT /note="Pros-phosphohistidine intermediate" FT Tag: act_site; Condition: H end case FT BINDING 8 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: K FT BINDING 56 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: F FT BINDING 84 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: R FT BINDING 90 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: T FT BINDING 101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: R FT BINDING 111 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: N XX Chop: Nter=0; Cter=0; Size: 21-180; Related: None; Repeats: 1-3; Topology: Undefined; Example: C3LT09; Scope: Bacteria Eukaryota Archaea Viruses; Mimivirus bradfordmassiliense Comments: None; XX # Revision 1.1 2023/12/20 // AC PRU00707; DC Domain; TR PROSITE; PS51376; DBB; 1; level=0 XX Names: DBB domain Function: The DBB domain in both Dof and BCAP is required to mediate self- association in yeast cells, indicating that this domain may have a more general role in mediating protein-protein interactions. XX XX FT From: PS51376 FT DOMAIN from..to FT /note="DBB #" XX Chop: Nter=0; Cter=0; Size: 125-130; Related: None; Repeats: 1; Topology: Cytoplasmic; Example: Q8NDB2; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00708; DC Domain; TR PROSITE; PS51375; PPR; 1; level=0 XX Names: AdoMet activation domain Function: Some of the proteins containing PPR repeats have been shown to play a role in post-transcriptional processes within organelles and they are thought to be sequence-specific RNA-binding proteins. XX FT From: PS51375 FT REPEAT entry..exit FT /note="PPR #" XX Chop: Nter=0; Cter=0; Size: 25-45; Related: None; Repeats: 1-30; Topology: Undefined; Example: Q76C99; Scope: Eukaryota Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00709; DC Domain; TR PROSITE; PS51377; KIND; 1; level=0 XX Names: KIND domain Function: The KIND (kinase non-catalytic C-lobe domain) is a putative protein interaction domain, which has been identified as being similar to the C- terminal protein kinase catalytic fold (C lobe). XX XX FT From: PS51377 FT DOMAIN from..to FT /note="KIND #" XX Chop: Nter=0; Cter=0; Size: 70-240; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: Q76NI1; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00710; DC Domain; TR PROSITE; PS51378; INVERT_DEFENSINS; 1; level=0 XX Names: Invertebrate defensins family arthropod defensins family insect defensins family Function: Invertebrate defensins are a family of cysteine-rich antimicrobial peptides, primarily active against Gram-positive bacteria. XX CC -!- FUNCTION: Antibacterial peptide mostly active against Gram-positive CC bacteria. case CC -!- SUBCELLULAR LOCATION: Secreted. end case CC -!- SIMILARITY: Belongs to the invertebrate defensin family. XX GO GO:0006952; P:defense response XX KW Antibiotic KW Antimicrobial KW Defensin case KW Disulfide bond end case XX FT From: PS51378 FT DISULFID 4..25 FT Tag: disulf; Condition: C-x*-C FT DISULFID 11..31 FT Tag: disulf; Condition: C-x*-C FT DISULFID 15..33 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 25-50; Related: None; Repeats: 1; Topology: Undefined; Example: P91793; Scope: Eukaryota; Fungi Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00711; DC Domain; TR PROSITE; PS51379; 4FE4S_FER_2; 1; level=0 XX Names: 4Fe-4S ferredoxin-type domain Function: binds 4Fe-4S XX case CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds #1 [4Fe-4S] cluster.; end case XX DR PROSITE; PS00198; 4FE4S_FER_1; 0-13; trigger=no XX case GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0046872; F:metal ion binding XX KW 4Fe-4S KW Iron KW Iron-sulfur KW Metal-binding end case XX FT From: PS51379 FT DOMAIN from..to FT /note="4Fe-4S ferredoxin-type #" case not FT BINDING 10 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 13 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 16 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 20 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C end case XX Chop: Nter=0; Cter=0; Size: 15-45; Related: None; Repeats: 1; Topology: Undefined; Example: P58324; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.10 2022/11/19 // AC PRU00712; DC Domain; TR PROSITE; PS51380; EXS; 1; level=0 XX Names: EXS domain Function: The function of the EXS domain is unknown, although it could be involved in either phosphate transport or sensing or in sorting proteins to endomembrane. XX XX FT From: PS51380 FT DOMAIN from..to FT /note="EXS #" XX Chop: Nter=0; Cter=0; Size: 175-215; Related: None; Repeats: 1; Topology: Undefined; Example: Q8S403; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00713; DC Domain; TR PROSITE; PS51381; C2_B9; 1; level=0 XX Names: C2 B9-type domain Function: The B9-type C2 domain is found in ciliary basal body associated proteins. B9-type C2 domain proteins show a very simple architecture with nearly all members being composed of just the C2 domain. XX XX FT From: PS51381 FT DOMAIN from..to FT /note="C2 B9-type #" XX Chop: Nter=0; Cter=0; Size: 115-130; Related: None; Repeats: 1; Topology: Undefined; Example: Q9NXB0; Scope: Eukaryota Comments: None XX # Revision 1.4 2020/01/06 // AC PRU00714; DC Domain; TR PROSITE; PS51382; SPX; 1; level=0 XX Names: SPX domain Function: The tripartite SPX domain could function as a sensor for inorganic phosphate (Pi) level and is most likely a domain for protein interaction. Possibly all SPX domains bind G-protein beta-subunits for the purpose of signal transduction. XX XX FT From: PS51382 FT DOMAIN from..to FT /note="SPX #" XX Chop: Nter=0; Cter=0; Size: 95-485; Related: None; Repeats: 1; Topology: Undefined; Example: Q8S403; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00715; DC Domain; TR PROSITE; PS51383; YJEF_C_3; 1; level=0 XX Names: YjeF C-terminal domain Function: The YjeF C-terminal domain has an alpha/beta fold and shows high structural homology to the members of a ribokinase-like superfamily. XX XX DR PROSITE; PS01049; YJEF_C_1; 1; trigger=no DR PROSITE; PS01050; YJEF_C_2; 1; trigger=no XX FT From: PS51383 FT DOMAIN from..to FT /note="YjeF C-terminal #" XX Chop: Nter=0; Cter=0; Size: 250-330; Related: None; Repeats: 1; Topology: Undefined; Example: P94368; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00716; DC Domain; TR PROSITE; PS51384; FAD_FR; 1; level=0 XX Names: Ferredoxin reductase-type FAD-binding domain Function: Binds flavin adenine dinucleotide (FAD) XX XX FT From: PS51384 FT DOMAIN from..to FT /note="FAD-binding FR-type #" XX Chop: Nter=0; Cter=0; Size: 71-135; Related: None; Repeats: 1; Topology: Undefined; Example: P00387; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00717; DC Domain; TR PROSITE; PS51386; RINT1_TIP20; 1; level=0 XX Names: RINT1/TIP20 domain Function: The RINT1/TIP20 domain might be a protein-protein interaction module necessary for the formation of functional complexes. XX XX FT From: PS51386 FT DOMAIN from..to FT /note="RINT1/TIP20 #" XX Chop: Nter=0; Cter=0; Size: 550-585; Related: None; Repeats: 1; Topology: Undefined; Example: P33891; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00718; DC Domain; TR PROSITE; PS51387; FAD_PCMH; 1; level=0 XX Names: PCMH-type FAD-binding domain Function: this domain binds the flavin adenine dinucleotide (FAD). XX XX DR PROSITE; PS51387; FAD_PCMH; 1; trigger=no XX FT From: PS51387 FT DOMAIN from..to FT /note="FAD-binding PCMH-type #" XX Chop: Nter=0; Cter=0; Size: 108-321; Related: None; Repeats: 1; Topology: Undefined; Example: O00116; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00719; DC Domain; TR PROSITE; PS51385; YJEF_N; 1; level=0 XX Names: YjeF N-terminal domain Function: The YjeF N-terminal domains represent a novel version of the Rossmann fold, one of the most common protein folds in nature observed in numerous enzyme families, that has acquired a set of catalytic residues and structural features that distinguish them from the conventional dehydrogenases. XX XX FT From: PS51385 FT DOMAIN from..to FT /note="YjeF N-terminal #" XX Chop: Nter=0; Cter=0; Size: 195-245; Related: None; Repeats: 1; Topology: Undefined; Example: P31806; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00720; DC Domain; TR PROSITE; PS51388; GED; 1; level=0 XX Names: GED domain Function: Dynamin superfamily members are large GTPases, conserved through evolution mainly described as mechanochemical enzymes involved in membrane scission events. All members display a common architecture: a large GTPase domain followed by a 'middle domain' of ill-defined function and a downstream coiled-coil GTPase effector domain (GED) that functions in higher order assembly and as a GTPase activating protein (GAP) for dynamin's GTPase activity. XX XX FT From: PS51388 FT DOMAIN from..to FT /note="GED #" XX Chop: Nter=0; Cter=0; Size: 70-100; Related: None; Repeats: 1; Topology: Undefined; Example: Q05193; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00721; DC Domain; TR PROSITE; PS51389; XIN; 1; level=0 XX Names: Xin repeat Function: The Xin repeat is an actin-binding motif, capable of binding to actin filaments and organizing microfilaments into loose networks. XX CC -!- DOMAIN: Xin repeats bind F-actin. CC -!- SIMILARITY: Belongs to the Xin family. XX GO GO:0003779; F:actin binding XX KW Actin-binding XX FT From: PS51389 FT REPEAT from..to FT /note="Xin #" XX Chop: Nter=0; Cter=0; Size: 15-20; Related: None; Repeats: 17-28; Topology: Undefined; Example: Q5PZ43; Scope: Eukaryota; Metazoa; Craniata Comments: None XX # Revision 1.4 2019/11/21 // AC PRU00722; DC Domain; TR PROSITE; PS51390; WAP; 1; level=0 XX Names: WAP four-disulfide core (4-DSC) domain Function: The 'four-disulfide core' or WAP domain comprises 8 cysteine residues involved in disulfide bonds. Single or multiple copies occur in eukaryotic proteins, such as whey acidic protein (WAP), antileukoproteinase and elastase-inhibitor proteins. XX XX case KW Disulfide bond end case XX FT From: PS51390 case and and and and and and and FT DOMAIN entry..exit FT /note="WAP #" else FT DOMAIN entry..exit FT /note="WAP #; atypical" end case FT DISULFID 8..36 FT Tag: disulf; Condition: C-x*-C FT DISULFID 18..40 FT Tag: disulf; Condition: C-x*-C FT DISULFID 23..35 FT Tag: disulf; Condition: C-x*-C FT DISULFID 29..44 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=5; Cter=3; Size: 30-65; Related: None; Repeats: 1-7; Topology: Undefined; Example: Q6V9X0; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00723; DC Domain; TR PROSITE; PS50103; ZF_C3H1; 1; level=0 XX Names: Zinc finger C3H1-type Function: In various proteins the C3H1-type zinc finger has been shown to interact with the 3'-untranslated region of mRNAs XX XX KW Zinc-finger KW Zinc KW Metal-binding XX FT From: PS50103 FT ZN_FING entry..exit FT /note="C3H1-type #" XX Chop: Nter=0; Cter=0; Size: 23-50; Related: None; Repeats: 1-10; Topology: Undefined; Example: Q96K80; Scope: Eukaryota Viruses Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00724; DC Domain; TR PROSITE; PS51391; CID; 1; level=0 XX Names: CID domain Function: Several RNA-processing factors recognize the C-terminal domain (CTD) of the large subunit of RNA polymerase II by means of a conserved CTD- interacting domain (CID). XX XX FT From: PS51391 FT DOMAIN from..to FT /note="CID #" XX Chop: Nter=0; Cter=0; Size: 125-165; Related: None; Repeats: 1; Topology: Undefined; Example: O94913; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00725; DC Domain; TR PROSITE; PS51392; KEN; 1; level=0 XX Names: KEN domain Function: The dimerization of the kinase domain activates the ribonuclease function of the ~135-residue globular kinase-extension nuclease (KEN) domain made of eight helices. XX XX FT From: PS51392 FT DOMAIN from..to FT /note="KEN #" XX Chop: Nter=0; Cter=0; Size: 119-189; Related: None; Repeats: 1; Topology: Undefined; Example: P32361; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00726; DC Domain; TR PROSITE; PS51393; LIPOXYGENASE_3; 1; level=0 XX Names: Lipoxygenase iron-binding catalytic domain Function: Lipoxygenases (EC 1.13.11.-) form a class of iron-containing fatty acid dioxygenases, which catalyze the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. XX case DE AltName: Full=lipoxygenase; DE EC=1.13.11.-; XX CC -!- FUNCTION: Plant lipoxygenases may be involved in a number of diverse CC aspects of plant physiology including growth and development, pest CC resistance, and senescence or responses to wounding. Catalyzes the CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene CC structure. end case XX case CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Note=Binds 1 Fe cation per subunit.; XX end case case CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. end case XX case CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case case CC -!- SUBCELLULAR LOCATION: Periplasm. end case XX XX case and DR PROSITE; PS00711; LIPOXYGENASE_1; 1; trigger=no end case case DR PROSITE; PS00081; LIPOXYGENASE_2; 1; trigger=no end case XX GO GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen case GO GO:0005506; F:iron ion binding GO GO:0046872; F:metal ion binding end case GO GO:0016491; F:oxidoreductase activity case GO GO:0006633; P:fatty acid biosynthetic process GO GO:0008610; P:lipid biosynthetic process GO GO:0031408; P:oxylipin biosynthetic process end case case GO GO:0042597; C:periplasmic space end case XX KW Dioxygenase case KW Iron KW Metal-binding end case KW Oxidoreductase case KW Lipid metabolism KW Lipid biosynthesis KW Fatty acid biosynthesis KW Fatty acid metabolism KW Oxylipin biosynthesis end case case KW Periplasm end case XX FT From: PS51393 FT DOMAIN from..to FT /note="Lipoxygenase #" FT BINDING 340 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 345 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 530 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 534 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: [NH] FT BINDING 678 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT Group: 1; Condition: I XX Chop: Nter=1; Cter=0; Size: 540-730; Related: None; Repeats: 1; Topology: Undefined; Example: Q84YK8; Q9BYJ1; Q8RNT4; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00727; DC Domain; TR PROSITE; PS51394; PFU; 1; level=0 XX Names: PFU domain Function: In addition to ubiquitin, the PFU domain of DOA1 has been shown to bind to the SH3 domain. XX XX FT From: PS51394 FT DOMAIN from..to FT /note="PFU #" XX Chop: Nter=0; Cter=0; Size: 95-105; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y263; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00729; DC Domain; TR PROSITE; PS51396; PUL; 1; level=0 XX Names: PUL domain Function: The PUL domain is a protein-protein interaction domain. XX XX FT From: PS51396 FT DOMAIN from..to FT /note="PUL #" XX Chop: Nter=0; Cter=0; Size: 250-265; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y263; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00730; DC Domain; TR PROSITE; PS51397; WLM; 1; level=0 XX Names: WLM domain Function: The WLM (WSS1-like metalloprotease) domain is a globular domain related to the zincin-like superfamily of Zn-dependent peptidase. Since the WLM domain contains all known active site residues of zincins, it is predicted to be a catalytically active peptidase domain. XX XX DR PROSITE; PS00142; ZINC_PROTEASE; 0-1; trigger=no XX FT From: PS51397 FT DOMAIN from..to FT /note="WLM #" XX Chop: Nter=0; Cter=0; Size: 165-215; Related: None; Repeats: 1; Topology: Undefined; Example: P38838; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00731; DC Domain; TR PROSITE; PS51398; PAW; 1; level=0 XX Names: PAW domain Function: The C-terminal PAW domain of PNGase binds to the mannose moieties of N-linked oligosaccharide chains. XX CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase CC family. XX FT From: PS51398 FT DOMAIN from..to FT /note="PAW #" XX Chop: Nter=0; Cter=0; Size: 185-210; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q96IV0; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00732; DC Domain; TR PROSITE; PS51399; SEP; 1; level=0 XX Names: SEP domain Function: The function of the SEP domain is as yet unknown but it has been proposed to act as a reversible competitive inhibitor of the lysosomal cysteine protease cathepsin L. XX XX FT From: PS51399 FT DOMAIN from..to FT /note="SEP #" XX Chop: Nter=0; Cter=0; Size: 60-70; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9UNZ2; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00734; DC Domain; TR PROSITE; PS51401; CHORD; 1; level=0 XX Names: CHORD domain Function: Cysteine- and histidine-rich domains (CHORDs) are 60-amino acid modules that bind two zinc ions. XX XX case or KW Zinc KW Metal-binding end case XX FT From: PS51401 FT DOMAIN from..to FT /note="CHORD #" FT BINDING 1 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 55-65; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: Q9UHD1; Scope: Eukaryota Comments: None XX # Revision 1.6 2022/11/19 // AC PRU00736; DC Domain; TR PROSITE; PS51403; NC1_IV; 1; level=0 XX Names: Collagen IV carboxyl-terminal non-collagenous (NC1) domain Function: Each type IV chain contains a long triple-helical collagenous domain flanked by a short 7S domain of 25 residues and a globular non-collagenous NC1 domain of ~230 residues at the N- and C-terminus, respectively. XX CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain CC (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats CC in the long central triple-helical domain (which may cause flexibility CC in the triple helix), and a short N-terminal triple-helical 7S domain. CC -!- PTM: Prolines at the third position of the tripeptide repeating unit CC (G-X-Y) are hydroxylated in some or all of the chains. CC -!- PTM: Type IV collagens contain numerous cysteine residues which are CC involved in inter- and intramolecular disulfide bonding. 12 of these, CC located in the NC1 domain, are conserved in all known type IV CC collagens. CC -!- SIMILARITY: Belongs to the type IV collagen family. XX GO GO:0005604; C:basement membrane GO GO:0031012; C:extracellular matrix XX KW Basement membrane KW Collagen KW Extracellular matrix KW Secreted case KW Disulfide bond end case XX FT From: PS51403 FT DOMAIN from..to FT /note="Collagen IV NC1 #" FT DISULFID 16..106 FT Tag: disulf; Condition: C-x*-C FT DISULFID 49..103 FT Tag: disulf; Condition: C-x*-C FT DISULFID 61..67 FT Tag: disulf; Condition: C-x*-C FT DISULFID 125..220 FT Tag: disulf; Condition: C-x*-C FT DISULFID 159..217 FT Tag: disulf; Condition: C-x*-C FT DISULFID 171..177 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 220-230; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P02462; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.10 2019/11/21 // AC PRU00739; DC Domain; TR PROSITE; PS51406; FIBRINOGEN_C_2; 1; level=0 XX Names: Fibrinogen C-terminal domain Function: The C-terminal domain of the alpha, beta and gamma chains of fibrinogen can function as a molecular recognition unit that interacts with either proteins or carbohydrates. XX case DR PROSITE; PS00514; FIBRINOGEN_C_1; 1; trigger=no end case XX case KW Disulfide bond end case XX FT From: PS51406 FT DOMAIN from..to FT /note="Fibrinogen C-terminal #" FT DISULFID 10..39 FT Tag: disulf; Condition: C-x*-C FT DISULFID 162..175 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=2; Cter=24; Size: 50-265; Related: None; Repeats: 1; Topology: Undefined; Example: O43827; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.5 2019/11/21 // AC PRU00740; DC Domain; TR PROSITE; PS51407; LAMP_3; 1; level=0 XX Names: Lysosome-associated membrane glycoprotein (lamp) family LAMP family Function: Lysosome-associated membrane glycoproteins (lamp) are integral membrane proteins, specific to lysosomes. XX case CC -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I membrane CC protein. else CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. end case CC -!- SIMILARITY: Belongs to the LAMP family. XX DR General; Transmembrane; -; 1; trigger=no XX case DR PROSITE; PS00310; LAMP_1; 1; trigger=no end case case DR PROSITE; PS00311; LAMP_2; 1; trigger=no end case XX case GO GO:0005764; C:lysosome GO GO:0005765; C:lysosomal membrane end case GO GO:0016020; C:membrane XX case KW Lysosome end case KW Membrane KW Transmembrane case KW Disulfide bond end case XX FT From: PS51407 case FT TRANSMEM 352..373 FT /note="Helical" FT TOPO_DOM 374..387 FT /note="Cytoplasmic" else FT TRANSMEM 352..376 FT /note="Helical" FT TOPO_DOM 377..387 FT /note="Cytoplasmic" end case FT DISULFID 11..50 FT Tag: disulf; Condition: C-x*-C FT DISULFID 124..160 FT Tag: disulf; Condition: C-x*-C FT DISULFID 202..240 FT Tag: disulf; Condition: C-x*-C FT DISULFID 308..345 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 230-410; Related: None; Repeats: 1; Topology: Undefined; Example: P13473; Q7TST5; Q11117; Scope: Eukaryota; Metazoa Comments: None XX # Revision 1.8 2022/09/30 // AC PRU00741; DC Domain; TR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 1; level=0 XX Names: Transferrin-like domain Function: The transferrin family is a group of glycosylated proteins found in both vertebrates and invertebrates. Most family members contain two transferrin-like domains of around 340 amino acids, the result of an ancient duplication event. XX case DE + RecName: EC=3.4.21.-; end case CC -!- SIMILARITY: Belongs to the transferrin family. case DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1; trigger=no DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 1; trigger=no DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 1; trigger=no end case XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0004252; F:serine-type endopeptidase activity end case case GO GO:0005506; F:iron ion binding GO GO:0046872; F:metal ion binding end case XX case KW Hydrolase KW Protease KW Serine protease end case case KW Iron KW Metal-binding end case case KW Disulfide bond end case XX FT From: PS51408 FT DOMAIN from..to FT /note="Transferrin-like #" FT ACT_SITE 68 FT Group: 1; Condition: K FT ACT_SITE 256 FT /note="Nucleophile" FT Group: 1; Condition: S FT BINDING 56 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="#1" FT Group: 2; Condition: D FT BINDING 85 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="#1" FT Group: 2; Condition: Y FT BINDING 184 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="#1" FT Group: 2; Condition: Y FT BINDING 249 FT /ligand="Fe(3+)" FT /ligand_id="ChEBI:CHEBI:29034" FT /ligand_label="#1" FT Group: 2; Condition: H FT BINDING 111 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="#1" FT Group: 2; Condition: T FT BINDING 115 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="#1" FT Group: 2; Condition: R FT BINDING 117 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="#1" FT Group: 2; Condition: A FT BINDING 118 FT /ligand="hydrogencarbonate" FT /ligand_id="ChEBI:CHEBI:17544" FT /ligand_label="#1" FT Group: 2; Condition: G FT DISULFID 4..41 FT Tag: disulf; Condition: C-x*-C FT DISULFID 14..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 109..190 FT Tag: disulf; Condition: C-x*-C FT DISULFID 151..169 FT Tag: disulf; Condition: C-x*-C FT DISULFID 154..175 FT Tag: disulf; Condition: C-x*-C FT DISULFID 166..173 FT Tag: disulf; Condition: C-x*-C FT DISULFID 227..241 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 245-610; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: P02788; Scope: Eukaryota Comments: None; XX # Revision 1.13 2022/11/19 // AC PRU00742; DC Domain; TR PROSITE; PS51409; ARGINASE_2; 1; level=0 XX Names: Arginase family ureohydrolase superfamily Function: Arginase family proteins are ureohydrolases with important roles in arginine/agmatine metabolism, the urea cycle, histidine degradation, and other pathways. The family includes arginase and related enzymes of ~300 amino acids that typically contain two manganese ions in the active site. XX case and and and and and DE + RecName: EC=3.5.3.-; end case XX case and and and and and CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 2 manganese ions per subunit.; else case or or or or or CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; end case CC -!- SIMILARITY: Belongs to the arginase family. XX case and DR PROSITE; PS01053; ARGINASE_1; 1; trigger=no end case XX case or or or or or GO GO:0016787; F:hydrolase activity GO GO:0030145; F:manganese ion binding GO GO:0046872; F:metal ion binding XX KW Hydrolase KW Manganese KW Metal-binding end case XX FT From: PS51409 FT BINDING 96 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#1" FT Condition: [HN] FT BINDING 120 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#1" FT Condition: D FT BINDING 120 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#2" FT Condition: D FT BINDING 122 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#2" FT Condition: H FT BINDING 124 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#1" FT Condition: D FT BINDING 213 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#1" FT Condition: [DC] FT BINDING 213 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#2" FT Condition: [DC] FT BINDING 215 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="#2" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 260-350; Related: None; Repeats: 1; Topology: Undefined; Example: Q9HQD7; P46637; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.8 2022/11/19 // AC PRU00744; DC Domain; TR PROSITE; PS51411; PSP1_C; 1; level=0 XX Names: PSP1 C-terminal domain Function: The actual biological significance of the PSP1 C-terminal domain has not yet been clearly established. XX XX FT From: PS51411 FT DOMAIN from..to FT /note="PSP1 C-terminal #" XX Chop: Nter=0; Cter=0; Size: 85-115; Related: None; Repeats: 1; Topology: Undefined; Example: P50896; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/21 // AC PRU00745; DC Domain; TR PROSITE; PS51412; MACPF_2; 1; level=0 XX Names: Membrane attack complex/perforin (MACPF) domain Function: The MACPF domain oligomerizes, undergoes conformational change, and is required for lytic activity. XX XX DR PROSITE; PS00279; MACPF_1; 1; trigger=no XX FT From: PS51412 FT DOMAIN from..to FT /note="MACPF #" XX Chop: Nter=0; Cter=0; Size: 315-385; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q29RU4; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00746; DC Domain; TR PROSITE; PS51413; DBINO; 1; level=0 XX Names: DBINO domain Function: The DBINO (DNA binding domain of INO80) domain is characteristic of the INO80 subfamily and is predicted to have DNA-binding function. XX CC -!- FUNCTION: ATPase component of the INO80 complex which remodels CC chromatin by shifting nucleosomes and is involved in DNA repair. CC -!- SUBUNIT: Component of the INO80 chromatin-remodeling complex. CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0006325; P:chromatin organization GO GO:0006974; P:DNA damage response GO GO:0006281; P:DNA repair GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Activator KW DNA damage KW DNA repair KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51413 FT DOMAIN from..to FT /note="DBINO #" XX Chop: Nter=0; Cter=0; Size: 125-135; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: O14148; Scope: Eukaryota Comments: None; XX # Revision 1.9 2023/02/13 // AC PRU00747; DC Domain; TR PROSITE; PS51414; HSR; 1; level=0 XX Names: HSR domain Function: The HSR domain is a nuclear dot (DT) targeting and dimerization domain of ~100 amino acids. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS51414 FT DOMAIN from..to FT /note="HSR #" XX Chop: Nter=0; Cter=0; Size: 100-120; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: P23497; Scope: Eukaryota; Vertebrata Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00748; DC Domain; TR PROSITE; PS51415; XYLOSE_ISOMERASE; 1; level=0 XX Names: Xylose isomerase family Function: Xylose isomerase (EC 5.3.1.5) is an enzyme found in microorganisms and plants which catalyzes the interconversion of the aldo sugars D-xylose or D-glucose to the keto sugars D-xylulose and D-fructose. The catalytic activity requires magnesium, cobalt or manganese. XX case DE AltName: Full=Xylose isomerase; DE EC=5.3.1.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-xylose = alpha-D-xylulofuranose; Xref=Rhea:RHEA:22816, CC ChEBI:CHEBI:28518, ChEBI:CHEBI:188998; EC=5.3.1.5; end case case not CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 magnesium ions per subunit.; else case CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 2 manganese ions per subunit.; end case CC -!- SUBUNIT: Homotetramer. case CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case CC -!- SIMILARITY: Belongs to the xylose isomerase family. XX GO GO:0009045; F:xylose isomerase activity GO GO:0042732; P:D-xylose metabolic process GO GO:0005975; P:carbohydrate metabolic process GO GO:0016853; F:isomerase activity GO GO:0000287; F:magnesium ion binding GO GO:0046872; F:metal ion binding GO GO:0006098; P:pentose-phosphate shunt case GO GO:0030145; F:manganese ion binding end case case GO GO:0005737; C:cytoplasm end case XX KW Carbohydrate metabolism KW Isomerase KW Magnesium KW Metal-binding KW Pentose shunt KW Xylose metabolism case KW Manganese end case case KW Cytoplasm end case XX FT From: PS51415 FT ACT_SITE 66 FT Condition: H case not FT BINDING 197 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: E FT BINDING 236 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: H FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D FT BINDING 272 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 274 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT BINDING 304 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Condition: D else case FT BINDING 197 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: E FT BINDING 233 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: E FT BINDING 236 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: H FT BINDING 261 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: D FT BINDING 272 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: D FT BINDING 274 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT Condition: D FT BINDING 304 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT Condition: D end case XX Chop: Nter=0; Cter=0; Size: 370-420; Related: None; Repeats: 1; Topology: Undefined; Example: Q93RJ9; Q9FKK7; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.12 2022/11/19 // AC PRU00749; DC Domain; TR PROSITE; PS51416; MIB_HERC2; 1; level=0 XX Names: MIB/HERC2 domain Function: The MIB/HERC2 domain is a conserved region of ~80 amino acids, which has been identified in animal Mind bomb 1 and 2 (MIB1 and MIB2) and HERC2 E3 ubiquitin ligases. XX XX GO GO:0006511; P:ubiquitin-dependent protein catabolic process XX KW Ubl conjugation pathway XX FT From: PS51416 FT DOMAIN from..to FT /note="MIB/HERC2 #" XX Chop: Nter=0; Cter=0; Size: 65-85; Related: None; Repeats: 1-2; Topology: Undefined; Example: O95714; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00750; DC Domain; TR PROSITE; PS51425; SCD; 1; level=0 XX Names: Stromalin conservative (SCD) domain Function: Stromalins are represented in several organisms from yeast to humans and are characterized by the stromalin conservative domain (SCD), an 86 amino acid motif found in all proteins of the family described to date. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS51425 FT DOMAIN from..to FT /note="SCD #" XX Chop: Nter=0; Cter=0; Size: 85-95; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q8WVM7; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00751; DC Domain; TR PROSITE; PS51426; ABL; 1; level=0 XX Names: ABL domain Function: The ABL (Alpha/Beta/Loop) domain is found between the histidine kinase domain and the response regulatory domain of all RcsC sequences of all enterobacteria sequenced so far. XX XX FT From: PS51426 FT DOMAIN from..to FT /note="ABL #" XX Chop: Nter=0; Cter=0; Size: 100-105; Related: None; Repeats: 1; Topology: Undefined; Example: P14376; Scope: Bacteria; Enterobacteriaceae Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00757; DC Domain; TR PROSITE; PS51423; MIRO; 1; level=0 XX Names: Miro domain Function: Small GTPase domain found in mitochondrial proteins involved in mitochondrial trafficking. XX DE + RecName: EC=3.6.5.-; XX CC -!- SIMILARITY: Belongs to the mitochondrial Rho GTPase family. XX GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity GO GO:0007005; P:mitochondrion organization GO GO:0010821; P:regulation of mitochondrion organization GO GO:0007266; P:Rho protein signal transduction XX KW GTP-binding KW Hydrolase KW Membrane KW Mitochondrion KW Mitochondrion outer membrane KW Nucleotide-binding XX FT From: PS51423 FT DOMAIN from..to FT /note="Miro #" XX Chop: Nter=0; Cter=0; Size: 160-225; Related: None; Repeats: 1; Topology: Undefined; Example: Q6CY37; Scope: Eukaryota Comments: None; XX # Revision 1.2 2022/09/30 // AC PRU00758; DC Domain; TR PROSITE; PS51424; ROC; 1; level=0 XX Names: small GTPase superfamily. Roc family Function: Small GTPase domain found always associated to a COR domain. XX GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity GO GO:0007264; P:small GTPase mediated signal transduction GO GO:0007165; P:signal transduction XX KW GTP-binding KW Hydrolase KW Nucleotide-binding XX FT From: PS51424 FT DOMAIN from..to FT /note="Roc #" FT BINDING 14..21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 65..69 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT BINDING 124..127 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8MVR1; Scope: Eukaryota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU00760; DC Domain; TR PROSITE; PS51430; KAIA_N; 1; level=0 XX Names: KaiA N-terminal domain Function: Although the fold of the kaiA N-terminal domain is that of a canonical receiver domain, the primary sequence is dissimilar, and it lacks the conserved aspartate residue necessary for phosphorylation. KaiA activation most likely involves direct protein-protein interactions of the N- terminal domain that result in functional modulation of the C-terminal effector domain. XX XX FT From: PS51430 FT DOMAIN from..to FT /note="KaiA N-terminal #" XX Chop: Nter=0; Cter=0; Size: 150-175; Related: None; Repeats: 1; Topology: Undefined; Example: Q6L8L7; Scope: Bacteria; Cyanobacteriota Comments: None; XX # Revision 1.4 2023/02/17 // AC PRU00761; DC Domain; TR PROSITE; PS51431; KAIA_C; 1; level=0 XX Names: KaiA C-terminal domain Function: KaiA activation most likely involves direct protein-protein interactions of the N- terminal domain that result in functional modulation of the C-terminal effector domain. XX CC -!- FUNCTION: Component of the kaiABC clock protein complex, which CC constitutes the main circadian regulator in cyanobacteria. The kaiABC CC complex may act as a promoter-nonspecific transcription regulator that CC represses transcription, possibly by acting on the state of chromosome CC compaction. In the complex, it enhances the phosphorylation status of CC kaiC. In contrast, the presence of kaiB in the complex decreases the CC phosphorylation status of kaiC, suggesting that kaiB acts by CC antagonizing the interaction between kaiA and kaiC. A kaiA dimer is CC sufficient to enhance kaiC hexamer phosphorylation. CC -!- SUBUNIT: Homodimer. Component of the kaiABC complex, at least composed CC of a kaiC homohexamer, a kaiB dimer and two kaiA dimers. The kaiABC CC complex also interacts with sasA. CC -!- DOMAIN: The kaiA domain mediates the interaction with kaiC, the CC homodimerization, and is responsible for the clock oscillation CC function. XX GO GO:0007623; P:circadian rhythm XX KW Biological rhythms XX FT From: PS51431 FT DOMAIN from..to FT /note="KaiA C-terminal #" XX Chop: Nter=0; Cter=0; Size: 100-110; Related: None; Repeats: 1; Topology: Undefined; Example: Q6L8L7; Scope: Bacteria; Cyanobacteriota Comments: None; XX # Revision 1.5 2023/02/17 // AC PRU00762; DC Domain; TR PROSITE; PS51433; PNT; 1; level=0 XX Names: Pointed (PNT) domain Function: A role in protein-protein association has been established for the PNT domain. XX XX FT From: PS51433 FT DOMAIN from..to FT /note="PNT #" XX Chop: Nter=0; Cter=0; Size: 80-90; Related: None; Repeats: 1; Topology: Undefined; Example: P51023; Scope: Eukaryota; Metazoa Viruses Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00763; DC Domain; TR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1; level=0 XX Names: AP endonucleases family 2 Function: Endonuclease 4 related enzymes play a role in DNA repair. These nucleases cleave phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. XX case or or DE AltName: Full=Probable endonuclease 4; DE EC=3.1.21.2; DE AltName: Full=Endonuclease IV; DE AltName: Full=Endodeoxyribonuclease IV; else case or or XX DE + RecName: EC=3.1.21.-; end case XX case or or CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end- CC products.; EC=3.1.21.2; end case XX case CC -!- SUBCELLULAR LOCATION: Nucleus. end case case and and CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 3 Zn(2+) ions.; else case or or CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. XX case DR PROSITE; PS00729; AP_NUCLEASE_F2_1; 1; trigger=no end case case and DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1; trigger=no end case case and and DR PROSITE; PS00731; AP_NUCLEASE_F2_3; 1; trigger=no end case XX GO GO:0006974; P:DNA damage response GO GO:0006281; P:DNA repair GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding GO GO:0003677; F:DNA binding case or or or GO GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity GO GO:0004519; F:endonuclease activity GO GO:0004518; F:nuclease activity GO GO:0016787; F:hydrolase activity else case or GO GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity end case case GO GO:0005634; C:nucleus else case or GO GO:0005737; C:cytoplasm end case XX KW DNA damage KW DNA repair KW Hydrolase KW Endonuclease KW Nuclease case or or KW Metal-binding KW Zinc end case case KW Nucleus end case XX FT From: PS51432 FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT Group: 1; Condition: E FT BINDING 143 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: E FT BINDING 177 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: D FT BINDING 180 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT Group: 3; Condition: H FT BINDING 214 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: H FT BINDING 227 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT Group: 3; Condition: D FT BINDING 229 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT Group: 3; Condition: H FT BINDING 259 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT Group: 2; Condition: E XX Chop: Nter=0; Cter=0; Size: 240-305; Related: None; Repeats: 1; Topology: Undefined; Example: A4IR02; Q966U0; Q5UPY4; Q10002; Scope: Bacteria Archaea Eukaryota Viruses Comments: None; XX # Revision 1.12 2023/02/13 // AC PRU00764; DC Domain; TR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1; level=0 XX Names: AP endonucleases family 1 Function: Exonuclease III and AP endonuclease 1 related enzymes play a role in DNA repair. These nucleases cleave phosphodiester bonds at apurinic or apyrimidinic sites (AP sites) to produce new 5'-ends that are base-free deoxyribose 5-phosphate residues. XX case DE AltName: Full=DNA-(apurinic or apyrimidinic site) endonuclease; DE EC=3.1.-.-; else case DE AltName: Full=Exodeoxyribonuclease III; DE Short=Exonuclease III; DE Short=EXO III; DE EC=3.1.11.2; end case XX case CC -!- SUBCELLULAR LOCATION: Nucleus. else case CC -!- CATALYTIC ACTIVITY: CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield CC nucleoside 5'-phosphates.; EC=3.1.11.2; CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family. XX case DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1; trigger=no end case DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1; trigger=no DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0004519; F:endonuclease activity GO GO:0006281; P:DNA repair case GO GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity GO GO:0005634; C:nucleus else case GO GO:0000287; F:magnesium ion binding GO GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity GO GO:0005737; C:cytoplasm end case XX KW DNA damage KW DNA repair KW Hydrolase KW Metal-binding KW Nuclease case KW Endonuclease KW Nucleus else case KW Cytoplasm KW Exonuclease KW Magnesium end case XX FT From: PS51435 FT ACT_SITE 258 FT /note="Proton acceptor" FT Condition: H FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: N FT BINDING 40 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: E FT BINDING 158 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 160 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: N FT BINDING 257 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: D FT BINDING 258 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Condition: H XX Chop: Nter=0; Cter=0; Size: 230-370; Related: None; Repeats: 1; Topology: Undefined; Example: P28352; P44318; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.12 2023/02/13 // AC PRU00765; DC Domain; TR PROSITE; PS51434; NUP_C; 1; level=0 XX Names: Peptidase S59 domain Function: The NUP C-terminal domains of Nup98 and Nup145 possess peptidase S59 autoproteolytic activity. XX XX FT From: PS51434 FT DOMAIN from..to FT /note="Peptidase S59 #" XX Chop: Nter=0; Cter=0; Size: 135-150; Related: None; Repeats: 1; Topology: Undefined; Example: P52948; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00766; DC Domain; TR PROSITE; PS51436; POTYVIRUS_NIA_PRO; 1; level=0 XX Names: Potyvirus NIa protease (NIa-pro) domain Function: The potyvirus NIa-pro has a His-Asp-Cys catalytic triad, which is homologous to the trypsin-like proteases except for Cys replacing Ser. XX XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0006508; P:proteolysis GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51436 FT DOMAIN from..to FT /note="Peptidase C4 #" FT ACT_SITE 46 FT /note="For nuclear inclusion protein A activity" FT Group: 1; Condition: H FT ACT_SITE 81 FT /note="For nuclear inclusion protein A activity" FT Group: 1; Condition: D FT ACT_SITE 151 FT /note="For nuclear inclusion protein A activity" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 942-3491; Related: None; Repeats: 1; Topology: Undefined; Example: P89509; Scope: Viruses; Potyviridae Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00767; DC Domain; TR PROSITE; PS51437; CG_1; 1; level=0 XX Names: CG-1 DNA-binding domain Function: The CG-1 domain of CAMTA recognizes specific CGCG box-containing DNA sequences, and a nearby region activates the transcription. XX XX DR PROSITE; PS50079; NLS_BP; 0-1; trigger=yes XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Activator KW Transcription KW Transcription regulation XX FT From: PS51437 FT DNA_BIND from..to FT /note="CG-1 #" XX Chop: Nter=0; Cter=0; Size: 105-135; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y6Y1; Scope: Eukaryota Comments: None; XX # Revision 1.5 2022/06/27 // AC PRU00768; DC Domain; TR PROSITE; PS50079; NLS_BP; 1; level=-1 XX Names: Bipartite nuclear localization signal Function: The uptake of protein by the nucleus is extremely selective and nuclear proteins must therefore contain within their final structure a signal that specifies selective accumulation in the nucleus. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW Nucleus XX FT From: PS50079 FT MOTIF 1-1..7 FT /note="Nuclear localization signal #" XX Chop: Nter=0; Cter=0; Size: 15-20; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y6Y1; Scope: Eukaryota Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00769; DC Domain; TR PROSITE; PS51438; ALBUMIN_2; 1; level=0 XX Names: Albumin domain Function: A domain consisting of 10 alpha-helices found in serum transport proteins. XX CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. XX GO GO:0005576; C:extracellular region XX KW Secreted case KW Disulfide bond end case XX FT From: PS51438 FT DOMAIN from..to FT /note="Albumin #" FT DISULFID 14..60 FT Tag: disulf; Condition: C-x*-C FT DISULFID 59..67 FT Tag: disulf; Condition: C-x*-C FT DISULFID 83..100 FT Tag: disulf; Condition: C-x*-C FT DISULFID 99..110 FT Tag: disulf; Condition: C-x*-C FT DISULFID 137..182 FT Tag: disulf; Condition: C-x*-C FT DISULFID 181..190 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 30-230; Related: None; Repeats: 1-7; Topology: Not cytoplasmic; Example: P49822; Scope: Eukaryota; Vertebrata Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00770; DC Domain; TR PROSITE; PS51439; MENTAL; 1; level=0 XX Names: MENTAL domain Function: The ~170-amino acid MENTAL (MLN64 N-terminal) domain mediates MLN64 and MENTHO homo- and hetero-interactions, targets both proteins to late endosomes and binds cholesterol. XX XX DR General; Transmembrane; -; 4; trigger=strict XX GO GO:0015485; F:cholesterol binding GO GO:0120020; F:cholesterol transfer activity GO GO:0005768; C:endosome GO GO:0008289; F:lipid binding GO GO:0006869; P:lipid transport GO GO:0016020; C:membrane GO GO:0006810; P:transport XX KW Endosome KW Lipid-binding KW Lipid transport KW Membrane KW Transport FT From: PS51439 FT DOMAIN from..to FT /note="MENTAL #" XX Chop: Nter=0; Cter=0; Size: 170-175; Related: None; Repeats: 1; Topology: Undefined; Example: Q14849; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00771; DC Domain; TR PROSITE; PS51441; CPCD_LIKE; 1; level=0 XX Names: CpcD-like domain Function: The cpcD-like domain is found in ferredoxin-NADP(+) oxydoreductase (FNR) (EC=1.18.1.2) and phycobilisome (PBS)-associated linker proteins from numerous cyanobacteria. XX XX GO GO:0030089; C:phycobilisome XX KW Phycobilisome XX FT From: PS51441 FT DOMAIN from..to FT /note="CpcD-like #" XX Chop: Nter=0; Cter=0; Size: 41-69; Related: None; Repeats: 1; Topology: Undefined; Example: P80558; Scope: Bacteria; Cyanobacteriota Comments: None; XX # Revision 1.4 2023/02/17 // AC PRU00772; DC Domain; TR PROSITE; PS51442; M_PRO; 1; level=0 XX Names: Coronavirus main protease (M-pro) domain 3C-like proteinase (3CL-pro) peptidase family C30 Function: It is a viral cysteine proteinase wich mediates most maturation cleavage events within the precursor polyprotein. XX case CC -!- FUNCTION: The main proteinase 3CL-PRO is responsible for the majority CC of cleavages as it cleaves the C-terminus of replicase polyprotein at CC 11 sites. Recognizes substrates containing the core sequence [ILMVF]- CC Q-|-[SGACN]. Inhibited by the substrate-analog Cbz-Val-Asn-Ser-Thr-Leu- CC Gln-CMK. XX GO GO:0019082; P:viral protein processing GO GO:0006508; P:proteolysis GO GO:0008233; F:peptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008234; F:cysteine-type peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51442 FT DOMAIN from..to FT /note="Peptidase C30 #" FT ACT_SITE 41 FT /note="For 3CL-PRO activity" FT Group: 1; Condition: H FT ACT_SITE 144 FT /note="For 3CL-PRO activity" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 292-317; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Coronavirinae Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00773; DC Domain; TR PROSITE; PS51443; PCS; 1; level=0 XX Names: Phytochelatin synthase (PCS) domain Function: Phytochelatins (PCs) are synthesized posttranslationally by the PC synthase (PCS) (EC 2.3.2.15), a gamma-glutamylcysteine (gamma-EC) transpeptidase. PC synthesis is proposed to have two distinct steps: (Step1) formation of gamma-EC concomitant with the cleavage of Gly from GSH; and (Step 2) transfer of the gamma-EC unit to an acceptor GSH molecule or an oligomeric PC peptide (PCn). XX case DE + AltName: Full=Glutathione gamma-glutamylcysteinyltransferase; DE EC=2.3.2.15; end case XX case CC -!- CATALYTIC ACTIVITY: CC Reaction=[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly CC + glycine; Xref=Rhea:RHEA:17917, Rhea:RHEA-COMP:12438, Rhea:RHEA- CC COMP:12439, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:131728; EC=2.3.2.15; end case CC -!- SIMILARITY: Belongs to the phytochelatin synthase family. XX case GO GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity GO GO:0046938; P:phytochelatin biosynthetic process GO GO:0016746; F:acyltransferase activity XX KW Transferase KW Acyltransferase end case XX FT From: PS51443 FT DOMAIN from..to FT /note="Peptidase C83 #" FT ACT_SITE 56 FT Group: 1; Condition: C FT ACT_SITE 168 FT Group: 1; Condition: H FT ACT_SITE 186 FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 210-231; Related: None; Repeats: 1; Topology: Undefined; Example: Q2TE74; Scope: Eukaryota Bacteria; Cyanobacteriota Comments: None; XX # Revision 1.10 2023/02/17 // AC PRU00774; DC Domain; TR PROSITE; PS51444; FH2; 1; level=0 XX Names: Formin homology-2 (FH2) domain Function: The defining feature of formins is a highly conserved ~400 residue region, the Formin Homology-2 (FH2) domain, which forms a head-to-tail ring- shaped dimer, and directly binds to the actin filament at its barbed end. The FH2 domain catalyzes the nucleation and elongation of actin filament, preventing capping proteins from binding to the barbed end. XX XX GO GO:0003779; F:actin binding GO GO:0030036; P:actin cytoskeleton organization GO GO:0005856; C:cytoskeleton XX KW Actin-binding KW Cytoskeleton FT From: PS51444 FT DOMAIN from..to FT /note="FH2 #" XX Chop: Nter=0; Cter=0; Size: 285-486; Related: None; Repeats: 1; Topology: Undefined; Example: O60610; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00775; DC Domain; TR PROSITE; PS51445; PBS_LINKER; 1; level=0 XX Names: Phycobilisome (PBS) linker domain Function: Phycobilisome (PBS) linker polypeptides share a conserved domain of ~180 residues, which can be present in one or multiple copies. XX CC -!- SIMILARITY: Belongs to the phycobilisome linker protein family. XX GO GO:0030089; C:phycobilisome XX KW Phycobilisome XX FT From: PS51445 FT DOMAIN from..to FT /note="PBS-linker #" XX Chop: Nter=0; Cter=0; Size: 62-194; Related: None; Repeats: 1-4; Topology: Undefined; Example: P51263; Scope: Bacteria; Cyanobacteriota Eukaryota Comments: None; XX # Revision 1.5 2023/02/17 // AC PRU00776; DC Domain; TR PROSITE; PS51446; PACIFASTIN; 1; level=0 XX Names: Pacifastin domain Function: Fill in XX CC -!- SIMILARITY: Belongs to the protease inhibitor I19 family. XX GO GO:0004866; F:endopeptidase inhibitor activity GO GO:0004867; F:serine-type endopeptidase inhibitor activity XX case KW Disulfide bond end case KW Protease inhibitor KW Serine protease inhibitor XX FT From: PS51446 FT DOMAIN from..to FT /note="Pacifastin #" FT SITE 29..30 FT /note="Reactive bond" FT Condition: x-K FT DISULFID 4..19 FT Tag: disulf; Condition: C-x*-C FT DISULFID 14..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 17..27 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 25-48; Related: None; Repeats: 1-3; Topology: Undefined; Example: O46163; Scope: Eukaryota; Arthropoda Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00777; DC Domain; TR PROSITE; PS51272; SLH; 1; level=0 XX Names: S-layer homology (SLH) domain Function: S-layers are paracrystalline mono-layered assemblies of (glyco)proteins which coat the surface of bacteria. Several S-layer proteins and some other cell wall proteins contain one or more copies of a domain of about 50-60 residues, which has been called SLH (for S-layer homology). XX XX FT From: PS51272 FT DOMAIN from..to FT /note="SLH #" XX Chop: Nter=0; Cter=0; Size: 33-84; Related: None; Repeats: 1-3; Topology: Undefined; Example: P49051; Scope: Bacteria Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00778; DC Domain; TR PROSITE; PS51447; FDX_ACB; 1; level=0 XX Names: Ferredoxin-fold anticodon binding (FDX-ACB) domain Function: Bacterial and mitochondrial phenylalanine-tRNA synthetases (PheRSs) share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split alpha+beta motif having no insertions. XX XX FT From: PS51447 FT DOMAIN from..to FT /note="FDX-ACB #" XX Chop: Nter=0; Cter=0; Size: 72-113; Related: None; Repeats: 1; Topology: Undefined; Example: Q98CQ1; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00779; DC Domain; TR PROSITE; PS51448; P_TREFOIL_2; 1; level=0 XX Names: P-type ('Trefoil') domain Function: The P-type domain is a cysteine-rich domain of approximately forty five amino-acid residues, which is found in some extracellular eukaryotic proteins. XX XX DR PROSITE; PS00025; P_TREFOIL_1; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51448 FT DOMAIN from..to FT /note="P-type #" FT DISULFID 3..29 FT Tag: disulf; Condition: C-x*-C FT DISULFID 13..28 FT Tag: disulf; Condition: C-x*-C FT DISULFID 23..40 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 31-62; Related: None; Repeats: 1-6; Topology: Undefined; Example: P04155; Scope: Eukaryota Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00780; DC Domain; TR PROSITE; PS51449; MTTASE_N; 1; level=0 TR PROSITE; PS01278; MTTASE_RADICAL; 1; level=0 XX Names: Methylthiotransferase domains Function: Methylthiotransferases (MTTases) catalyze a C-H to C-S bond conversion in the methylthiolation of tRNA or ribosomal protein substrate. XX case or DE + RecName: EC=2.-.-.-; end case XX CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine.; case CC -!- SUBCELLULAR LOCATION: Cytoplasm. end case XX GO GO:0005506; F:iron ion binding GO GO:0051539; F:4 iron, 4 sulfur cluster binding case or GO GO:0016740; F:transferase activity end case case GO GO:0005737; C:cytoplasm end case XX KW 4Fe-4S KW Iron KW Iron-sulfur KW Metal-binding KW S-adenosyl-L-methionine case or KW Transferase end case case KW Cytoplasm end case XX FT From: PS51449 FT DOMAIN from..to FT /note="MTTase N-terminal #" FT BINDING 10 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT Condition: C FT BINDING 46 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT Condition: C FT BINDING 77 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="1" FT Condition: C FT From: PS01278 FT BINDING 4 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT BINDING 5 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" FT BINDING 8 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="2" FT /ligand_note="4Fe-4S-S-AdoMet" XX Chop: Nter=0; Cter=0; Size: 90-150; Related: None; Repeats: 1; Topology: Undefined; Example: Q54KV4; B4RNW8; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.11 2022/11/19 // AC PRU00781; DC Domain; TR PROSITE; PS51455; PIPK; 1; level=0 XX Names: Phosphatidylinositol phosphate kinase (PIPK) domain Function: Phosphatidylinositol phosphate kinases (PIPKs) phosphorylate phosphatidylinositol phosphate (PtdInsP) to phosphatidylinositol bisphosphate (PtdInsP2). XX XX GO GO:0005524; F:ATP binding GO GO:0016301; F:kinase activity GO GO:0000166; F:nucleotide binding GO GO:0046488; P:phosphatidylinositol metabolic process GO GO:0016740; F:transferase activity XX KW ATP-binding KW Kinase KW Nucleotide-binding KW Transferase XX FT From: PS51455 FT DOMAIN from..to FT /note="PIPK #" XX Chop: Nter=0; Cter=0; Size: 314-442; Related: None; Repeats: 1; Topology: Undefined; Example: Q56YP2; Scope: Eukaryota Comments: None; XX # Revision 1.5 2023/05/30 // AC PRU00782; DC Domain; TR PROSITE; PS51456; MYOSIN_MOTOR; 1; level=0 XX Names: Myosin motor domain Function: The motor domain has been shown to interact with actin, hydrolyze ATP and produce movement. XX CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase CC superfamily. Myosin family. XX case GO GO:0005524; F:ATP binding GO GO:0003774; F:cytoskeletal motor activity XX KW ATP-binding KW Motor protein KW Nucleotide-binding end case KW Myosin KW Actin-binding XX FT From: PS51456 FT DOMAIN from..to FT /note="Myosin motor #" FT BINDING 94..101 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: G-x(4)-G-K-[TS] FT REGION 556..578 FT /note="Actin-binding" XX Chop: Nter=0; Cter=0; Size: 55-882; Related: None; Repeats: 1; Topology: Undefined; Example: Q99104; Scope: Eukaryota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU00783; DC Domain; TR PROSITE; PS50146; DAGK; 1; level=0 XX Names: DAG-kinase catalytic (DAGKc) domain diacylglycerol kinase catalytic domain DGK C4-a domain DgkB domain 1 Function: The DAG-kinase catalytic domain (DAGKc) is present in mammalian lipid kinases, such as diacylglycerol (DAG), ceramide and sphingosine kinases, as well as in related bacterial lipid kinases. XX DE + RecName: EC=2.7.-.-; XX XX GO GO:0016740; F:transferase activity GO GO:0016301; F:kinase activity case GO GO:0005524; F:ATP binding XX KW ATP-binding end case KW Kinase KW Transferase XX FT From: PS50146 FT DOMAIN from..to FT /note="DAGKc #" FT BINDING 11..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1 FT BINDING 69..75 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1 FT BINDING 43 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: [ST] FT BINDING 100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: [ST] XX Chop: Nter=0; Cter=0; Size: 110-195; Related: None; Repeats: 1; Topology: Undefined; Example: Q6GFF9; Q87ZA2; Q03603; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU00784; DC Domain; TR PROSITE; PS51457; BEN; 1; level=0 XX Names: BEN domain Function: The BEN domain is predicted to functions as an adaptor for the higher-order structuring of chromatin, and recruitment of chromatin modifying factors in transcriptional regulation. XX XX FT From: PS51457 FT DOMAIN from..to FT /note="BEN #" XX Chop: Nter=0; Cter=0; Size: 86-121; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q5T5X7; Scope: Eukaryota; Euteleostomi Viruses; Orthopoxvirus Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00791; DC Domain; TR PROSITE; PS51459; FIDO; 1; level=0 XX Names: Fido domain Function: The fido domain of Vibrio VopS covalently modifies Rho GTPase threonine with AMP to inhibit downstream signaling events in host cells. XX XX FT From: PS51459 FT DOMAIN from..to FT /note="Fido #" XX Chop: Nter=0; Cter=0; Size: 95-165; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q29JP8; Scope: Eukaryota; Metazoa Bacteria Viruses Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00792; DC Domain; TR PROSITE; PS51460; GAR; 1; level=0 XX Names: GAR domain Function: The GAR domain comprises ~57 amino acids and has been shown to bind to microtubules. XX CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. XX GO GO:0005856; C:cytoskeleton GO GO:0008017; F:microtubule binding GO GO:0008093; F:cytoskeletal anchor activity XX KW Cytoplasm KW Cytoskeleton XX FT From: PS51460 FT DOMAIN from..to FT /note="GAR #" XX Chop: Nter=0; Cter=0; Size: 63-89; Related: None; Repeats: 1; Topology: Undefined; Example: Q8JZP9; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.5 2022/02/11 // AC PRU00793; DC Domain; TR PROSITE; PS51461; NC1_FIB; 1; level=0 XX Names: Fibrillar collagen C-terminal non-collagenous (NC1) domain Function: The NC1 domain is the most conserved part of fibrillar collagens from invertebrates to vertebrates (types I-III, V, XI, XXIV and XXVII). XX case CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. end case case CC -!- SIMILARITY: Belongs to the fibrillar collagen family. XX GO GO:0005615; C:extracellular space GO GO:0005201; F:extracellular matrix structural constituent XX KW Collagen KW Extracellular matrix KW Secreted XX end case case KW Disulfide bond end case XX FT From: PS51461 FT DOMAIN from..to FT /note="Fibrillar collagen NC1 #" FT DISULFID 31 FT /note="Interchain" FT Tag: disulf; Condition: C FT DISULFID 37 FT /note="Interchain" FT Tag: disulf; Condition: C FT DISULFID 54 FT /note="Interchain" FT Tag: disulf; Condition: C FT DISULFID 63 FT /note="Interchain" FT Tag: disulf; Condition: C FT DISULFID 72..225 FT Tag: disulf; Condition: C-x*-C FT DISULFID 133..178 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 185-251; Related: None; Repeats: 1-4; Topology: Not cytoplasmic; Example: P02452; Scope: Eukaryota Comments: None; XX # Revision 1.8 2019/11/21 // AC PRU00794; DC Domain; TR PROSITE; PS51462; NUDIX; 1; level=0 XX Names: Nudix hydrolase domain Function: The Nudix superfamily is widespread among eucaryotes, bacteria, archaea and viruses and consists mainly of pyrophosphohydrolases that act upon substrates of general structure NUcleoside DIphosphate linked to another moiety, X (NDP-X) to yield NMP plus P-X. XX XX DR PROSITE; PS00893; NUDIX_BOX; 1; trigger=no DR PROSITE; PS01293; NUDIX_COA; 0-1; trigger=no XX GO GO:0016787; F:hydrolase activity GO GO:0046872; F:metal ion binding XX KW Hydrolase KW Metal-binding XX FT From: PS51462 FT DOMAIN from..to FT /note="Nudix hydrolase #" FT MOTIF 36..57 FT /note="Nudix box #" XX Chop: Nter=0; Cter=0; Size: 105-260; Related: None; Repeats: 1; Topology: Undefined; Example: Q5RD76; Scope: Eukaryota Bacteria Archaea Viruses Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00795; DC Domain; TR PROSITE; PS50219; CNH; 1; level=0 XX Names: Citron homology (CNH) domain Function: Little is known about the function of the CNH domain, although it has been proposed to regulate kinase activity and to mediate binding to the GTP-bound forms of Rac and Rho. XX XX FT From: PS50219 FT DOMAIN from..to FT /note="CNH #" XX Chop: Nter=0; Cter=0; Size: 263-421; Related: None; Repeats: 1; Topology: Undefined; Example: O95819; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00797; DC Domain; TR PROSITE; PS51464; SIS; 1; level=0 XX Names: SIS domain Function: The sugar isomerase (SIS) domain is a phosphosugar-binding module that is found in a variety of eubacterial, archaebacterial and eukaryotic glycolytic proteins that have a role in phosphosugar isomerization or regulation. XX XX GO GO:0030246; F:carbohydrate binding GO GO:0005975; P:carbohydrate metabolic process XX KW Carbohydrate metabolism XX FT From: PS51464 FT DOMAIN entry..exit FT /note="SIS #" XX Chop: Nter=0; Cter=0; Size: 90-150; Related: None; Repeats: 1-2; Topology: Undefined; Example: B0BP79; Scope: Bacteria Eukaryota Archaea Viruses; Mimivirus Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00798; DC Domain; TR PROSITE; PS51465; KAZAL_2; 1; level=0 XX Names: Kazal domain Function: Kazal-type inhibitors represent the most studied canonical proteinase inhibitors. XX XX DR PROSITE; PS00282; KAZAL_1; 1; trigger=no XX GO GO:0010466; P:negative regulation of peptidase activity GO GO:0004867; F:serine-type endopeptidase inhibitor activity case KW Disulfide bond end case KW Protease inhibitor KW Serine protease inhibitor XX FT From: PS51465 FT DOMAIN from..to FT /note="Kazal-like #" FT SITE 15..16 FT /note="Reactive bond" FT DISULFID 7..36 FT Tag: disulf; Condition: C-x*-C FT DISULFID 13..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 21..53 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 28-76; Related: None; Repeats: 1-9; Topology: Undefined; Example: P00995; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00799; DC Domain; TR PROSITE; PS51466; PINIT; 1; level=0 XX Names: PINIT domain Function: The PINIT domain serves as a scaffold to coordinate PCNA to promote SUMO conjugation to both consensus and nonconsensus lysine side chains. XX XX KW Ubl conjugation pathway KW Ubl conjugation XX FT From: PS51466 FT DOMAIN from..to FT /note="PINIT #" XX Chop: Nter=0; Cter=0; Size: 143-176; Related: None; Repeats: 1; Topology: Undefined; Example: Q04195; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00800; DC Domain; TR PROSITE; PS51467; HARP; 1; level=0 XX Names: HARP domain Function: The evolutionarily conserved HARP domain determines the annealing helicase activity required for the in vivo and in vitro functions of SMARCAL1. XX case and CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SMARCAL1 CC subfamily. end case XX FT From: PS51467 FT DOMAIN from..to FT /note="HARP #" XX Chop: Nter=0; Cter=0; Size: 61-89; Related: None; Repeats: 1-2; Topology: Undefined; Example: B4F769; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00801; DC Domain; TR PROSITE; PS51468; VIT; 1; level=0 XX Names: VIT domain Function: The VIT domain can be regarded as the characteristic domain of the inter-alpha-trypsin inhibitor heavy chain (ITIH) family. XX XX FT From: PS51468 FT DOMAIN from..to FT /note="VIT #" XX Chop: Nter=0; Cter=0; Size: 117-159; Related: None; Repeats: 1; Topology: Undefined; Example: O02668; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00802; DC Domain; TR PROSITE; PS51469; SUN; 1; level=0 XX Names: SUN domain Function: SUN proteins are anchored in the inner nuclear envelope by their transmembrane segment and oriented in the membrane such that the C-terminal SUN domain is located in the space between the inner and outer nuclear membrane. Here, the SUN domain can interact with the C-terminal tail of an outer nuclear envelope protein that binds to the cytoskeleton, including the centrosome. XX XX FT From: PS51469 FT DOMAIN from..to FT /note="SUN #" XX Chop: Nter=0; Cter=0; Size: 148-200; Related: None; Repeats: 1; Topology: Undefined; Example: Q12232; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00803; DC Domain; TR PROSITE; PS51470; FG_GAP; 1; level=0 XX Names: FG-GAP repeat Function: Seven 60 amino acids FG-GAP repeats fold into a beta-propeller domain. XX XX FT From: PS51470 FT REPEAT entry..exit FT /note="FG-GAP #" XX Chop: Nter=0; Cter=0; Size: 40-81; Related: None; Repeats: 1-7; Topology: Undefined; Example: P26008; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00804; DC Domain; TR PROSITE; PS51472; RRM_NUP35; 1; level=0 XX Names: RNA-recognition motif (RRM) Nup35-type domain Function: The vertebrate nuclear pore protein Nup35, the ortholog of Saccharomyces cerevisiae Nup53p, is suggested to interact with the NE membrane and to be required for nuclear morphology. The highly conserved region between vertebrate Nup35 and yeast Nup53p is predicted to contain an RNA-recognition motif (RRM) domain. XX XX GO GO:0005643; C:nuclear pore GO GO:0005634; C:nucleus GO GO:0006810; P:transport GO GO:0051028; P:mRNA transport XX KW Nuclear pore complex KW Nucleus KW Transport KW mRNA transport XX FT From: PS51472 FT DOMAIN from..to FT /note="RRM Nup35-type #" XX Chop: Nter=0; Cter=0; Size: 71-140; Related: None; Repeats: 1; Topology: Undefined; Example: Q03790; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00805; DC Domain; TR PROSITE; PS51471; FE2OG_OXY; 1; level=0 XX Names: Fe(2+) 2-oxoglutarate dioxygenase domain Fe(II) 2-oxoglutarate dioxygenase domain PKHD (prolyl/lysyl hydroxylase) domain P4Hc domain 2-oxoglutarate and Fe(II)-dependent oxygenases 2OG-Fe(II) oxygenase superfamily 2OG oxygenase families Function: Enzymes with the Fe(2+) and 2-oxoglutarate (2OG)-dependent dioxygenase domain typically catalyse the oxidation of an organic substrate using a dioxygen molecule, mostly by using ferrous iron as the active site cofactor and 2OG as a cosubstrate which is decarboxylated to succinate and CO2. XX case DE + RecName: EC=1.14.11.-; else case DE + RecName: EC=1.14.-.-; end case XX case CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Note=Binds 1 Fe(2+) ion per subunit.; end case XX case GO GO:0005506; F:iron ion binding end case case GO GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity else case GO GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen end case XX case KW Dioxygenase KW Iron KW Metal-binding KW Oxidoreductase end case XX FT From: PS51471 FT DOMAIN from..to FT /note="Fe2OG dioxygenase #" FT BINDING 20 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Group: 2; Condition: H FT BINDING 22 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Group: 2; Condition: D FT BINDING 70 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Group: 2; Condition: H FT BINDING 80 FT /ligand="2-oxoglutarate" FT /ligand_id="ChEBI:CHEBI:16810" FT Group: 2; Condition: [RK] XX Chop: Nter=0; Cter=0; Size: 80-160; Related: None; Repeats: 1; Topology: Undefined; Example: A1K320; Scope: Bacteria Eukaryota Viruses Comments: None; XX # Revision 1.12 2022/11/19 // AC PRU00806; DC Domain; TR PROSITE; PS51473; GNK2; 1; level=0 XX Names: Gnk2-homologous domain Function: The Gnk2-homologous domain is composed of two alpha-helices and a five stranded beta-sheet, which forms a compact single-domain architecture with an alpha+beta-fold. It contains a C-X(8)-C-X(2)-C motif. Cysteine residues form three intramolecular disulfide bridges: C1-C5, C2-C3, and C4-C6. XX XX case KW Disulfide bond end case XX FT From: PS51473 FT DOMAIN from..to FT /note="Gnk2-homologous #" FT DISULFID 8..84 FT Tag: disulf; Condition: C-x*-C FT DISULFID 60..69 FT Tag: disulf; Condition: C-x*-C FT DISULFID 72..97 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 88-135; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q9ZU94; Scope: Eukaryota; Viridiplantae Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00808; DC Domain; TR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1; level=0 XX Names: Proteasome alpha-type subunit Function: Subunits that belong to the alpha-type group are proteins of from 210 to 290 amino acids that share a number of conserved sequence regions. XX CC -!- SIMILARITY: Belongs to the peptidase T1A family. XX DR PROSITE; PS00388; PROTEASOME_A_1; 1; trigger=no XX GO GO:0019773; C:proteasome core complex, alpha-subunit complex XX KW Proteasome XX Chop: Nter=0; Cter=0; Size: 166-239; Related: None; Repeats: 1; Topology: Undefined; Example: B8GEZ3; Scope: Eukaryota Bacteria; Actinomycetota Archaea Comments: None; XX # Revision 1.5 2023/01/13 // AC PRU00809; DC Domain; TR PROSITE; PS51476; PROTEASOME_BETA_2; 1; level=0 XX Names: Proteasome beta-type subunit Function: Subunits that belong to the beta-type group are proteins of from 190 to 290 amino acids that share a number of conserved sequence regions. XX case DE + RecName: EC=3.4.25.-; XX end case CC -!- SUBCELLULAR LOCATION: Cytoplasm. case and not CC -!- SIMILARITY: Belongs to the peptidase T1B family. HslV subfamily. else CC -!- SIMILARITY: Belongs to the peptidase T1B family. end case XX case or or DR PROSITE; PS00854; PROTEASOME_BETA_1; 1; trigger=no end case XX case GO GO:0004298; F:threonine-type endopeptidase activity XX KW Hydrolase KW Protease KW Threonine protease end case KW Cytoplasm XX FT From: PS51476 FT ACT_SITE 2 FT Group: 1; Condition: T FT ACT_SITE 18 FT Group: 1; Condition: [DE] FT ACT_SITE 34 FT Group: 1; Condition: K XX Chop: Nter=0; Cter=0; Size: 92-209; Related: None; Repeats: 1; Topology: Undefined; Example: B9IVB9; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.4 2023/01/13 // AC PRU00810; DC Domain; TR PROSITE; PS51477; PAH; 1; level=0 XX Names: PAH domain Function: The paired amphipathic helix (PAH) domain is a protein-protein interaction domain present in eukaryotic proteins implied in transcription down-regulation, such as the SIN3 family of proteins. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX KW Nucleus XX FT From: PS51477 FT DOMAIN from..to FT /note="PAH #" XX Chop: Nter=0; Cter=0; Size: 59-96; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q60520; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00812; DC Domain; TR PROSITE; PS51479; ZF_RTR1; 1; level=0 XX Names: RTR1-type zinc Function: The eukaryotic protein family Rtr1/RPAP2 interacts with the C- terminal domain CTD of RNA polymerase II (RNAPII). It has been shown in yeast that Rtr1 is a CTD phosphatase that regulates RNAPII during the transition from serine 5 to serine 2 phosphorylation. Rtr1 proteins are poorly conserved overall, but they share a motif with three strictly conserved Cys residues and another residue conserved as His (in most fungi) or Cys (in animals and S. pombe), suggestive of a zinc finger motif (C-x(4)-C-x(n)-C-x(3)-[CH], where n ranges from 30 to 50). XX CC -!- SIMILARITY: Belongs to the RPAP2 family. XX case GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51479 case and and and FT ZN_FING from..to FT /note="RTR1-type #" else case and and and FT ZN_FING from..to FT /note="RTR1-type #; atypical" else FT ZN_FING from..to FT /note="RTR1-type #; degenerate" end case FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 70-90; Related: None; Repeats: 1; Topology: Undefined; Example: F6RRD7; Scope: Eukaryota Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU00813; DC Domain; TR PROSITE; PS51480; DHAL; 1; level=0 XX Names: DhaL domain Function: The DhaL domain is a nucleotide-binding domain found in dihydroxyacetone (Dha) kinases. XX XX FT From: PS51480 FT DOMAIN from..to FT /note="DhaL #" XX Chop: Nter=0; Cter=0; Size: 72-223; Related: None; Repeats: 1; Topology: Undefined; Example: Q9CIV7; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00814; DC Domain; TR PROSITE; PS51481; DHAK; 1; level=0 XX Names: DhaK domain Function: The DhaK domain is the dihydroxyacetone- (Dha-)binding domain of Dha kinases. XX XX GO GO:0016301; F:kinase activity GO GO:0016740; F:transferase activity XX KW Kinase KW Transferase XX FT From: PS51481 FT DOMAIN from..to FT /note="DhaK #" FT ACT_SITE 212 FT /note="Tele-hemiaminal-histidine intermediate" FT Condition: H FT BINDING 50 FT /ligand="dihydroxyacetone" FT /ligand_id="ChEBI:CHEBI:16016" FT Condition: H FT BINDING 103 FT /ligand="dihydroxyacetone" FT /ligand_id="ChEBI:CHEBI:16016" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 310-395; Related: None; Repeats: 1; Topology: Undefined; Example: P76015; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU00815; DC Domain; TR PROSITE; PS51482; DEGV; 1; level=0 XX Names: DegV domain Function: The function of DegV proteins is not yet completely understood, but structural evidence indicates that they can bind different fatty acids. XX XX FT From: PS51482 FT DOMAIN from..to FT /note="DegV #" XX Chop: Nter=0; Cter=0; Size: 127-315; Related: None; Repeats: 1; Topology: Undefined; Example: Q97RQ6; Scope: Bacteria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00816; DC Domain; TR PROSITE; PS51483; B5; 1; level=0 XX Names: B5 domain Function: The B5 domain has been shown to bind DNA. XX XX GO GO:0006432; P:phenylalanyl-tRNA aminoacylation case GO GO:0000287; F:magnesium ion binding XX KW Magnesium KW Metal-binding end case KW Aminoacyl-tRNA synthetase KW Protein biosynthesis XX FT From: PS51483 FT DOMAIN from..to FT /note="B5 #" FT BINDING 65 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: [DE] FT BINDING 55 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: D FT BINDING 61 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: D FT BINDING 64 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 59-174; Related: None; Repeats: 1; Topology: Undefined; Example: P27002; Scope: Bacteria Archaea Eukaryota Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU00817; DC Domain; TR PROSITE; PS51484; G8; 1; level=0 XX Names: G8 domain Function: The G8 domain may be involved in extracellular ligand binding and progress of catalysis. XX XX FT From: PS51484 FT DOMAIN from..to FT /note="G8 #" XX Chop: Nter=0; Cter=0; Size: 111-149; Related: None; Repeats: 1-2; Topology: Undefined; Example: A3KPQ7; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00818; DC Domain; TR PROSITE; PS51485; PHYTOCYANIN; 1; level=0 XX Names: Phytocyanin domain Function: Phytocyanins are blue copper proteins found in chloropasts of higher plants. XX XX case DR PROSITE; PS00196; COPPER_BLUE; 1; trigger=no end case XX case GO GO:0005507; F:copper ion binding end case XX case KW Disulfide bond end case XX FT From: PS51485 FT DOMAIN from..to FT /note="Phytocyanin #" FT BINDING 43 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT Group: 1; Condition: H FT BINDING 84 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT Group: 1; Condition: C FT BINDING 89 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT Group: 1; Condition: H FT BINDING 94 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT Group: 1; Condition: [MQ] FT DISULFID 56..90 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 57-116; Related: None; Repeats: 1; Topology: Undefined; Example: P29602; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU00819; DC Domain; TR PROSITE; PS51486; REKLES; 1; level=0 XX Names: REKLES domain Function: REKLES consists of two subdomains: a modestly conserved N-terminal REKLESalpha and a highly conserved C-terminal REKLESbeta. REKLESalpha and -beta are required, respectively, for nuclear entry and export of Bright during its nucleoplasmic shuttling. In addition to its function in nuclear export, the REKLESbeta subdomain regulates the binding of Bright to nuclear matrix association (or attachment) regions (MARs), its self- and paralogous (Bdp) association and stoichiometry, and its retention within the nuclear matrix. XX XX FT From: PS51486 FT DOMAIN from..to FT /note="REKLES #" XX Chop: Nter=0; Cter=0; Size: 76-119; Related: None; Repeats: 1; Topology: Undefined; Example: A2BEA6; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00820; DC Domain; TR PROSITE; PS51487; NBD; 1; level=0 XX Names: NBD domain Function: The Rag-1 nonamer binding domain (NBD) is a DNA-binding domain involved in the somatic site-specific recombination reaction known as V(D)J recombination. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- DOMAIN: The NBD (nonamer binding) DNA-binding domain mediates the CC specific binding to the nonamer RSS motif by forming a tightly CC interwoven homodimer that binds and synapses 2 nonamer elements, with CC each NBD making contact with both DNA molecules. Each RSS is composed CC of well-conserved heptamer (consensus 5'-CACAGTG-3') and nonamer CC (consensus 5'-ACAAAAACC-3') sequences separated by a spacer of either CC 12 bp or 23 bp. CC -!- SIMILARITY: Belongs to the RAG1 family. XX GO GO:0005634; C:nucleus GO GO:0043565; F:sequence-specific DNA binding GO GO:0033151; P:V(D)J recombination XX KW DNA recombination KW DNA-binding KW Nucleus XX FT From: PS51487 FT DNA_BIND 1..68 FT /note="NBD" XX Chop: Nter=0; Cter=0; Size: 58-78; Related: None; Repeats: 1; Topology: Undefined; Example: Q91829; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00821; DC Domain; TR PROSITE; PS51488; KBD; 1; level=0 XX Names: KBD domain Function: The c-Kit-binding domain (KBD) composed of about 50 amino acids is found in a family of membrane-bound molecules, Spreds, which contain an EVH1 domain in the N-terminus and a Sprouty-related cysteine rich region (SPR domain) in the C-terminus. XX XX FT From: PS51488 FT DOMAIN from..to FT /note="KBD #" XX Chop: Nter=0; Cter=0; Size: 40-67; Related: None; Repeats: 1; Topology: Undefined; Example: Q6P6N5; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00822; DC Domain; TR PROSITE; PS51489; BUB1_N; 1; level=0 XX Names: BUB1 N-terminal domain Function: The BUB1 N-terminal domain mediates the binding of BUB1 and BUBR1 to the mitotic kinetochore protein Blinkin. XX XX KW Cell cycle KW Nucleus XX FT From: PS51489 FT DOMAIN from..to FT /note="BUB1 N-terminal #" XX Chop: Nter=0; Cter=0; Size: 152-182; Related: None; Repeats: 1; Topology: Undefined; Example: O59767; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00823; DC Domain; TR PROSITE; PS51490; KHA; 1; level=0 XX Names: KHA domain Function: The KHA domain is essential for interaction of plant inward rectifying potassium (K(+)in) channels. The KHA domain mediates tetramerization and/or stabilization of the heteromers. XX XX FT From: PS51490 FT DOMAIN from..to FT /note="KHA #" XX Chop: Nter=0; Cter=0; Size: 56-91; Related: None; Repeats: 1; Topology: Undefined; Example: Q7L273; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00824; DC Domain; TR PROSITE; PS51491; TAU_MAP_2; 1; level=0 XX Names: Tau and MAP proteins tubulin-binding repeat Function: The C-terminal region of a subset of Microtubule Associated Proteins (MAPs) contain three or four tandem repeats of a conserved domain of about thirty amino acid residues which is implicated in tubulin- binding and which seems to have a stiffening effect on microtubules. XX XX DR PROSITE; PS00229; TAU_MAP_1; 1; trigger=no XX GO GO:0005874; C:microtubule GO GO:0007026; P:negative regulation of microtubule depolymerization XX KW Microtubule KW Repeat XX FT From: PS51491 FT REPEAT from..to FT /note="Tau/MAP #" XX Chop: Nter=0; Cter=0; Size: 21-42; Related: None; Repeats: 3-4; Topology: Undefined; Example: Q5S6V2; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00825; DC Domain; TR PROSITE; PS51492; PEPTIDASE_C23; 1; level=0 XX Names: Peptidase family C23 domain Function: The peptidase family C23 domain is a papain-like proteinase domain with catalytic cysteine and histidine residues. XX XX case GO GO:0004197; F:cysteine-type endopeptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51492 FT DOMAIN from..to FT /note="Peptidase C23 #" FT ACT_SITE 5 FT Group: 1; Condition: C FT ACT_SITE 86 FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 80-101; Related: None; Repeats: 1; Topology: Undefined; Example: Q64962; Scope: Viruses; Betaflexiviridae Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00826; DC Domain; TR PROSITE; PS51493; AV_NSP4_PRO; 1; level=0 XX Names: Arterivirus nsp4 proteinase domain Function: The arterivirus nsp4 proteinase domain forms peptidase family S32. XX XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0004252; F:serine-type endopeptidase activity GO GO:0019082; P:viral protein processing XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51493 FT DOMAIN from..to FT /note="Peptidase S32 #" FT ACT_SITE 39 FT /note="Charge relay system; for 3C-like serine proteinase FT activity" FT Group: 1; Condition: H FT ACT_SITE 64 FT /note="Charge relay system; for 3C-like serine proteinase FT activity" FT Group: 1; Condition: D FT ACT_SITE 117 FT /note="Charge relay system; for 3C-like serine proteinase FT activity" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 191-214; Related: None; Repeats: 1; Topology: Undefined; Example: Q9YN02; Scope: Viruses; Arteriviridae Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00827; DC Domain; TR PROSITE; PS51494; SPOIVB; 1; level=0 XX Names: SpoIVB peptidase domain Function: The catalytic domain of the SpoIVB serine peptidase is a 160-amino- acid residue segment at the carboxyl terminus of the protein. XX XX case GO GO:0008236; F:serine-type peptidase activity XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51494 FT DOMAIN from..to FT /note="Peptidase S55 #" FT REGION 206..208 FT /note="PDZ binding" FT Condition: T-H-V FT ACT_SITE 49 FT /note="Charge relay system" FT Group: 1; Condition: H FT ACT_SITE 176 FT /note="Charge relay system" FT Group: 1; Condition: D FT ACT_SITE 191 FT /note="Charge relay system" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 229-249; Related: None; Repeats: 1; Topology: Undefined; Example: P17896; Scope: Bacteria; Bacillus Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00828; DC Domain; TR PROSITE; PS51495; GLUE; 1; level=0 XX Names: GLUE domain Function: The GLUE domain binds both ubiquitin and a phosphoinositide. XX XX KW Protein transport KW Transport KW Endosome XX FT From: PS51495 FT DOMAIN from..90 FT /note="GLUE N-terminal #" FT DOMAIN 165..to FT /note="GLUE C-terminal #" XX Chop: Nter=0; Cter=0; Size: 113-292; Related: None; Repeats: 1; Topology: Undefined; Example: Q06696; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00829; DC Domain; TR PROSITE; PS51496; CVC; 1; level=0 XX Names: CVC domain Function: The CVC (standing for Chx10/Vsx-1 and ceh-10) domain consists of approximately 50-60 amino acid residues. The CVC domain is predicted to influence transcriptional regulation through DNA-binding, protein-protein interaction and/or protein degradation processes. It is possible that the CVC domain is necessary for protein folding or protein-protein interactions because this domain is hydrophobic. XX XX FT From: PS51496 FT DOMAIN from..to FT /note="CVC #" XX Chop: Nter=0; Cter=0; Size: 43-85; Related: None; Repeats: 1; Topology: Undefined; Example: Q9IAL2; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00830; DC Domain; TR PROSITE; PS51497; UMA; 1; level=0 XX Names: UMA domain Function: The UMA domain found in MVB12 and UBAP1 defines a novel adaptor that might recruit diverse targets to ESCRT-I. XX XX FT From: PS51497 FT DOMAIN from..to FT /note="UMA #" XX Chop: Nter=0; Cter=0; Size: 37-62; Related: None; Repeats: 1; Topology: Undefined; Example: Q7SXX7; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00831; DC Domain; TR PROSITE; PS51498; MABP; 1; level=0 XX Names: MABP domain Function: It is plausible that the eukaryotic MABP domains are adaptators that help linking other associated domains found in the same polypeptide to vesicular membranes XX XX FT From: PS51498 FT DOMAIN from..to FT /note="MABP #" XX Chop: Nter=0; Cter=0; Size: 129-170; Related: None; Repeats: 1; Topology: Undefined; Example: Q7SXX7; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00832; DC Domain; TR PROSITE; PS51499; APO; 1; level=0 XX Names: APO domain Function: All members of the APO gene family contain an ~100 amino acid residue-spanning region (APO motif 1) with conserved Cys, His, Gly, and acidic and basic amino acids. This highly conserved APO1 motif is duplicated at the C terminus (designated APO motif 2). The conserved Cys in both motifs could provide ligands for tetranuclear Fe-S centers. XX CC -!- SIMILARITY: Belongs to the APO family. XX FT From: PS51499 FT DOMAIN from..to FT /note="APO #" XX Chop: Nter=0; Cter=0; Size: 76-97; Related: None; Repeats: 2; Topology: Undefined; Example: Q9FH50; Scope: Eukaryota; Arabidopsis Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00833; DC Domain; TR PROSITE; PS51500; SIN; 1; level=0 XX Names: Sin domain Function: SinR and SinI share a multimerisation domain of ~40 amino acids. XX XX FT From: PS51500 FT DOMAIN from..to FT /note="Sin #" XX Chop: Nter=0; Cter=0; Size: 28-49; Related: None; Repeats: 1; Topology: Undefined; Example: P22755; Scope: Bacteria; Bacillus Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00834; DC Domain; TR PROSITE; PS51501; ZF_DNL; 1; level=0 XX Names: Zinc finger DNL-type Function: Tim15 contains a zinc-finger motif (CXXC and CXXC) of ~100 residues, which has been named DNL after a short C-terminal motif of D(N/H)L. XX XX case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51501 case and and and FT ZN_FING 1..98 FT /note="DNL-type" else case and and and FT ZN_FING from..to FT /note="DNL-type #; atypical" else FT ZN_FING from..to FT /note="DNL-type #; degenerate" end case FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 37 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 86-108; Related: None; Repeats: 1; Topology: Undefined; Example: B5VQB0; Scope: Eukaryota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU00835; DC Domain; TR PROSITE; PS51502; S_R_A_B_BARREL; 1; level=0 XX Names: Stress-response A/B barrel domain Function: The stress-response A/B barrel domain is found in a class of stress- response proteins in plants and in some bacterial fructose-bisphosphate aldolase. The function of the stress-response A/B barrel domain is unknown. XX XX FT From: PS51502 FT DOMAIN from..to FT /note="Stress-response A/B barrel #" XX Chop: Nter=0; Cter=0; Size: 34-105; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LUV2; Scope: Eukaryota; rosids Bacteria; Streptomyces Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00836; DC Domain; TR PROSITE; PS51503; HIG1; 1; level=0 XX Names: HIG1 domain Function: HIG1 is a member of a well conserved eukaryote protein family. The predicted transmembrane helice (TMH) and loop regions represent the most highly conserved regions in these proteins. XX CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane CC protein. XX DR General; Transmembrane; -; 2; trigger=yes XX GO GO:0031966; C:mitochondrial membrane XX KW Mitochondrion XX FT From: PS51503 FT DOMAIN from..to FT /note="HIG1 #" XX Chop: Nter=0; Cter=0; Size: 63-134; Related: None; Repeats: 1; Topology: Undefined; Example: Q6CWT4; Scope: Eukaryota Comments: None; XX # Revision 1.8 2022/09/30 // AC PRU00837; DC Domain; TR PROSITE; PS51504; H15; 1; level=0 XX Names: Linker histone H1/H5 globular (H15) domain Function: The highly conserved H15 domain is essential for the binding of H1 or H5 to the nucleosome. XX CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- SIMILARITY: Belongs to the histone H1/H5 family. XX GO GO:0003677; F:DNA binding GO GO:0006334; P:nucleosome assembly GO GO:0000786; C:nucleosome GO GO:0005634; C:nucleus XX KW Nucleus KW Chromosome KW DNA-binding XX FT From: PS51504 FT DOMAIN from..to FT /note="H15 #" XX Chop: Nter=0; Cter=0; Size: 18-89; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q94555; Scope: Eukaryota Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00838; DC Domain; TR PROSITE; PS51505; SCA7; 1; level=0 XX Names: SCA7 domain Function: ATXN7/Sgf73 and ATXN7L3, two subunits of the SAGA deubiquitination module, contain an ~50-residue SCA7 domain characterized by an atypical zinc- finger (ZnF) with a Cys-X(9,10)-Cys-X(5)-Cys-X(2)-His motif, which is characterized by a long sequence insertion between the first two zinc coordinating residues. XX XX FT From: PS51505 FT DOMAIN from..to FT /note="SCA7 #" XX Chop: Nter=0; Cter=0; Size: 57-78; Related: None; Repeats: 1; Topology: Undefined; Example: A1L209; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00839; DC Domain; TR PROSITE; PS51506; CBL_PTB; 1; level=0 XX Names: Cbl-type phosphotyrosine-binding (Cbl-PTB) domain Cbl N-terminal (Cbl-N) domain Tyrosine kinase binding (TKB) domain Function: Cbl-PTB is composed of three interacting domains: a four-helix bundle (4H), an EF-hand calcium-binding domain, and a divergent SH2 domain. The calcium-bound EF-hand wedges between the 4H and SH2 domains, and roughly determines their relative orientation. The three domains together form an integrated phosphoprotein-recognition module. XX CC -!- DOMAIN: The N-terminus is composed of the phosphotyrosine binding (PTB) CC domain, a short linker region and the RING-type zinc finger. The PTB CC domain, which is also called TKB (tyrosine kinase binding) domain, is CC composed of three different subdomains: a four-helix bundle (4H), a CC calcium-binding EF hand and a divergent SH2 domain. XX GO GO:0005509; F:calcium ion binding GO GO:0007166; P:cell surface receptor signaling pathway XX KW Calcium KW Metal-binding XX FT From: PS51506 FT DOMAIN from..to FT /note="Cbl-PTB #" FT REGION from..131 FT /note="4H #" FT REGION 132..204 FT /note="EF-hand-like #" FT REGION 205..to FT /note="SH2-like #" case FT BINDING 185 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 187 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 189 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 191 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] FT BINDING 196 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Tag: binds; Condition: [HCUEDKQNMYWSTRX] end case XX Chop: Nter=0; Cter=0; Size: 282-325; Related: None; Repeats: 1; Topology: Undefined; Example: Q557E7; Scope: Eukaryota Viruses; Murine leukemia virus Comments: None; XX # Revision 1.10 2022/11/19 // AC PRU00840; DC Domain; TR PROSITE; PS51507; IRF_2; 1; level=0 XX Names: IRF tryptophan pentad repeat DNA-binding domain Function: The IRF tryptophan pentad repeat DNA-binding domain has an alpha/ beta architecture comprising a cluster of three alpha-helices (alpha1-alpha3) flanked on one side by a mixed four-stranded beta-sheet (beta1-beta4). It forms a helix-turn-helix motif that binds to ISRE consensus sequences found in target promoters. XX CC -!- SIMILARITY: Belongs to the IRF family. XX DR PROSITE; PS00601; IRF_1; 1; trigger=no XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription GO GO:0005634; C:nucleus GO GO:0003677; F:DNA binding XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51507 FT DNA_BIND 1..107 FT /note="IRF tryptophan pentad repeat" XX Chop: Nter=0; Cter=0; Size: 95-128; Related: None; Repeats: 1; Topology: Undefined; Example: O14896; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.6 2022/06/27 // AC PRU00841; DC Domain; TR PROSITE; PS51508; CKK; 1; level=0 XX Names: CKK domain Function: The CKK domain binds microtubules. XX CC -!- DOMAIN: The CKK domain binds microtubules. CC -!- SIMILARITY: Belongs to the CAMSAP1 family. XX GO GO:0005874; C:microtubule XX KW Microtubule XX FT From: PS51508 FT DOMAIN from..to FT /note="CKK #" XX Chop: Nter=0; Cter=0; Size: 124-145; Related: None; Repeats: 1; Topology: Undefined; Example: A2AHC3; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00842; DC Domain; TR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1; level=0 XX Names: Phosphagen kinase N-terminal domain Function: The phosphagen kinase N-terminal domain is involved in dimer formation. XX CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. XX FT From: PS51509 FT DOMAIN from..to FT /note="Phosphagen kinase N-terminal #" XX Chop: Nter=0; Cter=0; Size: 42-98; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q5R7B5; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00843; DC Domain; TR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1; level=0 XX Names: Phosphagen kinase C-terminal domain Function: The phosphagen kinase C-terminal alpha/beta saddle domain contains many key residues involved in catalysis. XX CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family. XX GO GO:0005524; F:ATP binding XX KW ATP-binding KW Kinase KW Nucleotide-binding KW Transferase XX FT From: PS51510 FT DOMAIN from..to FT /note="Phosphagen kinase C-terminal #" FT BINDING 4..8 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 157..161 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 188..193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 67 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: H FT BINDING 106 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: R XX Chop: Nter=0; Cter=0; Size: 6-254; Related: None; Repeats: 1-3; Topology: Undefined; Example: A4IJG0; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU00844; DC Domain; TR PROSITE; PS51511; FIP_RBD; 1; level=0 XX Names: FIP-RBD domain Function: A family of Rab11 interacting proteins (FIPs) that conserve a C- terminal Rab-binding domain (RBD) selectively recognize the active form of Rab11. XX XX GO GO:0015031; P:protein transport XX KW Membrane KW Transport KW Endosome XX FT From: PS51511 FT DOMAIN from..to FT /note="FIP-RBD #" XX Chop: Nter=0; Cter=0; Size: 53-73; Related: None; Repeats: 1; Topology: Undefined; Example: Q9D620; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00845; DC Domain; TR PROSITE; PS51512; DFDF; 1; level=0 XX Names: DFDF domain Function: The DFDF domain is a heterodimerization domain, which adopts a helical conformation upon binding. It folds into two consecutive alpha helices that are preceded and connected by the FDF and a related FDK sequence. XX XX FT From: PS51512 FT DOMAIN from..to FT /note="DFDF #" XX Chop: Nter=0; Cter=0; Size: 27-47; Related: None; Repeats: 1; Topology: Undefined; Example: Q9VVI2; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00846; DC Domain; TR PROSITE; PS51513; FFD; 1; level=0 XX Names: FFD box Function: The strongly conserved FFD box motif Y-x-K-x(3)-FFD-x-[IL]-S contained in Lsm13-15, but not Lsm16, homologs succeed the DFDF-x(7)-F motif and is also predicted to be of helical nature. XX FT From: PS51513 FT MOTIF from..to FT /note="FFD box #" XX Chop: Nter=0; Cter=0; Size: 7-27; Related: None; Repeats: 1; Topology: Undefined; Example: Q9HGL3; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00847; DC Domain; TR PROSITE; PS51514; BRX; 1; level=0 XX Names: BRX domain Function: The BRX domain has been shown to mediate homo- and heterotypic protein-protein interactions. XX XX FT From: PS51514 FT DOMAIN from..to FT /note="BRX #" XX Chop: Nter=0; Cter=0; Size: 46-92; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q17TI5; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00848; DC Domain; TR PROSITE; PS51515; BIN3_SAM; 1; level=0 XX Names: Bin3-type S-adenosyl-L-methionine (SAM) domain Function: The Bin3 domain contains a tripartite S-adenosyl-L-methionine (SAM) binding motif with all three sequence motifs, I/Ia, II, and III. XX XX KW S-adenosyl-L-methionine XX FT From: PS51515 FT DOMAIN from..to FT /note="Bin3-type SAM #" XX Chop: Nter=0; Cter=0; Size: 196-320; Related: None; Repeats: 1; Topology: Undefined; Example: Q8K3A9; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00849; DC Domain; TR PROSITE; PS51516; SOX_C; 1; level=0 XX Names: Sox C-terminal domain Function: Bioinformatic analysis of the C-termini of subgroup F Sox family members from different species including humans, mice, rat, chicken and Xenopus revealed three conserved blocks including highly conserved residues. They were termed proline, charged, and serine according to the predominance of the respective amino acids. The charged block comprises a strong transactivating domain. XX XX FT From: PS51516 FT DOMAIN from..to FT /note="Sox C-terminal #" XX Chop: Nter=0; Cter=0; Size: 105-151; Related: None; Repeats: 1; Topology: Undefined; Example: O42342; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00850; DC Domain; TR PROSITE; PS51517; NDT80; 1; level=0 XX Names: NDT80 DNA-binding domain Function: The NDT80 DNA-binding domain is found in proteins, which might all be involved in sensing nutritional status. XX XX GO GO:0003700; F:DNA-binding transcription factor activity XX KW DNA-binding XX FT From: PS51517 FT DNA_BIND from..to FT /note="NDT80 #" XX Chop: Nter=0; Cter=0; Size: 185-318; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y2G1; Scope: Eukaryota Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00851; DC Domain; TR PROSITE; PS51518; SGF29_C; 1; level=0 XX Names: SGF29 C-terminal domain Function: The SGF29 C-terminal domain contains a double Tudor-like motif that binds the H3K4me2/3 lysine methylation site on the N terminus of histone H3. XX CC -!- DOMAIN: The SGF29 tudor-like domain mediates binding to methylated CC 'Lys-4' of histone H3 (H3K4me). CC -!- SIMILARITY: Belongs to the SGF29 family. XX GO GO:0006325; P:chromatin organization GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Chromatin regulator KW Transcription KW Transcription regulation XX FT From: PS51518 FT DOMAIN from..to FT /note="SGF29 C-terminal #" FT REGION 44..46 FT /note="Histone H3K4me3 N-terminus binding" FT Group: 1; Condition: D-x*-[DE] case FT REGION 91..94 FT /note="Histone H3K4me3 N-terminus binding" end case FT REGION 115..118 FT /note="Histone H3K4me3 binding" FT Group: 1; Condition: F-x* FT SITE 89 FT /note="Histone H3K4me3 binding" FT Group: 1; Condition: Y FT SITE 96 FT /note="Histone H3K4me3 binding" FT Group: 1; Condition: Y XX Chop: Nter=0; Cter=0; Size: 126-152; Related: None; Repeats: 1; Topology: Undefined; Example: Q96ES7; Scope: Eukaryota Comments: None; XX # Revision 1.9 2022/06/27 // AC PRU00852; DC Domain; TR PROSITE; PS51519; RWP_RK; 1; level=0 XX Names: RWP-RK domain Function: The RWP-RK putative DNA-binding domain has been named after its most striking feature, the invariant R-W-P-x-R-K motif. It could be involved in the regulation of genes controlled by nitrogen status. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription GO GO:0005634; C:nucleus GO GO:0003677; F:DNA binding XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51519 FT DOMAIN from..to FT /note="RWP-RK #" XX Chop: Nter=0; Cter=0; Size: 72-105; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LE38; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.6 2022/06/27 // AC PRU00853; DC Domain; TR PROSITE; PS51520; NSP2PRO; 1; level=0 XX Names: Alphavirus nsp2 protease (nsp2pro) domain Function: The nsp2pro domain is a member of peptidase family C9 of clan CA. XX XX KW Protease XX FT From: PS51520 FT DOMAIN from..to FT /note="Peptidase C9 #" FT ACT_SITE 10 FT /note="For cysteine protease nsP2 activity" FT Condition: C FT ACT_SITE 80 FT /note="For cysteine protease nsP2 activity" FT Condition: H XX Chop: Nter=0; Cter=0; Size: 310-369; Related: None; Repeats: 1; Topology: Undefined; Example: Q4QXJ8; Scope: Viruses; Togaviridae Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00854; DC Domain; TR PROSITE; PS51521; HTUSP; 1; level=0 XX Names: Herpesvirus tegument ubiquitin-specific protease (htUSP) domain Function: All herpesviruses contain a Ubiquitin (Ub)-specific cysteine protease (USP) domain embedded within their large tegument protein. XX CC -!- SIMILARITY: Belongs to the herpesviridae large tegument protein family. XX GO GO:0019033; C:viral tegument XX KW Virion KW Virion tegument XX FT From: PS51521 FT DOMAIN from..to FT /note="Peptidase C76 #" case FT SITE 8 FT /note="Important for catalytic activity" FT Condition: Q end case FT ACT_SITE 21 FT Group: 1; Condition: C FT ACT_SITE 156 FT Group: 1; Condition: D FT ACT_SITE 158 FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 203-236; Related: None; Repeats: 1; Topology: Undefined; Example: P52340; Scope: Viruses; Herpesviridae Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00855; DC Domain; TR PROSITE; PS51522; ZF_NANOS; 1; level=0 XX Names: Zinc finger nanos-type Function: The nanos-type zinc finger has two conserved Cys-Cys-His-Cys (CCHC)- type zinc-finger motifs that are indispensable for nanos function. XX case and and and and and and and CC -!- DOMAIN: The Nanos-type zinc finger is composed of two C2HC motifs, each CC motif binding one molecule of zinc. It is essential for the translation CC repression activity of the protein. end case CC -!- SIMILARITY: Belongs to the nanos family. XX GO GO:0006417; P:regulation of translation GO GO:0003723; F:RNA binding case ( and and and ) or ( and and and ) GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW RNA-binding KW Translation regulation KW Zinc-finger XX FT From: PS51522 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="Nanos-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="Nanos-type #; atypical" else FT ZN_FING from..to FT /note="Nanos-type #; degenerate" end case case FT MOTIF 2..29 FT /note="C2HC #1" end case case FT MOTIF 37..53 FT /note="C2HC #2" end case FT BINDING 2 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 37 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 45-65; Related: None; Repeats: 1; Topology: Undefined; Example: P60323; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU00856; DC Domain; TR PROSITE; PS51523; ZF_HD_DIMER; 1; level=0 XX Names: Zinc-finger ZF-HD dimerization-type Function: It constitutes a dimerization domain which is sufficient for the formation of homo- and heterodimers. XX XX case KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51523 case and and and and and and and FT ZN_FING from..to FT /note="ZF-HD dimerization-type #" FT Tag: Zinc else case and and and and and and and FT ZN_FING from..to FT /note="ZF-HD dimerization-type #; atypical" FT Tag: Zinc else FT ZN_FING from..to FT /note="ZF-HD dimerization-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 40-60; Related: None; Repeats: 1; Topology: Undefined; Example: Q9SB61; Scope: Eukaryota; Arabidopsis Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00857; DC Domain; TR PROSITE; PS51525; NET; 1; level=0 XX Names: NET domain Function: The function of the NET domain is assumed to be protein binding. XX XX FT From: PS51525 FT DOMAIN from..to FT /note="NET #" XX Chop: Nter=0; Cter=0; Size: 70-95; Related: None; Repeats: 1; Topology: Undefined; Example: Q55C84; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00858; DC Domain; TR PROSITE; PS51526; RFX_DBD; 1; level=0 XX Names: RFX-type winged-helix DNA-binding domain Function: The characteristic RFX-type HTH DNA binding domain has been recruited into otherwise very divergent regulatory factors functioning in a diverse spectrum of unrelated systems, including regulation of the mitotic cell cycle in fission yeast, the control of the immune response in mammals, and infection by human hepatitis B virus. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the RFX family. XX GO GO:0003677; F:DNA binding GO GO:0005634; C:nucleus GO GO:0006351; P:DNA-templated transcription GO GO:0006355; P:regulation of DNA-templated transcription XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51526 FT DNA_BIND from..to FT /note="RFX-type winged-helix #" XX Chop: Nter=0; Cter=0; Size: 65-90; Related: None; Repeats: 1; Topology: Undefined; Example: P48379; Scope: Eukaryota Comments: None; XX # Revision 1.7 2022/06/27 // AC PRU00859; DC Domain; TR PROSITE; PS51527; FLAVIVIRUS_NS2B; 1; level=0 XX Names: Flavivirus NS2B domain Function: The NS3pro has a classical serine protease catalytic triad (His, Asp, and Ser). The enzymatic activity of NS3pro is enhanced by interacting with the central 40 amino acid of NS2B which acts as an essential cofactor. XX CC -!- FUNCTION: Serine protease subunit NS2B: Required cofactor for the CC serine protease function of NS3. XX GO GO:0033644; C:host cell membrane GO GO:0016020; C:membrane GO GO:0044165; C:host cell endoplasmic reticulum XX KW Host membrane KW Membrane KW Transmembrane KW Transmembrane helix KW Host endoplasmic reticulum XX FT From: PS51527 FT REGION 54..93 FT /note="Interacts with and activates NS3 protease" XX Chop: Nter=0; Cter=0; Size: 120-143; Related: None; Repeats: 1; Topology: Undefined; Example: P07564; Scope: Viruses; Flavivirus Comments: None; XX # Revision 1.9 2022/09/30 // AC PRU00860; DC Domain; TR PROSITE; PS51528; FLAVIVIRUS_NS3PRO; 1; level=0 XX Names: Flavivirus NS3 protease (NS3pro) domain Function: The NS3pro has a classical serine protease catalytic triad (His, Asp, and Ser). The enzymatic activity of NS3pro is enhanced by interacting with the central 40 amino acid of NS2B which acts as an essential cofactor. XX case CC -!- FUNCTION: Serine protease NS3: Displays three enzymatic activities: CC serine protease, NTPase and RNA helicase. NS3 serine protease, in CC association with NS2B, performs its autocleavage and cleaves the CC polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B- CC NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and CC unwinds dsRNA in the 3' to 5' direction. CC -!- SUBCELLULAR LOCATION: Serine protease NS3: Host endoplasmic reticulum CC membrane; Peripheral membrane protein; Cytoplasmic side. Note=Remains CC non-covalently associated to serine protease subunit NS2B. end case XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0008236; F:serine-type peptidase activity XX KW Cleavage on pair of basic residues KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51528 FT CHAIN ? FT /note="Serine protease NS3" FT DOMAIN from..to FT /note="Peptidase S7 #" FT ACT_SITE 53 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: H FT ACT_SITE 77 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: D FT ACT_SITE 137 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 168-191; Related: None; Repeats: 1; Topology: Undefined; Example: P07564; Scope: Viruses; Flaviviridae Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00861; DC Domain; TR PROSITE; PS51529; CYSTATIN_FETUIN_A; 1; level=0 XX Names: Fetuin-A-type cystatin domain Function: The cystatin fold is formed by a five stranded anti-parallel beta- sheet wrapped around a five-turn alpha-helix. XX CC -!- SIMILARITY: Belongs to the fetuin family. XX DR PROSITE; PS01254; FETUIN_1; 1; trigger=no DR PROSITE; PS01255; FETUIN_2; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51529 FT DOMAIN from..to FT /note="Cystatin fetuin-A-type #" FT DISULFID 3..6 FT Tag: disulf; Condition: C-x*-C FT DISULFID 68..79 FT Tag: disulf; Condition: C-x*-C FT DISULFID 93..112 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 97-127; Related: None; Repeats: 1-2; Topology: Undefined; Example: P02765; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00862; DC Domain; TR PROSITE; PS51530; CYSTATIN_FETUIN_B; 1; level=0 XX Names: Fetuin-B-type cystatin domain Function: The cystatin fold is formed by a five stranded anti-parallel beta- sheet wrapped around a five-turn alpha-helix. XX CC -!- SIMILARITY: Belongs to the fetuin family. XX DR PROSITE; PS01254; FETUIN_1; 1; trigger=no DR PROSITE; PS01255; FETUIN_2; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51530 FT DOMAIN from..to FT /note="Cystatin fetuin-B-type #" FT DISULFID 3..6 FT Tag: disulf; Condition: C-x*-C FT DISULFID 67..78 FT Tag: disulf; Condition: C-x*-C FT DISULFID 91..111 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 97-125; Related: None; Repeats: 2; Topology: Undefined; Example: Q9UGM5; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00863; DC Domain; TR PROSITE; PS51531; FV_PR; 1; level=0 XX Names: Foamy virus protease (FV PR) domain Function: The FV PR domain forms peptidase family A9 (spumapepsin family). Retrovriral PRs belong to the family of aspartic proteases and are active as homodimers, with the active site triplets (Asp-Thr/Ser-Gly; D-T/S-G) from both chain contributing to the symetric active site of the enzyme. XX case CC -!- SUBUNIT: The protease is a homodimer, whose active site consists of two CC apposed aspartic acid residues. XX GO GO:0004190; F:aspartic-type endopeptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Aspartyl protease KW Hydrolase KW Protease end case XX FT From: PS51531 FT DOMAIN from..to FT /note="Peptidase A9 #" FT ACT_SITE 21 FT /note="For protease activity" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 130-153; Related: None; Repeats: 1; Topology: Undefined; Example: P14350; Scope: Viruses; Spumavirus Comments: None; XX # Revision 1.7 2019/11/21 // AC PRU00864; DC Domain; TR PROSITE; PS51532; PITH; 1; level=0 XX Names: PITH domain Function: The proteasome-interacting thioredoxin (PITH) domain is a general proteasome-interacting module. XX XX FT From: PS51532 FT DOMAIN from..to FT /note="PITH #" XX Chop: Nter=0; Cter=0; Size: 161-187; Related: None; Repeats: 1; Topology: Undefined; Example: Q6NYX8; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00865; DC Domain; TR PROSITE; PS51533; ADD; 1; level=0 XX Names: ADD domain Function: The ADD domain is present in chromatin-associated proteins that play a role in establishing and/or maintaining a normal pattern of DNA methylation. XX XX case ( and and and ) or ( and and and and and and and ) GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51533 FT DOMAIN from..to FT /note="ADD #" FT ZN_FING 12..46 FT /note="GATA-type #; atypical" FT ZN_FING 57..111 FT /note="PHD-type #; atypical" XX Chop: Nter=0; Cter=0; Size: 86-148; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UJW3; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00867; DC Domain; TR PROSITE; PS51534; SEFIR; 1; level=0 XX Names: SEFIR domain Function: The SEFIR domain (after SEFs and IL17Rs) is a conserved sequence segment identified in transmembrane receptors (including SEFs, IL17Rs) and soluble factors (including CIKS/ACT1) in eukaryotes and bacteria. It is related to the TIR domain. The similarity between the SEFIR and TIR domains involves the conserved boxes 1 and 2 of the TIR domain that are implicated in homotypic dimerization, but there is no sequence similarity between SEFIR domains and the TIR sequence box 3. XX XX FT From: PS51534 FT DOMAIN from..to FT /note="SEFIR #" XX Chop: Nter=0; Cter=0; Size: 127-175; Related: None; Repeats: 1; Topology: Undefined; Example: Q8QHJ9; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00868; DC Domain; TR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1; level=0 XX Names: Pestivirus NS3 protease (NS3pro) domain Function: The NS3 protease (NS3pro) domain is of some 180 aa with a catalytic triad of His-Asp-Ser. XX XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0008236; F:serine-type peptidase activity XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51535 FT DOMAIN from..to FT /note="Peptidase S31 #" FT ACT_SITE 69 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: H FT ACT_SITE 106 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: D FT ACT_SITE 163 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 164-184; Related: None; Repeats: 1; Topology: Undefined; Example: P19711; Scope: Viruses; Pestivirus Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00869; DC Domain; TR PROSITE; PS51536; TFG; 1; level=0 XX Names: TFG box Function: The strongly conserved TFG box sequence motif [RKH]-x(2,5)-E-x(0-2)-[RK]-x(3,4)-[DE]-TFG contained in Lsm13-15, but not Lsm16, homologs succeed the DFDF-x(7)-F motif and is also predicted to be of helical nature. XX FT From: PS51536 FT MOTIF from..to FT /note="TFG box #" XX Chop: Nter=0; Cter=0; Size: 11-31; Related: None; Repeats: 1; Topology: Undefined; Example: Q9HGL3; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00870; DC Domain; TR PROSITE; PS51537; NV_3CL_PRO; 1; level=0 XX Names: Norovirus 3C-like protease (NV 3CLpro) domain Function: NV 3CLpros belong to the chymotrypsin-like protease family, in that they appear to have chymotrypsin-like folds. Whether the 3CLpro domain has a catalytic dyad of composed of histidine and cysteine or tryad of histidine, glutamate and cysteine remains controversial. XX case DE + Contains: DE RecName: Full=3C-like protease; DE Short=3CLpro; DE EC=3.4.22.66; XX CC -!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp is CC first released by autocleavage, then all other proteins are cleaved. CC May cleave polyadenylate-binding protein thereby inhibiting cellular CC translation. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endopeptidase with a preference for cleavage when the P1 CC position is occupied by Glu-|-Xaa and the P1' position is occupied by CC Gly-|-Yaa.; EC=3.4.22.66; CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro CC is first autocatalytically cleaved, then processes the whole CC polyprotein. end case XX case GO GO:0008234; F:cysteine-type peptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51537 FT DOMAIN from..to FT /note="Peptidase C37 #" FT ACT_SITE 30 FT /note="For 3CLpro activity" FT Group: 1; Condition: H FT ACT_SITE 54 FT /note="For 3CLpro activity" FT Group: 1; Condition: E FT ACT_SITE 139 FT /note="For 3CLpro activity" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 171-191; Related: None; Repeats: 1; Topology: Undefined; Example: P54634; Scope: Viruses; Norovirus Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00871; DC Domain; TR PROSITE; PS51538; AV_CP; 1; level=0 XX Names: Arterivirus nsp2 cysteine protease (AV CP) domain Function: The AV CP is an unusual Cys protease with amino acid sequence similarities to both papain-like and chymotrypsin-like proteases. The catalytic dyad is composed of Cys and His residues. The AV CP domain forms peptidase family C33. XX XX case GO GO:0008234; F:cysteine-type peptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0019082; P:viral protein processing XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51538 FT DOMAIN from..to FT /note="Peptidase C33 #" FT ACT_SITE 10 FT /note="For Nsp2 cysteine proteinase activity" FT Group: 1; Condition: C FT ACT_SITE 79 FT /note="For Nsp2 cysteine proteinase activity" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 90-118; Related: None; Repeats: 1; Topology: Undefined; Example: Q9YN02; Scope: Viruses; Arteriviridae Comments: None; XX # Revision 1.7 2019/11/21 // AC PRU00872; DC Domain; TR PROSITE; PS51539; AV_PCP_ALPHA; 1; level=0 XX Names: Arterivirus papain-like cysteine protease alpha (PCPalpha) domain Function: The PCPalpha domain mediates the nsp1alpha|1beta cleavage. XX XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51539 case FT DOMAIN from..to FT /note="Peptidase C31 #" else FT DOMAIN from..to FT /note="Peptidase C31 (inactive) #" end case FT ACT_SITE 8 FT /note="For Nsp1-alpha papain-like cysteine proteinase FT activity" FT Group: 1; Condition: C FT ACT_SITE 77 FT /note="For Nsp1-alpha papain-like cysteine proteinase FT activity" FT Group: 1; Condition: H case FT SITE to..to+1 FT /note="Cleavage; by autolysis" end case XX Chop: Nter=0; Cter=0; Size: 81-123; Related: None; Repeats: 1; Topology: Undefined; Example: Q9YN02; Scope: Viruses; Arteriviridae Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00873; DC Domain; TR PROSITE; PS51540; AV_PCP_BETA; 1; level=0 XX Names: Arterivirus papain-like cysteine protease beta (PCPbeta) domain Function: The PCPbeta domain mediates the nsp1beta|2 cleavage. XX XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51540 case FT DOMAIN from..to FT /note="Peptidase C32 #" else FT DOMAIN from..to FT /note="Peptidase C32 (inactive) #" end case FT ACT_SITE 8 FT /note="For Nsp1-beta papain-like cysteine proteinase FT activity" FT Group: 1; Condition: C FT ACT_SITE 73 FT /note="For Nsp1-beta papain-like cysteine proteinase FT activity" FT Group: 1; Condition: H case and FT SITE to..to+1 FT /note="Cleavage; by autolysis" FT Condition: G-[GA] else case FT SITE to..to+1 FT /note="Cleavage; by autolysis" end case XX Chop: Nter=0; Cter=0; Size: 94-131; Related: None; Repeats: 1; Topology: Undefined; Example: Q9YN02; Scope: Viruses; Arteriviridae Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00875; DC Domain; TR PROSITE; PS51542; FYRN; 1; level=0 XX Names: FYR domain FYRN motif Function: The FYRN and FYRC regions are not separate independently folded domains, but are components of a distinct protein module, The FYRN and FYRC motifs both form part of a single folded module (the FYR domain), which adopts an alpha+beta fold. XX XX FT From: PS51542 FT DOMAIN from..to FT /note="FYR N-terminal #" XX Chop: Nter=0; Cter=0; Size: 54-61; Related: None; Repeats: 1; Topology: Undefined; Example: P20659; Scope: Eukaryota Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00876; DC Domain; TR PROSITE; PS51543; FYRC; 1; level=0 XX Names: FYR domain FYRC motif Function: The FYRN and FYRC regions are not separate independently folded domains, but are components of a distinct protein module, The FYRN and FYRC motifs both form part of a single folded module (the FYR domain), which adopts an alpha+beta fold. XX XX FT From: PS51543 FT DOMAIN from..to FT /note="FYR C-terminal #" XX Chop: Nter=0; Cter=0; Size: 80-149; Related: None; Repeats: 1; Topology: Undefined; Example: P20659; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00877; DC Domain; TR PROSITE; PS51544; PI3K_ABD; 1; level=0 XX Names: Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain Function: The adaptor-binding domain (ABD) binds to p85, the regulatory subunit. XX CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. XX FT From: PS51544 FT DOMAIN from..to FT /note="PI3K-ABD #" XX Chop: Nter=0; Cter=0; Size: 1043-1571; Related: None; Repeats: 1; Topology: Undefined; Example: O02697; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00878; DC Domain; TR PROSITE; PS51545; PIK_HELICAL; 1; level=0 XX Names: PIK helical domain Function: The phosphoinositide kinase (PIK) domain is a region conserved among all PI3 and PI4-kinases and although its role is presently unclear, it is likely to be involved in substrate presentation. XX XX FT From: PS51545 FT DOMAIN from..to FT /note="PIK helical #" XX Chop: Nter=0; Cter=0; Size: 801-2044; Related: None; Repeats: 1; Topology: Undefined; Example: P42339; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00879; DC Domain; TR PROSITE; PS51546; PI3K_RBD; 1; level=0 XX Names: Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain Function: PI3K RBD is a Ras-binding domain. XX CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. XX GO GO:0048015; P:phosphatidylinositol-mediated signaling XX FT From: PS51546 FT DOMAIN from..to FT /note="PI3K-RBD #" XX Chop: Nter=0; Cter=0; Size: 77-124; Related: None; Repeats: 1; Topology: Undefined; Example: Q8BTI9; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00880; DC Domain; TR PROSITE; PS51547; C2_PI3K; 1; level=0 XX Names: C2 phosphatidylinositol 3-kinase (PI3K)-type domain Function: The putative membrane-binding PI3K-type C2 domain is an eight- stranded antiparallel beta-sandwich consisting of two four-stranded beta- sheets. XX CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. XX FT From: PS51547 FT DOMAIN from..to FT /note="C2 PI3K-type #" XX Chop: Nter=0; Cter=0; Size: 801-1857; Related: None; Repeats: 1; Topology: Undefined; Example: P42339; Scope: Eukaryota Comments: None; XX # Revision 1.4 2020/01/03 // AC PRU00881; DC Domain; TR PROSITE; PS51548; BIRNAVIRUS_VP4_PRO; 1; level=0 XX Names: Birnavirus VP4 protease domain Function: The birnavirus VP4 protease domain displays a catalytic serine/ lysine dyad in its active site. XX case CC -!- FUNCTION: Protease VP4 is a serine protease that cleaves the CC polyprotein into its final products. Pre-VP2 is first partially CC cleaved, and may be completely processed by VP4 upon capsid maturation. end case XX case GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity GO GO:0008236; F:serine-type peptidase activity XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51548 FT DOMAIN from..to FT /note="Peptidase S50 #" FT ACT_SITE 125 FT /note="Nucleophile" FT Group: 1; Condition: S FT ACT_SITE 163 FT Group: 1; Condition: K XX Chop: Nter=0; Cter=0; Size: 972-1069; Related: None; Repeats: 1; Topology: Undefined; Example: P22351; Scope: Viruses; Birnaviridae Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00882; DC Domain; TR PROSITE; PS51549; DM13; 1; level=0 XX Names: DM13 domain Function: The DM13 domain contains a nearly absolutely conserved cysteine, which can be potentially involved in a redox reaction either as a nacked thiol group or by binding a prosthetic group like heme. XX XX FT From: PS51549 FT DOMAIN from..to FT /note="DM13 #" XX Chop: Nter=0; Cter=0; Size: 98-120; Related: None; Repeats: 2; Topology: Undefined; Example: Q9GPJ1; Scope: Eukaryota; Sophophora Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00883; DC Domain; TR PROSITE; PS51550; EPH_LBD; 1; level=0 XX Names: Eph receptor ligand-binding domain Function: The extracellular Eph receptor region contains a conserved 180- amino-acid N-terminal ligand-binding domain (LBD) which is both necessary and sufficient for bindings of the receptors to their ephrin ligands. XX XX FT From: PS51550 FT DOMAIN from..to FT /note="Eph LBD #" XX Chop: Nter=0; Cter=0; Size: 109-215; Related: None; Repeats: 1; Topology: Undefined; Example: Q91571; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00884; DC Domain; TR PROSITE; PS51551; EPHRIN_RBD_2; 1; level=0 XX Names: Ephrin receptor-binding (ephrin RBD) domain Function: Ephrins are a family of proteins that are ligands of class V (EPH- related) receptor protein-tyrosine kinases. XX CC -!- SIMILARITY: Belongs to the ephrin family. XX DR PROSITE; PS01299; EPHRIN_RBD_1; 1; trigger=no XX case KW Disulfide bond end case XX FT From: PS51551 FT DOMAIN from..to FT /note="Ephrin RBD #" FT DISULFID 35..75 FT Tag: disulf; Condition: C-x*-C FT DISULFID 63..127 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 121-169; Related: None; Repeats: 1; Topology: Undefined; Example: Q15768; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00886; DC Domain; TR PROSITE; PS51553; GMPS_ATP_PPASE; 1; level=0 XX Names: GMP synthetase ATP pyrophosphatase (GMPS ATP-PPase) domain Function: The GMP synthetase ATP-PPase ATP-binding domain is a twisted, five- stranded parallel beta-sheet sandwiched between helical layers. It contains a glycine rich ATP-binding motif called the "P-loop motif" located after the first beta-strand XX GO GO:0005524; F:ATP binding GO GO:0006177; P:GMP biosynthetic process GO GO:0000166; F:nucleotide binding GO GO:0006164; P:purine nucleotide biosynthetic process XX KW ATP-binding KW GMP biosynthesis KW Nucleotide-binding KW Purine biosynthesis XX FT From: PS51553 FT DOMAIN from..to FT /note="GMPS ATP-PPase #" FT BINDING 28..34 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="#" XX Chop: Nter=0; Cter=0; Size: 172-208; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TYD7; Scope: Bacteria Archaea Eukaryota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU00887; DC Domain; TR PROSITE; PS51554; PFL; 1; level=0 XX Names: Pyruvate formate (PFL) lyase domain Function: Pyruvate formate lyase (PFL) catalyzes the non-oxidative conversion of pyruvate and CoA to formate and acetyl-CoA. Several other enzymes have been identified in the pyruvate formate lyase family: ketoacid formate lyase, glycerol dehydratase (GD), benzyl succinate synthetase and p-hydroxyphenylacetate decarboxylase XX XX FT From: PS51554 FT DOMAIN from..to FT /note="PFL #" XX Chop: Nter=0; Cter=0; Size: 54-747; Related: None; Repeats: 1; Topology: Undefined; Example: Q8CTX6; Scope: Bacteria Eukaryota; Chlamydomonas Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00888; DC Domain; c? =872> and TR PROSITE; PS51555; SAM_MT12; 1; level=0 XX Names: Methionine S-methyltransferase (EC 2.1.1.12) Function: Methionine S-methyltransferase (EC 2.1.1.12) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-methionine to form S-methyl-L-methionine and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionine + S-adenosyl-L-methionine = S-adenosyl-L- CC homocysteine + S-methyl-L-methionine; Xref=Rhea:RHEA:13761, CC ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:58252, CC ChEBI:CHEBI:59789; EC=2.1.1.12; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. XX GO GO:0030732; F:methionine S-methyltransferase activity GO GO:0032259; P:methylation XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9SWR3; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.10 2019/11/21 // AC PRU00889; DC Domain; c? =200> and TR PROSITE; PS51556; SAM_MT_MG_PIX; 1; level=0 XX Names: Magnesium protoporphyrin IX methyltransferase (EC 2.1.1.11) Function: Magnesium protoporphyrin IX methyltransferase (EC 2.1.1.11) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to magnesium protoporphyrin IX to form magnesium protoporphyrin IX 13-methyl ester and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.11; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Mg-protoporphyrin IX + S-adenosyl-L-methionine = Mg- CC protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:17809, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:60491, ChEBI:CHEBI:60492; EC=2.1.1.11; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Magnesium protoporphyrin O-methyltransferase family. XX GO GO:0046406; F:magnesium protoporphyrin IX methyltransferase activity GO GO:0015979; P:photosynthesis GO GO:0030494; P:bacteriochlorophyll biosynthetic process GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Chlorophyll biosynthesis KW Methyltransferase KW Photosynthesis KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P26236; Scope: Bacteria Comments: None; XX # Revision 1.8 2019/11/21 // AC PRU00892; DC Domain; TR PROSITE; PS51559; SAM_RMT2; 1; level=0 XX Names: Arginine and arginine-like N-methyltransferase. Function: Guanidinoacetate N-methyltransferase (EC 2.1.1.2) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to guanidinoacetate to form creatine and S-adenosyl-L-homocysteine. XX case and =210> and DE + RecName: EC=2.1.1.2; else DE + RecName: EC=2.1.1.-; end case XX case and =210> and CC -!- CATALYTIC ACTIVITY: CC Reaction=guanidinoacetate + S-adenosyl-L-methionine = creatine + H(+) + CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10656, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57742, ChEBI:CHEBI:57856, ChEBI:CHEBI:57947, CC ChEBI:CHEBI:59789; EC=2.1.1.2; end case CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RMT2 methyltransferase family. XX case and =210> and GO GO:0030731; F:guanidinoacetate N-methyltransferase activity else case ( or ) and =315> and GO GO:0019702; F:protein arginine N5-methyltransferase activity else GO GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity end case GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51559 FT DOMAIN from..to FT /note="RMT2 #" FT BINDING 69..74 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [FH]-G-[LM]-[AGS]-[IL]-[AFISV] FT REGION 90..92 FT /note="S-adenosyl-L-methionine" FT Condition: E-[ACP]-[HN] FT BINDING 117..118 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: W-[EQ] case and =210> and FT BINDING 169..170 FT /ligand="guanidinoacetate" FT /ligand_id="ChEBI:CHEBI:57742" FT Condition: L-T end case FT BINDING 20 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [FWY] case and =210> and FT BINDING 41 FT /ligand="guanidinoacetate" FT /ligand_id="ChEBI:CHEBI:57742" FT Condition: M FT BINDING 45 FT /ligand="guanidinoacetate" FT /ligand_id="ChEBI:CHEBI:57742" FT Condition: E end case FT BINDING 49 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [MS] case and =210> and FT BINDING 137 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 137 FT /ligand="guanidinoacetate" FT /ligand_id="ChEBI:CHEBI:57742" FT Condition: D else FT BINDING 137 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D end case XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P10868; Scope: Eukaryota Comments: None; XX # Revision 1.20 2022/11/19 // AC PRU00893; DC Domain; c? =229> and TR PROSITE; PS51560; SAM_MT_NNT1; 1; level=0 XX Names: Nicotinamide N-methyltransferase (EC 2.1.1.1) Function: Nicotinamide N-methyltransferase (EC 2.1.1.1) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide to form 1-methylnicotinamide and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=nicotinamide + S-adenosyl-L-methionine = 1-methylnicotinamide CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23884, ChEBI:CHEBI:16797, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.1; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. NNT1 family. XX GO GO:0008112; F:nicotinamide N-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UT28; Scope: Eukaryota; Dikarya Comments: None; XX # Revision 1.9 2019/11/21 // AC PRU00894; DC Domain; c? =211> and TR PROSITE; PS51561; SAM_NNMT_PNMT_TEMT_1; 1; level=0 XX Names: Nicotinamide N-methyltransferase (EC 2.1.1.1) Function: Nicotinamide N-methyltransferase (EC 2.1.1.1) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide to form 1-methylnicotinamide and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=nicotinamide + S-adenosyl-L-methionine = 1-methylnicotinamide CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23884, ChEBI:CHEBI:16797, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.1; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. NNMT/PNMT/TEMT family. XX GO GO:0008112; F:nicotinamide N-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51561 FT BINDING 63..64 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 142..143 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 20 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 25 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 69 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 85 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 90 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: N FT BINDING 163 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [AFLT] XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q06AV1; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.14 2022/11/19 // AC PRU00895; DC Domain; TR PROSITE; PS51562; RNA_CAP0_MT; 1; level=0 XX Names: mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56) Function: mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to G(5')pppR-RNA to form m(7)G(5')pppR-RNA and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.56; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; case CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. mRNA cap 0 methyltransferase family. else case CC -!- SIMILARITY: In the C-terminal section; belongs to the class I-like SAM- CC binding methyltransferase superfamily. mRNA cap 0 methyltransferase CC family. end case XX GO GO:0003723; F:RNA binding GO GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity GO GO:0006370; P:7-methylguanosine mRNA capping GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW mRNA capping KW mRNA processing KW RNA-binding KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51562 FT DOMAIN from..to FT /note="mRNA cap 0 methyltransferase #" FT BINDING 10..11 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT Condition: x-N case FT BINDING 91..92 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE]-x end case FT BINDING 117..119 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: x-F-x FT BINDING 14 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: K FT BINDING 35 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [ADCG] FT BINDING 57 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT SITE 38 FT /note="mRNA cap binding" FT Condition: K FT SITE 44 FT /note="mRNA cap binding" FT Condition: K FT SITE 69 FT /note="mRNA cap binding" FT Condition: R FT SITE 121 FT /note="mRNA cap binding" FT Condition: H FT SITE 209 FT /note="mRNA cap binding" FT Condition: E FT SITE 278 FT /note="mRNA cap binding" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: 220-365; Related: None; Repeats: 1; Topology: Undefined; Example: Q8SR66; P04298; Scope: Eukaryota Viruses Comments: None; XX # Revision 1.28 2024/01/11 // AC PRU00896; DC Domain; c? =464> and TR PROSITE; PS51563; SAM_MTA70L_1; 1; level=0 XX Names: N6-adenosine-methyltransferase catalytic subunit (EC=2.1.1.348) N6-adenosine-methyltransferase 70 kDa subunit (MT-A70) Function: The N6-methyltransferase complex methylates adenosine residues at the N(6) position of some RNAs. XX DE + RecName: EC=2.1.1.348; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(6)- CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:55584, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; EC=2.1.1.348; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. MT-A70-like family. XX GO GO:0003723; F:RNA binding GO GO:0016422; F:mRNA (2'-O-methyladenosine-N6-)-methyltransferase activity GO GO:0001734; F:mRNA (N6-adenosine)-methyltransferase activity GO GO:0032259; P:methylation GO GO:0001510; P:RNA methylation XX KW Methyltransferase KW RNA-binding KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: F1R777; Scope: Eukaryota Comments: None; XX # Revision 1.11 2022/01/03 // AC PRU00897; DC Domain; c? =242> and TR PROSITE; PS51564; SAM_ICMT; 1; level=0 XX Names: Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) Function: Protein-S-isoprenylcysteine O-methyltransferase (EC 2.1.1.100) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to a protein C-terminal S-farnesyl-L-cysteine to form a protein C-terminal S- farnesyl-L-cysteine methyl ester and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.100; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=[protein]-C-terminal S-[(2E,6E)-farnesyl]-L-cysteine + S- CC adenosyl-L-methionine = [protein]-C-terminal S-[(2E,6E)-farnesyl]-L- CC cysteine methyl ester + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:21672, Rhea:RHEA-COMP:12125, Rhea:RHEA-COMP:12126, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90510, CC ChEBI:CHEBI:90511; EC=2.1.1.100; CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase CC superfamily. Isoprenylcysteine carboxyl methyltransferase family. XX GO GO:0004671; F:protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O60725; Scope: Eukaryota Comments: None; XX # Revision 1.8 2019/11/21 // AC PRU00898; DC Domain; TR PROSITE; PS51565; SAM_MT85_SETD3; 1; level=0 XX Names: SETD3 actin-histidine N-methyltransferase (EC 2.1.1.85) Function: SETD3 Actin-histidine N-methyltransferase (EC 2.1.1.85) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-histidine-[actin] to form N(tele)-methyl-L-histidine-[actin] and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.85; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + CC N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. SETD3 actin-histidine methyltransferase family. XX GO GO:0018021; P:peptidyl-histidine methylation GO GO:0030047; P:actin modification XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q86TU7; Scope: Eukaryota Comments: None; XX # Revision 1.14 2019/11/21 // AC PRU00899; DC Domain; c? =847> and TR PROSITE; PS51566; SAM_MT43_TRX_MLL; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. TRX/MLL CC subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9M364; Scope: Eukaryota Comments: None; XX # Revision 1.16 2023/03/27 // AC PRU00900; DC Domain; TR PROSITE; PS51567; SAM_MT43_SUVAR420_1; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar4-20 CC subfamily. XX GO GO:0042799; F:histone H4K20 methyltransferase activity XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5AZY3; Scope: Eukaryota Comments: None; XX # Revision 1.11 2022/09/30 // AC PRU00901; DC Domain; TR PROSITE; PS51568; SAM_MT43_SET2_1; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily. XX GO GO:0046975; F:histone H3K36 methyltransferase activity XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q757Y8; Scope: Eukaryota Comments: None; XX # Revision 1.11 2022/09/30 // AC PRU00902; DC Domain; TR PROSITE; PS51569; DOT1; 1; level=0 XX Names: Histone-lysine N-methyltransferase DOT1 (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX case DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. DOT1 family. end case XX case GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase end case XX FT From: PS51569 FT DOMAIN from..to FT /note="DOT1 #" case FT BINDING 120..123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y-G-E-x FT BINDING 143..152 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [FLV]-x-D-x-G-[ACS]-G-x-G-x FT BINDING 206..207 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: x-F end case FT BINDING 170 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: [DE] XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q04089; Scope: Eukaryota Comments: None; XX # Revision 1.22 2023/03/27 // AC PRU00903; DC Domain; TR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar4-20 CC subfamily. XX GO GO:0042799; F:histone H4K20 methyltransferase activity GO GO:0034773; P:histone H4-K20 trimethylation XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q86Y97; Scope: Eukaryota Comments: None; XX # Revision 1.10 2022/09/30 // AC PRU00904; DC Domain; TR PROSITE; PS51571; SAM_MT43_PR_SET; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. PR/SET subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51571 FT BINDING 221..223 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 293..294 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 266 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q0V9E9; Scope: Eukaryota Comments: None; XX # Revision 1.18 2023/03/27 // AC PRU00905; DC Domain; c? =891> and TR PROSITE; PS51572; SAM_MT43_1; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q75D88; Scope: Eukaryota Comments: None; XX # Revision 1.15 2023/03/27 // AC PRU00906; DC Domain; c? =1010> and TR PROSITE; PS51573; SAM_MT43_SUVAR39_1; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar3-9 CC subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q15047; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.13 2023/03/27 // AC PRU00907; DC Domain; c? =342> and TR PROSITE; PS51574; SAM_MT43_2; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9H7B4; Scope: Eukaryota Comments: None; XX # Revision 1.14 2023/03/27 // AC PRU00908; DC Domain; c? =583> and TR PROSITE; PS51575; SAM_MT43_SUVAR39_2; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar3-9 CC subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8VZ17; Scope: Eukaryota Comments: None; XX # Revision 1.13 2023/03/27 // AC PRU00909; DC Domain; TR PROSITE; PS51576; SAM_MT43_EZ; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. EZ subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9ZSM8; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.14 2023/03/27 // AC PRU00910; DC Domain; c? =315> and TR PROSITE; PS51577; SAM_MT43_SET7; 1; level=0 XX Names: Histone-lysine N-methyltransferase Function: Histone-lysine N-methyltransferase is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.364; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. SET7 subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51577 FT BINDING 247..249 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8WTS6; Scope: Eukaryota; Chordata Comments: None; XX # Revision 1.20 2023/03/27 // AC PRU00911; DC Domain; TR PROSITE; PS51578; SAM_MT43_SET2_2; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q945S8; Scope: Eukaryota Comments: None; XX # Revision 1.12 2023/03/27 // AC PRU00912; DC Domain; TR PROSITE; PS51579; SAM_MT43_SUVAR39_3; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. Suvar3-9 CC subfamily. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9EQQ0; Scope: Eukaryota Comments: None; XX # Revision 1.12 2023/03/27 // AC PRU00913; DC Domain; TR PROSITE; PS51580; SAM_MT43_3; 1; level=0 XX Names: Histone-lysine N-methyltransferase (EC 2.1.1.43) Function: Histone-lysine N-methyltransferase (EC 2.1.1.43) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to L-lysine- [histone] to form N(6)-methyl-L-lysine-[histone] and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)- CC methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Histone-lysine methyltransferase family. XX GO GO:0032259; P:methylation GO GO:0042054; F:histone methyltransferase activity GO GO:0034968; P:histone lysine methylation GO GO:0016740; F:transferase activity GO GO:0008168; F:methyltransferase activity GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8W595; Scope: Eukaryota; Arabidopsis Comments: None; XX # Revision 1.13 2023/03/27 // AC PRU00914; DC Domain; TR PROSITE; PS51581; SAM_GTMT; 1; level=0 XX Names: Gammma-tocopherol O-methyltransferase (gTMT) Function: Tocopherol O-methyltransferase (EC 2.1.1.95) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to gamma- tocopherol to form alpha-tocopherol and S-adenosyl-L-homocysteine. The cyanobacterial orthologue sll0418 (EC 2.1.1.295) methylates 2-methyl-6- phytyl-1,4-benzoquinone/2-methyl-6-solanyl-1,4-benzoquinone (MPBQ/MSBQ) to yield 2,3-dimethyl-5-phytylbenzoquinone/2,3-dimethyl/plastoquinol-9. XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. gTMT family. XX GO GO:0032259; P:methylation XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51581 FT REGION 76..85 FT /note="SAM motif I" FT REGION 139..147 FT /note="SAM motif II" FT REGION 166..175 FT /note="SAM motif III" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q6WEE4; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.11 2019/11/21 // AC PRU00915; DC Domain; c? =393> and TR PROSITE; PS51582; SAM_PEAMT; 1; level=0 XX Names: Phosphoethanolamine N-methyltransferase (EC 2.1.1.103) Function: Phosphoethanolamine N-methyltransferase (EC 2.1.1.103) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to ethanolamine phosphate to form N-methylethanolamine phosphate and S-adenosyl- L-homocysteine. XX DE + RecName: EC=2.1.1.103; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphoethanolamine + S-adenosyl-L-methionine = H(+) + N- CC methylethanolamine phosphate + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:20365, ChEBI:CHEBI:15378, ChEBI:CHEBI:57781, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58190, ChEBI:CHEBI:59789; CC EC=2.1.1.103; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. PEAMT family. XX GO GO:0000234; F:phosphoethanolamine N-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q944H0; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.10 2022/04/04 // AC PRU00916; DC Domain; c? =440> and TR PROSITE; PS51583; SAM_MT127; 1; level=0 XX Names: Protein-lysine methyltransferase LSMT Function: LSMT homologs from plants display different substrate specificities, with targets involved in carbon metabolism. XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. Plant protein-lysine LSMT methyltransferase family. XX GO GO:0016278; F:lysine N-methyltransferase activity XX KW Methyltransferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9XI84; Scope: Eukaryota; Pentapetalae Comments: None; XX # Revision 1.11 2019/11/21 // AC PRU00918; DC Domain; TR PROSITE; PS51585; SAM_MT_TPMT; 1; level=0 XX Names: Thiopurine or thiol or thiocyanate S-methyltransferase (TPMT). Function: Thiol S-methyltransferase (EC 2.1.1.9) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to a thiol to form a thioether and S-adenosyl-L-homocysteine. Thiocyanate S-methyltransferase (EC 2.1.1.n4) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to thiocyanate to form methyl thiocyanate and S-adenosyl-L-homocysteine. Thiopurine S-methyltransferase (EC 2.1.1.67) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to a thiopurine to form methyl a thiopurine S-methylether and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TPMT family. XX GO GO:0008172; F:S-methyltransferase activity GO GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity GO GO:0032259; P:methylation XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51585 FT BINDING 70 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: W FT BINDING 125 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q6AWU6; Scope: Eukaryota; Brassicaceae Comments: None; XX # Revision 1.13 2022/11/19 // AC PRU00922; DC Domain; c? =756> and TR PROSITE; PS51589; SAM_MT56_VP3; 1; level=0 XX Names: Viral protein 3 containing mRNA (guanine-N(7))-methyltransferase. Function: mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to G(5')pppR-RNA to form m(7)G(5')pppR-RNA and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.56; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; XX GO GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q65526; Scope: Viruses Comments: None; XX # Revision 1.16 2024/01/11 // AC PRU00923; DC Domain; TR PROSITE; PS51590; SAM_MT_MNV_L; 1; level=0 XX Names: Mononegavirus L protein 2'O-ribose MTase. Function: cap 1 MTase XX DE + RecName: EC=2.1.1.-; XX GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51590 FT DOMAIN from..to FT /note="Mononegavirus-type SAM-dependent 2'-O-MTase #" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: A4UHQ2; Scope: Viruses; Mononegavirales Comments: None; XX # Revision 1.11 2019/11/21 // AC PRU00924; DC Domain; TR PROSITE; PS51591; RNA_CAP01_NS5_MT; 1; level=0 XX Names: mRNA cap 0 and cap 1 methyltransferase (EC 2.1.1.56 and EC 2.1.1.57) Function: mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56) is an enzyme that transfers a methyl group from SAM to G(5')pppR-RNA to form m(7)G(5')pppR-RNA and SAH. mRNA (nucleoside-2'-O-)-methyltransferase (EC 2.1.1.57) is an enzyme that transfers a methyl group from SAM to m(7)G(5')pppR-RNA to form m(7)G(5')pppRm-RNA and SAH. XX DE + RecName: EC=2.1.1.56; DE EC=2.1.1.57; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S- CC adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA- CC COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, CC ChEBI:CHEBI:167617; EC=2.1.1.56; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside CC in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'- CC triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S- CC adenosyl-L-homocysteine; Xref=Rhea:RHEA:67020, Rhea:RHEA-COMP:17167, CC Rhea:RHEA-COMP:17168, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167609; CC EC=2.1.1.57; CC -!- SIMILARITY: In the N-terminal section; belongs to the class I-like SAM- CC binding methyltransferase superfamily. mRNA cap 0-1 NS5-type CC methyltransferase family. XX GO GO:0003723; F:RNA binding GO GO:0004482; F:mRNA 5'-cap (guanine-N7-)-methyltransferase activity GO GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity GO GO:0006370; P:7-methylguanosine mRNA capping GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW mRNA capping KW mRNA processing KW RNA-binding KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51591 FT DOMAIN from..to FT /note="mRNA cap 0-1 NS5-type MT #" FT BINDING 56 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S FT BINDING 86 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 87 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: W FT BINDING 104 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: T FT BINDING 105 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [ILK] FT BINDING 131 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 132 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [IV] FT BINDING 147 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: I FT BINDING 220 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT SITE 13 FT /note="mRNA cap binding" FT Condition: K FT SITE 16 FT /note="mRNA cap binding; via carbonyl oxygen" FT Condition: L FT SITE 17 FT /note="mRNA cap binding" FT Condition: N FT SITE 19 FT /note="mRNA cap binding; via carbonyl oxygen" FT Condition: [CLM] FT SITE 24 FT /note="mRNA cap binding" FT Condition: F FT SITE 28 FT /note="mRNA cap binding" FT Condition: [KR] FT SITE 61 FT /note="Essential for 2'-O-methyltransferase activity" FT Condition: K FT SITE 146 FT /note="Essential for 2'-O-methyltransferase and N-7 FT methyltransferase activity" FT Condition: D FT SITE 150 FT /note="mRNA cap binding" FT Condition: S FT SITE 182 FT /note="Essential for 2'-O-methyltransferase activity" FT Condition: K FT SITE 213 FT /note="mRNA cap binding" FT Condition: R FT SITE 215 FT /note="mRNA cap binding" FT Condition: S FT SITE 218 FT /note="Essential for 2'-O-methyltransferase activity" FT Condition: E XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P12823; P06935; P03314; Scope: Viruses; Flavivirus Comments: None; XX # Revision 1.21 2024/01/11 // AC PRU00925; DC Domain; c? =410> and TR PROSITE; PS51592; SAM_MTA70L_2; 1; level=0 XX Names: mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase-like (MT-A70-like) Function: mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase (EC 2.1.1.62) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to m(7)G(5')pppAm to form m(7)G(5')pppm(6)Am and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. MT-A70-like family. XX GO GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5ZK35; Scope: Eukaryota Comments: None; XX # Revision 1.7 2019/11/21 // AC PRU00929; DC Domain; c? =235> and TR PROSITE; PS51597; SAM_HNMT; 1; level=0 XX Names: Histamine N-methyltransferase Function: Histamine N-methyltransferase (EC 2.1.1.8) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to histamine to form N(tau) methylhistamine and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.8; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=histamine + S-adenosyl-L-methionine = H(+) + N(tau)- CC methylhistamine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19301, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58432, CC ChEBI:CHEBI:58600, ChEBI:CHEBI:59789; EC=2.1.1.8; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. HNMT family. XX GO GO:0046539; F:histamine N-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51597 FT BINDING 28 FT /ligand="substrate" FT Condition: E FT BINDING 283 FT /ligand="substrate" FT Condition: N FT BINDING 60 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 89 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: E FT BINDING 94 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Q FT BINDING 120 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S FT BINDING 142 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: I FT BINDING 283 FT /ligand="substrate" FT Condition: N XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5R7C3; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU00930; DC Domain; c? =725> and TR PROSITE; PS51598; SAM_CHO2; 1; level=0 XX Names: Phosphatidylethanolamine N-methyltransferase Function: Phosphatidylethanolamine N-methyltransferase (EC 2.1.1.17) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to phosphatidylethanolamine to form phosphatidyl-N-methylethanolamine and S- adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.17; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L- CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17; CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase CC superfamily. CHO2 family. XX GO GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity GO GO:0008654; P:phospholipid biosynthetic process GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Lipid biosynthesis KW Lipid metabolism KW Methyltransferase KW Phospholipid biosynthesis KW Phospholipid metabolism KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: A2R616; Scope: Eukaryota; Dikarya Comments: None; XX # Revision 1.7 2019/11/21 // AC PRU00931; DC Domain; TR PROSITE; PS51599; SAM_PEMT_PEM2; 1; level=0 XX Names: Phospholipid methyltransferases (EC 2.1.1.17 and EC=2.1.1.71) family Function: Phosphatidylethanolamine N-methyltransferase (EC 2.1.1.17) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to phosphatidylethanolamine to form phosphatidyl-N-methylethanolamine and S- adenosyl-L-homocysteine. Phosphatidyl-N-methylethanolamine N-methyltransferase (EC 2.1.1.71) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to phosphatidyl-N-methylethanolamine to form phosphatidyl-N- dimethylethanolamine and S-adenosyl-L-homocysteine. It also transfers a methyl group from S-adenosyl-L-methionine (SAM) to phosphatidyl-N- dimethylethanolamine to form phosphatidylcholine and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.17; DE + RecName: EC=2.1.1.71; XX CC -!- FUNCTION: Catalyzes three sequential methylation reactions of CC phosphatidylethanolamine (PE) by AdoMet, thereby producing CC phosphatidylcholine (PC). CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + S- CC adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N,N- CC dimethylethanolamine + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:32735, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572, ChEBI:CHEBI:64573; EC=2.1.1.71; CC -!- CATALYTIC ACTIVITY: CC Reaction=1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine + S- CC adenosyl-L-methionine = a 1,2-diacyl-sn-glycero-3-phosphocholine + CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32739, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57643, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:64572; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L- CC methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis. CC -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase CC superfamily. PEMT/PEM2 methyltransferase family. XX GO GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity GO GO:0000773; F:phosphatidyl-N-methylethanolamine N-methyltransferase activity GO GO:0080101; F:phosphatidyl-N-dimethylethanolamine N-methyltransferase activity GO GO:0006656; P:phosphatidylcholine biosynthetic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase KW Lipid biosynthesis KW Lipid metabolism KW Phospholipid biosynthesis KW Phospholipid metabolism XX Chop: Nter=0; Cter=0; Size: 174-211; Related: None; Repeats: 1; Topology: Undefined; Example: Q08388; Scope: Eukaryota Comments: None; XX # Revision 1.12 2019/11/21 // AC PRU00932; DC Domain; TR PROSITE; PS51600; SAM_GNMT; 1; level=0 XX Names: Glycine and glycine/sarcosine N-methyltransferase EC 2.1.1.20 and EC 2.1.1.156 Function: Glycine N-methyltransferase (EC 2.1.1.20) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to glycine to form sarcosine and S-adenosyl-L-homocysteine. Glycine/sarcosine N-methyltransferase (EC 2.1.1.156) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to glycine to form sarcosine and S-adenosyl-L-homocysteine AND transfers a methyl group from S-adenosyl-L-methionine (SAM) to sarcosine to form N,N-dimethylglycine and S-adenosyl-L-homocysteine. XX case and ( or ) DE + RecName: EC=2.1.1.156; else case DE + RecName: EC=2.1.1.20; end case XX case and ( or ) CC -!- CATALYTIC ACTIVITY: CC Reaction=glycine + 2 S-adenosyl-L-methionine = 2 H(+) + N,N- CC dimethylglycine + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:32463, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:58251, ChEBI:CHEBI:59789; EC=2.1.1.156; else case CC -!- CATALYTIC ACTIVITY: CC Reaction=glycine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L- CC homocysteine + sarcosine; Xref=Rhea:RHEA:19937, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57433, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789; EC=2.1.1.20; end case CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Glycine N-methyltransferase family. XX case GO GO:0017174; F:glycine N-methyltransferase activity end case case and ( or ) GO GO:0052730; F:sarcosine N-methyltransferase activity end case case GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process end case XX case KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase end case XX FT From: PS51600 case FT BINDING 122..123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DN]-W end case FT BINDING 27 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: Y case FT BINDING 36 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [WY] FT BINDING 39 FT /ligand="substrate" FT Condition: Y FT BINDING 46 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: R FT BINDING 70 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [AS] FT BINDING 91 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 143 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [FMLQ] FT BINDING 145 FT /ligand="substrate" FT Condition: [NS] end case FT BINDING 179 FT /ligand="substrate" FT Group: 1; Condition: R case FT BINDING 223 FT /ligand="substrate" end case XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P13255; Scope: Eukaryota; Eutheria Bacteria Comments: None; XX # Revision 1.13 2022/11/19 // AC PRU00933; DC Domain; c? =218> and TR PROSITE; PS51601; SAM_NNMT_PNMT_TEMT_3; 1; level=0 XX Names: NNMT, PNMT, TEMT and homologues. Function: Function: Nicotinamide N-methyltransferase (EC 2.1.1.1) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to nicotinamide to form 1-methylnicotinamide and S-adenosyl-L-homocysteine. Phenylethanolamine N-methyltransferase (EC 2.1.1.28) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to phenylethanolamine to form N-methylphenylethanolamine and S-adenosyl-L homocysteine. Amine N-methyltransferase (EC 2.1.1.49) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to an amine to form a methylated amine and S-adenosyl-L-homocysteine. Thioether S-methyltransferase (EC 2.1.1.96) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to dimethyl sulfide to form trimethylsulfonium and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. NNMT/PNMT/TEMT family. XX GO GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51601 FT BINDING 74..75 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 152..153 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 35 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 40 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 80 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 96 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 101 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: N FT BINDING 182 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [AFLT] XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5RFR7; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU00940; DC Domain; TR PROSITE; PS51608; SAM_MT_UBIE; 1; level=0 XX Names: UbiE family SAM-binding methyltransferase Function: 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase (EC 2.1.1.201) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to 2-methoxy-6-all-trans-polyprenyl-1,4 benzoquinol to form 6-methoxy-3-methyl- 2-all-trans polyprenyl-1,4-benzoquinol and S-adenosyl-L-homocysteine. XX case not DE + RecName: EC=2.1.1.163; end case case or DE + RecName: EC=2.1.1.201; end case XX case not CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2-demethylmenaquinol + S-adenosyl-L-methionine = a CC menaquinol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42640, CC Rhea:RHEA-COMP:9539, Rhea:RHEA-COMP:9563, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:18151, ChEBI:CHEBI:55437, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789; EC=2.1.1.163; end case case or CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2-methoxy-6-all-trans-polyprenyl-1,4-benzoquinol + S- CC adenosyl-L-methionine = a 6-methoxy-3-methyl-2-all-trans-polyprenyl- CC 1,4-benzoquinol + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:28286, Rhea:RHEA-COMP:10858, Rhea:RHEA-COMP:10859, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:84166, ChEBI:CHEBI:84167; EC=2.1.1.201; end case CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. MenG/UbiE family. XX DR PROSITE; PS01183; UBIE_1; 1; trigger=no DR PROSITE; PS01184; UBIE_2; 1; trigger=no XX GO GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity case or GO GO:0006744; P:ubiquinone biosynthetic process end case case not GO GO:0009234; P:menaquinone biosynthetic process end case GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX case not KW Menaquinone biosynthesis end case KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase case or KW Ubiquinone biosynthesis end case XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q54VN2; Scope: Eukaryota Comments: None; XX # Revision 1.11 2023/01/26 // AC PRU00942; DC Domain; c? =258> and TR PROSITE; PS51610; SAM_CLNMT; 1; level=0 XX Names: Calmodulin-lysine N-methyltransferase Function: Calmodulin-lysine N-methyltransferase (EC 2.1.1.60) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to calmodulin L-lysine to form calmodulin N(6)-methyl-L-lysine and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.60; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=[calmodulin]-L-lysine + S-adenosyl-L-methionine = CC [calmodulin]-N(6)-methyl-L-lysine + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:21556, Rhea:RHEA-COMP:11360, Rhea:RHEA-COMP:11361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.60; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. CLNMT methyltransferase family. XX GO GO:0018025; F:calmodulin-lysine N-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q7Z624; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00943; DC Domain; c? =400> and TR PROSITE; PS51611; SAM_MT59; 1; level=0 XX Names: [Cytochrome c]-lysine N-methyltransferase Function: [Cytochrome c]-lysine N-methyltransferase (EC 2.1.1.59) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to [cytochrome c]-L-lysine to form [cytochrome c]-N(6)-methyl-L-lysine and S- adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.59; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-[cytochrome c] + S-adenosyl-L-methionine = H(+) + CC N(6)-methyl-L-lysyl-[cytochrome c] + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:24312, Rhea:RHEA-COMP:9754, Rhea:RHEA-COMP:9755, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.59; CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase CC superfamily. XX GO GO:0000277; F:[cytochrome c]-lysine N-methyltransferase activity XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q6FR37; Scope: Eukaryota; Saccharomycetaceae Comments: None; XX # Revision 1.8 2019/11/21 // AC PRU00944; DC Domain; TR PROSITE; PS51612; SAM_MT_2O_PK; 1; level=0 XX Names: Poxvirus/kinetoplastid ribose 2'-O-methyltransferase (EC 2.1.1.57) family Function: Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Poxvirus/kinetoplastid 2'-O-MTase family. XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase KW mRNA capping KW mRNA processing XX FT From: PS51612 FT REGION 167..246 FT /note="Binding to NPH-I" FT Condition: P-[AIV]-A-S-S-L-K-W-R-C-P-F-P-D-Q-W-I-[KR]-D-F-Y-[IV]-P-[CH]-G-[DN]-[EK]-[FM]-[LS]-Q-P-F-A-P-[PS]-[FY]-S-A-E-M-R-L-L-S-[CI]-Y-[ST]-[GR]-[AET]-[NP]-[IM]-R-L-[IKT]-[CR]-[IV]-[DT]-[KQ]-[NQS]-[AD]-[ASV]-[ISV]-[EKN]-Y-E-K-K-M-[FY]-Y-L-N-[KT]-[IK]-[IV]-R-[NP]-[KR]-[IV]-[IV]-[ILV] FT BINDING 175..178 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT Condition: R-C-P-F FT BINDING 203..205 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT Condition: S-A-E FT ACT_SITE 173 FT /note="For methyltransferase activity" FT Condition: K FT BINDING 19 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT Condition: Y FT BINDING 38 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Q FT BINDING 65 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 67 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 71 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 90 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 93 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: R FT BINDING 112 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: V FT BINDING 134 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 180 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT Condition: D FT BINDING 230 FT /ligand="mRNA" FT /ligand_id="ChEBI:CHEBI:33699" FT /ligand_part="mRNA cap" FT Condition: E XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P07617; Scope: Viruses; Chordopoxvirinae Comments: None; XX # Revision 1.11 2022/11/19 // AC PRU00945; DC Domain; TR PROSITE; PS51613; SAM_MT_RRMJ; 1; level=0 XX Names: RrmJ-type ribose 2'-O-methyltransferase (EC 2.1.1.57) domain Function: mRNA (nucleoside-2'-O-)-methyltransferase (EC 2.1.1.57) XX case DE + RecName: EC=2.1.1.-; end case XX XX case KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase end case XX FT From: PS51613 FT DOMAIN from..to FT /note="RrmJ-type SAM-dependent 2'-O-MTase #" FT ACT_SITE 157 FT /note="Proton acceptor" FT Group: 1; Condition: K FT BINDING 37 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: G case FT BINDING 67 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: E end case FT BINDING 117 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 183-240; Related: None; Repeats: 1; Topology: Undefined; Example: D2HRF1; Scope: Eukaryota Viruses; Alphabaculovirus Comments: None; XX # Revision 1.10 2022/11/19 // AC PRU00946; DC Domain; TR PROSITE; PS51614; SAM_MT_ADRIFT; 1; level=0 XX Names: Adrift-type ribose 2'-O-methyltransferase (EC 2.1.1.-) domain Function: 2'-O-methyltransferase XX DE + RecName: EC=2.1.1.-; XX GO GO:0008168; F:methyltransferase activity XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51614 FT DOMAIN from..to FT /note="Adrift-type SAM-dependent 2'-O-MTase #" FT ACT_SITE 168 FT /note="Proton acceptor" FT Condition: K FT BINDING 40 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 59 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: W FT BINDING 128 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 199-224; Related: None; Repeats: 1; Topology: Undefined; Example: Q5RAY7; Scope: Viruses Eukaryota; Metazoa Comments: None; XX # Revision 1.10 2022/11/19 // AC PRU00947; DC Domain; c? =282> and TR PROSITE; PS51615; SAM_MT_PUTRESCINE; 1; level=0 XX Names: Putrescine N-methyltransferase Function: Putrescine N-methyltransferase (EC 2.1.1.53) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to putrescine to form N-methylputrescine and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.53; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=putrescine + S-adenosyl-L-methionine = H(+) + N- CC methylputrescine + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15037, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:58039, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:326268; EC=2.1.1.53; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Spermidine/spermine synthase family. XX GO GO:0030750; F:putrescine N-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51615 FT BINDING 201..202 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT ACT_SITE 220 FT /note="Proton acceptor" FT Condition: D FT BINDING 95 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Q FT BINDING 170 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: E FT BINDING 289 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O48659; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.11 2022/11/19 // AC PRU00948; DC Domain; c? =211> and TR PROSITE; PS51616; SAM_NNMT_PNMT_TEMT_2; 1; level=0 XX Names: Amine N-methyltransferase Function: Amine N-methyltransferase (EC 2.1.1.49) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to an amine to form a methylated amine and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.49; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a tertiary amine + S-adenosyl-L-methionine = a methylated CC tertiary amine + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:53928, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:137982, ChEBI:CHEBI:137983; CC EC=2.1.1.49; CC -!- CATALYTIC ACTIVITY: CC Reaction=a secondary amine + S-adenosyl-L-methionine = a methylated CC secondary amine + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:53924, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:137419, ChEBI:CHEBI:137984; CC EC=2.1.1.49; CC -!- CATALYTIC ACTIVITY: CC Reaction=a primary amine + S-adenosyl-L-methionine = a methylated CC primary amine + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:23136, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:65296, ChEBI:CHEBI:131823; CC EC=2.1.1.49; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. NNMT/PNMT/TEMT family. XX GO GO:0030748; F:amine N-methyltransferase activity GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51616 FT BINDING 64..65 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 143..144 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT BINDING 21 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 26 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 70 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 86 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 91 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: N FT BINDING 164 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [FLT] XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O97972; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.10 2022/11/19 // AC PRU00952; DC Domain; TR PROSITE; PS51620; SAM_TRM61; 1; level=0 XX Names: tRNA (adenine(57)-N(1)/adenine(58)-N(1) or adenine(58)-N(1))- methyltransferase Function: tRNA (adenine(58)-N(1))-methyltransferase (EC 2.1.1.220) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to adenine(58) in tRNA to form N(1)-methyladenine(58) in tRNA and S-adenosyl-L- homocysteine. tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase (EC=2.1.1.219) is an enzyme that transfers a methyl group from the S-adenosyl-L-methionine (SAM) to adenine(57)/adenine(58) in tRNA to form N(1)-methyladenine57/N(1)- methyladenine58 in tRNA and S-adenosyl-L- homocysteine. XX case DE + RecName: EC=2.1.1.219; else DE + RecName: EC=2.1.1.220; end case XX case CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(57)/adenosine(58) in tRNA + 2 S-adenosyl-L- CC methionine = 2 H(+) + N(1)-methyladenosine(57)/N(1)- CC methyladenosine(58) in tRNA + 2 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:41740, Rhea:RHEA-COMP:9580, Rhea:RHEA-COMP:9582, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.219; else CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)- CC methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220; end case CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TRM61 family. XX case GO GO:0043827; F:tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity else GO GO:0160107; F:tRNA (adenine(58)-N1)-methyltransferase activity end case GO GO:0032259; P:methylation XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase KW tRNA processing XX FT From: PS51620 FT BINDING 102 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S FT BINDING 123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: E FT BINDING 151 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 170 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q755M8; Scope: Eukaryota Comments: None; XX # Revision 1.14 2023/12/14 // AC PRU00955; DC Domain; c? and =1149> and TR PROSITE; PS51623; SAM_MT_TRMH_1; 1; level=0 XX Names: tRNA guanosine-2'-O-methyltransferase Function: tRNA guanosine-2'-O-methyltransferase (EC 2.1.1.34) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to tRNA to form tRNA containing 2'-O-methylguanosine and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.34; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(18) in tRNA + S-adenosyl-L-methionine = 2'-O- CC methylguanosine(18) in tRNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:20077, Rhea:RHEA-COMP:10190, Rhea:RHEA-COMP:10192, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.34; CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase CC superfamily. RNA methyltransferase TrmH family. XX GO GO:0003723; F:RNA binding GO GO:0141100; F:tRNA (guanine(18)-2'-O)-methyltransferase activity GO GO:0008033; P:tRNA processing GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW RNA-binding KW S-adenosyl-L-methionine KW Transferase KW tRNA processing KW tRNA-binding XX FT From: PS51623 FT BINDING 1389 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 1409 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: I XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q07527; Scope: Eukaryota; Saccharomyces Comments: None; XX # Revision 1.10 2023/10/13 // AC PRU00956; DC Domain; c? =1280> and TR PROSITE; PS51624; SAM_MT_TRMH_2; 1; level=0 XX Names: RNA methyltransferase TRMH Function: tRNA guanosine-2'-O-methyltransferase (EC 2.1.1.34) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to tRNA to form tRNA containing 2'-O-methylguanosine and S-adenosyl-L-homocysteine. 16S rRNA (guanine(527)-N(7))-methyltransferase (EC 2.1.1.170) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to guanosine(527) in 16S rRNA to form N(7)-methylguanosine(527) in 16S rRNA and S-adenosyl-L-homocysteine. tRNA (cytidine(32)/uridine(32)-2'-O)-methyltransferase (EC 2.1.1.200) is an enzyme that transfers a methyl group from S-adenosyl-L methionine (SAM) to (1)cytidine(32) in tRNA to form 2'-O-methylcytidine(32) in tRNA and S- adenosyl-L-homocysteine. tRNA (cytidine(34)-2'-O)-methyltransferase (EC 2.1.1.207) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to (1)cytidine(34) in tRNA to form 2'-O-methylcytidine(34) in tRNA and S adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase CC superfamily. RNA methyltransferase TrmH family. XX GO GO:0003723; F:RNA binding GO GO:0008173; F:RNA methyltransferase activity GO GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity GO GO:0006396; P:RNA processing GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW RNA-binding KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51624 FT BINDING 1545 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 1565 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: I FT BINDING 1574 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: L XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q13395; Scope: Eukaryota; Homo Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU00957; DC Domain; TR PROSITE; PS51625; SAM_MT_TRMB; 1; level=0 XX Names: tRNA (guanine-N(7)-)-methyltransferase Function: tRNA (guanine-N(7)-)-methyltransferase (EC 2.1.1.33) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to tRNA to form tRNA containing N(7)-methylguanine and S-adenosyl-L-homocysteine. XX DE + RecName: EC=2.1.1.33; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)- CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189, CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, CC ChEBI:CHEBI:74480; EC=2.1.1.33; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TrmB family. XX GO GO:0000049; F:tRNA binding GO GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity GO GO:0008033; P:tRNA processing GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase KW tRNA processing case KW tRNA-binding end case XX FT From: PS51625 case and FT BINDING 74..75 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" end case case and FT BINDING 101..102 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" end case case and FT BINDING 197..199 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" end case case and FT BINDING 197..200 FT /ligand="substrate" end case FT ACT_SITE 124 FT Condition: D case FT BINDING 49 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] end case case FT BINDING 51 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G end case case FT BINDING 74 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] FT BINDING 101 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DEN] end case case FT BINDING 121 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [CL] end case case FT BINDING 124 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 128 FT /ligand="substrate" FT Condition: K FT BINDING 160 FT /ligand="substrate" FT Condition: D end case XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q6NU94; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.12 2023/10/13 // AC PRU00958; DC Domain; TR PROSITE; PS51626; SAM_MT_TRM1; 1; level=0 XX Names: tRNA (guanine(26)-N(2))-dimethyltransferase (EC 2.1.1.216) Function: tRNA (guanine(26)-N(2))-dimethyltransferase (EC 2.1.1.216) is an enzyme that transfers a methyl group from 2 S-adenosyl-L-methionine (SAM) to guanine(26) in tRNA to form N(2)-dimethylguanine(26) in tRNA and 2 S- adenosyl-L-homocysteine. XX case and =425> and DE + RecName: EC=2.1.1.216; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216; end case CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Trm1 family. XX case and =425> and GO GO:0160104; F:tRNA (guanine(26)-N2)-dimethyltransferase activity end case GO GO:0000049; F:tRNA binding GO GO:0008033; P:tRNA processing GO GO:0032259; P:methylation XX KW Methyltransferase KW RNA-binding KW S-adenosyl-L-methionine KW Transferase KW tRNA processing KW tRNA-binding FT From: PS51626 FT DOMAIN from..to FT /note="Trm1 methyltransferase #" XX Chop: Nter=0; Cter=0; Size: 58-472; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LFU5; Scope: Archaea Eukaryota Bacteria; Aquifex Comments: None; XX # Revision 1.15 2023/12/14 // AC PRU00959; DC Domain; c? and =429> and TR PROSITE; PS51627; SAM_MT_TRM11; 1; level=0 XX Names: tRNA (guanine(10)-N2)-methyltransferase (EC 2.1.1.214) (TRM11) Function: tRNA (guanine(10)-N(2))-methyltransferase (EC 2.1.1.214) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to guanine(10) in tRNA to form N(2)-methylguanine(10) in tRNA and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TRM11 methyltransferase family. XX GO GO:0000049; F:tRNA binding GO GO:0016423; F:tRNA (guanine) methyltransferase activity GO GO:0008033; P:tRNA processing GO GO:0032259; P:methylation XX KW Methyltransferase KW RNA-binding KW S-adenosyl-L-methionine KW Transferase KW tRNA processing KW tRNA-binding XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O94636; Scope: Eukaryota Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00965; DC Domain; TR PROSITE; PS51270; ZF_CTCHY; 1; level=0 XX Names: Zinc finger CTCHY-type Function: The CTCHY-type zinc finger is required for binding to p53 in mammals. XX XX case ( and and and ) or ( and and and ) or ( and and and ) GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51270 case and and and and and and and and and and and FT ZN_FING from..to FT /note="CTCHY-type #" else case and and and and and and and and and and and FT ZN_FING from..to FT /note="CTCHY-type #; atypical" else FT ZN_FING from..to FT /note="CTCHY-type #; degenerate" end case FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 57 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 53-77; Related: None; Repeats: 1; Topology: Undefined; Example: Q96PM5; Scope: Eukaryota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU00966; DC Domain; TR PROSITE; PS51152; NFYA_HAP2_2; 1; level=0 XX Names: NF-YA/HAP2 family Function: The CCAAT-binding factor (CBF) or NF-Y is a heteromeric transcription factor that consists of two different components both needed for DNA-binding. The second subunit of CBF, known as CBF-B or NF-YA in vertebrates and HAP2 in budding yeast, contains a highly conserved region of about 60 residues. This region, called the 'essential core', seems to consist of two subdomains: an N-terminal subunit-association domain and a C-t erminal DNA recognition domain. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family. XX DR PROSITE; PS00686; NFYA_HAP2_1; 1; trigger=no XX GO GO:0003677; F:DNA binding GO GO:0006351; P:DNA-templated transcription GO GO:0003700; F:DNA-binding transcription factor activity GO GO:0016602; C:CCAAT-binding factor complex GO GO:0005634; C:nucleus XX KW Activator KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51152 FT DNA_BIND 36..61 FT /note="NFYA/HAP2-type #" FT MOTIF 6..29 FT /note="Subunit association domain (SAD) #" XX Chop: Nter=0; Cter=0; Size: 48-75; Related: None; Repeats: 1; Topology: Undefined; Example: P24488; Scope: Eukaryota Comments: None; XX # Revision 1.7 2022/06/27 // AC PRU00967; DC Domain; TR PROSITE; PS51003; CYTB_CTER; 1; level=0 XX Names: Cytochrome b/b6 C-terminal region Function: The cytochrome b/b6 are transmembrane proteins containing to protohemes responsible for vectorial electron transfer. XX CC -!- SIMILARITY: Belongs to the cytochrome b family. XX DR General; Transmembrane; -; 4; trigger=no XX GO GO:0016020; C:membrane GO GO:0016491; F:oxidoreductase activity GO GO:0006810; P:transport GO GO:0022900; P:electron transport chain XX KW Electron transport KW Membrane KW Transmembrane KW Transmembrane helix KW Transport XX FT From: PS51003 FT TRANSMEM 15..35 FT /note="Helical" FT TRANSMEM 79..99 FT /note="Helical" FT TRANSMEM 114..134 FT /note="Helical" FT TRANSMEM 140..160 FT /note="Helical" XX Chop: Nter=0; Cter=0; Size: 84-181; Related: None; Repeats: 1; Topology: Undefined; Example: P00163; Scope: Eukaryota Bacteria; Cyanobacteriota Comments: None; XX # Revision 1.8 2023/02/17 // AC PRU00968; DC Domain; TR PROSITE; PS51002; CYTB_NTER; 1; level=0 XX Names: Cytochrome b/b6 N-terminal region Function: The cytochrome b/b6 are transmembrane proteins containing to protohemes responsible for vectorial electron transfer. XX CC -!- SIMILARITY: Belongs to the cytochrome b family. XX DR General; Transmembrane; -; 5; trigger=no XX GO GO:0016491; F:oxidoreductase activity GO GO:0016020; C:membrane GO GO:0006810; P:transport GO GO:0022900; P:electron transport chain case GO GO:0046872; F:metal ion binding XX KW Heme KW Iron KW Metal-binding end case KW Membrane KW Transmembrane KW Transmembrane helix KW Transport KW Electron transport XX FT From: PS51002 FT TRANSMEM 33..53 FT /note="Helical" FT TRANSMEM 86..106 FT /note="Helical" FT TRANSMEM 117..137 FT /note="Helical" FT TRANSMEM 152..172 FT /note="Helical" FT TRANSMEM 180..201 FT /note="Helical" case FT BINDING 83 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 97 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 184 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b562" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 199 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_label="b566" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H else FT BINDING 83 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 97 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 184 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="2" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H FT BINDING 199 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_label="1" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Group: 1; Condition: H end case XX Chop: Nter=0; Cter=0; Size: 167-239; Related: None; Repeats: 1; Topology: Undefined; Example: P00163; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU00969; DC Domain; TR PROSITE; PS50979; BC; 1; level=0 XX Names: Biotin carboxylation domain Function: The biotin carboxylation domain is common to all biotin-dependent carboxylases and mediates the carboxylation of enzyme-bound biotin by bicarbonate and ATP. The biotin carboxylation domain can be divided in three subdomains (N-terminal, central and C-terminal). The N-terminal region provides part of the active site; the central region corresponds to the ATP- grasp domain, which is common to many ATP-dependent enzymes involved in macromolecular synthesis. The ATP-grasp module directly binds the ATP molecule. The C-terminal subdomain is involved in dimer formation. XX DR PROSITE; PS50975; ATP_GRASP; 1; trigger=yes XX GO GO:0004075; F:biotin carboxylase activity XX KW Ligase KW Biotin XX FT From: PS50979 FT DOMAIN from..to FT /note="Biotin carboxylation #" XX Chop: Nter=0; Cter=0; Size: 19-520; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UUE1; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00970; DC Domain; TR PROSITE; PS51633; CXC; 1; level=0 XX Names: CXC domain Function: The CXC domain is likely to be involved in an important function of XX CC -!- SIMILARITY: Belongs to the histone-lysine methyltransferase family. EZ CC subfamily. XX FT From: PS51633 FT DOMAIN from..to FT /note="CXC #" XX Chop: Nter=0; Cter=0; Size: 90-120; Related: None; Repeats: 1; Topology: Undefined; Example: Q92800; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00971; DC Domain; TR PROSITE; PS51634; CRC; 1; level=0 XX Names: CRC domain Function: The CRC domain (C1-RNPXAFXPK-C2) binds zinc and is able to bind DNA. XX XX FT From: PS51634 FT DOMAIN from..to FT /note="CRC #" XX Chop: Nter=0; Cter=0; Size: 435-950; Related: None; Repeats: 1; Topology: Undefined; Example: Q08CM4; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00972; DC Domain; TR PROSITE; PS51640; MRG; 1; level=0 XX Names: MRG domain Function: The ~170 amino acid MRG domain binds a plethora of transcriptional regulators and chromatin-remodeling factors, including the histone deacetylase transriptional corepressor mSin3A and the nuclear protein PAM14 (protein-associated MRG, 14kDa). XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0006325; P:chromatin organization GO GO:0006351; P:DNA-templated transcription GO GO:0006355; P:regulation of DNA-templated transcription XX KW Chromatin regulator KW Transcription KW Transcription regulation XX FT From: PS51640 FT DOMAIN from..to FT /note="MRG #" XX Chop: Nter=0; Cter=0; Size: 154-360; Related: None; Repeats: 1; Topology: Undefined; Example: Q9WVG9; Scope: Eukaryota Comments: None; XX # Revision 1.7 2022/06/27 // AC PRU00973; DC Domain; TR PROSITE; PS51641; AGENET_LIKE; 1; level=0 XX Names: Agenet-like domain Function: Biochemical analysis of the tandem Agenet-like domains reveals their ability to preferentially recognize trimethylated peptides in a sequence- specific manner. XX XX FT From: PS51641 FT DOMAIN from..to FT /note="Agenet-like #" XX Chop: Nter=0; Cter=0; Size: 37-63; Related: None; Repeats: 2; Topology: Undefined; Example: P35922; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00974; DC Domain; TR PROSITE; PS51643; HD_CAS3; 1; level=0 XX Names: HD Cas3-type domain Function: The Cas3-type HD domain has nuclease activity against ssDNA and ssRNA. XX XX GO GO:0016787; F:hydrolase activity GO GO:0004518; F:nuclease activity GO GO:0090304; P:nucleic acid metabolic process XX KW Hydrolase KW Nuclease XX FT From: PS51643 FT DOMAIN from..to FT /note="HD Cas3-type #" XX Chop: Nter=0; Cter=0; Size: 153-246; Related: None; Repeats: 1; Topology: Undefined; Example: O27158; Scope: Archaea Bacteria Comments: None; XX # Revision 1.4 2023/12/14 // AC PRU00975; DC Domain; TR PROSITE; PS51644; HTH_OST; 1; level=0 XX Names: OST-type HTH domain Oskar-TDRD5/TDRD7 HTH LOTUS domain Function: The OST-HTH domain is likely to bind RNA with a potential specificity for double-standed RNA (dsRNA) and might have key role in the assembly and localization of RNA-protein complexes with important post- transcriptional regulatory functions. XX XX FT From: PS51644 FT DOMAIN from..to FT /note="HTH OST-type #" XX Chop: Nter=0; Cter=0; Size: 56-94; Related: None; Repeats: 1-8; Topology: Undefined; Example: A6QLE1; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00976; DC Domain; TR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1; level=0 XX Names: Photolyase/cryptochrome alpha/beta domain Function: The photolyase/cryptochrome alpha/beta domain adopts a dinucleotide binding fold with a five-stranded parallel beta sheet flanked on both sides by alpha helices. XX XX FT From: PS51645 FT DOMAIN from..to FT /note="Photolyase/cryptochrome alpha/beta #" XX Chop: Nter=0; Cter=0; Size: 113-172; Related: None; Repeats: 1; Topology: Undefined; Example: Q5IZC5; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00977; DC Domain; TR PROSITE; PS50164; GIY_YIG; 1; level=0 XX Names: GIY-YIG domain Function: The GIY-YIG superfamily groups together nucleases characterized by the presence of a domain of typically ~100 amino acids, with two short motifs "GIY" and "YIG" in the N-terminal part, followed by an Arg residue in the center and a Glu residue in the C-terminal part. XX XX GO GO:0090304; P:nucleic acid metabolic process XX FT From: PS50164 FT DOMAIN from..to FT /note="GIY-YIG #" XX Chop: Nter=0; Cter=0; Size: 64-129; Related: None; Repeats: 1; Topology: Undefined; Example: B4TYW7; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Viruses Comments: None; XX # Revision 1.5 2023/12/14 // AC PRU00978; DC Domain; TR PROSITE; PS50217; BZIP; 1; level=0 XX Names: Basic-leucine zipper (bZIP) domain Function: The bZIP superfamily of eukaryotic DNA-binding transcription factors groups together proteins that contain a basic region mediating sequence- specific DNA-binding followed by a leucine zipper required for dimerization. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX DR PROSITE; PS00036; BZIP_BASIC; 0-1; trigger=no XX GO GO:0043565; F:sequence-specific DNA binding GO GO:0003700; F:DNA-binding transcription factor activity GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS50217 FT DOMAIN from..to FT /note="bZIP #" FT From: PS50217 :([KR]).*?([KR])[^KR]*?([LI])(?:.{6}[LI])*.{6}([LI]) FT REGION $1..$2 FT /note="Basic motif #" FT REGION $3..$4 FT /note="Leucine-zipper #" XX Chop: Nter=0; Cter=0; Size: 26-74; Related: None; Repeats: 1; Topology: Undefined; Example: P01102; Scope: Eukaryota Viruses Comments: None; XX # Revision 1.19 2019/11/21 // AC PRU00979; DC Domain; TR PROSITE; PS51647; CYSTATIN_KININOGEN; 1; level=0 XX Names: Kininogen-type cystatin domain Function: Kininogens are multifunctional and multidomain glycoproteins related to cystatins. XX XX GO GO:0004869; F:cysteine-type endopeptidase inhibitor activity GO GO:0010466; P:negative regulation of peptidase activity XX case KW Disulfide bond end case KW Protease inhibitor KW Thiol protease inhibitor XX FT From: PS51647 FT DOMAIN from..to FT /note="Cystatin kininogen-type #" FT DISULFID 56..67 FT Tag: disulf; Condition: C-x*-C FT DISULFID 56..69 FT Tag: disulf; Condition: C-x*-C FT DISULFID 80..99 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 94-115; Related: None; Repeats: 3; Topology: Undefined; Example: P08934; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00980; DC Domain; TR PROSITE; PS51648; YCGL; 1; level=0 XX Names: YcgL domain Function: YcgL represents a conserved class of small proteins widespread in gammaproteobacteria. This group of protein contains a 85-residue domain of unknown function. XX XX FT From: PS51648 FT DOMAIN from..to FT /note="YcgL #" XX Chop: Nter=0; Cter=0; Size: 71-105; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KQP1; Scope: Bacteria; Gammaproteobacteria Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU00981; DC Domain; TR PROSITE; PS50888; BHLH; 1; level=0 XX Names: Myc-type, basic helix-loop-helix (bHLH) domain Function: Fill in XX CC -!- SUBCELLULAR LOCATION: Nucleus. case not CC -!- CAUTION: Contains a degenerate basic motif not likely to bind DNA. end case XX GO GO:0005634; C:nucleus XX KW Nucleus case KW DNA-binding end case KW Transcription KW Transcription regulation XX FT From: PS50888 FT DOMAIN from..to FT /note="bHLH #" FT REGION 15..to FT /note="Helix-loop-helix motif #" case FT REGION from..14 FT /note="Basic motif #" FT Tag: basic else FT REGION from..14 FT /note="Basic motif #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 38-115; Related: None; Repeats: 1; Topology: Undefined; Example: Q9W6C8; Scope: Eukaryota Viruses; Retroviridae Comments: None; XX # Revision 1.6 2019/11/21 // AC PRU00982; DC Domain; TR PROSITE; PS51649; NPH3; 1; level=0 XX Names: NPH3 domain Function: The function of the NPH3 domain is not yet known. XX CC -!- SIMILARITY: Belongs to the NPH3 family. XX FT From: PS51649 FT DOMAIN from..to FT /note="NPH3 #" XX Chop: Nter=0; Cter=0; Size: 74-366; Related: None; Repeats: 1; Topology: Undefined; Example: Q9FN09; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00983; DC Domain; TR PROSITE; PS51650; C2_DOCK; 1; level=0 XX Names: C2 DOCK-type domain Function: The ~200 residue DOCK-type C2 domain is located toward the N- terminus and interacts with phosphatidylinositol 3,4,5-trisphosphate [PtdIns(3,4,5)P3] to mediate signalling and membrane localization. XX CC -!- SIMILARITY: Belongs to the DOCK family. XX FT From: PS51650 FT DOMAIN from..to FT /note="C2 DOCK-type #" XX Chop: Nter=0; Cter=0; Size: 150-195; Related: None; Repeats: 1; Topology: Undefined; Example: Q8C3J5; Scope: Eukaryota Comments: None; XX # Revision 1.4 2020/01/06 // AC PRU00984; DC Domain; TR PROSITE; PS51651; DOCKER; 1; level=0 XX Names: DOCKER domain Function: The DOCKER domain is a GEF catalytic domain of ~400 residues. XX CC -!- SIMILARITY: Belongs to the DOCK family. XX FT From: PS51651 FT DOMAIN from..to FT /note="DOCKER #" XX Chop: Nter=0; Cter=0; Size: 397-475; Related: None; Repeats: 1; Topology: Undefined; Example: Q8C3J5; Scope: Eukaryota Comments: None; XX # Revision 1.4 2020/01/07 // AC PRU00985; DC Domain; TR PROSITE; PS51652; AV_ZBD; 1; level=0 XX Names: Arteriviridae zinc-binding (AV ZBD) domain Function: The ZBD is comprised of about 80 to 100 residues, including 12 to 13 conserved Cys/His residues. It consists of a RING-like module and treble- cleft zinc finger, together coordinating three Zn atoms. XX XX case or or GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51652 FT DOMAIN from..to FT /note="AV ZBD #" FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 32 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 44 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 54-78; Related: None; Repeats: 1; Topology: Undefined; Example: Q9YN02; Scope: Viruses; Arteriviridae Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU00986; DC Domain; TR PROSITE; PS51653; CV_ZBD; 1; level=0 XX Names: Coronaviridae zinc-binding (CV ZBD) domain Function: The ZBD is comprised of about 80 to 100 residues, including 12 to 13 conserved Cys/His residues. It consists of a RING-like module and treble- cleft zinc finger, together coordinating three Zn atoms. XX XX case or or GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51653 FT DOMAIN from..to FT /note="CV ZBD #" FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 19 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 50 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 55 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [C] FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [HC] XX Chop: Nter=0; Cter=0; Size: 72-94; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Coronaviridae Comments: None; XX # Revision 1.7 2023/11/03 // AC PRU00989; DC Domain; TR PROSITE; PS51656; 4FE4S; 1; level=0 XX Names: 4Fe-4S domain Function: The low-potential [4Fe-4S]2(+)/1(+) cluster is involved in the reductive reactivation of CoFeSP and is able to transfer electrons to cob(II)amide from NiFe-containing carbon monoxyde dehydrogenase (CODH), pyruvate:ferredoxin oxydoreductase or reduced ferredoxins. XX case CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds #1 [4Fe-4S] cluster.; end case XX case GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0046872; F:metal ion binding XX KW 4Fe-4S KW Iron KW Iron-sulfur KW Metal-binding end case XX FT From: PS51656 FT DOMAIN from..to FT /note="4Fe-4S #" case not FT BINDING 18 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 21 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 26 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 43 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C end case XX Chop: Nter=0; Cter=0; Size: 49-74; Related: None; Repeats: 1; Topology: Undefined; Example: Q8PV87; Scope: Bacteria Archaea; Euryarchaeota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU00990; DC Domain; TR PROSITE; PS51657; PSRV_HELICASE; 1; level=0 XX Names: (+)RNA virus helicase core domain Function: The helicase core contains two structural domains, an N-terminal ATP-binding domain and a C-terminal domain. XX XX GO GO:0004386; F:helicase activity GO GO:0005524; F:ATP binding GO GO:0016787; F:hydrolase activity GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Helicase KW Hydrolase KW Nucleotide-binding XX FT From: PS51657 FT DOMAIN from..155 FT /note="(+)RNA virus helicase ATP-binding #" FT BINDING 33..40 FT /ligand="a ribonucleoside 5'-triphosphate" FT /ligand_id="ChEBI:CHEBI:61557" FT DOMAIN 156..to FT /note="(+)RNA virus helicase C-terminal #" XX Chop: Nter=0; Cter=0; Size: 206-377; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Riboviria Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU00991; DC Domain; TR PROSITE; PS51658; BFN; 1; level=0 XX Names: Bifunctional nuclease (BFN) domain Function: The bifunctional nuclease (BFN) domain is specific to bacteria and plant organisms. It has both RNase and DNase activities. XX XX GO GO:0004518; F:nuclease activity XX FT From: PS51658 FT DOMAIN from..to FT /note="BFN #" XX Chop: Nter=0; Cter=0; Size: 119-146; Related: None; Repeats: 1; Topology: Undefined; Example: Q5N8J3; Scope: Eukaryota; Magnoliopsida Bacteria; Mycobacterium tuberculosis complex Comments: None; XX # Revision 1.5 2019/11/21 // AC PRU00992; DC Domain; TR PROSITE; PS51659; GT23; 1; level=0 XX Names: Glycosyltransferase family 23 (GT23) domain Function: The GT23 domain is an alpha1,6-fucosyltransferase. XX DE + RecName: EC=2.4.1.-; XX CC -!- SIMILARITY: Belongs to the glycosyltransferase 23 family. XX GO GO:0016758; F:hexosyltransferase activity XX KW Glycosyltransferase KW Transferase XX FT From: PS51659 FT DOMAIN from..to FT /note="GT23 #" FT REGION 162..163 FT /note="Important for donor substrate binding" FT Condition: R-R XX Chop: Nter=0; Cter=0; Size: 275-325; Related: None; Repeats: 1; Topology: Undefined; Example: Q5NVB3; Scope: Eukaryota; Metazoa Bacteria; Hyphomicrobiales Comments: None; XX # Revision 1.9 2021/06/03 // AC PRU00995; DC Domain; TR PROSITE; PS50880; TOPRIM; 1; level=0 XX Names: Toprim domain Function: The Toprim domain is a catalytic domain involved in DNA strand breakage and rejoining. XX case and DE + RecName: EC=5.6.2.2; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-dependent breakage, passage and rejoining of double- CC stranded DNA.; EC=5.6.2.2; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=The magnesium ions form salt bridges with both the protein and the CC DNA. Can also accept other divalent metal cations, such as Mn(2+) or CC Ca(2+).; else case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; end case XX case GO GO:0000287; F:magnesium ion binding end case case GO GO:0003677; F:DNA binding XX KW DNA-binding end case case KW Magnesium KW Metal-binding end case XX FT From: PS50880 FT DOMAIN from..to FT /note="Toprim #" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: E FT BINDING 65 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: D FT SITE 38 FT /note="Interaction with DNA" FT Group: 2; Condition: K FT SITE 41 FT /note="Interaction with DNA" FT Group: 2; Condition: N XX Chop: Nter=0; Cter=0; Size: 105-128; Related: None; Repeats: 1; Topology: Undefined; Example: P06786; Scope: Eukaryota Bacteria Archaea Viruses Comments: None; XX # Revision 1.24 2022/11/19 // AC PRU00997; DC Domain; TR PROSITE; PS51662; BP_PHYTASE; 1; level=0 XX Names: Beta-propeller phytase (BPP) domain Function: The beta-propeller phytase domain is made of six blades. XX DE AltName: Full=3-phytase; DE EC=3.1.3.8; DE AltName: Full=Phytate 3-phosphatase; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol CC 1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798, CC ChEBI:CHEBI:58130; EC=3.1.3.8; XX GO GO:0016158; F:3-phytase activity XX KW Hydrolase XX FT From: PS51662 FT DOMAIN from..to FT /note="BPP #" XX Chop: Nter=0; Cter=0; Size: 325-345; Related: None; Repeats: 1; Topology: Undefined; Example: P42094; Scope: Bacteria; Bacillus Comments: None; XX # Revision 1.8 2019/11/21 // AC PRU00998; DC Domain; TR PROSITE; PS51663; STATHMIN_3; 1; level=0 XX Names: Stathmin-like (SLD) domain Function: The SLD binds two tubulins arranged longitudinally, head-to-tail, in protofilament-like complexes. XX XX DR PROSITE; PS00563; STATHMIN_1; 1; trigger=no DR PROSITE; PS01041; STATHMIN_2; 1; trigger=no XX GO GO:0031110; P:regulation of microtubule polymerization or depolymerization XX KW Coiled coil XX FT From: PS51663 FT DOMAIN from..to FT /note="SLD #" XX Chop: Nter=0; Cter=0; Size: 61-153; Related: None; Repeats: 1; Topology: Undefined; Example: Q90987; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.4 2019/11/21 // AC PRU00999; DC Domain; TR PROSITE; PS51664; YCAO; 1; level=0 XX Names: YcaO domain Function: The YcaO domain is likely to be involved in post-translational modification (PTM) of amino acid residues. XX XX FT From: PS51664 FT DOMAIN from..to FT /note="YcaO #" XX Chop: Nter=0; Cter=0; Size: 309-388; Related: None; Repeats: 1; Topology: Undefined; Example: P75838; Scope: Bacteria Archaea; Euryarchaeota Comments: None; XX # Revision 1.3 2019/11/21 // AC PRU01000; DC Domain; TR PROSITE; PS51665; ENKURIN; 1; level=0 XX Names: Enkurin domain Function: The enkurin domain is essential for channel interaction. XX XX FT From: PS51665 FT DOMAIN from..to FT /note="Enkurin #" XX Chop: Nter=0; Cter=0; Size: 83-103; Related: None; Repeats: 1; Topology: Undefined; Example: Q8TC29; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01001; DC Domain; TR PROSITE; PS51666; QLQ; 1; level=0 XX Names: QLQ domain Function: The QLQ domain might be involved in protein-protein interaction. XX XX FT From: PS51666 FT DOMAIN from..to FT /note="QLQ #" XX Chop: Nter=0; Cter=0; Size: 26-47; Related: None; Repeats: 1; Topology: Undefined; Example: Q8L8A7; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01002; DC Domain; TR PROSITE; PS51667; WRC; 1; level=0 XX Names: WRC domain Function: The WRC domain contains two distinctive features, namely a putative nuclear localization signal and a zinc-finger motif consisting of the conserved spacing of three Cys and one His residues (C3H motif). It has been suggested that the WRC domain functions in DNA binding. XX case CC -!- SUBCELLULAR LOCATION: Nucleus. end case XX case GO GO:0005634; C:nucleus XX KW Nucleus end case XX FT From: PS51667 FT DOMAIN from..to FT /note="WRC #" FT MOTIF 6..16 FT /note="Bipartite nuclear localization signal" FT Group: 1; Condition: R-C-[KR]-R-T-D-G-K-K-W-R FT MOTIF 34..41 FT /note="Bipartite nuclear localization signal" FT Group: 1; Condition: [KR]-[GNS]-[KR]-[GHKNP]-R-[AS]-R-K XX Chop: Nter=0; Cter=0; Size: 35-55; Related: None; Repeats: 1-2; Topology: Undefined; Example: O81001; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01003; DC Domain; TR PROSITE; PS51668; TSAA_2; 1; level=0 XX Names: TsaA-like domain Function: The tsaA-like domain may bind S-adenosylmethionine (AdoMet) and possesses a methyltransferase activity. XX XX DR PROSITE; PS01318; TSAA_1; 1; trigger=no XX FT From: PS51668 FT DOMAIN from..to FT /note="TsaA-like #" XX Chop: Nter=0; Cter=0; Size: 84-152; Related: None; Repeats: 1; Topology: Undefined; Example: P44740; Scope: Archaea; Euryarchaeota Bacteria; Pseudomonadota Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.5 2023/01/26 // AC PRU01004; DC Domain; TR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1; level=0 XX Names: Prokaryotic molybdopterin oxidoreductases 4Fe-4S domain Function: The Mo/W bis-MGD oxydoreductases contains a domain that coordinates a [4Fe-4S] cluster. The cluster is ligated either by four Cys residues or three Cys residues and one His residue. XX XX DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 0-1; trigger=no XX case GO GO:0051539; F:4 iron, 4 sulfur cluster binding XX KW Iron KW Iron-sulfur KW Metal-binding KW 4Fe-4S end case XX FT From: PS51669 FT DOMAIN from..to FT /note="4Fe-4S Mo/W bis-MGD-type #" FT BINDING 8 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: [CH] FT BINDING 11 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: [C] FT BINDING 15 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: [C] FT BINDING 43 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: [C] XX Chop: Nter=0; Cter=0; Size: 33-98; Related: None; Repeats: 1; Topology: Undefined; Example: A8GHJ4; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU01005; DC Domain; TR PROSITE; PS51670; SHKT; 1; level=0 XX Names: ShKT domain Function: In venomous creatures, the ShKT domain may have been modified to give rise to potent ion channel blockers, whereas the incorporation of this domain into plant oxidoreductases and prolyl hydroxylases and into worm astacin-like metalloproteases and trypsin-like serines protaeses produced enzymes with potential channel-modulatory activity. XX XX case KW Disulfide bond end case XX FT From: PS51670 FT DOMAIN from..to FT /note="ShKT #" FT DISULFID 1..35 FT Tag: disulf; Condition: C-x*-C FT DISULFID 10..28 FT Tag: disulf; Condition: C-x*-C FT DISULFID 19..32 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 0-49; Related: None; Repeats: 1-4; Topology: Undefined; Example: P29187; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01006; DC Domain; TR PROSITE; PS50236; CHCR; 1; level=0 XX Names: Clathrin heavy-chain (CHCR) repeat Function: The CHCR repeats could mediate protein-protein interactions. XX XX GO GO:0006886; P:intracellular protein transport XX FT From: PS50236 FT REPEAT from..to FT /note="CHCR #" XX Chop: Nter=0; Cter=0; Size: 130-188; Related: None; Repeats: 1-7; Topology: Undefined; Example: Q24314; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01007; DC Domain; TR PROSITE; PS51671; ACT; 1; level=0 XX Names: ACT domain Function: The ACT domain is found in a variety of contexts and is proposed to be a structurally conserved regulatory domain involved in the binding of small ligands, such as amino acids. XX XX FT From: PS51671 FT DOMAIN from..to FT /note="ACT #" XX Chop: Nter=0; Cter=0; Size: 51-102; Related: None; Repeats: 1-2; Topology: Undefined; Example: A6QHI5; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01008; DC Domain; TR PROSITE; PS51672; ACT_LIKE; 1; level=0 XX Names: ACT-like domain Function: Threonine dehydratases (TDs) contain an ACT-like regulatory domain that possesses structural, rather than sequence, homology to the ACT domain. XX XX FT From: PS51672 FT DOMAIN from..to FT /note="ACT-like #" XX Chop: Nter=0; Cter=0; Size: 61-91; Related: None; Repeats: 1-2; Topology: Undefined; Example: P66898; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01009; DC Domain; TR PROSITE; PS51673; SUZ; 1; level=0 XX Names: SUZ domain Function: The SUZ domain enrichment in positively charged residues, including four universally conserved positively charged positions, supports a role in direct RNA-binding. XX XX FT From: PS51673 FT DOMAIN from..to FT /note="SUZ #" XX Chop: Nter=0; Cter=0; Size: 56-88; Related: None; Repeats: 1; Topology: Undefined; Example: Q80TM6; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01010; DC Domain; TR PROSITE; PS51674; 4FE4S_WBL; 1; level=0 XX Names: 4Fe-4S WhiB-like (Wbl)-type iron-sulfur binding domain Function: Wbl-mediated transcription regulation is dependent upon the presence or absence and state (nitrosylated or non-nitrosylated) of the [4Fe-4S] cluster. XX case CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of CC the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.; CC -!- PTM: The Fe-S cluster can be nitrosylated by nitric oxide (NO). CC -!- PTM: Upon Fe-S cluster removal intramolecular disulfide bonds are CC formed. end case XX case GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0046872; F:metal ion binding GO GO:0035731; F:dinitrosyl-iron complex binding XX KW 4Fe-4S KW Disulfide bond KW Iron KW Iron-sulfur KW Metal-binding end case XX FT From: PS51674 FT DOMAIN from..to FT /note="4Fe-4S Wbl-type #" FT BINDING 2 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 29 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 32 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C FT BINDING 38 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 44-84; Related: None; Repeats: 1; Topology: Undefined; Example: Q6MX01; Scope: Bacteria; Actinomycetes Viruses; Timquatrovirus Comments: None; XX # Revision 1.13 2023/02/16 // AC PRU01011; DC Domain; TR PROSITE; PS51642; HEMOPEXIN_2; 1; level=0 XX Names: Hemopexin repeat Function: It is suggested that the hemopexin domain facilitates binding to a variety of molecules and proteins. The hemopexin domain is formed by the repetition of a basic unit of some 35 to 45 residues. XX XX DR PROSITE; PS00024; HEMOPEXIN_1; 1; trigger=no XX FT From: PS51642 FT REPEAT from..to FT /note="Hemopexin #" XX Chop: Nter=0; Cter=0; Size: 26-70; Related: None; Repeats: 1-8; Topology: Undefined; Example: O18927; Scope: Eukaryota Viruses; Ascovirus Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01012; DC Domain; TR PROSITE; PS51675; SAM_MT_TRM10; 1; level=0 XX Names: SAM-dependent methyltransferase TRM10-type domain Function: SAM-dependent methyltransferase XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase CC superfamily. TRM10 family. XX GO GO:0032259; P:methylation GO GO:0046500; P:S-adenosylmethionine metabolic process XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51675 FT DOMAIN from..to FT /note="SAM-dependent MTase TRM10-type #" XX Chop: Nter=0; Cter=0; Size: 172-259; Related: None; Repeats: 1; Topology: Undefined; Example: Q7L0Y3; Scope: Eukaryota Archaea Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01013; DC Domain; TR PROSITE; PS51676; FF; 1; level=0 XX Names: FF domain Function: The FF domain is a 60 amino acid residue phosphopeptide-binding module containing two conserved phenylalanine (FF) residues that give name to the domain. XX XX FT From: PS51676 FT DOMAIN from..to FT /note="FF #" XX Chop: Nter=0; Cter=0; Size: 42-89; Related: None; Repeats: 1-6; Topology: Undefined; Example: Q9VX32; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01014; DC Domain; TR PROSITE; PS51677; NODB; 1; level=0 XX Names: NodB homology domain Function: The NodB homology domain is a catalytic domain of ~200 amino acid residues. XX XX case KW Hydrolase end case case KW Metal-binding end case XX FT From: PS51677 FT DOMAIN from..to FT /note="NodB homology #" FT ACT_SITE 8 FT /note="Proton acceptor" FT Group: 1; Condition: [DN] FT ACT_SITE 158 FT /note="Proton donor" FT Group: 1; Condition: H FT BINDING 9 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 2; Condition: [DEN] FT BINDING 58 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 2; Condition: H FT BINDING 62 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 2; Condition: [HWY] XX Chop: Nter=0; Cter=0; Size: 167-309; Related: None; Repeats: 1; Topology: Undefined; Example: Q8DP63; Scope: Bacteria Eukaryota; Encephalitozoon Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU01015; DC Domain; TR PROSITE; PS51678; SAM_MT_PRMT; 1; level=0 XX Names: SAM-dependent methyltransferase PRMT-type domain Function:Protein arginine N-methyltransferase. XX DE + RecName: EC=2.1.1.-; XX case and CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Protein arginine N-methyltransferase family. PRMT7 CC subfamily. else CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Protein arginine N-methyltransferase family. end case XX KW Methyltransferase KW Transferase KW S-adenosyl-L-methionine XX FT From: PS51678 FT DOMAIN from..to FT /note="SAM-dependent MTase PRMT-type #" XX Chop: Nter=0; Cter=0; Size: 286-399; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q8GWT4; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01016; DC Domain; TR PROSITE; PS51679; SAM_MT_C5; 1; level=0 XX Names: C-5 cytosine-specific DNA methylase (Dnmt) domain Function: DNA (cytosine-5-)-methyltransferase (EC 2.1.1.37) and tRNA (cytosine(38)-C(5))-methyltransferase (EC 2.1.1.204) XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. C5-methyltransferase family. XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51679 FT DOMAIN from..to FT /note="SAM-dependent MTase C5-type" FT ACT_SITE 76 FT Condition: C XX Chop: Nter=0; Cter=0; Size: 116-555; Related: None; Repeats: 1; Topology: Undefined; Example: P25266; Scope: Bacteria Eukaryota Viruses Archaea; Methanomada group Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01017; DC Domain; TR PROSITE; PS51680; SAM_MT_DRM; 1; level=0 XX Names: SAM-dependent methyltransferase DRM-type domain Function: Domains rearranged methylase (DRM) C5 methyltransferase XX DE + RecName: EC=2.1.1.37; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5- CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. DRM-methyltransferase family. XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51680 FT DOMAIN from..to FT /note="SAM-dependent MTase DRM-type" XX Chop: Nter=0; Cter=0; Size: 322-342; Related: None; Repeats: 1; Topology: Undefined; Example: Q9M548; Scope: Eukaryota; Arabidopsis Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01019; DC Domain; TR PROSITE; PS51682; SAM_OMT_I; 1; level=0 XX Names: SAM-dependent O-methyltransferase class I-type Function: Cation-dependent O-methyltransferase XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Cation-dependent O-methyltransferase family. XX case KW Metal-binding end case KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51682 FT BINDING 66..67 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G-[TV] FT BINDING 42 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [ITV] FT BINDING 141 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: D FT BINDING 167 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: D FT BINDING 168 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: N FT BINDING 64 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] FT BINDING 72 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: S FT BINDING 90 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] FT BINDING 119 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [AS] FT BINDING 143 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 168-244; Related: None; Repeats: 1; Topology: Undefined; Example: Q9ZTT5; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU01020; DC Domain; TR PROSITE; PS51683; SAM_OMT_II; 1; level=0 XX Names: SAM-dependent O-methyltransferase class II-type Function: Cation-independent O-methyltransferase XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Cation-independent O-methyltransferase family. XX KW Transferase KW Methyltransferase KW S-adenosyl-L-methionine XX FT From: PS51683 FT BINDING 217..219 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G-D-F FT ACT_SITE 236 FT /note="Proton acceptor" FT Condition: H FT BINDING 133 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Y FT BINDING 148 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: W FT BINDING 195 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] FT BINDING 233 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [KR] XX Chop: Nter=0; Cter=0; Size: 66-374; Related: None; Repeats: 1; Topology: Undefined; Example: P46597; Scope: Eukaryota Bacteria Archaea; Methanocaldococcus Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01021; DC Domain; TR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1; level=0 XX Names: tRNA (guanine(37)-N(1))-methyltransferase (EC 2.1.1.228) Function: tRNA (guanine(37)-N(1))-methyltransferase (EC 2.1.1.228) is an enzyme that transfers a methyl group from S-adenosyl-L-methionine (SAM) to guanine(37) in tRNA to form N(1)-methylguanine(37) in tRNA and S-adenosyl-L- homocysteine. XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. TRM5/TYW2 family. XX GO GO:0032259; P:methylation XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase KW tRNA processing XX FT From: PS51684 FT BINDING 128..129 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE]-[ILM] FT BINDING 156..157 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE]-[AGNSV] FT BINDING 90 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [HKR] FT BINDING 180 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: N XX Chop: Nter=0; Cter=0; Size: 229-457; Related: None; Repeats: 1; Topology: Undefined; Example: Q4DPN8; Scope: Eukaryota Archaea; Euryarchaeota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01022; DC Domain; TR PROSITE; PS51685; SAM_MT_ERG6; 1; level=0 XX Names: SAM-dependent methyltransferase Erg6/SMT-type domain Function: SAM-dependent sterol/triterpene methylation XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Erg6/SMT family. XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX Chop: Nter=0; Cter=0; Size: 268-309; Related: None; Repeats: 1; Topology: Undefined; Example: Q6C2D9; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01023; DC Domain; TR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1; level=0 XX Names: SAM-dependent MTase RsmB/NOP-type domain Function: RNA m(5)C methyltransferase XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RsmB/NOP family. XX GO GO:0003723; F:RNA binding XX KW Methyltransferase KW Transferase KW S-adenosyl-L-methionine KW RNA-binding XX FT From: PS51686 FT BINDING 99..105 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [ACSV]-[ACPS]-[AGP]-[PQ]-[AG]-[GINS]-K FT ACT_SITE 222 FT /note="Nucleophile" FT Condition: C FT BINDING 123 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] FT BINDING 150 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 169 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 149-392; Related: None; Repeats: 1; Topology: Undefined; Example: B2VJ83; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01024; DC Domain; TR PROSITE; PS51687; SAM_MT_RNA_M5U; 1; level=0 XX Names: SAM-dependent methyltransferase RNA m(5)U-type domain Function: RNA 5-methyluridine (m(5)U) methyltransferase XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. RNA M5U methyltransferase family. XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51687 FT ACT_SITE 319 FT /note="Nucleophile" FT Condition: C FT BINDING 194 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: Q FT BINDING 223 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [FY] FT BINDING 244 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] FT BINDING 292 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DN] XX Chop: Nter=0; Cter=0; Size: 200-559; Related: None; Repeats: 1; Topology: Undefined; Example: B3PL62; Scope: Bacteria Eukaryota Archaea Viruses; Mimivirus Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01025; DC Domain; TR PROSITE; PS51688; ICA; 1; level=0 XX Names: Intramolecular chaperone auto-processing (ICA) domain Function: The Intramolecular Chaperone Auto-processing (ICA)] domain, also called Intramolecuar Chaperone Domain (ICD) or C-terminal Intramolecular Chaperone Domain (CIMCD), is capable of catalyzing trimerization-dependent auto-proteolysis. The ICA domain contains two absolutely conserved serine and lysine residues. They form a catalytic dyad that mediates cleavage at the serine residue. The ICA domain belongs to peptidase family S74. XX XX case KW Autocatalytic cleavage end case FT From: PS51688 FT DOMAIN from..to FT /note="Peptidase S74 #" FT SITE 1-1..1 FT /note="Cleavage; by autolysis" FT Group: 1; Condition: P-S XX Chop: Nter=0; Cter=0; Size: 88-238; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y2G1; Scope: Eukaryota Viruses Comments: None; XX # Revision 1.8 2019/11/22 // AC PRU01026; DC Domain; TR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1; level=0 XX Names: rRNA adenine N(6)-methyltransferase family Function: rRNA adenine N(6)-methyltransferase and adenine N(6), N(6)- dimethyltransferase XX DE + RecName: EC=2.1.1.-; XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. rRNA adenine N(6)-methyltransferase family. XX DR PROSITE; PS01131; RRNA_A_DIMETH; 1; trigger=no XX GO GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity GO GO:0031167; P:rRNA methylation GO GO:0003723; F:RNA binding XX KW Methyltransferase KW Transferase KW S-adenosyl-L-methionine KW RNA-binding XX FT From: PS51689 FT BINDING 8 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [HKN] FT BINDING 10 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [ILMTV] FT BINDING 35 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: G FT BINDING 56 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [DE] FT BINDING 81 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D FT BINDING 101 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: [ANS] XX Chop: Nter=0; Cter=0; Size: 230-334; Related: None; Repeats: 1; Topology: Undefined; Example: P45438; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01027; DC Domain; TR PROSITE; PS51690; ALPHAVIRUS_CP; 1; level=0 XX Names: Alphavirus core protein (CP) domain Function: The alphavirus CP forms peptidase family S3. XX case DE + RecName: EC=3.4.21.90; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Autocatalytic release of the core protein from the N-terminus CC of the togavirus structural polyprotein by hydrolysis of a -Trp-|- CC Ser- bond.; EC=3.4.21.90; end case XX case GO GO:0004252; F:serine-type endopeptidase activity GO GO:0006508; P:proteolysis XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51690 FT DOMAIN from..to FT /note="Peptidase S3 #" FT ACT_SITE 27 FT /note="Charge relay system" FT Group: 1; Condition: H FT ACT_SITE 49 FT /note="Charge relay system" FT Group: 1; Condition: D FT ACT_SITE 101 FT /note="Charge relay system" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 139-161; Related: None; Repeats: 1; Topology: Undefined; Example: P22056; Scope: Viruses; Alphavirus Comments: None; XX # Revision 1.8 2019/11/22 // AC PRU01028; DC Domain; TR PROSITE; PS51691; PEPTIDASE_S6; 1; level=0 XX Names: Peptidase family S6 domain Function: The peptidase family S6 domain mediates intermolecular autoproteolysis, resulting in release of the passenger domain from the bacterial surface. XX case DE + RecName: EC=3.4.21.-; end case XX case GO GO:0004252; F:serine-type endopeptidase activity GO GO:0006508; P:proteolysis end case XX case KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51691 FT DOMAIN from..to FT /note="Peptidase S6 #" FT ACT_SITE 72 FT /note="Charge relay system" FT Group: 1; Condition: H FT ACT_SITE 102 FT /note="Charge relay system" FT Group: 1; Condition: D FT ACT_SITE 207 FT /note="Charge relay system" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 233-328; Related: None; Repeats: 1; Topology: Undefined; Example: Q84GK0; Scope: Bacteria; Pseudomonadota Comments: None; XX # Revision 1.5 2023/01/26 // AC PRU01029; DC Domain; TR PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1; level=0 XX Names: Pestivirus nonstructural protein 2 (NS2) protease domain Function: The C-terminal-most domain of NS2 is a cysteine autoprotease responsible for NS2-3 cleavage. The catalytic triad is formed by His, Glu, and Cys. The pestivirus NS2 protease domain contains five Cys and one His organized in a linear fashion, suggesting the presence of a mononuclear ZnB site. The pestivirus NS2 protease domain forms peptidase family C74. XX case DE + Contains: DE RecName: Full=Cysteine protease NS2; DE EC=3.4.22.-; XX CC -!- FUNCTION: NS2 protease seems to play a vital role in viral RNA CC replication control and in the pathogenicity of the virus. CC -!- SUBCELLULAR LOCATION: Cysteine protease NS2: Host membrane; Multi-pass CC membrane protein. end case XX GO GO:0016020; C:membrane case GO GO:0019082; P:viral protein processing GO GO:0006508; P:proteolysis end case GO GO:0033644; C:host cell membrane case GO GO:0004197; F:cysteine-type endopeptidase activity end case XX KW Host membrane case KW Hydrolase end case KW Membrane case KW Protease KW Thiol protease end case KW Transmembrane KW Transmembrane helix XX FT From: PS51692 FT TRANSMEM 128..148 FT /note="Helical" FT DOMAIN from..to FT /note="Peptidase C74 #" FT ACT_SITE 7 FT /note="For cysteine protease NS2 activity" FT Group: 1; Condition: H FT ACT_SITE 21 FT /note="For cysteine protease NS2 activity" FT Group: 1; Condition: E FT ACT_SITE 72 FT /note="For cysteine protease NS2 activity" FT Group: 1; Condition: C case FT CHAIN ?..149 FT /note="Cysteine protease NS2" FT SITE 149..149+1 FT /note="Cleavage; partial; cysteine protease NS2" end case XX Chop: Nter=0; Cter=0; Size: 139-249; Related: None; Repeats: 1; Topology: Undefined; Example: P19711; Scope: Viruses; Pestivirus Comments: None; XX # Revision 1.9 2022/09/30 // AC PRU01030; DC Domain; TR PROSITE; PS51693; HCV_NS2_PRO; 1; level=0 XX Names: Hepacivirus nonstructural protein 2 (NS2) protease domain Function: NS2 is a 217 amino acids (aa) long cysteine-protease composed of a highly hydrophobic N-terminal membrane binding domain (MBD) and a C-terminal globular and cytosolic protease domain. The HCV NS2 protease domain forms the peptidase family C18. XX case DE + Contains: DE RecName: Full=Protease NS2-3; DE Short=p23; DE EC=3.4.22.-; end case XX XX case GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51693 FT DOMAIN from..to FT /note="Peptidase C18 #" FT ACT_SITE 50 FT /note="For protease NS2-3 activity; shared with dimeric FT partner" FT Group: 1; Condition: H FT ACT_SITE 70 FT /note="For protease NS2-3 activity; shared with dimeric FT partner" FT Group: 1; Condition: E FT ACT_SITE 91 FT /note="For protease NS2-3 activity; shared with dimeric FT partner" FT Group: 1; Condition: C case FT CHAIN ?..124 FT /note="Protease NS2-3" FT SITE 124..124+1 FT /note="Cleavage; by protease NS2-3" end case XX Chop: Nter=0; Cter=0; Size: 112-138; Related: None; Repeats: 1; Topology: Undefined; Example: Q9WMX2; Scope: Viruses; Flaviviridae Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01031; DC Domain; TR PROSITE; PS51694; PEPTIDASE_M66; 1; level=0 XX Names: Peptidase family M66 domain Function: The peptidase family M66 domain is a zinc metalloprotease. XX case DE + RecName: EC=3.4.24.-; end case XX case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; end case XX case GO GO:0046872; F:metal ion binding end case case GO GO:0006508; P:proteolysis GO GO:0004222; F:metalloendopeptidase activity end case XX case KW Hydrolase KW Metalloprotease KW Protease end case case KW Metal-binding KW Zinc end case XX FT From: PS51694 FT DOMAIN from..to FT /note="Peptidase M66" FT ACT_SITE 154 FT Group: 1; Condition: E FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Group: 2; Condition: H FT BINDING 157 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Group: 2; Condition: H FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Group: 2; Condition: H XX Chop: Nter=0; Cter=0; Size: 245-282; Related: None; Repeats: 1; Topology: Undefined; Example: O82882; Scope: Bacteria; Pseudomonadota Eukaryota; Dictyostelium Comments: None; XX # Revision 1.8 2023/01/26 // AC PRU01032; DC Domain; TR PROSITE; PS51695; SEDOLISIN; 1; level=0 XX Names: Sedolisin domain Function: Sedolisins (serine-carboxyl peptidases) are proteolytic enzymes whose fold ressembles that of subtilisin; however they are considerably larger, with the mature catalytic domains containing approximately 375 amino acids. The defining features of these enzymes are a unique catalytic triad, Ser-Glu-Asp (SED in single-letter notation), as well as the presence of an aspartic acid residue in the oxyanion hole. XX case CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Note=Binds 1 Ca(2+) ion per subunit.; end case XX case GO GO:0004252; F:serine-type endopeptidase activity end case case GO GO:0046872; F:metal ion binding end case XX case KW Hydrolase KW Protease KW Serine protease end case case KW Calcium KW Metal-binding end case XX FT From: PS51695 FT DOMAIN from..to FT /note="Peptidase S53 #" FT ACT_SITE 76 FT /note="Charge relay system" FT Group: 1; Condition: E FT ACT_SITE 80 FT /note="Charge relay system" FT Group: 1; Condition: D FT ACT_SITE 290 FT /note="Charge relay system" FT Group: 1; Condition: S FT BINDING 332 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: D FT BINDING 333 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: [IV] FT BINDING 354 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: G FT BINDING 356 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT Group: 2; Condition: D XX Chop: Nter=0; Cter=0; Size: 343-439; Related: None; Repeats: 1; Topology: Undefined; Example: C5FHK0; Scope: Eukaryota Bacteria; Pseudomonadota Comments: None; XX # Revision 1.7 2023/01/26 // AC PRU01033; DC Domain; TR PROSITE; PS51697; ALOG; 1; level=0 XX Names: ALOG domain Function: The ALOG domain is predicted to be a DNA-binding domain. XX XX FT From: PS51697 FT DOMAIN from..to FT /note="ALOG #" XX Chop: Nter=0; Cter=0; Size: 100-150; Related: None; Repeats: 1; Topology: Undefined; Example: Q6NNI3; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01034; DC Domain; TR PROSITE; PS51698; U_BOX; 1; level=0 XX Names: U-box domain Function: The U-box is a E3 ligase domain of ~70 amino acids that is present in proteins from yeast to human. XX XX GO GO:0000151; C:ubiquitin ligase complex GO GO:0004842; F:ubiquitin-protein transferase activity XX KW Ubl conjugation pathway XX FT From: PS51698 FT DOMAIN from..to FT /note="U-box #" XX Chop: Nter=0; Cter=0; Size: 59-93; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q8GZ84; Scope: Eukaryota Bacteria; Legionella Viruses; Mimivirus Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01035; DC Domain; TR PROSITE; PS50235; USP_3; 1; level=0 XX Names: Ubiquitin specific protease (USP) domain Function: The USP domain forms the peptidase family C19. XX CC -!- SIMILARITY: Belongs to the peptidase C19 family. XX DR PROSITE; PS00972; USP_1; 1; trigger=no DR PROSITE; PS00973; USP_2; 1; trigger=no XX case GO GO:0006511; P:ubiquitin-dependent protein catabolic process XX KW Hydrolase KW Protease KW Thiol protease end case KW Ubl conjugation pathway XX FT From: PS50235 FT DOMAIN from..to FT /note="USP #" FT ACT_SITE 10 FT /note="Nucleophile" FT Group: 1; Condition: C FT ACT_SITE 288 FT /note="Proton acceptor" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 94-892; Related: None; Repeats: 1; Topology: Undefined; Example: P39967; Scope: Eukaryota Viruses; Mimivirus Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01036; DC Domain; TR PROSITE; PS51699; SEA_DG; 1; level=0 XX Names: DG-type SEA domain Function: The DG-type SEA domain forms the peptidase S72 family. XX case CC -!- PTM: Autolytic cleavage produces the alpha and beta subunits. In CC cutaneous cells, as well as in certain pathological conditions, CC shedding of beta-dystroglcan can occur releasing a peptide of about 30 CC kDa. end case XX GO GO:0016020; C:membrane GO GO:0016011; C:dystroglycan complex XX FT From: PS51699 FT DOMAIN from..to FT /note="Peptidase S72 #" FT SITE 53..54 FT /note="Cleavage; by autolysis" FT Group: 1; Condition: G-S XX Chop: Nter=0; Cter=0; Size: 100-120; Related: None; Repeats: 1; Topology: Undefined; Example: Q62165; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.6 2022/09/30 // AC PRU01037; DC Domain; TR PROSITE; PS51700; SEPARIN; 1; level=0 XX Names: SEPARIN core domain Function: The separin core domain contains a conserved histidine and cyteine residue, which are hallmarks of cysteine proteases. The separin core domain forms the peptidase C50 family. XX XX case KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51700 FT DOMAIN from..to FT /note="Peptidase C50 #" FT ACT_SITE 85 FT Tag: protease; Condition: C XX Chop: Nter=0; Cter=0; Size: 85-110; Related: None; Repeats: 1; Topology: Undefined; Example: Q14674; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01038; DC Domain; TR PROSITE; PS51701; 6_CYS; 1; level=0 XX Names: 6-Cysteine (6-Cys) domain Function: The domain is of roughly 120 amino acids and contains six positionally conserved cysteines. XX XX case KW Disulfide bond end case XX FT From: PS51701 FT DOMAIN from..to FT /note="6-Cys #" FT DISULFID 5..29 FT Tag: disulf; Condition: C-x*-C FT DISULFID 44..117 FT Tag: disulf; Condition: C-x*-C FT DISULFID 60..115 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 103-276; Related: None; Repeats: 1-14; Topology: Undefined; Example: C6KSX1; Scope: Eukaryota; Plasmodium Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01039; DC Domain; TR PROSITE; PS51702; HTH_MU; 1; level=0 XX Names: Mu-type HTH domain Function: The Mu-type HTH is a DNA-binding, winged helix-turn-helix (wHTH) domain of about 75 residues. XX XX GO GO:0003677; F:DNA binding GO GO:0000166; F:nucleotide binding XX KW DNA-binding XX FT From: PS51702 FT DOMAIN from..to FT /note="HTH Mu-type #" FT DNA_BIND 7..30 FT /note="H-T-H motif" XX Chop: Nter=0; Cter=0; Size: 49-79; Related: None; Repeats: 1; Topology: Undefined; Example: P06019; Scope: Viruses; Muvirus Bacteria; Haemophilus Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01040; DC Domain; TR PROSITE; PS51703; DZF; 1; level=0 XX Names: DZF domain Function: The DZF domain (domain associated with zinc fingers) is a dimerization domain. XX XX FT From: PS51703 FT DOMAIN from..to FT /note="DZF #" XX Chop: Nter=0; Cter=0; Size: 327-387; Related: None; Repeats: 1; Topology: Undefined; Example: Q5REX3; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01041; DC Domain; TR PROSITE; PS51704; GP_PDE; 1; level=0 XX Names: GP-PDE domain Function: GD-PDEs are involved in glycerol metabolism and catalyze the reaction of glycerophosphodiester and water to alcohol and sn-glycerol-3- phosphate. XX case CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=CHEBI:60240; end case XX GO GO:0006071; P:glycerol metabolic process GO GO:0008889; F:glycerophosphodiester phosphodiesterase activity XX KW Hydrolase case KW Metal-binding end case XX FT From: PS51704 FT DOMAIN from..to FT /note="GP-PDE #" FT BINDING 33 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: E FT BINDING 35 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: D FT BINDING 48 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 223-356; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9SZ11; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU01042; DC Domain; TR PROSITE; PS51705; G_HFLX; 1; level=0 XX Names: HflX-type guanine nucleotide-binding (G) domain Function: The broad phylogenetic distribution pattern of HflX GTPases in Bacteria, Archaea, and Eukaryotes (including human) suggests a basic cellular function for this protein family. XX case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; end case CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity end case case GO GO:0046872; F:metal ion binding GO GO:0000287; F:magnesium ion binding end case XX case KW GTP-binding KW Nucleotide-binding end case case KW Magnesium KW Metal-binding end case XX FT From: PS51705 FT DOMAIN from..to FT /note="Hflx-type G #" FT BINDING 7..14 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT BINDING 32..36 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: x(2)-[TS]-x(2) FT BINDING 54..57 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: D-x(2)-G FT BINDING 120..123 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: [NT]-K-x-D FT BINDING 145..147 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1 FT BINDING 14 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] FT BINDING 34 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] XX Chop: Nter=0; Cter=0; Size: 151-250; Related: None; Repeats: 1; Topology: Undefined; Example: Q980M3; Scope: Bacteria Archaea Eukaryota Comments: None; XX # Revision 1.20 2022/11/19 // AC PRU01043; DC Domain; TR PROSITE; PS51706; G_ENGB; 1; level=0 XX Names: EngB-type guanine nucleotide-binding (G) domain Function: Proteins of the EngB-type GTPase family are involved in the biogenesis of ribosomes and are essential for the survival of a wide range of bacteria. XX case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; end case CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. EngB GTPase family. XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity end case case GO GO:0000287; F:magnesium ion binding GO GO:0046872; F:metal ion binding end case XX case KW GTP-binding KW Nucleotide-binding end case case KW Magnesium KW Metal-binding end case XX FT From: PS51706 FT DOMAIN from..to FT /note="EngB-type G #" FT BINDING 9..16 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT BINDING 36..40 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: x(2)-[ST]-x(2) FT BINDING 55..58 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: D-x(2)-G FT BINDING 122..125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: [NT]-K-x-D FT BINDING 157..159 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1 FT BINDING 16 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] FT BINDING 38 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] XX Chop: Nter=0; Cter=0; Size: 153-218; Related: None; Repeats: 1; Topology: Undefined; Example: P38424; Scope: Bacteria Archaea; Euryarchaeota Eukaryota Comments: None; XX # Revision 1.14 2022/11/19 // AC PRU01044; DC Domain; TR PROSITE; PS51707; CYTH; 1; level=0 XX Names: CYTH domain Function: CYTH domains are likely to be domains specialized to bind nucleotides and other organic phosphates. XX XX FT From: PS51707 FT DOMAIN from..to FT /note="CYTH #" XX Chop: Nter=0; Cter=0; Size: 157-219; Related: None; Repeats: 1; Topology: Undefined; Example: Q57692; Scope: Eukaryota Bacteria Archaea; Methanocaldococcus Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01045; DC Domain; TR PROSITE; PS51708; CHAD; 1; level=0 XX Names: CHAD domain Function: The CHAD (conserved histidine alpha-helical domain) is an uncharacterized domain, with a characteristic pattern of conserved histidines and other charged residues. The conserved charged residues could form a strongly polar surface that could participate, either in metal chelation, or act as phosphoacceptors. XX XX FT From: PS51708 FT DOMAIN from..to FT /note="CHAD #" XX Chop: Nter=0; Cter=0; Size: 206-289; Related: None; Repeats: 1; Topology: Undefined; Example: P30871; Scope: Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01046; DC Domain; TR PROSITE; PS51709; G_TRME; 1; level=0 XX Names: TrmE-type guanine nucleotide-binding (G) domain Function: TrmE (also called MnmE) contains a canonical G domain and is conserved in all three kingdoms of life. case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; end case XX case CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Note=Binds 1 potassium ion per subunit.; end case CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. TrmE GTPase family. XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity end case case GO GO:0000287; F:magnesium ion binding end case case GO GO:0030955; F:potassium ion binding end case case or GO GO:0046872; F:metal ion binding end case XX case KW GTP-binding KW Nucleotide-binding end case case KW Magnesium end case case KW Potassium end case case or KW Metal-binding end case XX FT From: PS51709 FT DOMAIN from..to FT /note="TrmE-type G #" FT BINDING 8..15 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT BINDING 34..38 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: x(2)-[ST]-x(2) FT BINDING 55..58 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: D-x(2)-G FT BINDING 115..118 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: [NT]-K-x-D FT BINDING 139..141 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1 FT BINDING 15 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] FT BINDING 36 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] FT BINDING 11 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Group: 3; Condition: N FT BINDING 30 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Group: 3; Condition: [ST] FT BINDING 32 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Group: 3; Condition: [ILV] FT BINDING 35 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT Group: 3; Condition: [ST] XX Chop: Nter=0; Cter=0; Size: 128-277; Related: None; Repeats: 1; Topology: Undefined; Example: P25522; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU01047; DC Domain; TR PROSITE; PS51710; G_OBG; 1; level=0 XX Names: OBG-type guanine nucleotide-binding (G) domain Function: Within the translation factor-related (TRAFAC) class of P-loop GTPases, the OBG family comprises a group of high-molecular mass GTPases conserved from bacteria to eukaryotes. XX case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; end case CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity end case case GO GO:0005524; F:ATP binding GO GO:0016887; F:ATP hydrolysis activity end case case GO GO:0046872; F:metal ion binding GO GO:0000287; F:magnesium ion binding end case XX case KW GTP-binding end case case KW ATP-binding end case case and KW Nucleotide-binding end case case KW Magnesium KW Metal-binding end case XX FT From: PS51710 FT DOMAIN from..to FT /note="OBG-type G #" FT BINDING 7..14 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT BINDING 32..36 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: x(2)-[ST]-x(2) FT BINDING 54..57 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: D-x(2)-G FT BINDING 126..129 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: [NT]-K-x-D FT BINDING 156..158 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1 FT BINDING 7..14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 2; Condition: G-x(4)-G-K-[ST] FT BINDING 32..36 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 2; Condition: x(2)-[ST]-x(2) FT BINDING 54..57 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 2; Condition: D-x(2)-G FT BINDING 126..129 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 2; Condition: N-x(2)-[EQ] FT BINDING 156..158 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 2 FT BINDING 14 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 3; Condition: [ST] FT BINDING 34 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 3; Condition: [ST] XX Chop: Nter=0; Cter=0; Size: 51-280; Related: None; Repeats: 1; Topology: Undefined; Example: Q72HR4; Q9NTK5; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Comments: None; XX # Revision 1.20 2022/11/19 // AC PRU01048; DC Domain; TR PROSITE; PS51711; G_FEOB; 1; level=0 XX Names: FeoB-type guanine nucleotide-binding (G) domain Function: FeoB is involved in the uptake of ferrous iron (Fe(2+)), an important cofactor in biological electron transfer and catalysis. XX CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. FeoB GTPase (TC 9.A.8) family. XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity end case case GO GO:0046872; F:metal ion binding GO GO:0000287; F:magnesium ion binding end case XX case KW GTP-binding KW Nucleotide-binding end case case KW Magnesium KW Metal-binding end case XX FT From: PS51711 FT DOMAIN from..to FT /note="FeoB-type G #" FT BINDING 8..15 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT BINDING 33..37 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#" FT Group: 1; Condition: x(2)-[ST]-x(2) FT BINDING 54..57 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#" FT Group: 1; Condition: D-x(2)-G FT BINDING 114..117 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1; Condition: N-x(2)-D FT BINDING 143..145 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT Group: 1 FT BINDING 15 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] FT BINDING 35 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT Group: 2; Condition: [ST] XX Chop: Nter=0; Cter=0; Size: 151-177; Related: None; Repeats: 1; Topology: Undefined; Example: P33650; Scope: Bacteria Archaea; Methanocaldococcus Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU01049; DC Domain; TR PROSITE; PS51712; G_ENGA; 1; level=0 XX Names: EngA-type guanine nucleotide-binding (G) domain Function: EngA (Essential neisserial GTPase A) proteins belong to TrmE-Era- EngA-YihA-Septin like superfamily of TRAFAC class and form a unique family of bacterial GTPases with two G domains in tandem, namely GD1 and GD2, followed by a C-terminal KH-like domain. They have been shown to interact with the bacterial ribosome and to be involved in its biogenesis. XX CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. EngA (Der) GTPase family. XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity XX KW GTP-binding KW Nucleotide-binding end case XX FT From: PS51712 FT DOMAIN from..to FT /note="EngA-type G #" FT BINDING 7..14 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#1" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT BINDING 33..37 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#1" FT Group: 1; Condition: x(2)-[ST]-x(2) FT BINDING 54..57 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#1" FT Group: 1; Condition: D-x(2)-G FT BINDING 119..122 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#1" FT Group: 1; Condition: N-K-x-[DE] FT BINDING 149..151 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /ligand_label="#1" FT Group: 1 XX Chop: Nter=0; Cter=0; Size: 152-194; Related: None; Repeats: 2; Topology: Undefined; Example: P50743; Scope: Bacteria Comments: None; XX # Revision 1.10 2022/11/19 // AC PRU01050; DC Domain; TR PROSITE; PS51713; G_ERA; 1; level=0 XX Names: Era-type guanine nucleotide-binding (G) domain profile Function: Era is a small G-protein widely conserved in eubacteria and eukaryotes. It is essential for bacterial cell viability and is required for the maturation of 16S rRNA and assembly of the 30S ribosomal subunit. XX CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. Era GTPase family. XX case GO GO:0005525; F:GTP binding XX KW GTP-binding KW Nucleotide-binding end case XX FT From: PS51713 FT DOMAIN from..to FT /note="Era-type G #" FT REGION 9..16 FT /note="G1 #" FT Group: 1; Condition: G-x(4)-G-K-S FT REGION 35..39 FT /note="G2 #" FT Group: 1; Condition: x(2)-T-x(2) FT REGION 56..59 FT /note="G3 #" FT Group: 1; Condition: D-x(2)-G FT REGION 118..121 FT /note="G4 #" FT Group: 1; Condition: [NST]-[K]-x-[DE] FT REGION 148..150 FT /note="G5 #" FT Group: 1 XX Chop: Nter=0; Cter=0; Size: 133-276; Related: None; Repeats: 1; Topology: Undefined; Example: C0PYG8; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.2 2020/05/20 // AC PRU01051; DC Domain; TR PROSITE; PS51714; G_BMS1; 1; level=0 XX Names: Bms1-type guanine nucleotide-binding (G) domain Function: Bms1p and Tsr1p represent a new family of factors required for ribosome biogenesis. They are each independently required for 40S ribosomal subunit biogenesis. Bms1p, a protein required for pre-rRNA processing, contains an evolutionarily conserved G domain with five conserved polypeptide loops designated G1 through G5, which form contact sites with the guanine nucleotide or coordinate the Mg(2+) ion. Tsr1p lacks a P-loop and is not predicted to bind GTP. XX CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Bms1-like GTPase family. XX case GO GO:0005525; F:GTP binding XX KW GTP-binding KW Nucleotide-binding end case XX FT From: PS51714 FT DOMAIN from..to FT /note="Bms1-type G #" FT REGION 10..17 FT /note="G1 #" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT REGION 42..46 FT /note="G2 #" FT Group: 1; Condition: x(2)-T-x(2) FT REGION 57..60 FT /note="G3 #" FT Group: 1; Condition: E-x(3) FT REGION 110..113 FT /note="G4 #" FT Group: 1; Condition: T-H-x-D FT REGION 144..146 FT /note="G5 #" FT Group: 1 XX Chop: Nter=0; Cter=0; Size: 157-195; Related: None; Repeats: 1; Topology: Undefined; Example: Q07381; Scope: Eukaryota Comments: None; XX # Revision 1.1 2020/05/20 // AC PRU01052; DC Domain; TR PROSITE; PS51715; G_GB1_RHD3; 1; level=0 XX Names: GB1/RHD3-type guanine nucleotide-binding (G) domain Function: The GB1/RHD3 GTPase family contains a large G domain (~230 amino acids). The GB1/RHD3-type G domain has a low intrinsic affinity for nucleotide and often depends on nucleotide-dependent homodimerization to facilitate GTP hydrolysis. XX CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. GB1/RHD3 GTPase family. XX case and and GO GO:0005525; F:GTP binding XX KW GTP-binding KW Hydrolase KW Nucleotide-binding end case XX FT From: PS51715 FT DOMAIN from..to FT /note="GB1/RHD3-type G #" XX Chop: Nter=0; Cter=0; Size: 205-282; Related: None; Repeats: 1; Topology: Undefined; Example: Q8NHH9; Scope: Eukaryota Comments: None; XX # Revision 1.3 2020/05/13 // AC PRU01053; DC Domain; TR PROSITE; PS51716; G_IRG; 1; level=0 XX Names: IRG-type guanine nucleotide-binding (G) domain Function: The p47 or immunity-related GTPases (IRG) are at least as old as the vertebrates. The IRG proteins are an essential resistance system in the mouse for immunity against pathogens that enter the cell via a vacuole. Despite its importance for the mouse, the IRG resistance system is absent from humans because it has been lost during the divergent evolution of the primates. The IRG proteins appear to be accompanied phylogenetically by homologous proteins, named 'quasi IRG' (IRGQ) proteins, that probably lack nucleotide binding or hydrolysis function, and that may form regulatory heterodimers with functional IRG proteins. XX CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. IRG family. XX case and and GO GO:0005525; F:GTP binding XX KW GTP-binding KW Hydrolase KW Nucleotide-binding end case XX FT From: PS51716 FT DOMAIN from..to FT /note="IRG-type G #" XX Chop: Nter=0; Cter=0; Size: 140-237; Related: None; Repeats: 1; Topology: Undefined; Example: Q6AYC2; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.1 2020/05/11 // AC PRU01054; DC Domain; TR PROSITE; PS51717; G_VLIG; 1; level=0 XX Names: Very large inducible GTPASE (VLIG)-type guanine nucleotide-binding (G) domain Function: The very large inducible GTPase (VLIG) family contributes to the cellular response to both type I and type II interferons (IFNs). The potential GTP-binding activity of mouse VLIG-1, the prototype VLIG, possesses a classical GTP-binding sequence motif. XX CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. Very large inducible GTPase (VLIG) family. XX XX GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity XX KW GTP-binding KW Nucleotide-binding XX FT From: PS51717 FT DOMAIN from..to FT /note="VLIG-type G #" XX Chop: Nter=0; Cter=0; Size: 230-250; Related: None; Repeats: 1; Topology: Undefined; Example: Q5NCI0; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.2 2020/04/24 // AC PRU01055; DC Domain; TR PROSITE; PS51718; G_DYNAMIN_2; 1; level=0 XX Names: Dynamin-type guanine nucleotide-binding (G) domain Function: Members of the dynamin GTPase family catalyze diverse membrane remodelling events in endocytosis, cell division, and plastid maintenance. The dynamin-type G domain consists of a central eight-stranded beta-sheet surrounded by seven alpha-helices and two one-turn helices. It contains the five canonical guanine nucleotide binding motifs (G1-5). XX CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase CC superfamily. Dynamin/Fzo/YdjA family. XX DR PROSITE; PS00410; G_DYNAMIN_1; 1; trigger=no XX GO GO:0003924; F:GTPase activity GO GO:0005525; F:GTP binding XX KW Nucleotide-binding KW GTP-binding XX FT From: PS51718 FT DOMAIN from..to FT /note="Dynamin-type G #" FT REGION 11..18 FT /note="G1 motif" FT REGION 37..39 FT /note="G2 motif" FT REGION 113..116 FT /note="G3 motif" FT REGION 179..182 FT /note="G4 motif" FT REGION 213..216 FT /note="G5 motif" XX Chop: Nter=0; Cter=0; Size: 101-347; Related: None; Repeats: 1; Topology: Undefined; Example: P21575; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01056; DC Domain; TR PROSITE; PS51719; G_SEPTIN; 1; level=0 XX Names: Septin-type guanine nucleotide-binding (G) domain Septin-type G domain Function: Septins are a family of eukaryotic cytoskeletal proteins conserved from yeasts to humans. The septin family belongs to the guanosine- triphosphate (GTP)ase superclass of P-loop nucleoside triphosphate (NTP)ases. XX CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. Septin GTPase family. XX GO GO:0005525; F:GTP binding GO GO:0031105; C:septin complex XX KW GTP-binding KW Nucleotide-binding XX FT From: PS51719 FT DOMAIN from..to FT /note="Septin-type G #" FT REGION 11..18 FT /note="G1 motif" FT REGION 68..71 FT /note="G3 motif" FT REGION 150..153 FT /note="G4 motif" XX Chop: Nter=0; Cter=0; Size: 241-335; Related: None; Repeats: 1; Topology: Undefined; Example: Q15019; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01057; DC Domain; TR PROSITE; PS51720; G_AIG1; 1; level=0 XX Names: AIG1-type G domain Function: The AIG1-type G domain contains a central beta-sheet sandwiched by two layers of alpha-helices. XX CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family. XX case GO GO:0005525; F:GTP binding XX KW GTP-binding KW Nucleotide-binding end case XX FT From: PS51720 FT DOMAIN from..to FT /note="AIG1-type G #" FT REGION 10..17 FT /note="G1 #" FT Group: 1; Condition: G-x(4)-G-K-S FT REGION 37..41 FT /note="G2 #" FT Group: 1 FT REGION 58..61 FT /note="G3 #" FT Group: 1; Condition: D-x(2)-[GD] FT REGION 129..132 FT /note="G4 #" FT Group: 1; Condition: T-x(3) FT REGION 166..168 FT /note="G5 #" FT Group: 1; Condition: x-N-x XX Chop: Nter=0; Cter=0; Size: 195-240; Related: None; Repeats: 1; Topology: Undefined; Example: Q8K3K9; Scope: Eukaryota Comments: None; XX # Revision 1.1 2020/06/17 // AC PRU01058; DC Domain; TR PROSITE; PS51721; G_CP; 1; level=0 XX Names: Circularly permuted (CP)-type guanine nucleotide-binding (G) domain Function: The TRAFAC (named after translation factors) class includes an atypical family characterized by a circularly permuted (CP) order of the GTPase motifs within the G domain: the normal G1-G2-G3-G4-G5 orientation of the G domain has been rearranged to G4(N/T-K-x-D)-G5(T/G-C/S-A)-G1(Walker A, P-loop)-G2(T)-G3(Walker B). XX case CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA CC subfamily. else CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. end case XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity XX KW GTP-binding KW Nucleotide-binding KW Hydrolase end case XX FT From: PS51721 FT DOMAIN from..to FT /note="CP-type G #" FT REGION 46..49 FT /note="G4 #" FT Group: 1; Condition: [NST]-K-x-D FT REGION 76..78 FT /note="G5 #" FT Group: 1 FT REGION 100..107 FT /note="G1 #" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT REGION 132..136 FT /note="G2 #" FT Group: 1; Condition: x(2)-[TS]-x(2) FT REGION 150..153 FT /note="G3 #" FT Group: 1; Condition: D-x(2)-G XX Chop: Nter=0; Cter=0; Size: 142-313; Related: None; Repeats: 1; Topology: Undefined; Example: Q9H089; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01059; DC Domain; TR PROSITE; PS51722; G_TR_2; 1; level=0 XX Names: Translational (tr)-type guanine nucleotide-binding (G) domain Function: Translational GTPases (trGTPases) are a family of proteins in which GTPase activity is stimulated by the large ribosomal subunit. XX CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. XX case GO GO:0005525; F:GTP binding GO GO:0003924; F:GTPase activity XX KW GTP-binding KW Nucleotide-binding end case XX FT From: PS51722 FT DOMAIN from..to FT /note="tr-type G #" FT REGION 10..17 FT /note="G1 #" FT Group: 1; Condition: G-x(4)-G-K-[ST] FT REGION 52..56 FT /note="G2 #" FT Group: 1; Condition: x(2)-[TS]-x(2) FT REGION 73..76 FT /note="G3 #" FT Group: 1; Condition: D-x(2)-G FT REGION 127..130 FT /note="G4 #" FT Group: 1; Condition: [NT]-K-x-D FT REGION 179..181 FT /note="G5 #" FT Group: 1 XX Chop: Nter=0; Cter=0; Size: 79-362; Related: None; Repeats: 1; Topology: Undefined; Example: O50293; Scope: Bacteria Eukaryota Archaea Viruses; Mimivirus Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01060; DC Domain; TR PROSITE; PS51723; PEPTIDASE_M60; 1; level=0 XX Names: Peptidase family M60 domain Function: The peptidase family M60 domain belongs to the zincin superfamily of zinc-requiring metalloproteases (clan MA, subclan MA(E)). The peptidase family M60 domain contains the metal-binding consensus motif HExxH. The peptidase family M60 domain targets complex host glycoproteins, such as mucins. XX XX FT From: PS51723 FT DOMAIN from..to FT /note="Peptidase M60 #" XX Chop: Nter=0; Cter=0; Size: 277-314; Related: None; Repeats: 1; Topology: Undefined; Example: P29998; Scope: Eukaryota Bacteria; Gammaproteobacteria Viruses; Betabaculovirus Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01061; DC Domain; TR PROSITE; PS51724; SPOR; 1; level=0 XX Names: SPOR domain Function: SPOR domain proteins are widespread in bacteria, many of these proteins are involved in sporulation and cell division, and SPOR domains are sufficient for septal localization, probaly because SPOR domains bind to septal peptidoglycan (PG). XX XX FT From: PS51724 FT DOMAIN from..to FT /note="SPOR #" XX Chop: Nter=0; Cter=0; Size: 63-94; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q9KTF4; Scope: Bacteria Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01062; DC Domain; TR PROSITE; PS51725; ABM; 1; level=0 XX Names: ABM domain Function: The antibiotic biosynthesis monooxygenase (ABM) domain is found in proteins involved in a diverse range of biological processes, including metabolism, transcription, translation and biosynthesis of secondary metabolites. XX XX FT From: PS51725 FT DOMAIN from..to FT /note="ABM #" XX Chop: Nter=0; Cter=0; Size: 77-110; Related: None; Repeats: 1; Topology: Undefined; Example: Q2G1J2; Scope: Bacteria Eukaryota Archaea; Halobacteriaceae Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01063; DC Domain; TR PROSITE; PS51726; MYST_HAT; 1; level=0 XX Names: MYST-type histone acetyltransferase (HAT) domain Function: The MYST-type HAT domain contains three regions: a central region associated with acetyl-CoA cofactor binding and catalysis in addition to flanking N- and C-terminal regions harboring respectively a C2HC-type zinc finger and a helix-turn-helix DNA-binding motif. XX case DE + RecName: EC=2.3.1.48; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; end case XX case GO GO:0004402; F:histone acetyltransferase activity end case case or GO GO:0046872; F:metal ion binding XX KW Zinc KW Metal-binding end case case KW Zinc-finger KW Acetylation KW Transferase end case XX FT From: PS51726 FT DOMAIN from..to FT /note="MYST-type HAT #" case and and and FT ZN_FING 34..59 FT /note="C2HC MYST-type #" else case and and and FT ZN_FING 34..59 FT /note="C2HC MYST-type #; atypical" else FT ZN_FING 34..59 FT /note="C2HC MYST-type #; degenerate" end case case FT BINDING 151..157 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1 end case case FT BINDING 142..146 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1 end case FT ACT_SITE 177 FT /note="Proton donor/acceptor" FT Group: 1; Condition: E FT BINDING 181 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1; Condition: S case FT BINDING 190 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Condition: S FT BINDING 260 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Condition: K end case FT MOD_RES 101 FT /note="N6-acetyllysine; by autocatalysis" FT Group: 1; Condition: K XX Chop: Nter=0; Cter=0; Size: 260-344; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LXD7; Scope: Eukaryota Comments: None; XX # Revision 1.12 2022/11/19 // AC PRU01064; DC Domain; TR PROSITE; PS51728; RTT109_HAT; 1; level=0 XX Names: Rtt109-type histone acetyltransferase (HAT) domain Function: Rtt109, also known as KAT11, is a recently characterized fungal- specific HAT that modifies histone H3 lysine 56 (H3K56) to promote genome stability and resistance to a variety of DNA-damaging agents. XX DE + RecName: EC=2.3.1.48; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; CC -!- SIMILARITY: Belongs to the RTT109 family. XX KW DNA damage XX FT From: PS51728 FT DOMAIN from..to FT /note="Rtt109-type HAT #" XX Chop: Nter=0; Cter=0; Size: 336-413; Related: None; Repeats: 1; Topology: Undefined; Example: Q5AAJ8; Scope: Eukaryota; Ascomycota Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01065; DC Domain; TR PROSITE; PS51727; CBP_P300_HAT; 1; level=0 XX Names: CBP/p300-type histone acetyltransferase (HAT) domain profile Function: CREB-binding protein (CBP)/p300 proteins are involved in various physiological events including proliferation, differentiation and apoptosis. CBP/p300 proteins contain several well-defined protein-interaction domains as well as a centrally located 380-residue HAT domain. XX case GO GO:0004402; F:histone acetyltransferase activity XX KW Acyltransferase KW Transferase end case XX FT From: PS51727 FT DOMAIN from..to FT /note="CBP/p300-type HAT #" FT BINDING 114..116 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1; Condition: [IL]-D-S FT BINDING 126..127 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1; Condition: R-T FT BINDING 173 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1; Condition: [I] FT BINDING 178 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1; Condition: [R] FT BINDING 182 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT Group: 1; Condition: W XX Chop: Nter=0; Cter=0; Size: 367-448; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LG11; Scope: Eukaryota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01066; DC Domain; TR PROSITE; PS50968; BIOTINYL_LIPOYL; 1; level=0 XX Names: Biotinyl/lipoyl domain Function: Biotin and lipoic acid moieties are the covalently bound cofactors of several multicomponent enzyme complexes that catalyze key metabolic reactions. They are attached to a lysine residue, via an amide bond, by specific biotinyl and lipoyl protein ligases. XX case or CC -!- COFACTOR: CC Name=biotin; Xref=ChEBI:CHEBI:57586; else case CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Note=Binds 1 lipoyl cofactor covalently.; end case XX case or KW Biotin else case KW Lipoyl end case XX FT From: PS50968 case or FT DOMAIN from..to FT /note="Biotinyl-binding #" FT MOD_RES 42 FT /note="N6-biotinyllysine" FT Condition: K else FT DOMAIN from..to FT /note="Lipoyl-binding #" FT MOD_RES 42 FT /note="N6-lipoyllysine" FT Condition: K end case XX Chop: Nter=0; Cter=0; Size: 57-96; Related: None; Repeats: 1-3; Topology: Undefined; Example: P0A6T9; P0ABD8; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01067; DC Domain; TR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1; level=0 XX Names: BPL/LPL catalytic domain Function: Lipoylating and biotinylating enzymes are evolutionarily related protein families containing a homologous catalytic module. XX XX DR PROSITE; PS01313; LIPB; 1; trigger=no XX FT From: PS51733 FT DOMAIN from..to FT /note="BPL/LPL catalytic #" XX Chop: Nter=0; Cter=0; Size: 103-239; Related: None; Repeats: 1; Topology: Undefined; Example: A0LIW0; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01068; DC Domain; TR PROSITE; PS51732; ASN_GLN_ASE_3; 1; level=0 XX Names: Asparaginase / glutaminase domain Function: Asparaginase (EC 3.5.1.1), glutaminase (EC 3.5.1.2) and glutaminase- asparaginase (EC 3.5.1.38) are aminohydrolases that catalyze the hydrolysis of asparagine (or glutamine) to aspartate (or glutamate) and ammonia. XX XX DR PROSITE; PS00144; ASN_GLN_ASE_1; 1; trigger=no DR PROSITE; PS00917; ASN_GLN_ASE_2; 1; trigger=no XX GO GO:0004067; F:asparaginase activity XX FT From: PS51732 FT DOMAIN from..to FT /note="Asparaginase/glutaminase #" XX Chop: Nter=0; Cter=0; Size: 23-362; Related: None; Repeats: 1; Topology: Undefined; Example: Q9X7E6; Scope: Archaea Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01069; DC Domain; TR PROSITE; PS51734; SAM_MPBQ_MSBQ_MT; 1; level=0 XX Names: MPBQ/MBSQ family SAM-binding methyltransferase Function: 2-methyl-6-phytyl-1,4-benzoquinone/2-methyl-6-solanyl-1,4- benzoquinone MT (MPBQ/MSBQ MT) (EC 2.1.1.295). XX CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. MPBQ/MBSQ MT family. XX GO GO:0032259; P:methylation XX KW Methyltransferase KW S-adenosyl-L-methionine KW Transferase XX FT From: PS51734 FT REGION 48..57 FT /note="SAM motif I" FT REGION 93..106 FT /note="SAM motif II" FT REGION 134..147 FT /note="SAM motif III" XX Chop: Nter=0; Cter=0; Size: 200-220; Related: None; Repeats: 1; Topology: Undefined; Example: Q9LY74; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01070; DC Domain; c? TR PROSITE; PS00409; PROKAR_NTER_METHYL; 1; level=0 XX Names: Prokaryotic N-terminal methylation Function: Gram-negative bacteria produce pilin which are characterized by the presence of a very short leader peptide of 6 to 7 residues, followed by a methylated N-terminal phenylalanine residue and by a highly conserved sequence of about 24 hydrophobic residues. This class of pilin is often referred to as NMePhe or type-4 pili. XX DE Flags: Precursor; XX FT From: PS00409 FT PROPEP Nter..2 FT CHAIN 3..Cter FT /note="" FT MOD_RES 3 FT /note="N-methylphenylalanine" FT Condition: F FT MOD_RES 3 FT /note="N-methyltyrosine" FT Condition: Y FT MOD_RES 3 FT /note="N-methylleucine" FT Condition: L FT MOD_RES 3 FT /note="N-methylisoleucine" FT Condition: I FT MOD_RES 3 FT /note="N-methylmethionine" FT Condition: M XX Chop: Nter=0; Cter=0; Size: 11-31; Related: None; Repeats: 1; Topology: Undefined; Example: P02975; Scope: Bacteria Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01071; DC Domain; TR PROSITE; PS51735; VP35_IID; 1; level=0 XX Names: Filoviruses VP35 interferon inhibitory domain profile VP35 IID domain Function: VP35 contains an N-terminal coiled-coil domain required for its oligomerization and a C-terminal interferon (IFN) inhibitory domain (IID). The VP35 IID can bind dsRNA and VP35-mediated IFN antagonism correlates with dsRNA-binding activity. XX CC -!- SIMILARITY: Belongs to the filoviridae polymerase cofactor VP35 family. XX FT From: PS51735 FT DOMAIN from..to FT /note="VP35 IID #" XX Chop: Nter=0; Cter=0; Size: 116-136; Related: None; Repeats: 1; Topology: Undefined; Example: Q6UY68; Scope: Viruses; Filoviridae Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01072; DC Domain; TR PROSITE; PS51736; RECOMBINASES_3; 1; level=0 XX Names: Resolvase/invertase-type recombinase catalytic domain Function: The serine recombinases or resolvase/invertase family groups enzymes which share the following structural characteristics: an N-terminal catalytic and dimerization domain that contains a conserved serine residue involved in the transient covalent attachment to DNA, and a C-terminal helix-turn-helix DNA-binding domain XX case DR PROSITE; PS00397; RECOMBINASES_1; 1; trigger=no end case DR PROSITE; PS00398; RECOMBINASES_2; 1; trigger=no XX case GO GO:0000150; F:DNA strand exchange activity GO GO:0015074; P:DNA integration XX KW DNA integration KW DNA recombination end case XX FT From: PS51736 FT DOMAIN from..to FT /note="Resolvase/invertase-type recombinase catalytic #" FT ACT_SITE 9 FT /note="O-(5'-phospho-DNA)-serine intermediate" FT Condition: S XX Chop: Nter=0; Cter=0; Size: 46-171; Related: None; Repeats: 1; Topology: Undefined; Example: P19241; Scope: Bacteria Viruses Archaea; Methanocaldococcus Comments: None; XX # Revision 1.7 2021/06/03 // AC PRU01073; DC Domain; TR PROSITE; PS51737; RECOMBINASE_DNA_BIND; 1; level=0 XX Names: DNA-binding recombinase domain Function: The large serine recombinases (LSRs) are DNA-rearranging enzymes that are members of the serine recombinase or resolvase/invertase superfamily. The LSRs are composed of three primary structural domains: an amino-terminal catalytic domain, a DNA-binding "recombinase" domain, and a DNA-binding zinc ribbon domain. XX XX GO GO:0003677; F:DNA binding GO GO:0000150; F:DNA strand exchange activity XX KW DNA-binding KW DNA recombination XX FT From: PS51737 FT DNA_BIND from..to FT /note="Recombinase #" XX Chop: Nter=0; Cter=0; Size: 72-152; Related: None; Repeats: 1; Topology: Undefined; Example: P77698; Scope: Bacteria Viruses; unclassified Lambdavirus Comments: None; XX # Revision 1.5 2021/06/03 // AC PRU01074; DC Domain; TR PROSITE; PS51738; PEPTIDASE_C21; 1; level=0 XX Names: Peptidase family C21 domain Function: The peptidase family C21 domain is a papain-like proteinase with catalytic cysteine and histidine residues. XX XX case GO GO:0004197; F:cysteine-type endopeptidase activity GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51738 FT DOMAIN from..to FT /note="Peptidase C21 #" FT ACT_SITE 54 FT /note="For protease activity" FT Group: 1; Condition: C FT ACT_SITE 140 FT /note="For protease activity" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 140-166; Related: None; Repeats: 1; Topology: Undefined; Example: P28477; Scope: Viruses; Tymoviridae Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01076; DC Domain; TR PROSITE; PS51740; SPOVT_ABRB; 1; level=0 XX Names: SpoVT-AbrB domain Function: The SpoVT-AbrB domain is a DNA-binding domain. XX XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS51740 FT DOMAIN from..to FT /note="SpoVT-AbrB #" XX Chop: Nter=0; Cter=0; Size: 33-73; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q7NPZ0; Scope: Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01077; DC Domain; TR PROSITE; PS51741; F_BAR; 1; level=0 XX Names: F-BAR domain Function: The F-BAR domain plays a role in dimerization and membrane phospholipid binding. XX XX KW Coiled coil XX FT From: PS51741 FT DOMAIN from..to FT /note="F-BAR #" XX Chop: Nter=0; Cter=0; Size: 65-450; Related: None; Repeats: 1; Topology: Undefined; Example: Q6WKZ7; Scope: Eukaryota Viruses; Orthoretrovirinae Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01078; DC Domain; TR PROSITE; PS51742; PPC; 1; level=0 XX Names: PPC domain Function: The Plants and Prokaryotes Conserved (PPC) domain contains a hydrophobic region in the C terminal, and in the case of plants, is often found in several proteins with the AT-hook motif. XX XX FT From: PS51742 FT DOMAIN from..to FT /note="PPC #" XX Chop: Nter=0; Cter=0; Size: 122-159; Related: None; Repeats: 1; Topology: Undefined; Example: Q2JVA4; Scope: Bacteria; Synechococcus Eukaryota; Arabidopsis Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01079; DC Domain; TR PROSITE; PS51743; ALPHAVIRUS_MT; 1; level=0 XX Names: Alphavirus-like methyltransferase (MT) domain Function: The alphavirus-like MT domain is involved in methylation of the cap during viral RNA maturation. XX GO GO:0008174; F:mRNA methyltransferase activity XX FT From: PS51743 FT DOMAIN from..to FT /note="Alphavirus-like MT #" XX Chop: Nter=0; Cter=0; Size: 152-261; Related: None; Repeats: 1; Topology: Undefined; Example: P28931; Scope: Viruses; Riboviria Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01080; DC Domain; TR PROSITE; PS51744; HC_PRO_CPD; 1; level=0 XX Names: Helper-component proteinase (HC-Pro) cysteine protease (CPD) domain Peptidase C6 domain Function: The HC-Pro CPD domain has a protease activity that autocatalytically cleaves a Gly-Gly dipeptide at its own C terminus to release HC-Pro from the rest of the viral polyprotein. XX case and DE Contains: DE RecName: Full=Helper component proteinase; DE Short=HC-pro; DE EC=3.4.22.45; XX CC -!- FUNCTION: Helper component proteinase: Cysteine protease that cleaves a CC Gly-Gly dipeptide at its own C-terminus. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in CC the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the CC potyviral polyprotein.; EC=3.4.22.45; end case XX case and GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease end case XX FT From: PS51744 FT DOMAIN from..to FT /note="Peptidase C6 #" FT ACT_SITE 9 FT /note="For helper component proteinase activity" FT Group: 1; Condition: C FT ACT_SITE 81 FT /note="For helper component proteinase activity" FT Group: 1; Condition: H case FT SITE 122..122+1 FT /note="Cleavage; by autolysis" FT Group: 2 end case XX Chop: Nter=0; Cter=0; Size: 110-133; Related: None; Repeats: 1; Topology: Undefined; Example: P0CJ95; Scope: Viruses; Potyviridae Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01081; DC Domain; TR PROSITE; PS51745; PB1; 1; level=0 XX Names: PB1 domain Function: It functions as a protein binding module through PB1-mediated heterodimerization or homo-oligomerization. XX XX FT From: PS51745 FT DOMAIN from..to FT /note="PB1 #" XX Chop: Nter=0; Cter=0; Size: 64-128; Related: None; Repeats: 1; Topology: Undefined; Example: Q258Y5; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01082; DC Domain; TR PROSITE; PS51746; PPM_2; 1; level=0 XX Names: PPM-type phosphatase domain Function: The 300-residue protein phosphatase Mg(2+)- or Mn(2+)-dependent (PPM)-type phosphatase domain that catalyzes the dephosphorylation of phosphoserine- and phosphothreonine-containing protein. XX DE + RecName: EC=3.1.3.16; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 2 magnesium or manganese ions per subunit XX DR PROSITE; PS01032; PPM_1; 1; trigger=no XX GO GO:0046872; F:metal ion binding XX KW Hydrolase KW Protein phosphatase KW Metal-binding XX FT From: PS51746 FT DOMAIN from..to FT /note="PPM-type phosphatase #" XX Chop: Nter=0; Cter=0; Size: 96-574; Related: None; Repeats: 1; Topology: Undefined; Example: Q7XR06; Scope: Eukaryota Bacteria Viruses; Mimivirus Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01083; DC Domain; TR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1; level=0 XX Names: Cytidine and deoxycytidylate deaminases domain Function: Fill in XX XX DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1-2; trigger=no XX case or GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case case KW Hydrolase end case XX FT From: PS51747 FT DOMAIN from..to FT /note="CMP/dCMP-type deaminase #" case and not FT ACT_SITE 54 FT /note="Proton donor" FT Group: 1; Condition: E FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: C FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: C else case not FT BINDING 52 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: H FT BINDING 82 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C end case XX Chop: Nter=0; Cter=0; Size: 30-176; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q6P6J0; Scope: Eukaryota Bacteria Archaea; Methanopyrus Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01084; DC Domain; TR PROSITE; PS51748; HEXOKINASE_2; 1; level=0 XX Names: Hexokinase domain Function: Hexokinase (EC 2.7.1.1) [1,2] is an important glycolytic enzyme that catalyzes the phosphorylation of keto- and aldohexoses (e.g. glucose, mannose and fructose) using MgATP as the phosphoryl donor. XX DE + RecName: EC=2.7.1.-; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+); CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; CC -!- SIMILARITY: Belongs to the hexokinase family. XX DR PROSITE; PS00378; HEXOKINASE_1; 1-2; trigger=no XX GO GO:0005524; F:ATP binding GO GO:0006096; P:glycolytic process XX KW ATP-binding KW Glycolysis KW Kinase KW Nucleotide-binding KW Transferase XX FT From: PS51748 FT DOMAIN from..to FT /note="Hexokinase #" FT REGION 56..191 FT /note="Hexokinase small subdomain #" FT REGION 192..435 FT /note="Hexokinase large subdomain #" XX Chop: Nter=0; Cter=0; Size: 414-497; Related: None; Repeats: 1-2; Topology: Undefined; Example: P27881; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01085; DC Domain; TR PROSITE; PS51749; HNH_CAS9; 1; level=0 XX Names: Cas9-type HNH domain Function: All known Cas9 enzymes contain an HNH domain that cleaves the DNA strand complementary to the guide RNA sequence (target strand). XX XX GO GO:0003677; F:DNA binding GO GO:0003723; F:RNA binding GO GO:0004519; F:endonuclease activity XX KW DNA-binding KW Endonuclease KW Hydrolase KW Nuclease XX FT From: PS51749 FT DOMAIN from..to FT /note="HNH Cas9-type #" XX Chop: Nter=0; Cter=0; Size: 139-182; Related: None; Repeats: 1; Topology: Undefined; Example: Q03JI6; Scope: Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01086; DC Domain; TR PROSITE; PS51750; BRO_N; 1; level=0 XX Names: Bro-N domain Function: The Bro-N domain appears to define a distinct superfamily of widespread viral DNA-binding domains. XX XX FT From: PS51750 FT DOMAIN from..to FT /note="Bro-N #" XX Chop: Nter=0; Cter=0; Size: 96-145; Related: None; Repeats: 1; Topology: Undefined; Example: Q5UP77; Scope: Viruses Bacteria; Haemophilus Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01087; DC Domain; TR PROSITE; PS51751; EXPERA; 1; level=0 XX Names: EXPERA domain Function: The EXPERA domain contains four transmembrane regions and is likely to possess a sterol isomerase catalytic activity. XX XX GO GO:0016020; C:membrane XX KW Membrane KW Transmembrane KW Transmembrane helix XX FT From: PS51751 FT DOMAIN from..to FT /note="EXPERA #" XX Chop: Nter=0; Cter=0; Size: 116-174; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q8R1J1; Scope: Eukaryota Comments: None; XX # Revision 1.5 2022/09/30 // AC PRU01088; DC Domain; TR PROSITE; PS51752; JACALIN_LECTIN; 1; level=0 XX Names: Jacalin-type lectin domain Function: Based on the known sugar specificity, the jacalin-type lectin domain can be broadly divided into two classes: (1) the galactose-specific domains and (2) the mannose/glucose-specific domains. XX CC -!- SIMILARITY: Belongs to the jacalin lectin family. XX GO GO:0030246; F:carbohydrate binding XX KW Lectin XX FT From: PS51752 FT DOMAIN from..to FT /note="Jacalin-type lectin #" XX Chop: Nter=0; Cter=0; Size: 17-193; Related: None; Repeats: 1-5; Topology: Undefined; Example: Q8GWI7; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01089; DC Domain; TR PROSITE; PS51753; HBM; 1; level=0 XX Names: HBM domain Function: The helical bimodular (HBM) domain is a small molecule binding domain of around 250 amino acids. XX XX FT From: PS51753 FT DOMAIN from..to FT /note="HBM #" XX Chop: Nter=0; Cter=0; Size: 233-253; Related: None; Repeats: 1; Topology: Undefined; Example: Q88E10; Scope: Bacteria; Pseudomonas Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01090; DC Domain; TR PROSITE; PS51754; OVATE; 1; level=0 XX Names: OVATE domain Function: OVATE family proteins (OFPs) are a plant-specific family of regulatory proteins that function as transcriptional repressors and regulate multiple aspects of plant growth and development. They are characterized by a conserved C-terminal OVATE domain of approximately 70 amino acids. XX XX GO GO:0006351; P:DNA-templated transcription GO GO:0045892; P:negative regulation of DNA-templated transcription XX KW Repressor KW Transcription KW Transcription regulation XX FT From: PS51754 FT DOMAIN from..to FT /note="OVATE #" XX Chop: Nter=0; Cter=0; Size: 50-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q9SJ45; Scope: Eukaryota; Arabidopsis Comments: None; XX # Revision 1.4 2022/06/27 // AC PRU01091; DC Domain; TR PROSITE; PS51755; OMPR_PHOB; 1; level=0 XX Names: OmpR/PhoB-type DNA-binding domain Function: The C-terminal effector domain of the OmpR/PhoB subfamily response regulators binds DNA. XX XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS51755 FT DNA_BIND from..to FT /note="OmpR/PhoB-type #" XX Chop: Nter=0; Cter=0; Size: 55-115; Related: None; Repeats: 1; Topology: Undefined; Example: B8H358; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01092; DC Domain; TR PROSITE; PS51756; LXG; 1; level=0 XX Names: LXG domain Function: The LXG is predicted to be a secretion signal for the type VII secretion system of Mycobacterium and Bacillus species. XX XX FT From: PS51756 FT DOMAIN from..to FT /note="LXG #" XX Chop: Nter=0; Cter=0; Size: 207-245; Related: None; Repeats: 1; Topology: Undefined; Example: Q813X6; Scope: Bacteria; Bacillus Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01093; DC Domain; TR PROSITE; PS51757; TH1; 1; level=0 XX Names: Class I myosin tail homology (TH1) domain Function: The TH1 domain is an extended PH domain capable of binding to lipids. XX XX FT From: PS51757 FT DOMAIN from..to FT /note="TH1 #" XX Chop: Nter=0; Cter=0; Size: 165-212; Related: None; Repeats: 1; Topology: Undefined; Example: A1C4A5; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01094; DC Domain; TR PROSITE; PS51758; LETM1_RBD; 1; level=0 XX Names: Letm1 ribosome-binding (RBD) domain Function: The Letm1 ribosome-binding domain (RBD) is necessary and sufficient for interaction with mitochondrial ribosomes. XX XX KW Mitochondrion XX FT From: PS51758 FT DOMAIN from..to FT /note="Letm1 RBD #" XX Chop: Nter=0; Cter=0; Size: 165-312; Related: None; Repeats: 1; Topology: Undefined; Example: Q7TNU7; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01095; DC Domain; TR PROSITE; PS51759; CBM15; 1; level=0 XX Names: Carbohydrate-binding module 15 (CBM15) domain Function: The family 15 CBM (CBM15) binds both soluble xylan and xylooligosaccharides. XX case KW Disulfide bond end case XX FT From: PS51759 FT DOMAIN from..to FT /note="CBM15 #" FT BINDING 16 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1; Condition: N FT BINDING 78 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1; Condition: Q FT BINDING 124 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT Group: 1; Condition: Q FT DISULFID 90..107 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 142-162; Related: None; Repeats: 1; Topology: Undefined; Example: Q59675; Scope: Bacteria; Cellvibrio Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01096; DC Domain; TR PROSITE; PS51760; GH10_2; 1; level=0 XX Names: Glycosyl hydrolases family 10 (GH10) domain Function: All family 10 xylanases hydrolyze the glycosidic bond in a double- displacement 'retaining' mechanism using two catalytic acidic residues, where one residue acts a nucleophile (base) and the other acts as a general acid/base. XX case DE + RecName: EC=3.2.1.8; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; CC -!- PATHWAY: Glycan degradation; xylan degradation. end case CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 10 (cellulase F) family. XX case DR PROSITE; PS00591; GH10_1; 1; trigger=no XX GO GO:0045493; P:xylan catabolic process GO GO:0031176; F:endo-1,4-beta-xylanase activity XX KW Carbohydrate metabolism KW Hydrolase KW Polysaccharide degradation KW Glycosidase KW Xylan degradation end case XX FT From: PS51760 FT DOMAIN from..to FT /note="GH10 #" FT ACT_SITE 137 FT /note="Proton donor" FT Group: 1; Condition: E FT ACT_SITE 242 FT /note="Nucleophile" FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 260-375; Related: None; Repeats: 1; Topology: Undefined; Example: O60206; Scope: Eukaryota; Fungi Bacteria Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01097; DC Domain; TR PROSITE; PS51761; GH11_3; 1; level=0 XX Names: Glycosyl hydrolases family 11 (GH11) domain Function: Family 11 is monospecific, only consisting of xylanases. XX case DE + RecName: EC=3.2.1.8; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; CC -!- PATHWAY: Glycan degradation; xylan degradation. end case CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 11 (cellulase G) family. case XX DR PROSITE; PS00776; GH11_1; 1; trigger=no DR PROSITE; PS00777; GH11_2; 1; trigger=no XX GO GO:0045493; P:xylan catabolic process GO GO:0031176; F:endo-1,4-beta-xylanase activity XX KW Carbohydrate metabolism KW Glycosidase KW Hydrolase KW Polysaccharide degradation KW Xylan degradation end case XX FT From: PS51761 FT DOMAIN from..to FT /note="GH11 #" FT ACT_SITE 87 FT /note="Nucleophile" FT Group: 1; Condition: E FT ACT_SITE 178 FT /note="Proton donor" FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 177-221; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q8J0K5; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01098; DC Domain; TR PROSITE; PS51762; GH16_2; 1; level=0 XX Names: Glycosyl hydrolases family 16 (GH16) domain Function: The glycosyl hydrolases family 16 (GH16) contains functionally heterogeneous members, including beta-agarases, endo-1,3-beta-glucanases (laminarinases), endo-beta-1,3-1,4-glucanases (lichenases), kappa- carrageenases, endo-beta-galactosidases and xyloglucan endotransferases. XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. case XX DR PROSITE; PS01034; GH16_1; 1; trigger=no XX KW Hydrolase KW Glycosidase end case XX FT From: PS51762 FT DOMAIN from..to FT /note="GH16 #" FT ACT_SITE 100 FT /note="Nucleophile" FT Group: 1; Condition: E FT ACT_SITE 105 FT /note="Proton donor" FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 168-406; Related: None; Repeats: 1; Topology: Undefined; Example: P93046; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01099; DC Domain; TR PROSITE; PS51763; CBM10; 1; level=0 XX Names: CBM10 (carbohydrate binding type-10) domain Function: CBM10s are small molecules, comprising only ca. 45 residues, that bind to insoluble forms of cellulose. XX case KW Disulfide bond end case XX FT From: PS51763 FT DOMAIN from..to FT /note="CBM10 #" FT DISULFID 12..34 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 20-51; Related: None; Repeats: 1-3; Topology: Undefined; Example: B8YG19; Scope: Eukaryota; Neocallimastigaceae Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01100; DC Domain; TR PROSITE; PS51764; GH26; 1; level=0 XX Names: Glycosyl hydrolases family 26 (GH26) domain Function: GH family 26 consists mainly of endo-beta-1,4-mannanases (mannanases), although some members of this family display beta-1,3-xylanase activity. XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 26 family. XX case KW Glycosidase KW Hydrolase end case XX FT From: PS51764 FT DOMAIN from..to FT /note="GH26 #" FT ACT_SITE 148 FT /note="Proton donor" FT Group: 1; Condition: E FT ACT_SITE 255 FT /note="Nucleophile" FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 266-364; Related: None; Repeats: 1; Topology: Undefined; Example: P55297; Scope: Bacteria Eukaryota; Fungi Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01101; DC Domain; TR PROSITE; PS51765; ZF_RAG1; 1; level=0 XX Names: Zinc finger RAG1-type Function: The dimerization domain of RAG1 proteins consists of a zinc C3HC4 RING finger and a C2H2 zinc RAG1-type finger. XX XX GO GO:0042803; F:protein homodimerization activity case and and and GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51765 case and and and FT ZN_FING from..to FT /note="RAG1-type #" else case and and and FT ZN_FING from..to FT /note="RAG1-type #; atypical" else FT ZN_FING from..to FT /note="RAG1-type #; degenerate" end case FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Condition: [CH] FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Condition: [CH] FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 20-40; Related: None; Repeats: 1; Topology: Undefined; Example: Q91829; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01102; DC Domain; TR PROSITE; PS51766; DOCKERIN; 1; level=0 XX Names: Dockerin domain Function: The dockerin domains consist of about 70 amino acid residues and contain two duplicated segments, each of about 22 amino acid residues. It binds tenaciously to the cohesin modules of the scaffoldin subunit of the cellulosome. XX XX case KW Calcium KW Metal-binding end case XX FT From: PS51766 FT DOMAIN from..to FT /note="Dockerin #" FT BINDING 7 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 9 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: [NVT] FT BINDING 11 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 12 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1 FT BINDING 13 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1 FT BINDING 18 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 41 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 1; Condition: D FT BINDING 41 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 1; Condition: D FT BINDING 42 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 1 FT BINDING 43 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 1; Condition: [NDY] FT BINDING 45 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 1; Condition: [DSN] FT BINDING 47 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 1 FT BINDING 47 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 1 FT BINDING 52 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 1; Condition: [DT] FT BINDING 52 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#3" FT Group: 1; Condition: [DT] XX Chop: Nter=0; Cter=0; Size: 46-90; Related: None; Repeats: 1; Topology: Undefined; Example: A3DH67; Scope: Bacteria; Eubacteriales Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01103; DC Domain; TR PROSITE; PS51767; PEPTIDASE_A1; 1; level=0 XX Names: Peptidase family A1 domain Function: Eukaryotic aspartyl proteases (APs) form peptidase family A1 of clan AA. APs use an Asp dyad to hydrolyze peptide bonds. XX CC -!- SIMILARITY: Belongs to the peptidase A1 family. XX DR PROSITE; PS00141; ASP_PROTEASE; 2; trigger=no XX case GO GO:0004190; F:aspartic-type endopeptidase activity XX KW Aspartyl protease KW Hydrolase KW Protease end case case KW Disulfide bond end case XX FT From: PS51767 FT DOMAIN from..to FT /note="Peptidase A1 #" FT ACT_SITE 19 FT Group: 1; Condition: D FT ACT_SITE 204 FT Group: 1; Condition: D FT DISULFID 239..274 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 211-432; Related: None; Repeats: 1; Topology: Undefined; Example: P32951; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01106; DC Domain; TR PROSITE; PS51770; HOTDOG_ACOT; 1; level=0 XX Names: HotDog acyl-CoA thioesterase (ACOT)-type domain Function: The largest HotDog domain subfamily represents over a hundred acyl- CoA thioesterases (ACOTs) that are widespread throughout the prokaryotic kingdom, with members also found in eukaryotes. XX KW Hydrolase XX FT From: PS51770 FT DOMAIN from..to FT /note="HotDog ACOT-type #" XX Chop: Nter=0; Cter=0; Size: 80-136; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q91V12; Scope: Bacteria Eukaryota; Eutheria Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01107; DC Domain; TR PROSITE; PS51771; CGT_MARTX_CPD; 1; level=0 XX Names: CGT/MARTX cysteine protease (CPD) domain Function: The clostridial glucosylating toxins (CGTs) produced by Gram- positive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria carry an embedded cysteine protease domain (CPD) that is regulated by a unique allosteric activation mechanism. The CGT/MARTX CPD catalytic dyad is composed of one His and one Cys residue. XX XX case XX KW Hydrolase KW Protease KW Thiol protease KW Toxin end case XX FT From: PS51771 FT DOMAIN from..to FT /note="Peptidase C80 #" FT ACT_SITE 72 FT Group: 1; Condition: H FT ACT_SITE 116 FT /note="Nucleophile" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 198-218; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KS12; Scope: Bacteria; Peptoclostridium Comments: None; XX # Revision 1.6 2021/06/03 // AC PRU01108; DC Domain; TR PROSITE; PS51772; ACD; 1; level=0 XX Names: Actin cross-linking (ACD) domain Function: ACDs are enzyme ligases that catalyze the formation of an irreversible iso-peptide bond on two actin molecules in an ATP- and Mg/ Mn(2+)-dependent manner. XX XX case KW ATP-binding KW Nucleotide-binding end case case KW Magnesium KW Metal-binding end case case and KW Ligase end case XX FT From: PS51772 FT DOMAIN from..to FT /note="ACD #" FT BINDING 12..16 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: S-I-G-[IT]-E FT BINDING 16 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for actin cross-linking FT activity" FT Group: 2; Condition: E FT BINDING 16 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for actin cross-linking FT activity" FT Group: 2; Condition: E FT BINDING 78 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /ligand_note="catalytic; for actin cross-linking FT activity" FT Group: 2; Condition: E FT BINDING 162 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for actin cross-linking FT activity" FT Group: 2; Condition: Q FT BINDING 339 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic; for actin cross-linking FT activity" FT Group: 2; Condition: E FT BINDING 81 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: [ST] FT BINDING 268 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Group: 1; Condition: R XX Chop: Nter=0; Cter=0; Size: 425-446; Related: None; Repeats: 1; Topology: Undefined; Example: A0A0H3AIG7; Scope: Bacteria; Vibrio Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01109; DC Domain; TR PROSITE; PS51773; OCP_N; 1; level=0 XX Names: Orange carotenoid protein (OCP) N-terminal domain Function: The OCP C-terminal is suggested to dynamically regulate the photoprotective activity on otherwise constitutively active carotenoid binding N-terminal domain. XX CC -!- SIMILARITY: Belongs to the orange carotenoid-binding protein family. XX GO GO:0016037; P:light absorption GO GO:0030089; C:phycobilisome XX KW Chromophore KW Membrane KW Phycobilisome KW Thylakoid XX FT From: PS51773 FT DOMAIN from..to FT /note="OCP N-terminal #" XX Chop: Nter=0; Cter=0; Size: 141-162; Related: None; Repeats: 1; Topology: Undefined; Example: Q8YMJ2; Scope: Bacteria; Cyanobacteriota Comments: None; XX # Revision 1.5 2023/02/17 // AC PRU01110; DC Domain; TR PROSITE; PS51774; NAB; 1; level=0 XX Names: Networked (NET) actin-binding (NAB) domain Function: The NET actin-binding (NAB) domain represents an actin-binding motif unique to plants. XX XX FT From: PS51774 FT DOMAIN from..to FT /note="NAB #" XX Chop: Nter=0; Cter=0; Size: 67-96; Related: None; Repeats: 1; Topology: Undefined; Example: Q4PSJ7; Scope: Eukaryota; Pentapetalae Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01111; DC Domain; TR PROSITE; PS51775; GTD_BINDING; 1; level=0 XX Names: GTD-binding domain Function: The GTD-binding domain is a plant-specific protein-protein interaction domain that binds to the globular tail domain (GTD) of myosin motor proteins. XX XX FT From: PS51775 FT DOMAIN from..to FT /note="GTD-binding #" XX Chop: Nter=0; Cter=0; Size: 89-109; Related: None; Repeats: 1; Topology: Undefined; Example: F4HVS6; Scope: Eukaryota; Viridiplantae Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01112; DC Domain; TR PROSITE; PS51776; RH1; 1; level=0 XX Names: RH1 domain Function: The RH1 domain binds to the myosin Va globular tail domain (MyoVa- GTD) in mainly hydrophobic interactions. XX XX FT From: PS51776 FT DOMAIN from..to FT /note="RH1 #" XX Chop: Nter=0; Cter=0; Size: 73-105; Related: None; Repeats: 1; Topology: Undefined; Example: A0PJP4; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01113; DC Domain; TR PROSITE; PS51777; RH2; 1; level=0 XX Names: RH2 domain Function: The RH2 (RILP homology 2) domain is a Rab-binding domain found in animal proteins. XX XX FT From: PS51777 FT DOMAIN from..to FT /note="RH2 #" XX Chop: Nter=0; Cter=0; Size: 56-130; Related: None; Repeats: 1; Topology: Undefined; Example: A0PJP4; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01114; DC Domain; TR PROSITE; PS51778; VAST; 1; level=0 XX Names: VASt domain Function: The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol. XX XX FT From: PS51778 FT DOMAIN from..to FT /note="VASt #" XX Chop: Nter=0; Cter=0; Size: 153-216; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q08001; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01115; DC Domain; TR PROSITE; PS51779; POTRA; 1; level=0 XX Names: POTRA domain Function: The POTRA domains are hypothesized to mediate protein-protein interactions, nucleate beta-strands formation in nascent outer membrane proteins (OMPs) and have chaperone-like activity. XX XX FT From: PS51779 FT DOMAIN from..to FT /note="POTRA #" XX Chop: Nter=0; Cter=0; Size: 58-99; Related: None; Repeats: 1-5; Topology: Undefined; Example: A8AW16; Scope: Bacteria Eukaryota; Oryza Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01116; DC Domain; TR PROSITE; PS51780; GW; 1; level=0 XX Names: GW domain Cell wall targeting (CWT) signal Function: GW domains may constitute a motif for cell-surface anchoring in Listeria and other Gram-positive bacteria. XX XX FT From: PS51780 FT DOMAIN from..to FT /note="GW #" XX Chop: Nter=0; Cter=0; Size: 64-89; Related: None; Repeats: 1-10; Topology: Undefined; Example: Q5HQB9; Scope: Bacteria; Bacillales Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01117; DC Domain; TR PROSITE; PS51781; SH3B; 1; level=0 XX Names: SH3b domain Function: The SH3b domain might have two possible functions: (1) promoting survival of a pathogen within the invaded cell by modulating pathways controlled by SH3 domains; or (2) promoting invasion by binding to receptors on eukaryotic cells. XX XX FT From: PS51781 FT DOMAIN from..to FT /note="SH3b #" XX Chop: Nter=0; Cter=0; Size: 51-87; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q2FG95; Scope: Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01118; DC Domain; TR PROSITE; PS51782; LYSM; 1; level=0 XX Names: LysM (lysin-like motif) domain Function: LysM modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidoglycan, an essential component of the bacterial cell wall. XX XX FT From: PS51782 FT DOMAIN from..to FT /note="LysM #" XX Chop: Nter=0; Cter=0; Size: 34-69; Related: None; Repeats: 1-5; Topology: Undefined; Example: P39700; Scope: Bacteria Eukaryota Viruses; Salasvirus Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01119; DC Domain; TR PROSITE; PS51783; PH_BEACH; 1; level=0 XX Names: BEACH-type PH domain Function: The PH domain in the BEACH proteins cannot bind phospholipids. XX XX FT From: PS51783 FT DOMAIN from..to FT /note="BEACH-type PH #" XX Chop: Nter=0; Cter=0; Size: 86-187; Related: None; Repeats: 1; Topology: Undefined; Example: E7FAW3; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01120; DC Domain; TR PROSITE; PS51784; EXOI_SH3; 1; level=0 XX Names: Exonuclease I (ExoI) SH3-like domain Function: Exonuclease I (ExoI) consists of three domains: an N-terminal nuclease domain with homology to the proofreading domain of E. coli DNA polymereae I and other DnaQ superfamily enzymes, a central domain with a portion that resembles an SH3 domain fold and a C-terminal alpha-helical domain. XX XX FT From: PS51784 FT DOMAIN from..to FT /note="ExoI SH3-like #" XX Chop: Nter=0; Cter=0; Size: 139-166; Related: None; Repeats: 1; Topology: Undefined; Example: Q89A43; Scope: Bacteria; Gammaproteobacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01121; DC Domain; TR PROSITE; PS51785; EXOI_C; 1; level=0 XX XX Names: Exonuclease I (ExoI) SH3-like domain Function: Exonuclease I (ExoI) consists of three domains: an N-terminal nuclease domain with homology to the proofreading domain of E. coli DNA polymereae I and other DnaQ superfamily enzymes, a central domain with a portion that resembles an SH3 domain fold and a C-terminal alpha-helical domain. XX XX FT From: PS51785 FT DOMAIN from..to FT /note="ExoI C-terminal #" XX Chop: Nter=0; Cter=0; Size: 54-128; Related: None; Repeats: 1; Topology: Undefined; Example: Q89A43; Scope: Bacteria; Gammaproteobacteria Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01122; DC Domain; TR PROSITE; PS51786; LON_PROTEOLYTIC; 1; level=0 XX Names: Lon proteolytic domain Function: The Lon proteolytic domain forms peptidase family S16 of clan SJ. It has a serine-lysine catalytic dyad in which a lysine assists the catalytic serine in proteolytic cleavage. XX case and DE + RecName: EC=3.4.21.53; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; CC -!- SIMILARITY: Belongs to the peptidase S16 family. else case DE + RecName: EC=3.4.21.-; XX CC -!- SIMILARITY: Belongs to the peptidase S16 family. end case XX case GO GO:0004252; F:serine-type endopeptidase activity GO GO:0004176; F:ATP-dependent peptidase activity XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51786 FT DOMAIN from..to FT /note="Lon proteolytic #" FT ACT_SITE 91 FT Group: 1; Condition: S FT ACT_SITE 134 FT Group: 1; Condition: K XX Chop: Nter=0; Cter=0; Size: 169-262; Related: None; Repeats: 1; Topology: Undefined; Example: B7FSL4; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Viruses; Mimivirus Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01123; DC Domain; TR PROSITE; PS51787; LON_N; 1; level=0 XX Names: Lon N-terminal domain Function: The Lon N-terminal domain is thought to be involved in substrate binding and might represent a general protein and polypeptide interaction domain. XX XX FT From: PS51787 FT DOMAIN from..to FT /note="Lon N-terminal #" XX Chop: Nter=0; Cter=0; Size: 178-391; Related: None; Repeats: 1; Topology: Undefined; Example: B7FSL4; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01124; DC Domain; TR PROSITE; PS51788; CULT; 1; level=0 XX Names: CULT (for Cereblon domain of Unknown activity, binding cellular Ligands and Thalidomide) domain Function: The thalidomide-binding region of cereblon is a conserved domain, CULT, carrying several invariant cysteine and tryptophan residues. The nature of the binding pocket, an aromatic cage of three tryptophan residues, suggests a role in the recognition of cationic ligands. XX XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS51788 FT DOMAIN from..to FT /note="CULT #" FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 76 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 99-120; Related: None; Repeats: 1; Topology: Undefined; Example: Q56AP7; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU01125; DC Domain; TR PROSITE; PS51789; RLR_CTR; 1; level=0 XX Names: RIG-I-like receptor (RLR) C-terminal regulatory (CTR) domain Function: The RLR CTR domain helps recognize non-self RNAs within the cellular environment. XX XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS51789 FT DOMAIN from..to FT /note="RLR CTR #" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 118-146; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BYX4; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01126; DC Domain; TR PROSITE; PS51790; MSRB; 1; level=0 XX Names: Methionine-R-sulfoxide reductase (MsrB) domain Function: MsrB catalyzes the reduction of methionine-R-sulfoxide back to methionine. XX case DE + RecName: EC=1.8.4.-; end case XX CC -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family. XX case GO GO:0008270; F:zinc ion binding end case case GO GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity GO GO:0006979; P:response to oxidative stress XX KW Oxidoreductase end case case KW Metal-binding KW Zinc end case XX FT From: PS51790 FT DOMAIN from..to FT /note="MsrB #" FT ACT_SITE 112 FT /note="Nucleophile" FT Tag: Cat; Condition: [CU] FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 89 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 94-145; Related: None; Repeats: 1; Topology: Undefined; Example: A8A0X0; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01127; DC Domain; TR PROSITE; PS51791; HSAC2; 1; level=0 XX Names: hSac2 domain Function: The hSac2 domain plays a role in Sac2 dimerization and intracellular localization. XX XX FT From: PS51791 FT DOMAIN from..to FT /note="hSac2 #" XX Chop: Nter=0; Cter=0; Size: 158-198; Related: None; Repeats: 1; Topology: Undefined; Example: Q9DBS2; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01128; DC Domain; TR PROSITE; PS51792; YIPPEE; 1; level=0 XX Names: Yippee domain Function: YPEL proteins contain a Yippee domain, which is a putative zinc- finger-like, metal-binding domain. XX CC -!- SIMILARITY: Belongs to the yippee family. XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS51792 FT DOMAIN from..to FT /note="Yippee #" FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 88-108; Related: None; Repeats: 1; Topology: Undefined; Example: Q65Z56; Scope: Eukaryota Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01129; DC Domain; TR PROSITE; PS51793; MIS18; 1; level=0 XX Names: Mis18 domain Function: The oligomerization of Mis18, mediated by its conserved N-terminal globular domain, is crucial for its centromere localization and function. XX CC -!- SIMILARITY: Belongs to the mis18 family. XX GO GO:0000775; C:chromosome, centromeric region case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Centromere KW Chromosome XX FT From: PS51793 FT DOMAIN from..to FT /note="Mis18 #" FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 63 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 66 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 87-110; Related: None; Repeats: 1; Topology: Undefined; Example: A5D7N9; Scope: Eukaryota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01130; DC Domain; TR PROSITE; PS51794; DAC; 1; level=0 XX Names: Diadenylate cyclase (DAC) domain Function: The 120-amino acid-long diadenylate cyclase (DAC) domain converts two ATP or ADP molecules into one c-di-AMP molecule. XX XX FT From: PS51794 FT DOMAIN from..to FT /note="DAC #" XX Chop: Nter=0; Cter=0; Size: 123-171; Related: None; Repeats: 1; Topology: Undefined; Example: Q81J64; Scope: Bacteria Archaea; Methanocaldococcus Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01131; DC Domain; TR PROSITE; PS51795; ZF_FLZ; 1; level=0 XX Names: Zinc finger FLZ-type Function: The FLZ-type zinc finger is likely to be involved in protein-protein interaction. XX XX case and and and KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51795 FT ZN_FING from..to FT /note="FLZ-type #" XX Chop: Nter=0; Cter=0; Size: 30-60; Related: None; Repeats: 1; Topology: Undefined; Example: Q8LGS1; Scope: Eukaryota; Viridiplantae Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01132; DC Domain; TR PROSITE; PS51796; MSS4; 1; level=0 XX Names: Mss4 domain Function: Although it was first proposed to function as a guanine exchange factor (GEF) for Rab GTPases, it was soon described as a quite inefficient GEF and was thus suggested to function rather as a chaperone, protecting nucleotide free Rabs from degradation, than as a GEF. XX CC -!- SIMILARITY: Belongs to the DSS4/MSS4 family. XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS51796 FT DOMAIN from..to FT /note="MSS4 #" FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 89 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 76-141; Related: None; Repeats: 1; Topology: Undefined; Example: Q9U1X4; Scope: Eukaryota Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01133; DC Domain; TR PROSITE; PS51797; TCTP_3; 1; level=0 XX Names: Translationally controlled tumor protein (TCTP) domain Function: The translationally controlled tumor proteins (TCTPs, such as p21, p23 and histamine releasing factor (HRF)) are a highly conserved and abundantly expressed family of eukaryotic proteins that are implicated in a variety of cellular functions, including microtubule stabilization, cell cycle, apoptosis, and cytokine release. XX CC -!- SIMILARITY: Belongs to the TCTP family. XX DR PROSITE; PS01002; TCTP_1; 1; trigger=no DR PROSITE; PS01003; TCTP_2; 1; trigger=no XX FT From: PS51797 FT DOMAIN from..to FT /note="TCTP #" XX Chop: Nter=0; Cter=0; Size: 10-204; Related: None; Repeats: 1; Topology: Undefined; Example: Q7RYV5; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01134; DC Domain; TR PROSITE; PS51144; ALPHA_CA_2; 1; level=0 XX Names: Alpha-carbonic anhydrase domain Function: Fill in XX case and DE + AltName: Full=Carbonic anhydrase; DE EC=4.2.1.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:17544; EC=4.2.1.1; end case XX case DR PROSITE; PS00162; ALPHA_CA_1; 1; trigger=no end case XX case and GO GO:0004089; F:carbonate dehydratase activity end case case or GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS51144 FT DOMAIN from..to FT /note="Alpha-carbonic anhydrase #" FT ACT_SITE 64 FT /note="Proton acceptor" FT Group: 1; Condition: H FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 3; Condition: H FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 3; Condition: H FT BINDING 93 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 3; Condition: H XX Chop: Nter=0; Cter=0; Size: 15-523; Related: None; Repeats: 1-2; Topology: Undefined; Example: P22748; Scope: Eukaryota Viruses; Orthopoxvirus Bacteria Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01135; DC Domain; TR PROSITE; PS51173; CBM2; 1; level=0 XX Names: CBM2 (Carbohydrate-binding type-2) domain Function: Structurally, cellulases and xylanases generally consist of a catalytic domain and a conserved region of ~100 amino acid residues, the carbohydrate-binding module 2 (CBM2). XX XX DR PROSITE; PS00561; CBM2_A; 0-1; trigger=no XX GO GO:0030247; F:polysaccharide binding XX FT From: PS51173 FT DOMAIN from..to FT /note="CBM2 #" XX Chop: Nter=0; Cter=0; Size: 80-122; Related: None; Repeats: 1-2; Topology: Undefined; Example: P9WLQ0; Scope: Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01136; DC Domain; TR PROSITE; PS50980; COA_CT_NTER; 1; level=0 XX Names: Coenzyme A (CoA) carboxyltransferase N-terminal domain Function: The N- and C-terminal domains of the carboxyltransferase share similar polypeptide backbone folds, with a central beta-beta-alpha superhelix. The CoA molecule is mostly associated with the N-terminal domain. In bacterial acetyl coenzyme A carboxylase the N and C domains are encoded by two different polypeptides. XX XX FT From: PS50980 FT DOMAIN from..to FT /note="CoA carboxyltransferase N-terminal #" XX Chop: Nter=0; Cter=0; Size: 129-288; Related: None; Repeats: 1; Topology: Undefined; Example: P0A9Q5; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01137; DC Domain; TR PROSITE; PS50989; COA_CT_CTER; 1; level=0 XX Names: Coenzyme A (CoA) carboxyltransferase C-terminal domain Function: The N- and C-terminal domains of the carboxyltransferase share similar polypeptide backbone folds, with a central beta-beta-alpha superhelix. In bacterial acetyl coenzyme A carboxylase the N and C domains are encoded by two different polypeptides. XX XX FT From: PS50989 FT DOMAIN from..to FT /note="CoA carboxyltransferase C-terminal #" XX Chop: Nter=0; Cter=0; Size: 231-405; Related: None; Repeats: 1; Topology: Undefined; Example: Q5WYB5; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01138; DC Domain; TR Metamotif; -; ]=[PS50980>| XX Names: CoA carboxyltransferase domain Function: The N- and C-terminal regions of the carboxyltransferase domain share similar polypeptide backbone folds, with a central beta-beta-alpha superhelix. The CoA molecule is mostly associated with the N subdomain. XX DR PROSITE; PS50989; COA_CT_CTER; 1; trigger=no DR PROSITE; PS50980; COA_CT_NTER; 1; trigger=no XX FT From: ]=[PS50980>| FT REGION from..to FT /note="Carboxyltransferase #" XX Chop: Nter=0; Cter=0; Size: 350-700; Related: None; Repeats: 1; Topology: Undefined; Example: A8L4H3; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01140; DC Domain; TR PROSITE; PS51799; ZF_C2H2_AKAP95; 1; level=0 XX Names: Zinc finger C2H2 AKAP95-type Function: AKAP95 harbours two zinc fingers, designated ZF1 and ZF2. ZF1 mediates the binding of AKAP95 to DNA. ZF2 is dispensable for chromatin binding; however it may substitute for ZF1 when the latter is rendered non- functional by mutation. XX CC -!- SIMILARITY: Belongs to the AKAP95 family. XX case and and and KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51799 case and and and FT ZN_FING from..to FT /note="C2H2 AKAP95-type #" else case and and and FT ZN_FING from..to FT /note="C2H2 AKAP95-type #; atypical" else FT ZN_FING from..to FT /note="C2H2 AKAP95-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 13-34; Related: None; Repeats: 2; Topology: Undefined; Example: O88291; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01141; DC Domain; TR PROSITE; PS51800; ZF_CHHC_U11_48K; 1; level=0 XX Names: Zinc finger CHHC U11-48K-type Function: The CHHC U11-48K-type zinc finger may function as a RNA recognition and binding module. XX XX case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51800 case and and and FT ZN_FING from..to FT /note="CHHC U11-48K-type #" else case and and and FT ZN_FING from..to FT /note="CHHC U11-48K-type #; atypical" else FT ZN_FING from..to FT /note="CHHC U11-48K-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 18-38; Related: None; Repeats: 2; Topology: Undefined; Example: Q4R8M9; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01142; DC Domain; TR PROSITE; PS51801; ZF_CCHC_NOA; 1; level=0 XX Names: Zinc finger CCHC NOA-type Function: The CCHC NOA (NEMO Optineurin ABIN2)-type zinc finger has been shown to function as an ubiquitin-binding domain. XX XX case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51801 case and and and FT ZN_FING from..to FT /note="CCHC NOA-type #" else case and and and FT ZN_FING from..to FT /note="CCHC NOA-type #; atypical" else FT ZN_FING from..to FT /note="CCHC NOA-type #; degenerate" end case FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 21-43; Related: None; Repeats: 1; Topology: Undefined; Example: Q95KA2; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01143; DC Domain; TR PROSITE; PS51802; ZF_CCHHC; 1; level=0 XX Names: Zinc finger CCHHC-type Function: The CCHHC-type zinc finger is able to bind specific double-stranded DNA sequences. XX XX case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51802 case and and and FT ZN_FING from..to FT /note="CCHHC-type #" else case and and and FT ZN_FING from..to FT /note="CCHHC-type #; atypical" else FT ZN_FING from..to FT /note="CCHHC-type #; degenerate" end case FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 34 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 34-55; Related: None; Repeats: 1-7; Topology: Undefined; Example: Q8CFC2; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01144; DC Domain; TR PROSITE; PS51803; ZF_C2HC_RNF; 1; level=0 XX Names: Zinc finger C2HC RNF-type Function: The closely related proteins RNF125/TRAC-1, RNF114 (also known as Zpf313), RNF138 (or NARF) and RNF166 contain, apart from the RING domain, a C2HC (Cys2-His-Cys)- and two C2H2 (Cys2-His2)-type zinc fingers, as well as an ubiquitin interacting motif (UIM). XX XX case and and and GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51803 case and and and FT ZN_FING from..to FT /note="C2HC RNF-type #" else case and and and FT ZN_FING from..to FT /note="C2HC RNF-type #; atypical" else FT ZN_FING from..to FT /note="C2HC RNF-type #; degenerate" end case FT BINDING 1 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 10-30; Related: None; Repeats: 1; Topology: Undefined; Example: Q1L721; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01145; DC Domain; TR PROSITE; PS51804; ZF_C2HC_LYAR; 1; level=0 XX Names: Zinc finger C2HC LYAR-type Function: Ly-1 antibody reactive clone (Lyar), which is known to be expressed abundantly in the testis, encodes a nucleolar protein that contain a LYAR- type C2HC zinc finger motif and three nuclear localization signals. XX case and and and GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51804 case and and and FT ZN_FING from..to FT /note="C2HC LYAR-type #" else case and and and FT ZN_FING from..to FT /note="C2HC LYAR-type #; atypical" else FT ZN_FING from..to FT /note="C2HC LYAR-type #; degenerate" end case FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 15-36; Related: None; Repeats: 2; Topology: Undefined; Example: O94311; Scope: Eukaryota Comments: None; XX # Revision 1.7 2022/11/19 // AC PRU01146; DC Domain; TR PROSITE; PS51805; EPHD; 1; level=0 XX Names: Extended PHD (ePHD) domain Function: The extended plant homeodomain (ePHD) domain contains an N-terminal pre-PHD (C2HC zinc finger), a long linker, and a noncanonical PHD finger (C4HC3 zinc finger). The ePHD domain can bind dsDNA but not histones. XX case ( and and and ) or ( and and and ) or ( and and and ) GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51805 case and and and FT ZN_FING from..37 FT /note="C2HC pre-PHD-type #" else case and and and FT ZN_FING from..37 FT /note="C2HC pre-PHD-type #; atypical" else FT ZN_FING from..37 FT /note="C2HC pre-PHD-type #; degenerate" end case case ( and and and ) and ( and and and ) FT ZN_FING 61..to FT /note="PHD-type #" else case ( and and and ) and ( and and and ) FT ZN_FING 61..to FT /note="PHD-type #; atypical" else FT ZN_FING 61..to FT /note="PHD-type #; degenerate" end case case not FT REGION from..to FT /note="Extended PHD# domain (ePHD#)" end case XX Chop: Nter=0; Cter=0; Size: 95-155; Related: None; Repeats: 1-2; Topology: Undefined; Example: P20659; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01147; DC Domain; TR PROSITE; PS51806; DOG1; 1; level=0 XX Names: DOG1 domain Function: The DOG1 domain is formed by Glutamine rich regions QI and QII and acidic amino acids and is likely to be a transcriptional activation domain. XX XX GO GO:0003700; F:DNA-binding transcription factor activity GO GO:0006351; P:DNA-templated transcription XX KW Activator KW Transcription KW Transcription regulation XX FT From: PS51806 FT DOMAIN from..to FT /note="DOG1 #" XX Chop: Nter=0; Cter=0; Size: 201-229; Related: None; Repeats: 1; Topology: Undefined; Example: Q93ZE2; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.7 2022/06/27 // AC PRU01148; DC Domain; TR PROSITE; PS51807; ZF_C2HC_BV; 1; level=0 XX Names: Zinc finger C2HC baculovirus (BV)-type Function: The C2HC BV-type zinc finger may perform a pivotal role in the association of Vp91 with other per os infectivity factors (PIFs). XX case ( and and and ) GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51807 case and and and FT ZN_FING from..to FT /note="C2HC BV-type #" else case and and and FT ZN_FING from..to FT /note="C2HC BV-type #; atypical" else FT ZN_FING from..to FT /note="C2HC BV-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 40-60; Related: None; Repeats: 1; Topology: Undefined; Example: Q91GH8; Scope: Viruses; Baculoviridae Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01150; DC Domain; TR PROSITE; PS51808; CHCH; 1; level=0 XX Names: Coiled coil-helix-coiled coil-helix (CHCH) domain Function: Twin CX(9)C proteins are eukaryotic proteins that adopt a coiled coil-helix-coiled coil helix (CHCH) fold stabilized by two disulfide bonds, which are formed by the four cysteines in the twin CX(9)C motifs (i.e., two pairs of cysteines each spaced by nine residues). XX case KW Disulfide bond end case KW Mitochondrion XX FT From: PS51808 FT DOMAIN from..to FT /note="CHCH #" FT MOTIF 4..14 FT /note="Cx9C motif #" FT Condition: C-x(9)-C FT MOTIF 4..14 FT /note="Cx10C motif #" FT Condition: C-x(10)-C FT MOTIF 25..35 FT /note="Cx9C motif #" FT Condition: C-x(9)-C FT MOTIF 25..35 FT /note="Cx10C motif #" FT Condition: C-x(10)-C FT DISULFID 4..35 FT Tag: disulf; Condition: C-x*-C FT DISULFID 14..25 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 24-67; Related: None; Repeats: 1; Topology: Undefined; Example: Q5RFJ0; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01151; DC Domain; TR PROSITE; PS50991; PYR_CT; 1; level=0 XX Names: Pyruvate carboxyltransferase domain Function: The pyruvate carboxyltransferase domain is found in pyruvate binding enzymes and acetyl-CoA dependent enzymes suggesting that this domain can be associated with different enzymatic activities. XX XX FT From: PS50991 FT DOMAIN from..to FT /note="Pyruvate carboxyltransferase #" XX Chop: Nter=0; Cter=0; Size: 70-292; Related: None; Repeats: 1; Topology: Undefined; Example: Q3Z554; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01153; DC Domain; TR PROSITE; PS51810; ZF_CCHC_FOG; 1; level=0 XX Names: Zinc finger CCHC FOG-type Function: Transcriptional cofactors of the Friend of GATA (FOG) family contain either eight or nine ZnFs that are related to the classical CCHH ZnFs (which have a conserved C-X(2,5)-C-X(12)-H-X(2,5)-H sequence). Several of the fingers in each FOG protein, however, have an altered consensus sequence in which the final zinc binding histidine is replaced with a cysteine. Interestingly, it is only these variant CCHC ZbFs that mediate interactions with GATA N-terminal zinc fingers (NFs). XX CC -!- SIMILARITY: Belongs to the FOG (Friend of GATA) family. XX GO GO:0006351; P:DNA-templated transcription case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Transcription KW Transcription regulation KW Zinc-finger XX FT From: PS51810 case and and and FT ZN_FING from..to FT /note="CCHC FOG-type #" else case and and and FT ZN_FING from..to FT /note="CCHC FOG-type #; atypical" else FT ZN_FING from..to FT /note="CCHC FOG-type #; degenerate" end case FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 30 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 24-44; Related: None; Repeats: 2-5; Topology: Undefined; Example: Q9VPQ6; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.10 2022/11/19 // AC PRU01154; DC Domain; TR PROSITE; PS51811; ZF_CCHC_HIVEP; 1; level=0 XX Names: Zinc finger CCHC HIVEP-type Function: HIVEP and the Drosophila Schnurri proteins contain two pairs of C2H2 Znf and, with the exception of the HIVEP2 family, a conserved CCHC-type Znf. XX XX GO GO:0006351; P:DNA-templated transcription case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Transcription KW Transcription regulation KW Zinc-finger XX FT From: PS51811 case and and and FT ZN_FING from..to FT /note="CCHC HIVEP-type #" else case and and and FT ZN_FING from..to FT /note="CCHC HIVEP-type #; atypical" else FT ZN_FING from..to FT /note="CCHC HIVEP-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 21-41; Related: None; Repeats: 1; Topology: Undefined; Example: Q03172; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.4 2022/06/27 // AC PRU01160; DC Domain; TR PROSITE; PS51817; PEPTIDASE_A3B; 1; level=0 XX Names: Peptidase family A3B domain Function: The rice tungro bacilliform virus (RTBV) aspartate protease (PR) domain forms peptidase family A3 subfamily B. The sequence DSGS is believed to be the RTBV protease active site. XX case DE + RecName: EC=3.4.23.-; end case XX XX case GO GO:0004190; F:aspartic-type endopeptidase activity XX KW Aspartyl protease KW Hydrolase KW Protease end case XX FT From: PS51817 FT DOMAIN from..to FT /note="Peptidase A3B #" FT ACT_SITE 18 FT /note="For protease activity" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 98-118; Related: None; Repeats: 1; Topology: Undefined; Example: P27502; Scope: Viruses; Tungrovirus Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01161; DC Domain; TR PROSITE; PS51635; PNPLA; 1; level=0 XX Names: Patatin-like phospholipase (PNPLA) domain Function: PNPLA domain containing proteins display lipase and transacylase properties and appear to have major roles in the regulation of lipid metabolism. The PNPLA domain has a Ser-Asp catalytic dyad. XX XX case GO GO:0016787; F:hydrolase activity GO GO:0016042; P:lipid catabolic process XX KW Hydrolase KW Lipid degradation KW Lipid metabolism end case XX FT From: PS51635 FT DOMAIN from..to FT /note="PNPLA #" FT MOTIF 5..10 FT /note="GXGXXG #" FT Condition: G-x-G-x-x-G FT MOTIF 35..39 FT /note="GXSXG #" FT Condition: G-x-S-x-G FT MOTIF 168..170 FT /note="DGA/G #" FT Condition: D-G-[AG] FT ACT_SITE 37 FT /note="Nucleophile" FT Group: 1; Condition: S FT ACT_SITE 168 FT /note="Proton acceptor" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 188-208; Related: None; Repeats: 1; Topology: Undefined; Example: Q8LPW4; Scope: Eukaryota Bacteria Viruses Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01162; DC Domain; TR PROSITE; PS51818; HOMEO_PROSPERO; 1; level=0 XX Names: Homeo-Prospero (HPD) domain Function: The HPD domain is required for nearly all the known functions of Prospero, including regulation of nuclear/cytoplasmic localization, sequence- specific DNA binding, and transcriptional activation. XX CC -!- DOMAIN: The Prospero-type homeodomain and the adjacent Prospero domain CC act as a single structural unit, the Homeo-Prospero domain. CC -!- SIMILARITY: Belongs to the Prospero homeodomain family. XX GO GO:0006351; P:DNA-templated transcription GO GO:0003677; F:DNA binding GO GO:0045944; P:positive regulation of transcription by RNA polymerase II GO GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific GO GO:0000122; P:negative regulation of transcription by RNA polymerase II XX KW DNA-binding KW Homeobox KW Transcription KW Transcription regulation XX FT From: PS51818 FT DOMAIN from..59 FT /note="Prospero-type homeo #" FT DOMAIN 60..to FT /note="Prospero #" FT REGION from..to FT /note="Homeo-Prospero #" XX Chop: Nter=0; Cter=0; Size: 146-169; Related: None; Repeats: 1; Topology: Undefined; Example: Q91018; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.7 2022/06/27 // AC PRU01163; DC Domain; TR PROSITE; PS51819; VOC; 1; level=0 XX Names: Vicinal oxygen chelate (VOC) domain Function: The vicinal oxygen chelate (VOC) family of enzymes catalyzes a highly diverse set of chemistries that derives from one common mechanistic trait: bidentate coordination to a divalent metal center by a substrate or intermediate or transition state through vicinal oxygen atoms. XX XX case KW Metal-binding end case XX FT From: PS51819 FT DOMAIN from..to FT /note="VOC #" FT ACT_SITE 118 FT /note="Proton donor/acceptor" FT Condition: [EV] FT BINDING 4 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: [HQ] FT BINDING 45 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: E FT BINDING 70 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: [HQ] FT BINDING 118 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: [EV] XX Chop: Nter=0; Cter=0; Size: 68-190; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q8GPH6; Scope: Bacteria Eukaryota Archaea; Pyrococcus Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01164; DC Domain; TR PROSITE; PS51820; PA14; 1; level=0 XX Names: PA14 domain Function: It could be a carbohydrate-binding module. XX XX FT From: PS51820 FT DOMAIN from..to FT /note="PA14 #" XX Chop: Nter=0; Cter=0; Size: 100-186; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q54P69; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01165; DC Domain; TR PROSITE; PS51821; VELVET; 1; level=0 XX Names: Velvet domain Function: The velvet domain is involved in specific DNA binding as well as in the dimerization of the different velvet proteins, resulting in the formation of homo- and heterodimers. XX XX GO GO:0006351; P:DNA-templated transcription GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0005634; C:nucleus XX KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51821 FT DOMAIN from..to FT /note="Velvet #" XX Chop: Nter=0; Cter=0; Size: 111-498; Related: None; Repeats: 1; Topology: Undefined; Example: B2CQJ9; Scope: Eukaryota; Dikarya Comments: None; XX # Revision 1.5 2022/06/27 // AC PRU01166; DC Domain; TR PROSITE; PS51822; HV_PV_NS3_PRO; 1; level=0 XX Names: Hepacivirus/Pegivirus NS3 protease domain Function: The NS3/A4 protease is not only essential for generating mature viral proteins required for viral replication, but also hydrolyzes proteins, which are part of the innate immune system, thereby confounding the innate immune response to viral infection. XX case DE Contains: DE RecName: Full=Serine protease NS3; DE EC=3.4.21.98; DE AltName: Full=Hepacivirin; DE AltName: Full=NS3P; DE AltName: Full=p70; end case case and and XX CC -!- FUNCTION: NS3 displays three enzymatic activities: serine protease, CC NTPase and RNA helicase. NS3 serine protease, in association with NS4A, CC is responsible for the cleavages of NS3-NS4A, NS4A-NS4B, NS4B-NS5A and CC NS5A-NS5B. NS3/NS4A complex also prevents phosphorylation of human CC IRF3, thus preventing the establishment of dsRNA induced antiviral CC state. NS3 RNA helicase binds to RNA and unwinds dsRNA in the 3' to 5' CC direction, and likely RNA stable secondary structure in the template CC strand. Cleaves and inhibits the host antiviral protein MAVS. end case case CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of four peptide bonds in the viral precursor CC polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr CC in P1 and Ser or Ala in P1'.; EC=3.4.21.98; end case case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per NS3 protease domain; end case case and CC -!- ACTIVITY REGULATION: Activity of auto-protease NS2-3 is dependent on CC zinc ions and completely inhibited by EDTA. Serine protease NS3 is also CC activated by zinc ions. end case case and and CC -!- DOMAIN: The N-terminal one-third of serine protease NS3 contains the CC protease activity. This region contains a zinc atom that does not CC belong to the active site, but may play a structural rather than a CC catalytic role. This region is essential for the activity of protease CC NS2-3, maybe by contributing to the folding of the latter. The helicase CC activity is located in the C-terminus of NS3. end case XX case GO GO:0008270; F:zinc ion binding end case case GO GO:0004252; F:serine-type endopeptidase activity GO GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway GO GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity end case XX case KW Metal-binding KW Zinc end case case KW Hydrolase KW Protease KW Serine protease KW Viral immunoevasion KW Interferon antiviral system evasion KW Inhibition of host RLR pathway by virus KW Inhibition of host innate immune response by virus KW Inhibition of host interferon signaling pathway by virus KW Inhibition of host MAVS by virus end case XX FT From: PS51822 FT DOMAIN from..to FT /note="Peptidase S29 #" FT ACT_SITE 57 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: H FT ACT_SITE 81 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: D FT ACT_SITE 139 FT /note="Charge relay system; for serine protease NS3 FT activity" FT Group: 1; Condition: S FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C FT BINDING 149 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: H XX Chop: Nter=0; Cter=0; Size: 172-192; Related: None; Repeats: 1; Topology: Undefined; Example: Q9WMX2; Scope: Viruses; Hepacivirus Comments: None; XX # Revision 1.9 2022/11/19 // AC PRU01167; DC Domain; TR PROSITE; PS51823; CLU; 1; level=0 XX Names: Clueless (Clu) domain Function: Clu-related proteins are highly conserved and share a ~245-amino acid region (the 'Clu domain') and TPR repeats. XX XX FT From: PS51823 FT DOMAIN from..to FT /note="Clu #" XX Chop: Nter=0; Cter=0; Size: 233-305; Related: None; Repeats: 1; Topology: Undefined; Example: A6SFG0; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01168; DC Domain; TR PROSITE; PS51824; FLO11; 1; level=0 XX Names: Flocculin 11 (Flo11) domain Function: The Flo11 domain can make homotypic interactions. XX XX FT From: PS51824 FT DOMAIN from..to FT /note="Flo11 #" XX Chop: Nter=0; Cter=0; Size: 145-234; Related: None; Repeats: 1; Topology: Undefined; Example: Q12140; Scope: Eukaryota; Ascomycota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01169; DC Domain; TR PROSITE; PS51825; DIPSY; 1; level=0 XX Names: DIPSY domain Function: The DIPSY domain is a functional adhesion domain. XX CC -!- SIMILARITY: Belongs to the mam3/map4 family. XX FT From: PS51825 FT DOMAIN from..to FT /note="DIPSY #" XX Chop: Nter=0; Cter=0; Size: 142-173; Related: None; Repeats: 1; Topology: Undefined; Example: O74346; Scope: Eukaryota; Schizosaccharomyces Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01170; DC Domain; TR PROSITE; PS51826; PSBD; 1; level=0 XX Names: Peripheral subunit-binding (PSBD) domain Function: The PSBD domain binds E1 or E3, but not both simultaneously. XX FT From: PS51826 FT DOMAIN from..to FT /note="Peripheral subunit-binding (PSBD) #" XX Chop: Nter=0; Cter=0; Size: 16-52; Related: None; Repeats: 1; Topology: Undefined; Example: O06159; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01171; DC Domain; TR PROSITE; PS51827; XTBD; 1; level=0 XX Names: XRN2-binding domain (XTBD) Function: The ~80-residue XRN2-binding domain (XTBD) constitutes an XRN2- binding module that is employed by different metazoan proteins to link to XRN2. XX FT From: PS51827 FT DOMAIN from..to FT /note="XRN2-binding (XTBD) #" XX Chop: Nter=0; Cter=0; Size: 75-125; Related: None; Repeats: 1; Topology: Undefined; Example: Q8BI72; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01172; DC Domain; TR PROSITE; PS51828; PTX_2; 1; level=0 XX Names: Pentraxin (PTX) domain Function: Pentraxins (earlier also termed pentaxins), named for their homopentameric quaternary structure, are a superfamily of multifunctional conserved proteins that are characterized by a cyclic multimeric structure and by the presence in their carboxyl-terminal of an ~200 aa-long conserved domain, called pentraxin (PTX) domain. XX DR PROSITE; PS00289; PTX_1; 1; trigger=no XX case or KW Calcium KW Metal-binding end case case KW Disulfide bond end case XX FT From: PS51828 FT DOMAIN from..to FT /note="Pentraxin (PTX) #" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 55 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: N FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: E FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: E FT BINDING 134 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: Q FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT Group: 1; Condition: D FT BINDING 135 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: D FT BINDING 145 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#2" FT Group: 2; Condition: Q FT DISULFID 32..91 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 12-222; Related: None; Repeats: 1; Topology: Undefined; Example: Q6QNK2; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01173; DC Domain; TR PROSITE; PS51829; P_HOMO_B; 1; level=0 XX Names: P/Homo B domain Function: The P/Homo B domain appears to be necessary to both fold and maintain the subtilisin-like active catalytic module and to regulate its specialized features of calcium and more acidic pH dependence. XX FT From: PS51829 FT DOMAIN from..to FT /note="P/Homo B #" XX Chop: Nter=0; Cter=0; Size: 89-176; Related: None; Repeats: 1; Topology: Undefined; Example: P13134; Scope: Eukaryota Bacteria Viruses; Ictalurivirus Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01174; DC Domain; TR PROSITE; PS51830; FIIND; 1; level=0 XX Names: FIIND domain Function: CARD8 and NLRP1 undergo autoproteolytic cleavage at a conserved SF/S motif within the "Function to Find Domain" (FIIND). XX case GO GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process end case XX FT From: PS51830 FT DOMAIN from..to FT /note="FIIND #" case FT SITE 132..133 FT /note="Cleavage; by autolysis" end case XX Chop: Nter=0; Cter=0; Size: 108-296; Related: None; Repeats: 1; Topology: Undefined; Example: Q9C000; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01175; DC Domain; TR PROSITE; PS51831; HD; 1; level=0 XX Names: HD domain Function: It defines a superfamily of phosphohydrolases that can catalyze both metal-dependent and -independent phosphomonoesterase and phosphodiesterase reactions for a broad range of substrates. XX FT From: PS51831 FT DOMAIN from..to FT /note="HD #" XX Chop: Nter=0; Cter=0; Size: 82-224; Related: None; Repeats: 1-2; Topology: Undefined; Example: B7LGM2; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Viruses; Mimivirus Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01176; DC Domain; TR PROSITE; PS51832; HD_GYP; 1; level=0 XX Names: HD-GYP domain Function: The HD-GYP domain is likely to be a conserved scaffold whose main role is to allow protein-protein interactions with partner GGDEF domains while achieving (a) different function(s) through diversification of the active-site cavity and the N-terminal regulatory domains. XX FT From: PS51832 FT DOMAIN from..to FT /note="HD-GYP #" XX Chop: Nter=0; Cter=0; Size: 182-222; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KL18; Scope: Bacteria Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01177; DC Domain; TR PROSITE; PS51833; HDOD; 1; level=0 XX Names: HD-related output (HDOD) domain Function: Proteins containing the HDOD are widespread in diverse bacteria; it can be present as a stand-alone domain, and also associated with other domains, such as response regulatory (RR), GGDEF, and EAL, suggesting a role in regulation and signaling. XX FT From: PS51833 FT DOMAIN from..to FT /note="HDOD #" XX Chop: Nter=0; Cter=0; Size: 178-204; Related: None; Repeats: 1; Topology: Undefined; Example: P14203; Scope: Bacteria Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01178; DC Domain; TR PROSITE; PS51834; DENN_FLCN_SMCR8; 1; level=0 XX Names: Tripartite DENN FLCN/SMCR8-type domain Function: The tripartite DENN domain is a GDP-GTP exchange factor (GEF) for Rab GTPases. XX FT From: PS51834 FT DOMAIN from..153 FT /note="uDENN FLCN/SMCR8-type #" FT DOMAIN 258..402 FT /note="cDENN FLCN/SMCR8-type #" FT DOMAIN 411..to FT /note="dDENN FLCN/SMCR8-type #" XX Chop: Nter=0; Cter=0; Size: 185-926; Related: None; Repeats: 1; Topology: Undefined; Example: P53237; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01179; DC Domain; TR PROSITE; PS51835; DENN_C9ORF72; 1; level=0 XX Names: Tripartite DENN C9ORF72-type domain Function: The tripartite DENN domain is a GDP-GTP exchange factor (GEF) for Rab GTPases. XX FT From: PS51835 FT DOMAIN from..121 FT /note="uDENN C9ORF72-type #" FT DOMAIN 127..265 FT /note="cDENN C9ORF72-type #" FT DOMAIN 283..to FT /note="dDENN C9ORF72-type #" XX Chop: Nter=0; Cter=0; Size: 388-452; Related: None; Repeats: 1; Topology: Undefined; Example: Q96LT7; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.5 2019/11/22 // AC PRU01180; DC Domain; TR PROSITE; PS51836; DENN_FNIP12; 1; level=0 XX Names: Tripartite DENN FNIP1/2-type domain Function: The tripartite DENN domain is a GDP-GTP exchange factor (GEF) for Rab GTPases. XX FT From: PS51836 FT DOMAIN from..363 FT /note="uDENN FNIP1/2-type #" FT DOMAIN 371..730 FT /note="cDENN FNIP1/2-type #" FT DOMAIN 738..to FT /note="dDENN FNIP1/2-type #" XX Chop: Nter=0; Cter=0; Size: 611-1131; Related: None; Repeats: 1; Topology: Undefined; Example: Q757Y7; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01181; DC Domain; TR PROSITE; PS51837; LITAF; 1; level=0 XX Names: LITAF domain SIMPLE-like domain Function: LITAF is a monotypic membrane protein anchored to membranes via an in-plane helical membrane anchor, present within the highly conserved C- terminal region known as the LITAF domain. XX CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. XX KW Membrane case KW Metal-binding KW Zinc end case XX FT From: PS51837 FT DOMAIN from..to FT /note="LITAF" FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 76 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 71-98; Related: None; Repeats: 1; Topology: Undefined; Example: Q5U2U6; Scope: Eukaryota Viruses; Ranavirus Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01182; DC Domain; TR PROSITE; PS50249; MPN; 1; level=0 XX Names: MPN (Mpr1, Pad1 N-terminal) domain Mov34 domain JAB domain PAD-1 domain JAMM (JAB1/MPN/Mov34 metalloenzyme) domain Function: MPN+ domain-containing proteins are classified as metalloenzymes responsible for isopeptidase activity. These proteins contain a conserved glutamate (E) and a JAMM (Jab1/MPN/Mov34 metalloenzyme) motif, typically consisting of a canonical sequence (H-x-H-x[7]-S-x[2]-D) and coordinating a zinc ion. MPN- domains are recognizable by the absence of essential Zn(2+)- coordinating residues that are required for catalytic function. In protein complexes, an MPN+ domain can associate with MPN- domains for purposes that are not well understood. XX case KW Hydrolase KW Metal-binding KW Metalloprotease KW Protease KW Zinc end case XX FT From: PS50249 FT DOMAIN from..to FT /note="MPN #" FT MOTIF 77..90 FT /note="JAMM motif #" FT Condition: H-[NST]-H-x(7)-S-x(2)-D FT BINDING 77 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 79 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 57-178; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KVC9; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Viruses Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01183; DC Domain; TR PROSITE; PS51838; HDAG; 1; level=0 XX Names: Hepatitis delta antigen (HDAg) domain Function: The C-terminus of the HDAg domain forms the RNAPII-binding motif conserved in humans and virus, while the NELF-C (or NELF-D)-binding region of NELF-A is localized in the middle of the HDAg domain. The region of HDAg corresponding to the NELF-C (or NELF-D)-binding region of NELF-A has an RNA- binding function. XX FT From: PS51838 FT DOMAIN from..to FT /note="HDAg #" case FT REGION 64..74 FT /note="RNA-binding" FT REGION 107..117 FT /note="RNA-binding" end case case FT REGION 37..100 FT /note="NELF-C/D-binding" end case FT REGION 101..to FT /note="RNAPII-binding" XX Chop: Nter=0; Cter=0; Size: 150-186; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6L6; Scope: Viruses; Deltavirus Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01184; DC Domain; TR PROSITE; PS51839; 4FE4S_HC3; 1; level=0 XX Names: His(Cys)3-ligated-type [4Fe-4S] domain Function: The His(Cys)3-ligated-type [4Fe-4S] domain consists of just two alpha helices separated by a loop region that coordinates a [4Fe-4S] cluster through an unusual H-x(3)-C-x(2)-C-x(5)-C motif that includes one His and three Cys residues. XX case CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; end case XX DR PROSITE; PS00642; COMPLEX1_75K_2; 0-1; trigger=no XX case GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0005506; F:iron ion binding XX KW 4Fe-4S KW Iron KW Iron-sulfur KW Metal-binding end case XX FT From: PS51839 FT DOMAIN from..to FT /note="4Fe-4S His(Cys)3-ligated-type #" FT BINDING 17 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 19 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 21 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 24 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 30 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_label="#1" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 30-51; Related: None; Repeats: 1; Topology: Undefined; Example: P15690; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01185; DC Domain; TR PROSITE; PS50250; PCI; 1; level=0 XX Names: PCI domain PINT domain Function: The PCI domain mediates and stabilizes protein-protein interactions within complexes. XX FT From: PS50250 FT DOMAIN from..to FT /note="PCI #" XX Chop: Nter=0; Cter=0; Size: 42-223; Related: None; Repeats: 1; Topology: Undefined; Example: Q2H9N4; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01186; DC Domain; TR PROSITE; PS51840; C2_NT; 1; level=0 XX Names: C2 NT-type domain Function: The primary function of the NT-type C2 domain appears to be the linking of actin/microfilament-binding adaptors to the membrane and to act as a link that tethers endosomal vesicles to the cytoskeleton in course of their intracellular trafficking. XX FT From: PS51840 FT DOMAIN from..to FT /note="C2 NT-type #" XX Chop: Nter=0; Cter=0; Size: 101-206; Related: None; Repeats: 1; Topology: Undefined; Example: Q8NDI1; Scope: Eukaryota Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01187; DC Domain; TR PROSITE; PS51841; LTD; 1; level=0 XX Names: Lamin-tail (LTD) domain Function: The LTD domain could be involved both in protein and DNA binding. XX FT From: PS51841 FT DOMAIN from..to FT /note="LTD #" XX Chop: Nter=0; Cter=0; Size: 88-147; Related: None; Repeats: 1; Topology: Undefined; Example: Q8IXW0; Scope: Eukaryota Bacteria; Bacillus Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01188; DC Domain; TR PROSITE; PS51842; IF_ROD_2; 1; level=0 XX Names: Intermediate filament (IF) rod domain Function: IF proteins have a very strong tendency to dimerize via the formation of an alpha-helical coiled coil (CC) by their rod domains. XX CC -!- SIMILARITY: Belongs to the intermediate filament family. XX DR PROSITE; PS00226; IF_ROD_1; 1; trigger=no XX GO GO:0005198; F:structural molecule activity XX KW Coiled coil KW Intermediate filament XX FT From: PS51842 FT DOMAIN from..to FT /note="IF rod #" XX Chop: Nter=0; Cter=0; Size: 13-467; Related: None; Repeats: 1; Topology: Undefined; Example: Q9D646; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01189; DC Domain; TR PROSITE; PS51843; NR_LBD; 1; level=0 XX Names: Nuclear receptor (NR) ligand-binding (LBD) domain HOLI domain Function: The NR LBD plays a crucial role in ligand-mediated NR activity. In addition to its role in ligand recognition, the LBD also contains a ligand- dependent AF-2 region. XX KW Receptor XX FT From: PS51843 FT DOMAIN from..to FT /note="NR LBD #" FT REGION 226..to FT /note="AF-2" XX Chop: Nter=0; Cter=0; Size: 200-400; Related: None; Repeats: 1; Topology: Undefined; Example: P49843; Scope: Eukaryota; Metazoa Viruses; Alpharetrovirus Comments: None; XX # Revision 1.3 2023/12/07 // AC PRU01190; DC Domain; TR PROSITE; PS51844; SH3_LIKE; 1; level=0 XX Names: Myosin N-terminal SH3-like domain Function: The myosin N-terminal SH3-like domain may mediate some aspect of the conformational communication that occurs within the myosin head during actin and nucleotide binding. XX FT From: PS51844 FT DOMAIN from..to FT /note="Myosin N-terminal SH3-like #" XX Chop: Nter=0; Cter=0; Size: 39-74; Related: None; Repeats: 1; Topology: Undefined; Example: F4K0A6; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01191; DC Domain; TR PROSITE; PS50985; GRAS; 1; level=0 XX Names: GRAS domain Function: The GRAS domain is typically composed of ~380 amino acids and contains five highly conserved motifs, found in the following order: leucine heptad repeat I (LRI), the VHIID motif, leucine heptad repeat II (LRII), the PFYRE motif and the SAW motif. XX CC -!- SIMILARITY: Belongs to the GRAS family. XX FT From: PS50985 FT DOMAIN from..to FT /note="GRAS #" FT REGION 8..68 FT /note="Leucine repeat I (LRI)" FT REGION 87..152 FT /note="VHIID" FT REGION 168..200 FT /note="Leucine repeat II (LRII)" FT REGION 210..301 FT /note="PFYRE" FT REGION 304..to FT /note="SAW" FT MOTIF 15..19 FT /note="LxCxE motif" FT Condition: L-x-C-x-E FT MOTIF 118..122 FT /note="VHIID" FT Condition: [VILFP]-H-[IV]-[ILV]-D FT MOTIF 218..222 FT /note="LXXLL motif" FT Condition: L-x-x-[LV]-L XX Chop: Nter=0; Cter=0; Size: 350-430; Related: None; Repeats: 1; Topology: Undefined; Example: Q6EI06; Scope: Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01192; DC Domain; TR PROSITE; PS51845; PDEASE_I_2; 1; level=0 XX Names: 3'5'-cyclic nucleotide phosphodiesterase (PDEase) domain Function: 3'5'-cyclic nucleotide phosphodiesterases (EC 3.1.4.17) (PDEases) contain a catalytic domain of approximately 270 amino acids at the carboxyl terminus. XX case CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Note=Binds 2 divalent metal cations per subunit. Site 1 may CC preferentially bind zinc ions, while site 2 has a preference for CC magnesium and/or manganese ions end case CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family. XX DR PROSITE; PS00126; PDEASE_I_1; 1; trigger=no XX XX case GO GO:0046872; F:metal ion binding XX KW Metal-binding end case case and KW Hydrolase end case XX FT From: PS51845 FT DOMAIN from..to FT /note="PDEase #" FT ACT_SITE 77 FT /note="Proton donor" FT Tag: act_site; Condition: H FT BINDING 81 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 117 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Group: 1; Condition: H FT BINDING 118 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Group: 1; Condition: D FT BINDING 118 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="2" FT Group: 1; Condition: D FT BINDING 229 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_label="1" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 300-450; Related: None; Repeats: 1; Topology: Undefined; Example: P16586; Scope: Eukaryota Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01193; DC Domain; TR PROSITE; PS51846; CNNM; 1; level=0 XX Names: CNNM transmembrane domain Function: The CNNM integral membrane domain has been proposed to contain three full membrane-spanning regions and an additional re-entrant loop . XX GO GO:0016020; C:membrane XX KW Membrane KW Transmembrane KW Transmembrane helix XX FT From: PS51846 FT DOMAIN from..to FT /note="CNNM transmembrane #" XX Chop: Nter=0; Cter=0; Size: 150-250; Related: None; Repeats: 1; Topology: Undefined; Example: Q49399; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2022/09/30 // AC PRU01194; DC Domain; TR PROSITE; PS51847; SMP; 1; level=0 XX Names: Synaptotagmin-like mitochondrial lipid-binding proteins (SMP) domain Function: The SMP domain is able to homo- or heterodimerize, harbors lipids in a hydrophobic cavity and mediates lipid transfer between two adjacent bilayers independently of membrane fusion and fission reactions. XX CC -!- DOMAIN: The SMP-LTD domain is a barrel-like domain that can bind CC various types of glycerophospholipids in its interior and mediate their CC transfer between two adjacent bilayers. KW Membrane KW Transport KW Lipid-binding KW Lipid transport XX FT From: PS51847 FT DOMAIN from..to FT /note="SMP-LTD #" XX Chop: Nter=0; Cter=0; Size: 150-700; Related: None; Repeats: 1; Topology: Undefined; Example: C5DLL1; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01195; DC Domain; TR PROSITE; PS51848; BMERB; 1; level=0 XX Names: Bivalent Mical/EHBP Rab binding" (bMERB) domain Function: The bMERB domain is a Rab effector domain that is present in proteins of the Mical and EHBP families, both known to act in endosomal trafficking. XX KW Coiled coil XX FT From: PS51848 FT DOMAIN from..to FT /note="bMERB #" XX Chop: Nter=0; Cter=0; Size: 130-180; Related: None; Repeats: 1; Topology: Undefined; Example: E1BBG2; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01196; DC Domain; TR PROSITE; PS51849; RSGI_N; 1; level=0 XX Names: RsgI N-terminal anti-sigma domain Function: Interaction of the ~50- to ~60-residue N-terminal intracellular domain of the transmembrane protein RsgI with SigI sequesters and inactivates SigI on the inner surface of the cytoplasmic membrane. XX FT From: PS51849 FT DOMAIN from..to FT /note="RsgI N-terminal anti-sigma #" XX Chop: Nter=0; Cter=0; Size: 45-55; Related: None; Repeats: 1; Topology: Undefined; Example: A3DBH1; Scope: Bacteria; Bacillota Comments: None; XX # Revision 1.3 2023/01/13 // AC PRU01197; DC Domain; TR PROSITE; PS51850; KARI_N; 1; level=0 XX Names: KARI N-terminal domain Function: Ketol-acid reductoisomerase (KARI; EC 1.1.1.86), also known as acetohydroxy acid isomeroreductase (AHIR or AHAIR), catalyzes the conversion of acetohydroxy acids into dihydroxy valerates in the second step of the biosynthetic pathway for the essential branched-chain amino acids valine, leucine, and isoleucine. KARIs are composed of two types of domains, an N- terminal Rossmann fold domain and one or two C-terminal knotted domains. XX CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. XX GO GO:0004455; F:ketol-acid reductoisomerase activity GO GO:0009097; P:isoleucine biosynthetic process GO GO:0009099; P:valine biosynthetic process case GO GO:0050661; F:NADP binding XX KW NADP end case KW Amino-acid biosynthesis KW Branched-chain amino acid biosynthesis KW Oxidoreductase XX FT From: PS51850 FT DOMAIN from..to FT /note="KARI N-terminal Rossmann #" FT BINDING 27..30 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Group: 1 FT ACT_SITE 110 FT Condition: H FT BINDING 50 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Group: 1; Condition: R FT BINDING 55 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Group: 1; Condition: S FT BINDING 136 FT /ligand="NADP(+)" FT /ligand_id="ChEBI:CHEBI:58349" FT Group: 1; Condition: G XX Chop: Nter=0; Cter=0; Size: 135-205; Related: None; Repeats: 1; Topology: Undefined; Example: A7GMU0; Scope: Bacteria Archaea Eukaryota Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01198; DC Domain; TR PROSITE; PS51851; KARI_C; 1; level=0 XX Names: KARI C-terminal domain Function: Ketol-acid reductoisomerase (KARI; EC 1.1.1.86), also known as acetohydroxy acid isomeroreductase (AHIR or AHAIR), catalyzes the conversion of acetohydroxy acids into dihydroxy valerates in the second step of the biosynthetic pathway for the essential branched-chain amino acids valine, leucine, and isoleucine. KARIs are composed of two types of domains, an N- terminal Rossmann fold domain and one or two C-terminal knotted domains. XX CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. XX GO GO:0004455; F:ketol-acid reductoisomerase activity GO GO:0009097; P:isoleucine biosynthetic process GO GO:0009099; P:valine biosynthetic process case or GO GO:0046872; F:metal ion binding XX KW Magnesium KW Metal-binding end case KW Amino-acid biosynthesis KW Branched-chain amino acid biosynthesis KW Oxidoreductase XX FT From: PS51851 FT DOMAIN from..to FT /note="KARI C-terminal knotted #" FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Group: 1; Condition: D FT BINDING 9 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Group: 1; Condition: D FT BINDING 13 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT Group: 1; Condition: E FT BINDING 45 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Group: 2; Condition: E FT BINDING 49 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Group: 2; Condition: E case FT BINDING 70 FT /ligand="substrate" FT Condition: S end case XX Chop: Nter=0; Cter=0; Size: 125-155; Related: None; Repeats: 1; Topology: Undefined; Example: A7GMU0; Scope: Bacteria Archaea Eukaryota Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01199; DC Domain; TR PROSITE; PS51852; PG1; 1; level=0 XX Names: pG1 pseudoGTPase domain Function: The pG1 pseudoGTPase domain adopts a small GTPase fold, with a central 6-stranded beta-sheet surrounded by four alpha-helices. The conserved GTPase motifs from the pG1 pseudoGTPase domain, which is not a nucleotide- binding domain. XX FT From: PS51852 FT DOMAIN from..to FT /note="pG1 pseudoGTPase #" XX Chop: Nter=0; Cter=0; Size: 150-200; Related: None; Repeats: 1; Topology: Undefined; Example: Q9VX32; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01200; DC Domain; TR PROSITE; PS51853; PG2; 1; level=0 XX Names: pG2 pseudoGTPase domain Function: The five G motifs of the pG2 pseudoGTPase are highly degraded. XX FT From: PS51853 FT DOMAIN from..to FT /note="pG2 pseudoGTPase #" XX Chop: Nter=0; Cter=0; Size: 150-200; Related: None; Repeats: 1; Topology: Undefined; Example: Q9VX32; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01201; DC Domain; TR PROSITE; PS51854; CSPG; 1; level=0 XX Names: CSPG repeat Function: The CSPG (chondroitin sulfate proteoglycan) repeat is a cadherin- like and tumor-relevant protein module which is thought to mediate interactions between cells and the extracellular matrix (ECM) in species as divergent as cyanobacteria, fly, worm, sea urchin and human. XX FT From: PS51854 FT REPEAT from..to FT /note="CSPG #" XX Chop: Nter=0; Cter=0; Size: 85-120; Related: None; Repeats: 1; Topology: Undefined; Example: Q96PW8; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01202; DC Domain; TR PROSITE; PS51855; MGS; 1; level=0 XX Names: MGS-like domain Function: MGS-like domains share a conserved phosphate binding site. XX case and and DR PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1; trigger=no end case FT From: PS51855 FT DOMAIN from..to FT /note="MGS-like #" case and FT ACT_SITE 62 FT Condition: D end case XX Chop: Nter=0; Cter=0; Size: 90-200; Related: None; Repeats: 1; Topology: Undefined; Example: B1IL57; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01203; DC Domain; TR PROSITE; PS51856; RHO_RNA_BD; 1; level=0 XX Names: Rho RNA-binding (RNA-BD) domain Function: Rho protomers have an RNA-binding region at the N-terminus linked by a connector loop to a C-terminal ATPase domain. The RNA binding region comprises a variable N-terminal helix bundle (NHBD) domain and a core RNA- binding domain which forms the primary RNA binding site. XX CC -!- SIMILARITY: Belongs to the Rho family. XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS51856 FT DOMAIN from..to FT /note="Rho RNA-BD #" XX Chop: Nter=0; Cter=0; Size: 60-90; Related: None; Repeats: 1; Topology: Undefined; Example: P0AG33; Scope: Bacteria Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01204; DC Domain; TR PROSITE; PS51857; CSD_2; 1; level=0 XX Names: Cold-shock (CSD) domain Function: The cold-shock domain (CSD) is an ancient beta-barrel fold of about 70 amino acids that binds single-stranded nucleic acids (both RNA and DNA). XX DR PROSITE; PS00352; CSD_1; 1; trigger=no XX FT From: PS51857 FT DOMAIN from..to FT /note="CSD #" XX Chop: Nter=0; Cter=0; Size: 40-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q7A5P3; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01205; DC Domain; TR PROSITE; PS51858; PPPDE; 1; level=0 XX Names: PPPDE domain Function: The PPPDE domain has a papain-like fold, in which a catalytic dyad is formed by a conserved N-terminal histidine residue on a beta-strand (beta2) and a conserved C-terminal cysteine residue on a following alpha- helix (alpha3). XX case GO GO:0008233; F:peptidase activity XX KW Hydrolase KW Protease end case XX FT From: PS51858 FT DOMAIN from..to FT /note="PPPDE #" FT ACT_SITE 32 FT Group: 1; Condition: H FT ACT_SITE 107 FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 130-230; Related: None; Repeats: 1; Topology: Undefined; Example: Q9D291; Scope: Eukaryota Viruses; Reovirales Comments: None; XX # Revision 1.3 2023/01/05 // AC PRU01206; DC Domain; TR PROSITE; PS51859; RHO_BD; 1; level=0 XX Names: Rho-binding (RhoBD) domain Function: The Rho-binding (RhoBD) domain is responsible for the recognition and binding of the active Rho proteins. XX GO GO:0007266; P:Rho protein signal transduction XX KW Coiled coil XX FT From: PS51859 FT DOMAIN from..to FT /note="RhoBD #" XX Chop: Nter=0; Cter=0; Size: 55-75; Related: None; Repeats: 1; Topology: Undefined; Example: P92199; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01207; DC Domain; TR PROSITE; PS51860; REM_1; 1; level=0 XX Names: REM-1 domain Function: The Rho effector motif class 1 (REM-1) domain specifically binds GTP-Rho. XX KW Coiled coil XX FT From: PS51860 FT DOMAIN from..to FT /note="REM-1 #" XX Chop: Nter=0; Cter=0; Size: 1000000; Related: None; Repeats: 1; Topology: Undefined; Example: Q16512; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01208; DC Domain; TR PROSITE; PS51861; OXYTX_ICK; 1; level=0 XX Names: Oxytoxin-type inhibitor cystine knot (ICK) domain Function: Oxytoxins are disulphide-rich polypeptides that contain five disulfide bridges and block L-, N- and P/Q-type voltage-sensitive calcium ion channels (VSCCs) . XX CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot' CC structurally defines this protein as a knottin. XX GO GO:0005576; C:extracellular region GO GO:0090729; F:toxin activity XX case KW Disulfide bond end case KW Knottin KW Secreted KW Toxin XX FT From: PS51861 FT DOMAIN from..to FT /note="Oxytoxin-type inhibitor cystine knot (ICK) #" FT DISULFID 4..18 FT Tag: disulf; Condition: C-x*-C FT DISULFID 11..23 FT Tag: disulf; Condition: C-x*-C FT DISULFID 15..50 FT Tag: disulf; Condition: C-x*-C FT DISULFID 17..39 FT Tag: disulf; Condition: C-x*-C FT DISULFID 25..37 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 50-70; Related: None; Repeats: 1; Topology: Undefined; Example: P86716; Scope: Eukaryota; Oxyopes Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01209; DC Domain; TR PROSITE; PS51862; BSPN_CSAB; 1; level=0 XX Names: BetaSPN-type cysteine-stabilized alpha/beta (CS-alpha/beta) domain Function: The betaSPN-type CS-alpha/beta has K(+) channel blocking activity. XX CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. XX GO GO:0090729; F:toxin activity XX case KW Disulfide bond end case KW Toxin XX FT From: PS51862 FT DOMAIN from..to FT /note="BetaSPN-type CS-alpha/beta #" FT DISULFID 4..24 FT Tag: disulf; Condition: C-x*-C FT DISULFID 11..29 FT Tag: disulf; Condition: C-x*-C FT DISULFID 15..31 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 30-45; Related: None; Repeats: 1; Topology: Undefined; Example: Q0GY40; Scope: Eukaryota; Scorpiones Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01210; DC Domain; TR PROSITE; PS51863; LCN_CSAB; 1; level=0 XX Names: LCN-type cysteine-stabilized alpha/beta (CS-alpha/beta) domain Function: Most long-chain neurotoxins (LCNs) are composed of 60-70 residues and are cross-linked by four disulphide bridges. The long chain or voltage- gated sodium channels scorpion neurotoxins (NaScTxs) can be classified either as alpha-toxins, which slow down Na(+) channel inactivation, or beta-toxins, which affect the channel activation process. XX CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the venom gland. XX GO GO:0090729; F:toxin activity GO GO:0005576; C:extracellular region GO GO:0008200; F:ion channel inhibitor activity XX KW Secreted KW Toxin KW Neurotoxin case KW Disulfide bond end case KW Ion channel impairing toxin KW Voltage-gated sodium channel impairing toxin XX FT From: PS51863 FT DOMAIN from..to FT /note="LCN-type CS-alpha/beta #" FT DISULFID 11..62 FT Tag: disulf; Condition: C-x*-C FT DISULFID 15..37 FT Tag: disulf; Condition: C-x*-C FT DISULFID 23..43 FT Tag: disulf; Condition: C-x*-C FT DISULFID 27..45 FT Tag: disulf; Condition: C-x*-C FT DISULFID 38..62 FT Tag: disulf; Condition: C-x*-C FT DISULFID 56..62 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 50-75; Related: None; Repeats: 1; Topology: Undefined; Example: P54135; Scope: Eukaryota; Scorpiones Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01211; DC Domain; TR PROSITE; PS51864; ASTACIN; 1; level=0 XX Names: Astacin-like domain Peptidase family M12A domain Function: Astacin or M12A family zinc metalloproteases are found in bacteria and animals. They belong to the metzincin protease family and are synthesized as inactive precursors. The zinc atom in these enzymes acts as an electrophilic center to enhance the reactivity of a water molecule prior to nucleophilic attack on the carbonyl carbon of the scissile peptide bond. XX case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit end case XX case and DR PROSITE; PS00142; ZINC_PROTEASE; 1; trigger=no XX GO GO:0004222; F:metalloendopeptidase activity end case case GO GO:0008270; F:zinc ion binding end case XX case and KW Hydrolase KW Protease KW Metalloprotease end case case KW Zinc KW Metal-binding end case case KW Disulfide bond end case FT From: PS51864 FT DOMAIN from..to FT /note="Peptidase M12A #" FT ACT_SITE 95 FT Tag: catalytic; Condition: E FT BINDING 94 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 98 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT DISULFID 5..8 FT Tag: disulf; Condition: C-x*-C FT DISULFID 43..198 FT Tag: disulf; Condition: C-x*-C FT DISULFID 64..86 FT Tag: disulf; Condition: C-x*-C FT DISULFID 66..67 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 185-215; Related: None; Repeats: 1; Topology: Undefined; Example: P07584; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01212; DC Domain; TR PROSITE; PS51865; PDZ_GRASP; 1; level=0 XX Names: GRASP-type PDZ domain Function: Essentially all GRASPs contain a conserved N-terminal GRASP region, which comprises two tandem PDZ domains (PDZ1 and PDZ2), a classical protein- peptide interaction domain, and is responsible for GRASP homo-oligomerization and for the attachment to the Golgi membrane. XX CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane. XX GO GO:0007030; P:Golgi organization GO GO:0005794; C:Golgi apparatus XX KW Golgi apparatus KW Membrane XX FT From: PS51865 FT DOMAIN from..to FT /note="PDZ GRASP-type #" XX Chop: Nter=0; Cter=0; Size: 80-125; Related: None; Repeats: 2; Topology: Undefined; Example: Q04410; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01213; DC Domain; TR PROSITE; PS51866; MOP; 1; level=0 XX Names: Mop domain Function: Mop domains, which occur in a variety of bacterial and archeal proteins specifically bind molybdate (or tungstate). XX KW Molybdenum XX FT From: PS51866 FT DOMAIN from..to FT /note="Mop #" XX Chop: Nter=0; Cter=0; Size: 60-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q8FXI7; Scope: Bacteria Archaea; Pyrococcus Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01214; DC Domain; TR Metamotif; -; PS51865~PS51865 XX Names: GRASP region Function: Essentially all GRASPs contain a conserved N-terminal GRASP region, which comprises two tandem PDZ domains (PDZ1 and PDZ2), a classical protein- peptide interaction domain, and is responsible for GRASP homo-oligomerization and for the attachment to the Golgi membrane. XX DR PROSITE; PS51865; PDZ_GRASP; 2; trigger=yes XX FT From: PS51865~PS51865 FT REGION from..to+16 FT /note="GRASP #" XX Chop: Nter=0; Cter=0; Size: 175-230; Related: None; Repeats: 1-2; Topology: Cytoplasmic; Example: Q9BQQ3; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/22 // AC PRU01215; DC Domain; TR PROSITE; PS51867; ZF_RING_GID; 1; level=0 XX Names: Gid-type RING finger Function: The degenerated Gid-type RING finger is characterized by an incomplete series of Zn(2+) ion-ccordinating residues compared with the canonical RING finger, which encompasses eight Cys/His residues coordinating two Zn cations. A complete cysteine and histidine pattern is not necessarily critical for the E3 function. XX KW Zinc-finger XX FT From: PS51867 FT ZN_FING from..to FT /note="RING-Gid-type #" XX Chop: Nter=0; Cter=0; Size: 40-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q7SXR3; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01216; DC Domain; TR PROSITE; PS51868; PEPTIDASE_S39; 1; level=0 XX Names: Peptidase family S39 domain Function: A triad composed of a histidine, an aspartate and a serine residue constitute the active centre of the peptidase S39 family domain. XX case DE Contains: DE RecName: Full=Serine protease; DE EC=3.4.21.-; XX GO GO:0004252; F:serine-type endopeptidase activity XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51868 FT DOMAIN from..to FT /note="Peptidase S39 #" FT ACT_SITE 49 FT /note="For protease activity" FT Group: 1; Condition: H FT ACT_SITE 83 FT /note="For protease activity" FT Group: 1; Condition: D FT ACT_SITE 153 FT /note="For protease activity" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 180-200; Related: None; Repeats: 1; Topology: Undefined; Example: O73564; Scope: Viruses; Riboviria Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01217; DC Domain; TR PROSITE; PS51869; APP_E1; 1; level=0 XX Names: Amyloid precursor protein (APP) E1 domain Function: The E1 domain is a cysteine-rich region consisting of a growth factor like subdomain (GFLD), which binds heparin and can stimulate neurite outgrowth, and a copper-binding subdomain (CuBD) that binds Cu and Zn. XX CC -!- SIMILARITY: Belongs to the APP family. XX DR PROSITE; PS00319; APP_CUBD; 1; trigger=no XX GO GO:0008201; F:heparin binding case GO GO:0046914; F:transition metal ion binding XX KW Metal-binding KW Copper end case case KW Disulfide bond end case XX FT From: PS51869 FT DOMAIN from..to FT /note="E1 #" FT REGION from..94 FT /note="GFLD subdomain #" FT REGION 102..to FT /note="CuBD subdomain #" FT DISULFID 11..34 FT Tag: disulf; Condition: C-x*-C FT DISULFID 45..89 FT Tag: disulf; Condition: C-x*-C FT DISULFID 70..77 FT Tag: disulf; Condition: C-x*-C FT DISULFID 104..158 FT Tag: disulf; Condition: C-x*-C FT DISULFID 129..157 FT Tag: disulf; Condition: C-x*-C FT DISULFID 115..145 FT Tag: disulf; Condition: C-x*-C FT BINDING 118 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 122 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 139 FT /ligand="Cu(2+)" FT /ligand_id="ChEBI:CHEBI:29036" FT /ligand_label="#1" FT Group: 1; Condition: Y case FT SITE 141 FT /note="Required for Cu(2+) reduction" FT Condition: M end case XX Chop: Nter=0; Cter=0; Size: 155-175; Related: None; Repeats: 1; Topology: Undefined; Example: P12023; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01218; DC Domain; TR PROSITE; PS51870; APP_E2; 1; level=0 XX Names: Amyloid precursor protein (APP) E2 domain Function: The E2 domain forms an antiparallel dimer. E2 dimerization is a dynamic and reversible process and heparin binding to E2 shifts the association-dissociation equilibrium in favor of dimer. XX CC -!- SIMILARITY: Belongs to the APP family. XX GO GO:0008201; F:heparin binding XX FT From: PS51870 FT DOMAIN from..to FT /note="E2 #" XX Chop: Nter=0; Cter=0; Size: 185-210; Related: None; Repeats: 1; Topology: Undefined; Example: P12023; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01219; DC Domain; TR PROSITE; PS51871; PV_P1_PRO; 1; level=0 XX Names: Potyviridae P1 protease domain Function: The potyviral P1 protease domain bears the catalytic triad formed by histidine, aspartic and serine that is characteristic of the serine protease family. XX case DE Contains: DE RecName: Full=P1 proteinase; DE EC=3.4.-.-; XX GO GO:0004252; F:serine-type endopeptidase activity XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51871 FT DOMAIN from..to FT /note="Peptidase S30 #" FT ACT_SITE 54 FT /note="For P1 proteinase activity" FT Group: 1; Condition: H FT ACT_SITE 63 FT /note="For P1 proteinase activity" FT Group: 1; Condition: [DE] FT ACT_SITE 97 FT /note="For P1 proteinase activity" FT Group: 1; Condition: S case and FT SITE to..to+1 FT /note="Cleavage; by P1 proteinase" end case XX Chop: Nter=0; Cter=0; Size: 130-160; Related: None; Repeats: 1; Topology: Undefined; Example: P0CJ95; Scope: Viruses; Potyviridae Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01220; DC Domain; TR PROSITE; PS51872; ZF_ZBR; 1; level=0 XX Names: Zinc finger ZBR-type Function: The ZBR-type zinc finger is an autonomously folded domain with a central, twisted, four-stranded beta-sheet and two zinc ions on opposite ends of the sheet. XX case ( and and and ) or ( and and and ) GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51872 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="ZBR-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="ZBR-type #; atypical" else FT ZN_FING from..to FT /note="ZBR-type #; degenerate" end case FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 46 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 45-55; Related: None; Repeats: 1; Topology: Undefined; Example: Q66H04; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01221; DC Domain; TR PROSITE; PS51873; TRIAD; 1; level=0 XX Names: TRIAD supradomain Function: The cysteine and histidine rich TRIAD domain architecture is highly conserved and found only in eukaryotes. The three fingers that define the TRIAD supradomain always appear in the same order RING1-IBR-RING2. All characterized proteins containing the TRIAD supradomain have been found to possess E3 ligase activity. XX DR PROSITE; PS00518; ZF_RING_1; 1; trigger=no DR PROSITE; PS50089; ZF_RING_2; 1; trigger=no XX case or or or or or or GO GO:0046872; F:metal ion binding end case case GO GO:0000209; P:protein polyubiquitination GO GO:0061630; F:ubiquitin protein ligase activity GO GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process GO GO:0031624; F:ubiquitin conjugating enzyme binding GO GO:0000151; C:ubiquitin ligase complex end case XX case or or or or or or KW Metal-binding KW Zinc end case KW Zinc-finger case KW Transferase KW Ubl conjugation pathway end case XX FT From: PS51873 FT ZN_FING 5..56 FT /note="RING-type #" FT ZN_FING 75..138 FT /note="IBR-type" FT ZN_FING 165..194 FT /note="RING-type #; atypical" FT REGION from..to FT /note="TRIAD supradomain" FT ACT_SITE 178 FT Condition: C FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 100 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 117 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 120 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 4; Condition: C FT BINDING 128 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 4; Condition: C FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 4; Condition: H FT BINDING 138 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#4" FT Group: 4; Condition: C FT BINDING 165 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#5" FT Group: 5; Condition: C FT BINDING 168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#5" FT Group: 5; Condition: C FT BINDING 183 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#5" FT Group: 5; Condition: C FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#5" FT Group: 5; Condition: C case FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 6; Condition: C FT BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 6; Condition: C FT BINDING 202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 6; Condition: C FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 6; Condition: H else FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 7; Condition: C FT BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 7; Condition: C FT BINDING 202 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 7; Condition: H FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#6" FT Group: 7; Condition: C end case XX Chop: Nter=0; Cter=0; Size: 190-285; Related: None; Repeats: 1; Topology: Undefined; Example: Q924T7; Scope: Eukaryota Viruses; Mimivirus Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01222; DC Domain; TR PROSITE; PS51874; PCV_3C_PRO; 1; level=0 XX Names: Picornavirales 3C/3C-like protease domain Function: The 3C (for the family Picornaviridae) or 3C-like (3CL) protease (for other families) plays a central role in the cleavage of the viral precursor polyprotein. In addition to its key role in processing the polyprotein, 3C/3C-like protease is able to cleave a number of host proteins to remodel the cellular environment for virus reproduction. XX case or DE Contains: DE RecName: Full=Protease 3C; DE EC=3.4.22.28; DE AltName: Full=Picornain 3C; DE Short=P3C; else case DE Contains: DE RecName: Full=Picornain 3C-like protease; DE EC=3.4.22.-; DE Short=3C-like protease; else case DE Contains: DE RecName: Full=3C-like protease; DE EC=3.4.22.-; DE Short=3CL-PRO; end case XX case or CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus CC polyprotein. In other picornavirus reactions Glu may be substituted CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; end case XX case or or or GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51874 FT DOMAIN from..to FT /note="Peptidase C3 #" case FT ACT_SITE 41 FT /note="For protease 3C activity; Proton donor/acceptor" FT Group: 1; Condition: H FT ACT_SITE 78 FT /note="For protease 3C activity" FT Group: 1; Condition: [ED] FT ACT_SITE 164 FT /note="For protease 3C activity" FT Group: 1; Condition: C else case FT ACT_SITE 41 FT /note="For protease 3C activity" FT Group: 2; Condition: H FT ACT_SITE 78 FT /note="For protease 3C activity" FT Group: 2; Condition: [ED] FT ACT_SITE 164 FT /note="For protease 3C activity" FT Group: 2; Condition: C else case FT ACT_SITE 41 FT /note="For picornain 3C-like protease activity" FT Group: 3; Condition: H FT ACT_SITE 78 FT /note="For picornain 3C-like protease activity" FT Group: 3; Condition: [ED] FT ACT_SITE 164 FT /note="For picornain 3C-like protease activity" FT Group: 3; Condition: C else FT ACT_SITE 41 FT /note="For 3C-like protease activity" FT Group: 4; Condition: H FT ACT_SITE 78 FT /note="For 3C-like protease activity" FT Group: 4; Condition: [ED] FT ACT_SITE 164 FT /note="For 3C-like protease activity" FT Group: 4; Condition: C end case XX Chop: Nter=0; Cter=0; Size: 170-250; Related: None; Repeats: 1; Topology: Undefined; Example: P06209; Scope: Viruses; Riboviria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01223; DC Domain; TR PROSITE; PS51875; HAV_P48_PRO; 1; level=0 XX Names: Hypovirulence-associated virus (HAV) papain-like protease p48 domain Peptidase C8 domain Function: The HAV papain-like protease p48 is a cysteine protease, which forms the peptidase family C8. A Cys and a His catalytic residue are essential for autocatalytic cleavage between the cleavage site residues Gly and Ala located at the C-terminus of the domain. XX case DE + Contains: DE RecName: Full=Papain-like protease p48; DE EC=3.4.22.-; XX CC -!- FUNCTION: Papain-like protease p48 is a cysteine protease of the CC peptidase family C8. XX GO GO:0008234; F:cysteine-type peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51875 FT DOMAIN from..to FT /note="Peptidase C8 #" FT ACT_SITE 71 FT /note="For papain-like protease p48 activity" FT Group: 1; Condition: C FT ACT_SITE 118 FT /note="For papain-like protease p48 activity" FT Group: 1; Condition: H FT SITE to..to+1 FT /note="Cleavage; by papain-like protease p48" FT Condition: G-A XX Chop: Nter=0; Cter=0; Size: 130-140; Related: None; Repeats: 1; Topology: Undefined; Example: Q9YTU2; Scope: Viruses; Hypovirus Comments: None; XX # Revision 1.6 2019/11/22 // AC PRU01224; DC Domain; TR PROSITE; PS51876; PV_NPRO; 1; level=0 XX Names: Pestivirus N-terminal protease (Npro) domain Peptidase C53 domain Function: The pestivirus N-terminal protease Npro is a cysteine autoprotease that cleaves between its own C-terminus and the N-terminus of the core protein. Following the first cleavage reaction, Npro does not possess any proteolytic trans-activity but acts as a viral immediate effector to modulate the host cell's antiviral defenses. XX case DE + Contains: DE RecName: Full=N-terminal protease; DE Short=N-pro; DE EC=3.4.22.-; DE AltName: Full=Autoprotease p20; XX GO GO:0019082; P:viral protein processing GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case KW Inhibition of host IRF3 by virus KW Inhibition of host RLR pathway by virus KW Inhibition of host innate immune response by virus XX FT From: PS51876 FT DOMAIN from..to FT /note="Peptidase C53 #" FT ACT_SITE 49 FT /note="For N-terminal protease activity" FT Group: 1; Condition: H FT ACT_SITE 69 FT /note="For N-terminal protease activity" FT Group: 1; Condition: C case FT SITE to..to+1 FT /note="Cleavage; by autolysis" FT Condition: C-{P} end case XX Chop: Nter=0; Cter=0; Size: 165-175; Related: None; Repeats: 1; Topology: Undefined; Example: P19711; Scope: Viruses; Pestivirus Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01225; DC Domain; TR PROSITE; PS51877; HAV_P29_PRO; 1; level=0 XX Names: Hypovirulence-associated virus (HAV) papain-like protease p29 domain Peptidase C7 domain Function: The HAV papain-like protease p29 is a cysteine protease, which forms the peptidase family C7. A Cys and a His catalytic residue are essential for autocatalytic cleavage at a glycine dipeptide clevage site located at the C- terminus of the domain. XX case DE + Contains: DE RecName: Full=Papain-like protease p29; DE EC=3.4.22.-; XX CC -!- FUNCTION: Papain-like protease p29 is a cysteine protease of the CC peptidase family C7 that contributes to hypovirulence-associated traits CC like the reduction in conidiation and laccase activity, but not to CC virulence attenuation. Acts as suppressor of RNA-mediated gene CC silencing, also known as post-transcriptional gene silencing (PTGS), a CC mechanism of viral defense that limits the accumulation of viral RNAs. CC Enhances viral dsRNA accumulation and virus transmission. Also involved CC in the reduction in orange pigmentation of the host, an effect CC independent of the intrinsic protease activity. XX GO GO:0008234; F:cysteine-type peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51877 FT DOMAIN from..to FT /note="Peptidase C7 #" FT ACT_SITE 142 FT /note="For papain-like protease p29 activity" FT Group: 1; Condition: C FT ACT_SITE 195 FT /note="For papain-like protease p29 activity" FT Group: 1; Condition: H FT SITE to..to+1 FT /note="Cleavage; by papain-like protease p29" FT Condition: G-x XX Chop: Nter=0; Cter=0; Size: 245-255; Related: None; Repeats: 1; Topology: Undefined; Example: P10941; Scope: Viruses; Hypovirus Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01227; DC Domain; TR PROSITE; PS51879; RST; 1; level=0 XX Names: RST domain Function: The RST domain is a protein-protein interaction domain suggested to be critical for the interaction with several, mostly plant-specific transcription factors. XX FT From: PS51879 FT DOMAIN from..to FT /note="RST #" XX Chop: Nter=0; Cter=0; Size: 60-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q9STU1; Scope: Eukaryota; Viridiplantae Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01228; DC Domain; TR PROSITE; PS51880; TGS; 1; level=0 XX Names: TGS domain Function: The presence of the TGS domain in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role. XX FT From: PS51880 FT DOMAIN from..to FT /note="TGS #" XX Chop: Nter=0; Cter=0; Size: 45-90; Related: None; Repeats: 1; Topology: Undefined; Example: Q3K1Z4; Scope: Bacteria Eukaryota Archaea; Euryarchaeota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01229; DC Domain; TR PROSITE; PS51881; OCT; 1; level=0 XX Names: Obg C-terminal (OCT) domain Function: A potential role of the OCT domain in the regulation of the nucleotide-binding state has been suggested. XX FT From: PS51881 FT DOMAIN from..to FT /note="OCT #" XX Chop: Nter=0; Cter=0; Size: 70-95; Related: None; Repeats: 1; Topology: Undefined; Example: A0Q1T4; Scope: Bacteria Eukaryota; Magnoliopsida Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01230; DC Domain; TR PROSITE; PS51882; G_ALPHA; 1; level=0 XX Names: G-alpha domain Function: The G-alpha domain contains a binding site for guanine nucleotide and possesses GTPase activity. XX GO GO:0031683; F:G-protein beta/gamma-subunit complex binding GO GO:0003924; F:GTPase activity GO GO:0005525; F:GTP binding case GO GO:0046872; F:metal ion binding end case GO GO:0005834; C:heterotrimeric G-protein complex XX KW GTP-binding KW Nucleotide-binding KW Transducer case KW Metal-binding end case XX FT From: PS51882 FT DOMAIN from..to FT /note="G-alpha #" FT REGION 4..17 FT /note="G1 motif" FT REGION 146..154 FT /note="G2 motif" FT REGION 169..178 FT /note="G3 motif" FT REGION 238..245 FT /note="G4 motif" FT REGION 298..303 FT /note="G5 motif" FT BINDING 16 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: S FT BINDING 154 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: T XX Chop: Nter=0; Cter=0; Size: 310-490; Related: None; Repeats: 1; Topology: Undefined; Example: P87032; Scope: Eukaryota Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01231; DC Domain; TR PROSITE; PS51883; OBG; 1; level=0 XX Names: Obg domain Function: The Obg domain is a structural mimic of the acceptor arm of the A- site tRNA, which exhibits specific interactions with the ribosomal peptidyl- transferase center. XX GO GO:0042254; P:ribosome biogenesis XX FT From: PS51883 FT DOMAIN from..to FT /note="Obg #" XX Chop: Nter=0; Cter=0; Size: 130-210; Related: None; Repeats: 1; Topology: Undefined; Example: Q87SU2; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01232; DC Domain; TR PROSITE; PS51884; CHAPLIN; 1; level=0 XX Names: Chaplin domain Function: The chaplins self-assemble via their chaplin domains into amyloid- like filaments on the surface of the aerial hyphae and spores of streptomycetes. XX KW Amyloid XX FT From: PS51884 FT DOMAIN from..to FT /note="Chaplin #" XX Chop: Nter=0; Cter=0; Size: 35-45; Related: None; Repeats: 1; Topology: Undefined; Example: Q9L1J9; Scope: Bacteria; Streptomyces Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01233; DC Domain; TR PROSITE; PS51885; NEPRILYSIN; 1; level=0 XX Names: Neprilysin-like (M13) protease domain Function: The neprilysin (M13) family of endopeptidases are zinc- metalloenzymes, the majority of which are type II integral membrane proteins with their active sites facing the extracellular environment. XX CC -!- SIMILARITY: Belongs to the peptidase M13 family. XX case and DR PROSITE; PS00142; ZINC_PROTEASE; 1; trigger=no XX GO GO:0004222; F:metalloendopeptidase activity XX KW Hydrolase KW Metalloprotease KW Protease end case case KW Metal-binding KW Zinc end case case KW Disulfide bond end case XX FT From: PS51885 FT DOMAIN from..to FT /note="Peptidase M13 #" FT ACT_SITE 510 FT Group: 1; Condition: E FT ACT_SITE 575 FT /note="Proton donor" FT Group: 1; Condition: D FT BINDING 509 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 513 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 571 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 2; Condition: E FT DISULFID 2..7 FT Tag: disulf; Condition: C-x*-C FT DISULFID 25..659 FT Tag: disulf; Condition: C-x*-C FT DISULFID 33..619 FT Tag: disulf; Condition: C-x*-C FT DISULFID 89..338 FT Tag: disulf; Condition: C-x*-C FT DISULFID 175..183 FT Tag: disulf; Condition: C-x*-C FT DISULFID 546..671 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 600-800; Related: None; Repeats: 1; Topology: Undefined; Example: P0C2B4; Scope: Eukaryota; Metazoa Bacteria; Lactobacillales Viruses; Mimivirus Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01234; DC Domain; TR PROSITE; PS51886; TLDC; 1; level=0 XX Names: Tre2/Bub2/Cdc16 (TBC), lysin motif (LysM), domain catalytic (TLDc) domain Function: The TLDc domain is present in several proteins that share a protective function against oxidative stress (OS). The TLDc domain alone is able to confer oxidative resistance properties to all the TLDc members. XX FT From: PS51886 FT DOMAIN from..to FT /note="TLDc #" XX Chop: Nter=0; Cter=0; Size: 150-260; Related: None; Repeats: 1; Topology: Undefined; Example: E4ZUJ1; Scope: Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01235; DC Domain; TR PROSITE; PS51887; APHTHOVIRUS_LPRO; 1; level=0 XX Names: Aphthovirus leader protease (L(pro)) domain Peptidase C28 domain Function: Aphthovirus L(pro) is a papain-like proteinase that self-cleaves from the nascent viral polyprotein precursor during infection and plays an important role in viral pathogenesis. L(pro) is known to contribute to virus propagation by suppressing host antiviral activity. L(pro) has an antagonistic effect on host antiviral responses via at least three mechanisms. XX case GO GO:0039579; P:suppression by virus of host ISG15-protein conjugation GO GO:0019049; P:virus-mediated perturbation of host defense response GO GO:0039503; P:suppression by virus of host innate immune response GO GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway XX KW Hydrolase KW Protease KW Thiol protease KW Modulation of host ubiquitin pathway by virus KW Modulation of host ubiquitin pathway by viral deubiquitinase KW Inhibition of host ISG15 by virus KW Viral immunoevasion KW Inhibition of host innate immune response by virus KW Inhibition of host interferon signaling pathway by virus end case XX FT From: PS51887 FT DOMAIN from..to FT /note="Peptidase C28 #" FT ACT_SITE 23 FT /note="For leader protease activity" FT Group: 1; Condition: C FT ACT_SITE 120 FT /note="For leader protease activity" FT Group: 1; Condition: H FT ACT_SITE 135 FT /note="For leader protease activity" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 150-160; Related: None; Repeats: 1; Topology: Undefined; Example: P03311; Scope: Viruses; Aphthovirus Comments: None; XX # Revision 1.10 2023/12/14 // AC PRU01236; DC Domain; TR PROSITE; PS51888; CLIP; 1; level=0 XX Names: Clip domain Function: Although the functions of clip domains are not completely clear, the clip domain in arthropods has been demonstrated to act in the regulation of proteinase activity, protein-protein interaction and bactericidal activities. XX CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted' CC together usually by 3 conserved disulfide bonds forming a clip-like CC compact structure. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily. XX case KW Disulfide bond end case XX FT From: PS51888 FT DOMAIN from..to FT /note="Clip #" FT DISULFID 2..52 FT Tag: disulf; Condition: C-x*-C FT DISULFID 12..42 FT Tag: disulf; Condition: C-x*-C FT DISULFID 18..53 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 40-65; Related: None; Repeats: 1; Topology: Undefined; Example: Q9VB68; Scope: Eukaryota; Arthropoda Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU01237; DC Domain; TR PROSITE; PS51889; RUBV_NS_PRO; 1; level=0 XX Names: Rubella virus (RUBV) nonstructural (NS) protease domain Function: This RUBV NS protease domain is a papain-like protease with catalytic dyad of Cys and His. XX case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Zn(2+) is necessary for the protease activity. The protease can CC also function efficiently with Cd(2+) and Co(2+) end case CC -!- PTM: Non-structural polyprotein p200: Specific enzymatic cleavage by CC its own cysteine protease yield mature proteins p150 and p90. XX case GO GO:0046872; F:metal ion binding end case case GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case case KW Metal-binding KW Zinc end case XX FT From: PS51889 FT DOMAIN from..to FT /note="Peptidase C27 #" FT REGION 153..184 FT /note="Interaction with host CALM1" FT REGION 194..229 FT /note="EF-hand-like" FT ACT_SITE 153 FT /note="For cysteine protease activity" FT Group: 1; Condition: C FT ACT_SITE 274 FT /note="For cysteine protease activity" FT Group: 1; Condition: H FT BINDING 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C FT BINDING 228 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: C FT BINDING 274 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 2; Condition: H case FT SITE to..to+1 FT /note="Cleavage; autocatalytic" FT Condition: G-G end case XX Chop: Nter=0; Cter=0; Size: 295-310; Related: None; Repeats: 1; Topology: Undefined; Example: Q86500; Scope: Viruses; Rubivirus Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01238; DC Domain; TR PROSITE; PS51890; DAZ; 1; level=0 XX Names: DAZ domain Function: The function of the DAZ domain is not known, but may be involved in protein-protein interactions. XX CC -!- SIMILARITY: Belongs to the RRM DAZ family. XX GO GO:0007281; P:germ cell development XX KW Differentiation XX FT From: PS51890 FT DOMAIN from..to FT /note="DAZ #" XX Chop: Nter=0; Cter=0; Size: 20-30; Related: None; Repeats: 1; Topology: Undefined; Example: Q76CY5; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01239; DC Domain; TR PROSITE; PS51891; CENPV_GFA; 1; level=0 XX Names: CENP-V/GFA domain Function: At the C-terminal end, CENP-V possesses an evolutionally conserved domain that comprises an array of seven cysteines and shows high structural similarity to glutathione-dependent formaldehyde-activating enzyme (Gfa), an enzyme responsible for formaldehyde detoxification in prokaryotes. CENP-V could be an enzyme that scavenges the formaldehyde produced in histone demethylation reactions. XX case and CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 2 Zn(2+) ions per subunit else case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case XX case or GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS51891 FT DOMAIN from..to FT /note="CENP-V/GFA" FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: C FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: C FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: C FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C FT BINDING 75 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="structural" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 110-155; Related: None; Repeats: 1; Topology: Undefined; Example: Q7Z7K6; Scope: Eukaryota Bacteria; Pseudomonadota Comments: None; XX # Revision 1.5 2023/01/26 // AC PRU01240; DC Domain; TR PROSITE; PS51892; SUBTILASE; 1; level=0 XX Names: Serine proteases, subtilase domain Function: Subtilases are an extensive family of serine proteases which occur in Archaea, Bacteria, fungi, yeasts, and higher eukaryotes. Their catalytic activity is provided by a charge relay system similar to that of the trypsin family of serine proteases but which evolved by independent convergent evolution. XX case DR PROSITE; PS00136; SUBTILASE_ASP; 1; trigger=no end case case DR PROSITE; PS00137; SUBTILASE_HIS; 1; trigger=no end case case DR PROSITE; PS00138; SUBTILASE_SER; 1; trigger=no end case XX CC -!- SIMILARITY: Belongs to the peptidase S8 family. XX case GO GO:0004252; F:serine-type endopeptidase activity XX KW Hydrolase KW Protease KW Serine protease end case XX FT From: PS51892 FT DOMAIN from..to FT /note="Peptidase S8" FT ACT_SITE 31 FT /note="Charge relay system" FT Group: 1; Condition: D FT ACT_SITE 66 FT /note="Charge relay system" FT Group: 1; Condition: H FT ACT_SITE 230 FT /note="Charge relay system" FT Group: 1; Condition: S XX Chop: Nter=0; Cter=0; Size: 240-560; Related: None; Repeats: 1; Topology: Undefined; Example: B8N106; Scope: Eukaryota Bacteria Archaea; Euryarchaeota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01241; DC Domain; TR PROSITE; PS51893; AKAP_CAM_BD; 1; level=0 XX Names: AKAP calmodulin (CaM)-binding motif Function: The AKAP CaM-binding motif contains hydrophobic amino acids in a 1-4-7-8 pattern within an helix . XX GO GO:0005516; F:calmodulin binding XX KW Calmodulin-binding XX FT From: PS51893 FT MOTIF from..to FT /note="AKAP CaM-binding #" XX Chop: Nter=0; Cter=0; Size: 20-25; Related: None; Repeats: 1; Topology: Undefined; Example: P24275; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01242; DC Domain; TR PROSITE; PS51894; CV_3CL_PRO; 1; level=0 XX Names: Caliciviridae (CV) 3C-like protease (3CLpro) domain Function: The generation of mature Caliciviridae proteins requires that proteolytic clevages be effected at specific sites of the large polyprotein translated from the viral genomic RNA. This polyprotein processing is carried out by a 3C-like cysteine protease (3CLpro). The CV 3CLpro domain is predicted to contain a catalytic triad constituted of His, Asp and Cys residues, where the Cys likely represents the nucleophilic residue and Asp the acidic residue. XX DE + RecName: EC=3.4.22.66; case CC -!- CATALYTIC ACTIVITY: CC Reaction=Endopeptidase with a preference for cleavage when the P1 CC position is occupied by Glu-|-Xaa and the P1' position is occupied by CC Gly-|-Yaa.; EC=3.4.22.66; XX GO GO:0004197; F:cysteine-type endopeptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51894 FT DOMAIN from..to FT /note="Peptidase C24" FT ACT_SITE 32 FT /note="For 3CLpro activity" FT Group: 1; Condition: H FT ACT_SITE 53 FT /note="For 3CLpro activity" FT Group: 1; Condition: [DE] FT ACT_SITE 116 FT /note="For 3CLpro activity" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 130-160; Related: None; Repeats: 1; Topology: Undefined; Example: Q9QEJ5; Scope: Viruses; Caliciviridae Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01243; DC Domain; TR PROSITE; PS51895; AA1; 1; level=0 XX Names: Alt a 1 (AA1)-like domain Function: AA1-like proteins are fungal toxins that can induce plant defense responses and cell death. They may contribute to virulence by protecting the cell wall, thus allowing fungal growth to be maintained and preventing the recognition of degraded beta-1,3-glucan by the plant. AA1 proteins comprise ~150 amino acids and contain two pairs of highly conserved disulfide bonds. XX case KW Disulfide bond end case XX FT From: PS51895 FT DOMAIN from..to FT /note="AA1-like" FT DISULFID 40..55 FT Tag: disulf; Condition: C-x*-C FT DISULFID 97..109 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 105-125; Related: None; Repeats: 1; Topology: Undefined; Example: Q5EZ82; Scope: Eukaryota; Pezizomycotina Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01244; DC Domain; TR PROSITE; PS51896; ZF_C4H2; 1; level=0 XX Names: Zinc finger C4H2-type Function: ZC4H2, which belongs to a conserved gene family found in all metazoans, plays an important role during embryonic development of the central and peripheral nervous systems. The ZC4H2 gene encodes a zinc-finger protein with a C-terminal domain, which includes a putative C4H2 zinc-finger characterized by four cysteine residues and two histidine residues, and a coiled-coil domain. XX case and and and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51896 case and and and and and FT ZN_FING 9..26 FT /note="C4H2-type #" else case and and and and and FT ZN_FING 9..26 FT /note="C4H2-type #; atypical" else FT ZN_FING 9..26 FT /note="C4H2-type #; degenerate" end case XX Chop: Nter=0; Cter=0; Size: 40-45; Related: None; Repeats: 1; Topology: Undefined; Example: Q68FG0; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01245; DC Domain; TR PROSITE; PS51897; ANNEXIN_2; 1; level=0 XX Names: Annexin repeat Function: Annexins are a group of calcium-binding proteins that associate reversibly with membranes. Each of these proteins consist of a unique N- terminal domain followed by four or eight copies (in annexin A6) of a conserved segment of approximately 70 residues. Each of the repeats has the potential to have a type II Ca(2+)-binding bipartite motif, located on two different alpha-helices (GxGT-(38-40 residues)-D/E), but typically some of them are non-functional. XX DR PROSITE; PS00223; ANNEXIN_1; 4-8; trigger=no XX CC -!- SIMILARITY: Belongs to the annexin family. XX GO GO:0005509; F:calcium ion binding GO GO:0005544; F:calcium-dependent phospholipid binding XX KW Annexin KW Calcium KW Calcium/phospholipid-binding XX FT From: PS51897 FT REPEAT from..to FT /note="Annexin #" XX Chop: Nter=0; Cter=0; Size: 60-80; Related: None; Repeats: 4-8; Topology: Undefined; Example: P09525; Scope: Eukaryota Comments: None; XX # Revision 1.4 2019/11/22 // AC PRU01246; DC Domain; TR PROSITE; PS51898; TYR_RECOMBINASE; 1; level=0 XX Names: Tyrosine recombinase domain Function: Tyrosine-type site-specific recombinases catalyze a variety of sequence-specific DNA rearrangement in biological systems, including the integration and excision of phage genomes into and out of their bacterial hosts, conjugative transposition, resolution of catenated DNA circles, regulation of plasmid copy number, DNA excision to control gene expression for nitrogen fixation in Anabaena and DNA inversions controlling expression of cell surface proteins or DNA replication. XX CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XX GO GO:0003677; F:DNA binding GO GO:0009037; F:tyrosine-based site-specific recombinase activity XX KW DNA recombination XX FT From: PS51898 FT DOMAIN from..to FT /note="Tyr recombinase #" FT ACT_SITE 41 FT Condition: R FT ACT_SITE 66 FT Condition: K FT ACT_SITE 134 FT Condition: H FT ACT_SITE 137 FT Condition: R FT ACT_SITE 160 FT Condition: [HW] FT ACT_SITE 170 FT /note="O-(3'-phospho-DNA)-tyrosine intermediate" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: 140-220; Related: None; Repeats: 1; Topology: Undefined; Example: P9WMB3; Scope: Bacteria Viruses Archaea Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01247; DC Domain; TR PROSITE; PS51899; TYR_RECOMBINASE_FLP; 1; level=0 XX Names: Flp-type tyrosine recombinase domain Function: The yeast Flp recombinase is a tyrosine site-specific recombinase responsible for the control of plasmid copy number. All members of the tyrosine, or lambda integrase family of site-specific recombinases proceed via a 3' covalent phosphotyrosine intermediate to catalyze a variety of DNA rearrangements, including insertions, deletions, and inversions, depending on the location and orientation of cognate recombination target sites. XX CC -!- SIMILARITY: Belongs to the 'phage' integrase family. XX case GO GO:0015074; P:DNA integration GO GO:0006310; P:DNA recombination XX KW DNA integration KW DNA recombination end case XX FT From: PS51899 FT DOMAIN from..to FT /note="Tyr recombinase Flp-type #" FT ACT_SITE 207 FT /note="O-(3'-phospho-DNA)-tyrosine intermediate" FT Condition: Y XX Chop: Nter=0; Cter=0; Size: 280-290; Related: None; Repeats: 1; Topology: Undefined; Example: P13769; Scope: Eukaryota; Saccharomycetaceae Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01248; DC Domain; TR PROSITE; PS51900; CB; 1; level=0 XX Names: Core-binding (CB) domain Function: The core-binding (CB) domain, which interacts primarily with the major groove on the attachment site and facilitates binding to the core DNA sequence, is widely conserved among viral, eubacterial and archaeal recombinases. It is also involved in protein-protein interactions. XX GO GO:0003677; F:DNA binding XX KW DNA-binding XX FT From: PS51900 FT DOMAIN from..to FT /note="Core-binding (CB) #" XX Chop: Nter=0; Cter=0; Size: 65-110; Related: None; Repeats: 1; Topology: Undefined; Example: P9WMB3; Scope: Bacteria Viruses Archaea Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01249; DC Domain; TR PROSITE; PS51901; ACP_MB; 1; level=0 XX Names: Archaeal CBS proteins (ACP)-type metal binding (MB) domain Function: An archaeal family of CBS domain (see ) proteins that are able to function as electron transfer proteins contains a small (~35 amino acids) C-terminal metal-binding (MB) domain containing four cysteine residues arranged in a Cys-X(2)-Cys-X(14-19)-Cys-X(1-4)-Cys motif. The ACP-type MB domain can bind several metals, with iron and zinc being the most abundant metals. XX case KW Metal-binding KW Iron KW Zinc end case XX FT From: PS51901 FT DOMAIN from..to FT /note="ACP-type MB #" FT BINDING 6 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Condition: C FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 9 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Condition: C FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 25 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Condition: C FT BINDING 25 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 28 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT Group: 1; Condition: C FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 25-40; Related: None; Repeats: 1; Topology: Undefined; Example: P50100; Scope: Archaea; Euryarchaeota Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01250; DC Domain; TR PROSITE; PS51902; CLPX_ZB; 1; level=0 XX Names: ClpX zinc binding (ZB) domain Function: ClpX consists of an NH(2)-terminal zinc binding (ZB) domain that is involved in substrate and cofactor recognition and a AAA(+) domain that arranges into a hexamer in an ATP-dependent manner. The ClpX ZB domain contains the characteristic pattern C-X(2)-C-X(18)-C-X(2)-C of four cysteine residues and forms a constitutive dimer that is essential for the degradation of some ClpX substrates such as lambdaO and MuA but is not required for the degradation of other substrates such as green fluorescent protein SsrA. XX CC -!- SIMILARITY: Belongs to the ClpX chaperone family. XX GO GO:0051082; F:unfolded protein binding GO GO:0006457; P:protein folding case GO GO:0046983; F:protein dimerization activity GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Chaperone XX FT From: PS51902 FT DOMAIN from..to FT /note="ClpX-type ZB #" FT BINDING 13 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 16 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 35 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 45-60; Related: None; Repeats: 1; Topology: Undefined; Example: Q6G177; Scope: Bacteria Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01251; DC Domain; TR PROSITE; PS51903; CLP_R; 1; level=0 XX Names: Clp repeat (R) domain Function: The Clp repeat (R) domain contains two repeats and is involved in substrate binding and interaction with adaptor proteins. XX KW Repeat XX FT From: PS51903 FT DOMAIN from..to FT /note="Clp R #" FT REGION 4..69 FT /note="Repeat #1" FT REGION 82..to FT /note="Repeat #2" XX Chop: Nter=0; Cter=0; Size: 130-300; Related: None; Repeats: 1; Topology: Undefined; Example: Q89YY3; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01252; DC Domain; TR PROSITE; PS51904; GLYCOSYL_HYDROL_F25_2; 1; level=0 XX Names: Chalaropsis (Ch)-type lyzozyme domain Glycosyl hydrolases family 25 (GH25) domain Function: The Ch-type lysozymes family GH25 domain exhibits both beta-1,4-N- acetylmuramidase and beta-1,4-N,6-O-diacetylmuramidase activities and its evolutionary spread is diverse, comprising bacterial, viral (mainly phage) and eukaryotic representatives. XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 25 family. XX case DR PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1; trigger=no end case XX case GO GO:0003824; F:catalytic activity GO GO:0019835; P:cytolysis GO GO:0042742; P:defense response to bacterium GO GO:0016798; F:hydrolase activity, acting on glycosyl bonds GO GO:0008152; P:metabolic process GO GO:0016787; F:hydrolase activity GO GO:0003796; F:lysozyme activity GO GO:0009253; P:peptidoglycan catabolic process GO GO:0016998; P:cell wall macromolecule catabolic process XX KW Antimicrobial KW Bacteriolytic enzyme KW Glycosidase KW Hydrolase end case FT From: PS51904 FT DOMAIN from..to FT /note="Ch-type lysozyme #" FT ACT_SITE 6 FT Group: 1; Condition: D FT ACT_SITE 94 FT Group: 1; Condition: D FT ACT_SITE 96 FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 190-230; Related: None; Repeats: 1; Topology: Undefined; Example: P34020; Scope: Eukaryota Bacteria Viruses Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01253; DC Domain; TR PROSITE; PS51905; ZF_UBZ1; 1; level=0 XX Names: Zinc finger UBZ1-type Function: The ubiquitin-binding zinc finger (UBZ) is a type of zinc- coordinating beta-beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families. Type 1 UBZs are CCHH-type zinc fingers found in tandem UBZ domains of TAX1-binding protein 1 (TAX1BP1). XX KW Zinc-finger case and and and KW Zinc KW Metal-binding end case XX FT From: PS51905 case and and and FT ZN_FING from..to FT /note="UBZ1-type #" else case and and and FT ZN_FING from..to FT /note="UBZ1-type #; atypical" else FT ZN_FING from..to FT /note="UBZ1-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 20-30; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9V9Y9; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01254; DC Domain; TR PROSITE; PS51906; ZF_UBZ2; 1; level=0 XX Names: Zinc finger UBZ2-type Function: The ubiquitin-binding zinc finger (UBZ) is a type of zinc- coordinating beta-beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families. Type 2 UBZs are CCHC-type zinc fingers found in FAAP20 which is a subunit of the Fanconi anemia (FA) core complex. XX CC -!- DOMAIN: The UBZ2-type zinc finger binds both 'Lys-48'-and 'Lys-63'- CC linked polyubiquitin with preference for 'Lys-63'-linked polyubiquitin. XX GO GO:0043130; F:ubiquitin binding GO GO:0043240; C:Fanconi anaemia nuclear complex case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51906 case and and and FT ZN_FING from..to FT /note="UBZ2-type #" else case and and and FT ZN_FING from..to FT /note="UBZ2-type #; atypical" else FT ZN_FING from..to FT /note="UBZ2-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 35-40; Related: None; Repeats: 1; Topology: Undefined; Example: Q6NZ36; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01255; DC Domain; TR PROSITE; PS51907; ZF_UBZ3; 1; level=0 XX Names: Zinc finger UBZ3-type Function: The ubiquitin-binding zinc finger (UBZ) is a type of zinc- coordinating beta-beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families. Type 3 UBZs are CCHH-type zinc fingers found only in the Y-family translesion polymerase eta. XX CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. XX GO GO:0042276; P:error-prone translesion synthesis GO GO:0035861; C:site of double-strand break GO GO:0009314; P:response to radiation case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger KW DNA damage KW DNA repair XX FT From: PS51907 case and and and FT ZN_FING from..to FT /note="UBZ3-type #" else case and and and FT ZN_FING from..to FT /note="UBZ3-type #; atypical" else FT ZN_FING from..to FT /note="UBZ3-type #; degenerate" end case FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 11 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 27 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 30-40; Related: None; Repeats: 1; Topology: Undefined; Example: Q9Y253; Scope: Eukaryota Comments: None; XX # Revision 1.8 2022/11/19 // AC PRU01256; DC Domain; TR PROSITE; PS51908; ZF_UBZ4; 1; level=0 XX Names: Zinc finger UBZ4-type Function: The ubiquitin-binding zinc finger (UBZ) is a type of zinc- coordinating beta-beta-alpha fold domain found mainly in proteins involved in DNA repair and transcriptional regulation. UBZ domains coordinate a zinc ion with cysteine or histidine residues; depending on their amino acid sequence, UBZ domains are classified into several families. Type 4 UBZs are CCHC-type zinc fingers found in Y-family translesion polymerase kappa, Werner helicase- interacting protein 1 (WRNIP1), and Rad18. XX case and and and GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger KW DNA damage KW DNA repair XX FT From: PS51908 case and and and FT ZN_FING from..to FT /note="UBZ4-type #" else case and and and FT ZN_FING from..to FT /note="UBZ4-type #; atypical" else FT ZN_FING from..to FT /note="UBZ4-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 19 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 20-35; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9UBT6; Scope: Eukaryota Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01257; DC Domain; TR PROSITE; PS51909; LYSOZYME_I; 1; level=0 XX Names: Invertebrate (I)-type lysozyme domain Function: I-type lysozymes have been identified in phylogenetically diverse organisms, including mollusca, nematoda, annelida, arthropoda and echinodermata. I-type lysozymes play an important role in immunity and digestion in invertebrates and are usually regarded as the first barrier against pathogens. I-type lysozymes exert multiple activities, such as muramidase, isopeptidase, chitinase, and non-enzymatic antibacterial activities. XX case DE + RecName: EC=3.2.1.17; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and CC between N-acetyl-D-glucosamine residues in chitodextrins.; CC EC=3.2.1.17; end case CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 22 family. Type-I CC lysozyme subfamily. case GO GO:0003824; F:catalytic activity GO GO:0019835; P:cytolysis GO GO:0042742; P:defense response to bacterium GO GO:0016798; F:hydrolase activity, acting on glycosyl bonds GO GO:0008152; P:metabolic process GO GO:0016787; F:hydrolase activity XX KW Antimicrobial KW Bacteriolytic enzyme KW Glycosidase KW Hydrolase KW Antibiotic end case case KW Disulfide bond end case XX FT From: PS51909 FT DOMAIN from..to FT /note="I-type lysozyme #" FT ACT_SITE 16 FT /note="Proton donor" FT Group: 1; Condition: E FT ACT_SITE 26 FT /note="Nucleophile" FT Group: 1; Condition: D FT DISULFID 8..91 FT Tag: disulf; Condition: C-x*-C FT DISULFID 11..123 FT Tag: disulf; Condition: C-x*-C FT DISULFID 13..19 FT Tag: disulf; Condition: C-x*-C FT DISULFID 23..32 FT Tag: disulf; Condition: C-x*-C FT DISULFID 45..73 FT Tag: disulf; Condition: C-x*-C FT DISULFID 63..69 FT Tag: disulf; Condition: C-x*-C FT DISULFID 87..105 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 110-130; Related: None; Repeats: 1; Topology: Undefined; Example: Q8IU26; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2019/11/22 // AC PRU01258; DC Domain; TR PROSITE; PS51910; GH18_2; 1; level=0 XX Names: Glycosyl hydrolases family 18 (GH18) domain Function: The GH18 family contains hydrolytic enzymes with chitinase or endo- N-acetyl-beta-D-glucosaminidase (ENGase) activity as well as chitinase like lectins (chi-lectins/proteins (CLPs). Chitinases (EC 3.2.1.14) are hydrolytic enzymes that cleave the beta-1,4-bond releasing oligomeric, dimeric (chitobiose) or monomeric (N-actetylglucosamine, GlcNAc) products. ENGases (EC 3.2.1.96) hydrolyze the beta-1,4 linkage in the chitobiose core of N- linked glycans from glycoproteins leaving one GlcNAc residue on the substrate. CLPs do not display chitinase activity but some of them have been reported to have specific functions and carbohydrate binding property. XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. case XX DR PROSITE; PS01095; GH18_1; 1; trigger=no XX KW Hydrolase KW Glycosidase end case case KW Disulfide bond end case XX FT From: PS51910 FT DOMAIN from..to FT /note="GH18 #" FT ACT_SITE 120 FT /note="Proton donor" FT Tag: ACT_SITE; Condition: E case FT BINDING 51..52 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT BINDING 78..81 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT BINDING 183..186 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" end case FT BINDING 121 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT Group: 1; Condition: Y FT BINDING 302 FT /ligand="chitin" FT /ligand_id="ChEBI:CHEBI:17029" FT Group: 1; Condition: W FT DISULFID 5..27 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 250-490; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BWS9; Scope: Eukaryota Bacteria Viruses; Alphabaculovirus Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01259; DC Domain; TR PROSITE; PS51911; C2_AIDA; 1; level=0 XX Names: C2 Aida-type domain Function: The Aida-type C2 domain associates with membranes via a novel extended positively charged surface - the basic loop connecting strands beta7' and beta8, and probably the positively CBR3 loop. XX CC -!- SIMILARITY: Belongs to the AIDA family. XX FT From: PS51911 FT DOMAIN from..to FT /note="C2 Aida-type #" XX Chop: Nter=0; Cter=0; Size: 140-155; Related: None; Repeats: 1; Topology: Undefined; Example: Q6PBN2; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.1 2020/01/03 // AC PRU01260; DC Domain; TR PROSITE; PS51912; DMAP1_BIND; 1; level=0 XX Names: DMAP1-binding domain Function: The DMAP1-binding domain is a ~120-amino acid protein-protein interaction module that binds notably DMAP1, a transcriptional co-repressor. XX FT From: PS51912 FT DOMAIN from..to FT /note="DMAP1-binding #" XX Chop: Nter=0; Cter=0; Size: 90-130; Related: None; Repeats: 1; Topology: Undefined; Example: Q24K09; Scope: Eukaryota Comments: None; XX # Revision 1.1 2020/01/17 // AC PRU01261; DC Domain; TR PROSITE; PS51913; HTH_HARE; 1; level=0 XX Names: HARE-type HTH domain ASXN domain Function: The HARE-type HTH domain adopts the winged helix-turn-helix fold and is predicted to bind DNA. XX FT From: PS51913 FT DOMAIN from..to FT /note="HTH HARE-type #" XX Chop: Nter=0; Cter=0; Size: 65-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q5M1S8; Scope: Bacteria Eukaryota Comments: None; XX # Revision 1.2 2020/02/27 // AC PRU01262; DC Domain; TR PROSITE; PS51914; MRH; 1; level=0 XX Names: MRH domain Function: The MRH domain can function in protein-carbohydrate and protein- protein interactions. XX case KW Disulfide bond end case FT From: PS51914 FT DOMAIN from..to FT /note="MRH #" FT DISULFID 3..37 FT Tag: disulf; Condition: C-x*-C FT DISULFID 47..54 FT Tag: disulf; Condition: C-x*-C FT DISULFID 96..129 FT Tag: disulf; Condition: C-x*-C FT DISULFID 110..141 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 90-240; Related: None; Repeats: 1; Topology: Undefined; Example: Q96DZ1; Scope: Eukaryota Comments: None; XX # Revision 1.1 2020/02/13 // AC PRU01263; DC Domain; TR PROSITE; PS51915; ZAD; 1; level=0 XX Names: Zinc finger-associated domain (ZAD) C4Dm domain Function: The ZAD is a protein-protein interaction module with the capability to form homodimers. XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51915 FT DOMAIN from..to FT /note="ZAD #" FT BINDING 3 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 6 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 70-90; Related: None; Repeats: 1; Topology: Undefined; Example: Q9VHM6; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2022/11/19 // AC PRU01264; DC Domain; TR PROSITE; PS51916; DEUBAD; 1; level=0 XX Names: DEUBAD (DEUBiquitinase ADaptor) domain Uch37-binding domain ASXH domain ASXM domain Function: The DEUBAD domain stabilizes different conformations of the UCH37- like domain (ULD) to modulate the activity of the ubiquitin (Ub) C-terminal hydrolase (UCH) family of deubiquitinases (DUBs). XX FT From: PS51916 FT DOMAIN from..to FT /note="DEUBAD #" XX Chop: Nter=0; Cter=0; Size: 100-130; Related: None; Repeats: 1; Topology: Undefined; Example: Q7K2G1; Scope: Eukaryota Comments: None; XX # Revision 1.1 2020/03/03 // AC PRU01265; DC Domain; TR PROSITE; PS51917; PRU; 1; level=0 XX Names: Pru (pleckstrin-like receptor for the Ub) domain ubiquitin-binding domain (UBD) Function: The Pru domain binds K48-linked diubiquitin. XX case CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. end case XX GO GO:0043130; F:ubiquitin binding case GO GO:0070628; F:proteasome binding XX KW Proteasome KW Cytoplasm KW Nucleus end case XX FT From: PS51917 FT DOMAIN from..to FT /note="Pru #" XX Chop: Nter=0; Cter=0; Size: 110-135; Related: None; Repeats: 1; Topology: Undefined; Example: Q7K2G1; Scope: Eukaryota Comments: None; XX # Revision 1.1 2020/03/06 // AC PRU01266; DC Domain; TR PROSITE; PS51918; RADICAL_SAM; 1; level=0 XX Names: Radical SAM core domain Function: The radical SAM enzymes biochemically characterized to date have in common the cleavage of the [4Fe-4S]1+-SAM complex to [4Fe-4S]2+-Met and the 5'-deoxyadenosyl radical, which abstracts a hydrogen atom from the substrate to initiate a radical mechanism. XX case CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; XX GO GO:0051539; F:4 iron, 4 sulfur cluster binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Iron KW Iron-sulfur KW S-adenosyl-L-methionine KW 4Fe-4S end case XX FT From: PS51918 FT DOMAIN from..to FT /note="Radical SAM core #" FT BINDING 15 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Group: 1; Condition: C FT BINDING 19 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Group: 1; Condition: C FT BINDING 22 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="4Fe-4S-S-AdoMet" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 200-300; Related: None; Repeats: 1; Topology: Undefined; Example: Q5YT08; Scope: Bacteria Eukaryota Archaea Viruses Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01267; DC Domain; TR PROSITE; PS51919; X4E; 1; level=0 XX Names: Sarbecovirus X4e domain Function: The Sarbecovirus accessory protein X4, also called 7a or U122, is likely to be a type I membrane protein, with the amino-terminal hydrophilic domain oriented inside the lumen of the ER/Golgi or on the surface of the cell membrane or virus particle, depending on the localization of the protein. It has been suggested that X4e contains a binding site for the alpha(L) integrin subunit I-domain of LFA-1. XX CC -!- FUNCTION: Non-structural protein which is dispensable for virus CC replication in cell culture. CC -!- SUBCELLULAR LOCATION: Virion. Host endoplasmic reticulum membrane; CC Single-pass membrane protein. Host endoplasmic reticulum-Golgi CC intermediate compartment membrane; Single-pass type I membrane CC protein. Host Golgi apparatus membrane; Single-pass membrane CC protein. CC -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum CC localization for type I membrane proteins. XX GO GO:0016020; C:membrane GO GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane GO GO:0044167; C:host cell endoplasmic reticulum membrane GO GO:0039646; P:perturbation by virus of host G0/G1 transition checkpoint GO GO:0044178; C:host cell Golgi membrane XX case KW Disulfide bond end case KW G0/G1 host cell cycle checkpoint dysregulation by virus KW Host Golgi apparatus KW Host endoplasmic reticulum KW Host membrane KW Host-virus interaction KW Membrane KW Modulation of host cell cycle by virus KW Signal KW Transmembrane KW Transmembrane helix KW Virion FT From: PS51919 FT DOMAIN from..to FT /note="X4e #" FT DISULFID 8..43 FT Tag: disulf; Condition: C-x*-C FT DISULFID 20..52 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 60-75; Related: None; Repeats: 1; Topology: Undefined; Example: P59635; Scope: Viruses; Sarbecovirus Comments: None; XX # Revision 1.4 2023/07/27 // AC PRU01268; DC Domain; TR PROSITE; PS51920; SARS_9B; 1; level=0 XX Names: Sarbecovirus 9b domain Function: p9b could have a role in membrane interactions during the assembly of the virus. XX CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Host cytoplasmic vesicle membrane; CC Peripheral membrane protein. Host cytoplasm. Note=Binds non- CC covalently to intracellular lipid bilayers. CC -!- MISCELLANEOUS: The gene encoding this protein is included within CC the N gene (alternative ORF). XX GO GO:0016020; C:membrane GO GO:0044162; C:host cell cytoplasmic vesicle membrane XX KW Host cytoplasm KW Host cytoplasmic vesicle KW Host membrane KW Membrane XX FT From: PS51920 FT DOMAIN from..to FT /note="9b #" XX Chop: Nter=0; Cter=0; Size: 85-95; Related: None; Repeats: 1; Topology: Undefined; Example: P0C5A6; Scope: Viruses; Sarbecovirus Comments: None; XX # Revision 1.1 2020/03/26 // AC PRU01269; DC Domain; TR PROSITE; PS51921; BCOV_S1_CTD; 1; level=0 XX Names: Betacoronavirus spike (S) glycoprotein S1 subunit C-terminal (CTD) domain BetaCoV S1-CTD Function: The receptor binding domain (RBD) of betaCoV that directly engages the receptor is commonly located in the C-terminal half of S1 [C-terminal domain (CTD)] such as in SARS-CoV, SARS-CoV-2, MERS-CoV,and BatCoV HKU4, though in rare cases such as with mouse hepatitis virus (MHV), the RBD region was identified in the S1 N-terminal domain (NTD). XX CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family. XX GO GO:0016020; C:membrane GO GO:0019064; P:fusion of virus membrane with host plasma membrane GO GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane GO GO:0075509; P:endocytosis involved in viral entry into host cell GO GO:0055036; C:virion membrane GO GO:0046813; P:receptor-mediated virion attachment to host cell GO GO:0019031; C:viral envelope GO GO:0039654; P:fusion of virus membrane with host endosome membrane GO GO:0020002; C:host cell plasma membrane XX case KW Disulfide bond end case KW Fusion of virus membrane with host endosomal membrane KW Fusion of virus membrane with host membrane KW Host cell membrane KW Host membrane KW Host-virus interaction KW Membrane KW Transmembrane KW Transmembrane helix KW Viral attachment to host cell KW Viral envelope protein KW Viral penetration into host cytoplasm KW Virion KW Virulence KW Virus entry into host cell FT From: PS51921 FT DOMAIN from..to FT /note="BetaCoV S1-CTD #" FT DISULFID 3..28 FT Tag: disulf; Condition: C-x*-C FT DISULFID 46..99 FT Tag: disulf; Condition: C-x*-C FT DISULFID 58..218 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 150-300; Related: None; Repeats: 1; Topology: Undefined; Example: P25194; Scope: Viruses; Betacoronavirus Comments: None; XX # Revision 1.4 2022/09/30 // AC PRU01270; DC Domain; TR PROSITE; PS51922; BCOV_S1_NTD; 1; level=0 XX Names: Betacoronavirus spike (S) glycoprotein S1 subunit N-terminal (NTD) domain BetaCoV S1-NTD Function: The receptor binding domain (RBD) of betaCoV that directly engages the receptor is commonly located in the C-terminal half of S1 [C-terminal domain (CTD)] such as in SARS-CoV, SARS-CoV-2, MERS-CoV,and BatCoV HKU4, though in rare cases such as with mouse hepatitis virus (MHV), the RBD region was identified in the S1 N-terminal domain (NTD). XX CC -!- SIMILARITY: Belongs to the betacoronaviruses spike protein family. XX GO GO:0016020; C:membrane GO GO:0019064; P:fusion of virus membrane with host plasma membrane GO GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane GO GO:0075509; P:endocytosis involved in viral entry into host cell GO GO:0055036; C:virion membrane GO GO:0046813; P:receptor-mediated virion attachment to host cell GO GO:0019031; C:viral envelope GO GO:0039654; P:fusion of virus membrane with host endosome membrane GO GO:0020002; C:host cell plasma membrane XX case KW Disulfide bond end case KW Fusion of virus membrane with host endosomal membrane KW Fusion of virus membrane with host membrane KW Host cell membrane KW Host membrane KW Host-virus interaction KW Membrane KW Transmembrane KW Transmembrane helix KW Viral attachment to host cell KW Viral envelope protein KW Viral penetration into host cytoplasm KW Virion KW Virulence KW Virus entry into host cell FT From: PS51922 FT DOMAIN from..to FT /note="BetaCoV S1-NTD #" FT DISULFID 7..146 FT Tag: disulf; Condition: C-x*-C FT DISULFID 141..175 FT Tag: disulf; Condition: C-x*-C FT DISULFID 153..238 FT Tag: disulf; Condition: C-x*-C FT DISULFID 277..287 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 275-345; Related: None; Repeats: 1; Topology: Undefined; Example: P25194; Scope: Viruses; Betacoronavirus Comments: None; XX # Revision 1.3 2022/09/30 // AC PRU01271; DC Domain; TR PROSITE; PS51923; COV_S2_HR1; 1; level=0 XX Names: Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 1 (HR1) region Function: The S2 subunit contains two 4-3 heptad repeats (HRs) of hydrophobic residues, HR1 and HR2, typical of coiled coils, separated by an ~170-aa-long intervening domain. The S2 subunit is expected to present rearrangement of its HRs to form a stable 6-helix bundle fusion core. XX GO GO:0016020; C:membrane GO GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane GO GO:0055036; C:virion membrane GO GO:0019031; C:viral envelope GO GO:0039654; P:fusion of virus membrane with host endosome membrane GO GO:0019064; P:fusion of virus membrane with host plasma membrane GO GO:0075509; P:endocytosis involved in viral entry into host cell GO GO:0046813; P:receptor-mediated virion attachment to host cell XX KW Coiled coil KW Host membrane KW Host-virus interaction KW Membrane KW Viral attachment to host cell KW Viral envelope protein KW Virion KW Virulence KW Virus entry into host cell FT From: PS51923 FT REGION from..to FT /note="Heptad repeat 1 (HR1) #" XX Chop: Nter=0; Cter=0; Size: 100-125; Related: None; Repeats: 1; Topology: Undefined; Example: P12650; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.4 2022/09/30 // AC PRU01272; DC Domain; TR PROSITE; PS51924; COV_S2_HR2; 1; level=0 XX Names: Coronavirus spike (S) glycoprotein S2 subunit heptad repeat 2 (HR2) region Function: The S2 subunit contains two 4-3 heptad repeats (HRs) of hydrophobic residues, HR1 and HR2, typical of coiled coils, separated by an ~170-aa-long intervening domain. The S2 subunit is expected to present rearrangement of its HRs to form a stable 6-helix bundle fusion core. XX GO GO:0016020; C:membrane GO GO:0044173; C:host cell endoplasmic reticulum-Golgi intermediate compartment membrane GO GO:0055036; C:virion membrane GO GO:0019031; C:viral envelope GO GO:0039654; P:fusion of virus membrane with host endosome membrane GO GO:0019064; P:fusion of virus membrane with host plasma membrane GO GO:0075509; P:endocytosis involved in viral entry into host cell GO GO:0046813; P:receptor-mediated virion attachment to host cell XX KW Coiled coil KW Host membrane KW Host-virus interaction KW Membrane KW Viral attachment to host cell KW Viral envelope protein KW Virion KW Virulence KW Virus entry into host cell FT From: PS51924 FT REGION from..to FT /note="Heptad repeat 2 (HR2) #" XX Chop: Nter=0; Cter=0; Size: 80-100; Related: None; Repeats: 1; Topology: Undefined; Example: P12650; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.3 2022/09/30 // AC PRU01273; DC Domain; TR PROSITE; PS51925; SWIB_MDM2; 1; level=0 XX Names: SWIB/MDM2 domain Function: SWIB/MDM2 domains participate in activities such as protein-protein and chromatin-related interactions, but their precise functional role(s) in the cell are poorly characterized. XX FT From: PS51925 FT DOMAIN from..to FT /note="SWIB/MDM2 #" XX Chop: Nter=0; Cter=0; Size: 75-90; Related: None; Repeats: 1; Topology: Undefined; Example: Q5UQ74; Scope: Eukaryota Viruses Comments: None; XX # Revision 1.1 2020/04/21 // AC PRU01274; DC Domain; TR PROSITE; PS51926; COV_E; 1; level=0 XX Names: Coronavirus envelope (CoV E) protein Function: Coronavirus envelope (CoV E) proteins are involved in several aspects of the virus' life cycle, such as assembly, budding, envelope formation, and pathogenesis. They are ~100-residue-long polypeptides that are minor components in virions but are abundantly expressed inside infected cells. They are localized mainly to the endoplasmic reticulum (ER) and Golgi- complex where they participate in the assembly, budding, and intracellular trafficking of infectious virions. XX CC -!- FUNCTION: Plays a central role in virus morphogenesis and CC assembly. Acts as a viroporin and self-assembles in host membranes CC forming pentameric protein-lipid pores that allow ion transport. CC Also plays a role in the induction of apoptosis. CC -!- SUBUNIT: Homopentamer. Interacts with membrane protein M in the CC budding compartment of the host cell, which is located between CC endoplasmic reticulum and the Golgi complex. Interacts with CC Nucleoprotein. XX GO GO:0016020; C:membrane GO GO:0044178; C:host cell Golgi membrane GO GO:0039707; P:virus-mediated pore formation in host cell membrane XX KW Host Golgi apparatus KW Host membrane KW Membrane KW Transmembrane KW Transmembrane helix XX Chop: Nter=0; Cter=0; Size: 70-120; Related: None; Repeats: 1; Topology: Undefined; Example: P09048; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.3 2023/10/13 // AC PRU01275; DC Domain; TR PROSITE; PS51927; COV_M; 1; level=0 XX Names: Coronavirus membrane (CoV M) protein Function: The CoV M protein, which functions as a homodimer, adapts a region of membrane for virus assembly and captures other structural proteins at the budding site. XX CC -!- FUNCTION: Component of the viral envelope that plays a central CC role in virus morphogenesis and assembly via its interactions with CC other viral proteins. CC -!- SUBUNIT: Homomultimer. Interacts with envelope E protein in the CC budding compartment of the host cell, which is located between CC endoplasmic reticulum and the Golgi complex. Forms a complex with CC HE and S proteins. Interacts with nucleocapsid N protein. This CC interaction probably participates in RNA packaging into the virus. XX GO GO:0016020; C:membrane GO GO:0055036; C:virion membrane GO GO:0019031; C:viral envelope GO GO:0019058; P:viral life cycle GO GO:0044178; C:host cell Golgi membrane GO GO:0039660; F:structural constituent of virion XX KW Host Golgi apparatus KW Host membrane KW Membrane KW Transmembrane KW Transmembrane helix KW Viral envelope protein KW Viral matrix protein KW Virion XX Chop: Nter=0; Cter=0; Size: 210-250; Related: None; Repeats: 1; Topology: Undefined; Example: Q5MQC7; Scope: Viruses; Riboviria Comments: None; XX # Revision 1.2 2022/09/30 // AC PRU01276; DC Domain; TR PROSITE; PS51928; COV_N_NTD; 1; level=0 XX Names: Coronavirus nucleocapsid (CoV N) protein N-terminal domain (NTD) Function: CoV N proteins contain two structured domains: the N-terminal domain (NTD; also called RBD), which is responsible for RNA binding, and the C- terminal domain (CTD; also called DD), which mediates oligomerization and RNA binding. XX GO GO:0019013; C:viral nucleocapsid GO GO:0003723; F:RNA binding XX KW RNA-binding KW Ribonucleoprotein KW Viral nucleoprotein KW Virion XX FT From: PS51928 FT DOMAIN from..to FT /note="CoV N NTD #" XX Chop: Nter=0; Cter=0; Size: 120-135; Related: None; Repeats: 1; Topology: Undefined; Example: Q64960; Scope: Viruses; Riboviria Comments: None; XX # Revision 1.1 2020/06/24 // AC PRU01277; DC Domain; TR PROSITE; PS51929; COV_N_CTD; 1; level=0 XX Names: Coronavirus nucleocapsid (CoV N) protein C-terminal domain Function: CoV N proteins contain two structured domains: the N-terminal domain (NTD; also called RBD), which is responsible for RNA binding, and the C- terminal domain (CTD; also called DD), which mediates oligomerization and RNA binding. XX GO GO:0019013; C:viral nucleocapsid GO GO:0003723; F:RNA binding XX KW RNA-binding KW Ribonucleoprotein KW Viral nucleoprotein KW Virion XX FT From: PS51929 FT DOMAIN from..to FT /note="CoV N CTD #" XX Chop: Nter=0; Cter=0; Size: 110-130; Related: None; Repeats: 1; Topology: Undefined; Example: Q64960; Scope: Viruses; Riboviria Comments: None; XX # Revision 1.1 2020/06/24 // AC PRU01278; DC Domain; TR PROSITE; PS51930; BMC_2; 1; level=0 XX Names: Bacterial microcompartment (BMC) domain Function: Bacterial microcompartments (BMCs) are large virion-sized protein assemblies comprised of specific enzymes encased within a protein shell. The shells of all BMCs are architecturally similar, being composed of homohexamers of proteins containing a single BMC domain, homotrimer of proteins containing two BMC domains (that resemble the hexamers in size and shape) and pentamers of proteins containing one BMV domain that assemble into an icosahedral shell. XX CC -!- SIMILARITY: Belongs to the bacterial microcompartments protein CC family. XX DR PROSITE; PS51930; BMC_1; 1; trigger=no XX GO GO:0031469; C:bacterial microcompartment XX FT From: PS51930 FT DOMAIN from..to FT /note="BMC #" XX Chop: Nter=0; Cter=0; Size: 80-90; Related: None; Repeats: 1; Topology: Undefined; Example: P76540; Scope: Bacteria Comments: None; XX # Revision 1.4 2022/02/14 // AC PRU01279; DC Domain; TR PROSITE; PS51931; BMC_CP; 1; level=0 XX Names: Bacterial microcompartment (BMC) circularly permuted domain Function: Bacterial microcompartments (BMCs) are large virion-sized protein assemblies comprised of specific enzymes encased within a protein shell. The shells of all BMCs are architecturally similar, being composed of homohexamers of proteins containing a single BMC domain, homotrimer of proteins containing two BMC domains (that resemble the hexamers in size and shape) and pentamers of proteins containing one BMV domain that assemble into an icosahedral shell. Some instances of the BMC shell domain reveal a circular permutation in which a highly similar tertiary structure is built from secondary structure elements occurring in a different order. XX case CC -!- SIMILARITY: Belongs to the EutS/PduU family. else case CC -!- SIMILARITY: Belongs to the EutL/PduB family. end case XX GO GO:0031469; C:bacterial microcompartment XX FT From: PS51931 FT DOMAIN from..to FT /note="BMC circularly permuted #" XX Chop: Nter=0; Cter=0; Size: 90-120; Related: None; Repeats: 1; Topology: Undefined; Example: P0A1D1; Scope: Bacteria Comments: None; XX # Revision 1.5 2022/02/14 // AC PRU01280; DC Domain; TR PROSITE; PS51932; BMV; 1; level=0 XX Names: Bacterial microcompartment vertex (BMV) domain Function: Bacterial microcompartments (BMCs) are large virion-sized protein assemblies comprised of specific enzymes encased within a protein shell. The shells of all BMCs are architecturally similar, being composed of homohexamers of proteins containing a single BMC domain, homotrimer of proteins containing two BMC domains (that resemble the hexamers in size and shape) and pentamers of proteins containing one BMV domain that assemble into an icosahedral shell. XX GO GO:0031469; C:bacterial microcompartment XX FT From: PS51932 FT DOMAIN from..to FT /note="BMV #" XX Chop: Nter=0; Cter=0; Size: 75-90; Related: None; Repeats: 1; Topology: Undefined; Example: P72759; Scope: Bacteria Comments: None; XX # Revision 1.4 2022/02/22 // AC PRU01281; DC Domain; TR PROSITE; PS51933; EUTK_C; 1; level=0 XX Names: EutK-Ctail domain Function: The EutK-Ctail domain is a helix-turn-helix domain that might bind nucleic acids. XX FT From: PS51933 FT DOMAIN from..to FT /note="EutK-Ctail #" XX Chop: Nter=0; Cter=0; Size: 50-60; Related: None; Repeats: 1; Topology: Undefined; Example: Q9ZFU8; Scope: Bacteria; Enterobacteriaceae Comments: None; XX # Revision 1.1 2020/07/27 // AC PRU01282; DC Domain; TR PROSITE; PS51353; ARSC; 1; level=0 XX Names: ArsC family Function: ArsC is an ~150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. The arsC family also comprises the Spx proteins which are GRAM-positive bacterial transcription factors that regulate the transcription of multiple genes in response to disulfide stress. XX CC -!- SIMILARITY: Belongs to the ArsC family. XX case KW Disulfide bond KW Redox-active center end case FT From: PS51353 case FT DISULFID 10..13 FT /note="Redox-active" FT Tag: disulf else case FT ACT_SITE 10 FT Tag: ArsC end case XX Chop: Nter=0; Cter=0; Size: 110-135; Related: None; Repeats: 1; Topology: Undefined; Example: P52147; Scope: Bacteria Viruses; Fromanvirus Comments: None; XX # Revision 1.1 2020/07/28 // AC PRU01283; DC Domain; TR PROSITE; PS51934; LRAT; 1; level=0 XX Names: LRAT domain Function: The NlpC/P60 LRAT-type family includes lecithin-retinol acyltransferase (LRAT), nematode developmental regulator Egl-26, class II tumor suppressor H-rev107 and proteins from poxviruses and animal positive- strand RNA viruses, which share a common catalytic domain fold and an unconventional active site. Several members of the NlpC/P60 LRAT-type family are able to act as transferases/esterases utilizing glycerophospholipids as acyl donors. XX FT From: PS51934 FT DOMAIN from..to FT /note="LRAT #" FT ACT_SITE 11 FT Group: 1; Condition: H FT ACT_SITE 23 FT Group: 1; Condition: H FT ACT_SITE 102 FT /note="Acyl-thioester intermediate" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 85-155; Related: None; Repeats: 1; Topology: Undefined; Example: Q9JI61; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.1 2020/08/06 // AC PRU01284; DC Domain; TR PROSITE; PS51935; NLPC_P60; 1; level=0 XX Names: NlpC/P60 domain Function: The NlpC/P60 domain consists of ~110-140 residues and is a primitive papain-like peptidase in the CA clan of cysteine peptidase with a Cys/His/His catalytic triad and a conserved catalytic core. XX case DE + RecName: EC=3.4.-.-; end case XX CC -!- SIMILARITY: Belongs to the peptidase C40 family. XX case GO GO:0008234; F:cysteine-type peptidase activity XX KW Hydrolase KW Protease KW Thiol protease end case XX FT From: PS51935 FT DOMAIN from..to FT /note="NlpC/P60 #" FT ACT_SITE 31 FT /note="Nucleophile" FT Group: 1; Condition: C FT ACT_SITE 82 FT /note="Proton acceptor" FT Group: 1; Condition: H FT ACT_SITE 94 FT Group: 1; Condition: [DEHNQ] XX Chop: Nter=0; Cter=0; Size: 110-150; Related: None; Repeats: 1; Topology: Undefined; Example: P0AFV7; Scope: Bacteria Viruses; Caudoviricetes Comments: None; XX # Revision 1.2 2023/02/16 // AC PRU01285; DC Domain; TR PROSITE; PS51936; POU_4; 1; level=0 XX Names: POU-specific (POUs) atypical domain Function: HNF1alpha (MODY3 gene product, the most commonly mutated MODY protein) and HNF1beta (hepatocyte nuclear factor 1beta; also known as vHNF1 or TCF2) (MODY5 gene product) are atypical members of the POU transcription factors. Their atypical POUs domains have at least one additional alpha-helix at the N-terminus, and the second helix and adjacent loop of their POUh domains are much longer, creating a more extensive interface between the POUs and POUh domains. XX GO GO:0045893; P:positive regulation of DNA-templated transcription GO GO:0005634; C:nucleus GO GO:0006357; P:regulation of transcription by RNA polymerase II XX KW DNA-binding KW Nucleus KW Transcription KW Transcription regulation XX FT From: PS51936 FT DOMAIN from..to FT /note="POU-specific atypical #" XX Chop: Nter=0; Cter=0; Size: 90-100; Related: None; Repeats: 1; Topology: Undefined; Example: P27889; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.2 2022/06/27 // AC PRU01286; DC Domain; TR PROSITE; PS51937; HNF_P1; 1; level=0 XX Names: HNF-1 dimerization (HNF-p1) domain Function: The homeodomain proteins hepatocyte nuclear factor (HNF)-1alpha and HNF-1beta comprise a functionnally important family in which dimerization is essential for DNA binding. HNF-1alpha and HNF-1beta regulate tissue-specific genes in liver, kidney, intestine, and pancreas. These proteins form homo- and heterodimers through an autonomously folded domain encompassing the 32 N- terminal amino acids (HNF-p1). The dimerization domain also binds the transcriptional coactivator DCoH, which stimulates HNF-1alpha activity. XX FT From: PS51937 FT DOMAIN from..to FT /note="HNF-p1 #" XX Chop: Nter=0; Cter=0; Size: 30-35; Related: None; Repeats: 1; Topology: Undefined; Example: P27889; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2020/08/24 // AC PRU01287; DC Domain; TR PROSITE; PS51938; SUZ_C; 1; level=0 XX Names: SUZ-C domain Function: The SUZ-C domain is a putative RNA-binding domain. XX FT From: PS51938 FT DOMAIN from..to FT /note="SUZ-C #" XX Chop: Nter=0; Cter=0; Size: 25-65; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BRS8; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.1 2020/08/28 // AC PRU01288; DC Domain; TR PROSITE; PS51939; XRRM; 1; level=0 XX Names: xRRM domain Function: The xRRM interacts with both single- and double-stranded RNA using the beta-sheet surface and the C-terminal tail, which forms a helical extension of alpha3 (alpha3x) that binds to the RNA major groove. XX GO GO:1990904; C:ribonucleoprotein complex XX KW RNA-binding XX FT From: PS51939 FT DOMAIN from..to FT /note="xRRM #" XX Chop: Nter=0; Cter=0; Size: 110-170; Related: None; Repeats: 1; Topology: Undefined; Example: Q05CL8; Scope: Eukaryota Comments: None; XX # Revision 1.3 2020/09/17 // AC PRU01289; DC Domain; TR PROSITE; PS51942; BCOV_NSP3C_C; 1; level=0 XX Names: DPUP (Domain Preceding Ubl and PLpro) domain Function: The DPUP domain binds to single-stranded RNA and recognizes purine bases more strongly than pyrimidine bases. XX KW RNA-binding XX FT From: PS51942 FT DOMAIN from..to FT /note="DPUP #" XX Chop: Nter=0; Cter=0; Size: 60-80; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6F7; Scope: Viruses; Betacoronavirus Comments: None; XX # Revision 1.1 2020/09/30 // AC PRU01290; DC Domain; TR PROSITE; PS51945; BCOV_NSP3E_NAB; 1; level=0 XX Names: Betacoronavirus Nsp3e nucleic acid-binding (NAB) domain Function: Nsp3e is unique to Betacoronaviruses and consists of a nucleic acid- binding domain (NAB) and the so-called group 2-specific marker (G2M). The Nsp3e NAB was shown to bind G-rich single-stranded RNA (ssRNA) and to possess double-stranded DNA (dsDNA) unwinding capability. XX KW RNA-binding XX FT From: PS51945 FT DOMAIN from..to FT /note="Nucleic acid-binding #" XX Chop: Nter=0; Cter=0; Size: 95-125; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6F7; Scope: Viruses; Betacoronavirus Comments: None; XX # Revision 1.1 2020/10/08 // AC PRU01291; DC Domain; TR PROSITE; PS51946; COV_NSP4C; 1; level=0 XX Names: Coronavirus Nsp4 C-terminal (Nsp4C) domain Function: The Nsp4C domain could be engaged in protein-protein interactions. XX FT From: PS51946 FT DOMAIN from..to FT /note="Nsp4C #" XX Chop: Nter=0; Cter=0; Size: 90-100; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2020/10/12 // AC PRU01292; DC Domain; TR PROSITE; PS51947; NIRAN; 1; level=0 XX Names: Nidovirus RdRp-associated nucleotidyl transferase (NiRAN) domain Function: The NiRAN domain has an essential nucleotidylation activity and its potential functions in nidovirus replication may include RNA ligation, protein-primed RNA synthesis, and the guanylly-transferase function that is necessary for mRNA capping. XX FT From: PS51947 FT DOMAIN from..to FT /note="NiRAN #" XX Chop: Nter=0; Cter=0; Size: 150-270; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Nidovirales Comments: None; XX # Revision 1.1 2020/10/26 // AC PRU01293; DC Domain; TR PROSITE; PS51948; COV_NSP12_RDRP; 1; level=0 XX Names: Coronavirus Nsp12 RNA-dependent RNA polymerase (RdRp) domain Function: The Nsp12 RNA-dependent RNA polymerase, that includes an RdRp catalytic domain conserved in all RNA viruses, possesses some minimal activity on its own, but the addition of the Nsp7 and Nsp8 cofactors greatly stimulates polymerase activity. XX case DE + AltName: Full=RNA-directed RNA polymerase; DE EC=2.7.7.48; XX CC -!- CATALYTIC ACTIVITY: [RNA-directed RNA polymerase]: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.48; end case CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX GO GO:0000166; F:nucleotide binding GO GO:0003723; F:RNA binding GO GO:0039694; P:viral RNA genome replication case GO GO:0016740; F:transferase activity GO GO:0016779; F:nucleotidyltransferase activity GO GO:0003968; F:RNA-dependent RNA polymerase activity XX KW Nucleotidyltransferase KW RNA-directed RNA polymerase KW Transferase end case KW RNA-binding KW Viral RNA replication KW Nucleotide-binding case KW Zinc KW Metal-binding end case XX FT From: PS51948 FT DOMAIN from..to FT /note="Nsp12 RNA-dependent RNA polymerase #" FT REGION 3..217 FT /note="RdRp Fingers N-ter #" FT REGION 218..256 FT /note="RdRp Palm N-ter #" FT REGION 257..315 FT /note="RdRp Fingers C-ter #" FT REGION 316..451 FT /note="RdRp Palm C-ter #" FT REGION 452..568 FT /note="RdRp Thumb #" FT ACT_SITE 395 FT Group: 1; Condition: S FT ACT_SITE 396 FT Group: 1; Condition: D FT ACT_SITE 397 FT Group: 1; Condition: D FT BINDING 123 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] FT BINDING 278 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [HC] FT BINDING 281 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] FT BINDING 282 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 560-570; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01294; DC Domain; TR PROSITE; PS51949; COV_NSP7; 1; level=0 XX Names: Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp7 cofactor domain Function: The Nsp12 RNA-dependent RNA polymerase, that includes an RdRp catalytic domain conserved in all RNA viruses, possesses some minimal activity on its own, but the addition of the Nsp7 and Nsp8 cofactors greatly stimulates polymerase activity. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX FT From: PS51949 FT DOMAIN from..to FT /note="RdRp Nsp7 cofactor #" XX Chop: Nter=0; Cter=0; Size: 75-95; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2020/12/02 // AC PRU01295; DC Domain; TR PROSITE; PS51950; COV_NSP8; 1; level=0 XX Names: Coronavirus RNA-dependent RNA polymerase (RdRp) Nsp8 cofactor domain Function: The Nsp12 RNA-dependent RNA polymerase, that includes an RdRp catalytic domain conserved in all RNA viruses, possesses some minimal activity on its own, but the addition of the Nsp7 and Nsp8 cofactors greatly stimulates polymerase activity. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX FT From: PS51950 FT DOMAIN from..to FT /note="RdRp Nsp8 cofactor #" XX Chop: Nter=0; Cter=0; Size: 190-215; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2020/12/02 // AC PRU01296; DC Domain; TR PROSITE; PS51951; COV_NSP9_SSRNA_BD; 1; level=0 XX Names: Coronavirus (CoV) Nsp9 ssRNA-binding domain Function: Nsp9 is able to bind single-stranded (ss)DNA or ssRNA, although binding of ssRNA is expected to be the native function. The CoV Nsp9 ssRNA- binding domain is a seemingly obligate homodimer but CoV Nsp9 ssRNA-binding domains have diverse forms of dimerization that promote their biological function. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX KW RNA-binding XX FT From: PS51951 FT DOMAIN from..to FT /note="Nsp9 ssRNA-binding #" XX Chop: Nter=0; Cter=0; Size: 100-120; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2020/12/09 // AC PRU01297; DC Domain; TR PROSITE; PS51952; COV_EXON_MTASE_COACT; 1; level=0 XX Names: Coronavirus (CoV) ExoN/MTase coactivator domain Function: Nsp10, a critical cofactor for activation of multiple replicative enzyme, is a small protein of ca. 140 amino acid residues that exists exclusively in viruses and not in prokaryotes or eukaryotes. Nsp10 is known to interact with both Nsp14 and Nsp16, acting as a scaffolding protein and stimulating their respective 3'-5' exoribonuclease (ExoN) and 2'-O-methyltransferase (2'-O-MTase) activities. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX case or GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Zinc KW Metal-binding KW Zinc-finger end case XX FT From: PS51952 FT DOMAIN from..to FT /note="ExoN/MTase coactivator #" FT BINDING 74 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 77 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 116 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 119 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 127 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 129 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C XX Chop: Nter=0; Cter=0; Size: 135-145; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.5 2022/11/19 // AC PRU01298; DC Domain; TR PROSITE; PS51953; NIV_EXON; 1; level=0 XX Names: Nidovirus 3'-5' exoribonuclease (ExoN) domain Function: The nidovirus 3'-5' exoribonuclease (ExoN) domain may enhance the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. XX case GO GO:0004527; F:exonuclease activity end case XX case or GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Zinc KW Metal-binding KW Zinc-finger end case case KW Exonuclease KW Nuclease end case XX FT From: PS51953 FT DOMAIN from..to FT /note="ExoN #" FT ACT_SITE 19 FT Group: 1; Condition: D FT ACT_SITE 21 FT Group: 1; Condition: E FT ACT_SITE 120 FT Group: 1; Condition: [ED] FT ACT_SITE 198 FT Group: 1; Condition: H FT ACT_SITE 203 FT Group: 1; Condition: D FT BINDING 136 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: C FT BINDING 139 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: C FT BINDING 155 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: C FT BINDING 158 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 2; Condition: H FT BINDING 186 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 3; Condition: H FT BINDING 190 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 3; Condition: C FT BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 3; Condition: H FT BINDING 209 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 3; Condition: C XX Chop: Nter=0; Cter=0; Size: 230-265; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6Y1; Scope: Viruses; Nidovirales Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01299; DC Domain; TR PROSITE; PS51954; COV_N7_MTASE; 1; level=0 XX Names: The Coronavirus (CoV) guanine-N7-methyltransferase (N7-MTase) domain Function: The S-adenosyl methionine (SAM)-dependent guanine-N7- methyltransferase (N7-MTase) domain methylates the 5' guanine of the Gppp-RNA at the N7 position for mRNA capping. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX GO GO:0032259; P:methylation GO GO:0008168; F:methyltransferase activity XX KW Methyltransferase KW Transferase case KW Metal-binding KW Zinc KW Zinc-finger end case FT From: PS51954 FT DOMAIN from..to FT /note="N7-MTase #" FT BINDING 36..42 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT Condition: D-x-G-x-P-x-[GA] FT REGION 116..130 FT /note="GpppA-binding" FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 174 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 185 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 220-235; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6X7; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.6 2022/11/19 // AC PRU01300; DC Domain; TR PROSITE; PS51955; NIV_2_O_MTASE; 1; level=0 XX Names: Nidovirus 2'-O-methyltransferase (2'-O-MTase) domain Function: The 3'-terminal domain of the most conserved ORF1b in three of the four families of the order Nidovirales (except for the family Arteriviridae) encodes a 2'-O-methyltransferase (2'-O-MTase), known as non structural protein (Nsp) 16 in the family Coronaviridae and implicated in methylation of the 5' cap structure of nidoviral mRNAs. XX case GO GO:0032259; P:methylation GO GO:0008168; F:methyltransferase activity XX KW Transferase KW Methyltransferase end case FT From: PS51955 FT DOMAIN from..to FT /note="Nidovirus-type SAM-dependent 2'-O-MTase #" FT ACT_SITE 45 FT Group: 1; Condition: K FT ACT_SITE 125 FT Group: 1; Condition: D FT ACT_SITE 155 FT Group: 1; Condition: K FT ACT_SITE 188 FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 255-305; Related: None; Repeats: 1; Topology: Undefined; Example: P18457; Scope: Viruses; Nidovirales Comments: None; XX # Revision 1.1 2021/01/20 // AC PRU01302; DC Domain; TR PROSITE; PS51957; LID; 1; level=0 XX Names: LIM interaction domain (LID) domain Function: It can bind the LIM domains of different LMO and LIM-HD proteins (which have sequence identities of as low as 35% within the LIM domains) but not to the LIM domains from other proteins, such as the LIM kinases, which have closely related LIM domains. XX CC -!- SIMILARITY: Belongs to the LDB family. XX GO GO:0030274; F:LIM domain binding XX FT From: PS51957 FT DOMAIN from..to FT /note="LIM interaction domain (LID) #" XX Chop: Nter=0; Cter=0; Size: 35-45; Related: None; Repeats: 1; Topology: Undefined; Example: O55203; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2020/10/16 // AC PRU01303; DC Domain; TR PROSITE; PS51958; NENDOU; 1; level=0 XX Names: Nidoviral uridylate-specific endoribonuclease (NendoU) domain Function: Among the Nsps found in Nidovirales, nonstructural protein 15 (nsp15) from coronaviruses and Nsp11 from arteriviruses contain in their C- terminal region a conserved endoribonuclease domain called nidoviral uridylate-specific endoribonuclease (NendoU) with cleavage specificity for single- and double-stranded RNA 5' of uridine nucleotides to produce a 2'-3'- cyclic phosphate end product. XX XX case GO GO:0004519; F:endonuclease activity XX KW Hydrolase KW Endonuclease KW Nuclease end case XX FT From: PS51958 FT DOMAIN from..to FT /note="NendoU #" FT ACT_SITE 31 FT Group: 1; Condition: H FT ACT_SITE 46 FT Group: 1; Condition: H FT ACT_SITE 86 FT Group: 1; Condition: K XX Chop: Nter=0; Cter=0; Size: 120-150; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6X9; Scope: Viruses; Nidovirales Comments: None; XX # Revision 1.2 2021/01/27 // AC PRU01304; DC Domain; TR PROSITE; PS51959; ENDOU; 1; level=0 XX Names: Eukaryotic uridylate-specific endoribonuclease (EndoU) domain Function: The EndoU domain cleaves RNA at uridylates and release 2',3'-cyclic phosphodiester ends. XX DE + RecName: EC=3.1.-.-; XX CC -!- FUNCTION: Endoribonuclease that cleaves single-stranded RNAs at CC uridylates and releases products that have 2'-3'-cyclic phosphate CC termini. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the ENDOU family. XX case GO GO:0003723; F:RNA binding GO GO:0004521; F:RNA endonuclease activity GO GO:0046872; F:metal ion binding XX KW Endonuclease KW Hydrolase KW Manganese KW Metal-binding KW Nuclease KW RNA-binding end case XX FT From: PS51959 FT DOMAIN from..to FT /note="EndoU #" FT ACT_SITE 149 FT Group: 1; Condition: H FT ACT_SITE 164 FT Group: 1; Condition: H FT ACT_SITE 207 FT Group: 1; Condition: K XX Chop: Nter=0; Cter=0; Size: 260-280; Related: None; Repeats: 1; Topology: Undefined; Example: A8E627; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.3 2023/02/13 // AC PRU01305; DC Domain; TR PROSITE; PS51960; COV_NSP15_NTD; 1; level=0 XX Names: Coronavirus (CoV) Nsp15 N-terminal oligomerization domain Function: Nsp15 is a nidoviral uridylate-specific endoribonuclease (NendoU) that consists of three distinct domains, a small N-terminal, an intermediate- sized middle, and a large C-terminal NendoU domain. CoV Nsp15 forms double- ring hexamers made of dimers of trimers. The hexameric form is thought to be the fully active form of CoV Nsp15 and the hexamer is stabilized by interactions of the N-terminal oligomerization domain. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX FT From: PS51960 FT DOMAIN from..to FT /note="Nsp15 N-terminal oligomerization #" XX Chop: Nter=0; Cter=0; Size: 55-65; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6W9; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2021/02/01 // AC PRU01306; DC Domain; TR PROSITE; PS51961; AV_NSP11N_COV_NSP15M; 1; level=0 XX Names: Arterivirus Nsp11 N-terminal/coronavirus NSP15 middle (AV-Nsp11N/CoV-Nsp15M) domain Function: The AV-Nsp11N/CoV-Nsp15M domain may serve as an interaction hubs with other proteins and RNA. XX FT From: PS51961 FT DOMAIN from..to FT /note="AV-Nsp11N/CoV-Nsp15M #" XX Chop: Nter=0; Cter=0; Size: 90-135; Related: None; Repeats: 1; Topology: Undefined; Example: P12723; Scope: Viruses; Nidovirales Comments: None; XX # Revision 1.1 2021/02/13 // AC PRU01307; DC Domain; TR PROSITE; PS51962; COV_NSP1; 1; level=0 XX Names: Coronavirus (CoV) Nsp1 globular domain Function: Nsp1 is a characteristic feature of AlphaCoVs and BetaCoVs, which exhibits both functional conservation and mechanistic diversity in inhibiting host gene expression and antiviral responses. Although the sequence homologies among CoV Nsp1 proteins are low, the core structures share a relatively conserved domain. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX XX KW Inhibition of host innate immune response by virus KW Viral immunoevasion KW Eukaryotic host translation shutoff by virus KW Host mRNA suppression by virus KW Inhibition of host interferon signaling pathway by virus XX FT From: PS51962 FT DOMAIN from..to FT /note="CoV Nsp1 globular #" XX Chop: Nter=0; Cter=0; Size: 100-150; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6U5; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2021/03/02 // AC PRU01308; DC Domain; TR PROSITE; PS51963; BCOV_NSP1_C; 1; level=0 XX Names: Betacoronavirus (BetaCoV) Nsp1 C-terminal domain Function: The Sarbecovirus Nsp1 C-terminal domain binds to the mRNA channel of the 40S ribosome, where it interferes with mRNA binding and inhibits host protein translation. This inhibition mechanism may be unique to Sarbecoviruses, because the C-terminal region of Nsp1 is shorter in AlphaCoVs and is not highly conserved amongst other BetaCoVs, including MERS-CoV. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX GO GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway GO GO:0039595; P:induction by virus of catabolism of host mRNA XX KW Inhibition of host innate immune response by virus KW Inhibition of host interferon signaling pathway by virus KW Viral immunoevasion KW Eukaryotic host translation shutoff by virus KW Host mRNA suppression by virus XX FT From: PS51963 FT DOMAIN from..to FT /note="BetaCoV Nsp1 C-terminal #" XX Chop: Nter=0; Cter=0; Size: 25-40; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6X7; Scope: Viruses; Betacoronavirus Comments: None; XX # Revision 1.1 2021/03/03 // AC PRU01309; DC Domain; TR PROSITE; PS51964; SARS_ORF8_IG; 1; level=0 XX Names: SARS ORF8 accessory protein immunoglobulin (Ig)-like domain Function: The SARS related (SARSr) ORF8 accessory protein is thought to exert important functions in modulating the host infected cell metabolism and antiviral immunity. The SARSr ORF8 contains an immunoglobulin (Ig)-like domain. XX case KW Disulfide bond end case XX FT From: PS51964 FT DOMAIN from..to FT /note="SARS ORF8 Ig-like #" case FT DISULFID 2 FT /note="Interchain" FT Tag: disulf; Condition: C end case FT DISULFID 7..72 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 19..84 FT Tag: disulf; Group: 1; Condition: C-x*-C FT DISULFID 43..65 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 20-90; Related: None; Repeats: 1; Topology: Undefined; Example: P0DTC8; Scope: Viruses; Sarbecovirus Comments: None; XX # Revision 1.2 2021/04/12 // AC PRU01310; DC Domain; TR PROSITE; PS51965; AG_I_II_AR; 1; level=0 XX Names: Streptococcus antigen I/II alanine-rich (Ag I/II A) repeat Function: The Streptococcus Ag I/II A repeat forms a long alpha-helix that intimately intertwines into a left-handed supercoiled structure with the P repeat polyproline II (PPII) helix to form an unusually long and narrow stalk. XX CC -!- SIMILARITY: Belongs to the antigen I/II family. XX FT From: PS51965 FT REPEAT from..to FT /note="Ag I/II A #" XX Chop: Nter=0; Cter=0; Size: 70-85; Related: None; Repeats: 2-6; Topology: Undefined; Example: P16952; Scope: Bacteria; Streptococcus Comments: None; XX # Revision 1.1 2021/02/19 // AC PRU01311; DC Domain; TR PROSITE; PS51966; COV_VIROPORIN_3A_TM; 1; level=0 XX Names: Coronavirus (CoV) 3a-like viroporin transmembrane (TM) domain Function: 3a-like accessory proteins are transmembrane proteins of the viroporin family that form ion channels in the host membrane and have been implicated in inducing apoptosis, pathogenicity, and virus release. 3a-like viroporins contain a transmembrane domain (TM) and a cytosolic domain (CD). XX GO GO:0016020; C:membrane XX KW Host membrane KW Membrane KW Transmembrane KW Transmembrane helix XX FT From: PS51966 FT DOMAIN from..to FT /note="CoV 3a-like viroporin TM #" XX Chop: Nter=0; Cter=0; Size: 85-105; Related: None; Repeats: 1; Topology: Undefined; Example: Q3I5J4; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.3 2022/09/30 // AC PRU01312; DC Domain; TR PROSITE; PS51967; COV_VIROPORIN_3A_CD; 1; level=0 XX Names: Coronavirus (CoV) 3a-like viroporin transmembrane (CD) domain Function: 3a-like accessory proteins are transmembrane proteins of the viroporin family that form ion channels in the host membrane and have been implicated in inducing apoptosis, pathogenicity, and virus release. 3a-like viroporins contain a transmembrane domain (TM) and a cytosolic domain (CD). XX FT From: PS51967 FT DOMAIN from..to FT /note="CoV 3a-like viroporin CD #" XX Chop: Nter=0; Cter=0; Size: 50-100; Related: None; Repeats: 1; Topology: Undefined; Example: P0DTC3; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.2 2021/03/10 // AC PRU01313; DC Domain; TR PROSITE; PS51968; GRH_CP2_DB; 1; level=0 XX Names: Grh/CP2 DNA-binding (DB) domain Function: Grh/CP2 transcription factors (TFs) are highly conserved in multicellular organisms as key regulators of epithelial differentiation, organ development and skin barrier formation. Members of this TF family are widely found in diverse taxa, ranging from fungi to animals. All Grh/CP2 family members share a common domain architecture characterized by an intrinsically unstructured N-terminal transactivation domain (TAD), a conserved DNA-binding domain (DBD), also termed CP2 binding domain, and a C- terminal dimerization domain (DD). XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus XX KW DNA-binding KW Nucleus XX FT From: PS51968 FT DOMAIN from..to FT /note="Grh/CP2 DB #" XX Chop: Nter=0; Cter=0; Size: 225-245; Related: None; Repeats: 1; Topology: Undefined; Example: Q5RAR8; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2021/03/23 // AC PRU01314; DC Domain; TR PROSITE; PS51969; CBM39; 1; level=0 XX Names: CBM39 (carbohydrate binding type-39) domain Function: The carbohydrate binding type-39 (CBM39) domain is a beta-1,3- glucan-recognition domain. XX CC -!- SIMILARITY: Belongs to the insect beta-1,3-glucan binding protein CC family. XX GO GO:0005975; P:carbohydrate metabolic process GO GO:0045088; P:regulation of innate immune response GO GO:0045087; P:innate immune response GO GO:0038187; F:pattern recognition receptor activity XX KW Immunity KW Innate immunity XX FT From: PS51969 FT DOMAIN from..to FT /note="CBM39 #" XX Chop: Nter=0; Cter=0; Size: 90-110; Related: None; Repeats: 1; Topology: Undefined; Example: Q8MU95; Scope: Eukaryota; Endopterygota Comments: None; XX # Revision 1.1 2021/04/12 // AC PRU01319; DC Domain; TR PROSITE; PS51975; RNASE_H_2; 1; level=0 XX Names: RNase H type-2 domain Function: Ribonuclease H (RNase H) (EC 3.1.26.4) recognizes and cleaves the RNA strand of RNA-DNA heteroduplexes. XX case DE + RecName: EC=3.1.26.4; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in CC the absence of substrate. May bind a second metal ion after substrate CC binding. end case XX GO GO:0003723; F:RNA binding case GO GO:0004523; F:RNA-DNA hybrid ribonuclease activity GO GO:0006401; P:RNA catabolic process XX KW Endonuclease KW Hydrolase KW Metal-binding KW Nuclease end case XX FT From: PS51975 FT DOMAIN from..to FT /note="RNase H type-2" FT BINDING 7 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: D FT BINDING 8 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: E FT BINDING 105 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 170-235; Related: None; Repeats: 1; Topology: Undefined; Example: B8DHN2; Scope: Bacteria Archaea Eukaryota Comments: None; XX # Revision 1.4 2022/11/19 // AC PRU01321; DC Domain; TR PROSITE; PS51977; WGR; 1; level=0 XX Names: WGR domain Function: The 80-90 amino acid long tryptophane-, glycine-, arginine-rich (WGR) domain participates in binding DNA near the 5' terminus and mediates domain-domain contacts essential for DNA-dependent activity. XX FT From: PS51977 FT DOMAIN from..to FT /note="WGR #" XX Chop: Nter=0; Cter=0; Size: 75-110; Related: None; Repeats: 1; Topology: Undefined; Example: P78271; Scope: Eukaryota Bacteria; Pseudomonadota Comments: None; XX # Revision 1.2 2023/01/26 // AC PRU01322; DC Domain; TR PROSITE; PS51978; PBC; 1; level=0 XX Names: PBC domain Function: The PBC class of TALE homeodomain proteins includes the products of the vertebrate Pbx1, Pbx2, Pbx3 and Pbx4, Caenorhabditis elegans ceh-20, ceh-40 and ceh-60 and the Drosophila extradenticle (exd) genes. The sequence similarity between the PBC proteins extends downstream of the homeodomain for about 15 amino acids, and upstream of the homeodomain is a 180-amino acid dimerization domain termed PBC. The PBC domain can be further subdivided into an A and B region. XX CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the TALE/PBX homeobox family. XX XX KW Nucleus XX FT From: PS51978 FT DOMAIN from..to FT /note="PBC #" FT REGION 8..89 FT /note="PBC-A #" FT REGION 92..188 FT /note="PBC-B #" XX Chop: Nter=0; Cter=0; Size: 175-205; Related: None; Repeats: 1; Topology: Undefined; Example: Q6IR52; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2021/06/16 // AC PRU01323; DC Domain; TR PROSITE; PS51979; YEBF_CMI; 1; level=0 XX Names: YebF/Cmi domain Function: ColM-producing strains are protected from the toxin that they produce by coexpression of a specific immunity protein, named Cmi. Cmi is anchored in the cytoplasmic membrane with an alpha-helix and contains a periplasmic domain that shows sequence similarity to YebF-like proteins which are known to be secreted into the external medium by some Gram-negative bacteria. The YebF/Cmi domain is typified by two cysteine residues, required for Cmi folding and structure stabilization. XX case KW Disulfide bond end case XX FT From: PS51979 FT DOMAIN from..to FT /note="YebF/Cmi #" FT DISULFID 5..78 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 85-95; Related: None; Repeats: 1; Topology: Undefined; Example: Q57NB9; Scope: Bacteria; Enterobacterales Comments: None; XX # Revision 1.1 2021/07/15 // AC PRU01324; DC Domain; TR PROSITE; PS51980; OCEL; 1; level=0 XX Names: Occludin/ELL (OCEL) domain Function: The ~110-amino acid occludin/ELL (OCEL) domain is necessary for interactions between occludin and ZO-1, actin, and multiple kinases and may also mediate homotypic occludin-occludin interactions. The C-terminal OCEL domain of ELL is also important for its function due to its interaction with other proteins. XX CC -!- SIMILARITY: Belongs to the ELL/occludin family. XX FT From: PS51980 FT DOMAIN from..to FT /note="OCEL #" XX Chop: Nter=0; Cter=0; Size: 105-115; Related: None; Repeats: 1; Topology: Undefined; Example: Q3UZP0; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2021/07/21 // AC PRU01325; DC Domain; TR PROSITE; PS51981; ZF_RZ; 1; level=0 XX Names: Zinc finger RZ-type Function: The ubiquitylation of LPS on Salmonella that invade the cytosol relies on the RZ-type zinc finger in the E3 module of RNF213. XX KW Zinc-finger case and and and KW Ubl conjugation pathway KW Metal-binding KW Zinc end case XX FT From: PS51981 case and and and FT ZN_FING from..to FT /note="RZ-type #" else case and and and FT ZN_FING from..to FT /note="RZ-type #; atypical" else FT ZN_FING from..to FT /note="RZ-type #; degenerate" end case FT ACT_SITE 35 FT /note="Nucleophile" FT Condition: C FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 28 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 44 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 47 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 70-75; Related: None; Repeats: 1; Topology: Undefined; Example: Q9P2E3; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.3 2022/11/19 // AC PRU01326; DC Domain; TR PROSITE; PS51982; ULD; 1; level=0 XX Names: Ubiquitin-like (ULD) domain Compass domain Function: The ULD domain of SATB1 assembles into a tetramer and the tetramerization of SATB1 is essential for recognizing specific DNA sequences (such as multiple AT-rich DNA fragments). XX FT From: PS51982 FT DOMAIN from..to FT /note="ULD #" XX Chop: Nter=0; Cter=0; Size: 100-105; Related: None; Repeats: 1; Topology: Undefined; Example: Q01826; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2021/07/27 // AC PRU01327; DC Domain; TR PROSITE; PS51983; CUTL; 1; level=0 XX Names: CUT repeat-like (CUTL) domain Function: The DNA binding ability of SATB1 requires the contribution of the CUTL domain, as well as the tandem CUT domains and the homeodomain. XX KW DNA-binding XX FT From: PS51983 FT DOMAIN from..to FT /note="CUTL #" XX Chop: Nter=0; Cter=0; Size: 70-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q8VI24; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.1 2021/07/28 // AC PRU01328; DC Domain; TR PROSITE; PS51984; CPB1; 1; level=0 XX Names: Cryptic Polo-Box 1 (CPB1) domain Function: Plk4s target mother centrioles through an interaction between their CPB and acidic regions in the centriolar receptors SPD-2/Cep192 and/or Asterless/Cep152. XX CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. CDC5/Polo subfamily. XX GO GO:0007099; P:centriole replication GO GO:0005814; C:centriole GO GO:0005737; C:cytoplasm XX KW Cytoplasm KW Cytoskeleton XX FT From: PS51984 FT DOMAIN from..to FT /note="Cryptic POLO box 1 (CPB1) #" XX Chop: Nter=0; Cter=0; Size: 110-125; Related: None; Repeats: 1; Topology: Undefined; Example: B4LDJ6; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2021/09/20 // AC PRU01329; DC Domain; TR PROSITE; PS51985; CPB2; 1; level=0 XX Names: Cryptic Polo-Box 2 (CPB2) domain Function: Plk4s target mother centrioles through an interaction between their CPB and acidic regions in the centriolar receptors SPD-2/Cep192 and/or Asterless/Cep152. XX CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. CDC5/Polo subfamily. XX GO GO:0005737; C:cytoplasm GO GO:0007099; P:centriole replication GO GO:0005814; C:centriole XX KW Cytoplasm KW Cytoskeleton XX FT From: PS51985 FT DOMAIN from..to FT /note="Cryptic POLO box 2 (CPB2) #" XX Chop: Nter=0; Cter=0; Size: 100-120; Related: None; Repeats: 1; Topology: Undefined; Example: Q2LYK3; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2021/09/20 // AC PRU01330; DC Domain; TR PROSITE; PS51986; GS_BETA_GRASP; 1; level=0 XX Names: Glutamine synthetase (GS) beta-grasp domain Function: Glutamine synthetases (GSs) contain a homology region that consists of a regulatory N-terminal beta-grasp domain and a catalytic C-terminal domain, with the N-terminal domain of one subunit and the C-terminal domain of the neighboring subunit forming an active site. XX CC -!- SIMILARITY: Belongs to the glutamine synthetase family. XX FT From: PS51986 FT DOMAIN from..to FT /note="GS beta-grasp #" XX Chop: Nter=0; Cter=0; Size: 75-110; Related: None; Repeats: 1; Topology: Undefined; Example: P07694; Scope: Eukaryota Bacteria Archaea Viruses; Mimivirus Comments: None; XX # Revision 1.1 2021/09/30 // AC PRU01331; DC Domain; TR PROSITE; PS51987; GS_CATALYTIC; 1; level=0 XX Names: Glutamine synthetase (GS) catalytic domain Function: Glutamine synthetases (GSs) contain a homology region that consists of a regulatory N-terminal beta-grasp domain and a catalytic C-terminal domain, with the N-terminal domain of one subunit and the C-terminal domain of the neighboring subunit forming an active site. XX CC -!- SIMILARITY: Belongs to the glutamine synthetase family. XX FT From: PS51987 FT DOMAIN from..to FT /note="GS catalytic #" XX Chop: Nter=0; Cter=0; Size: 200-440; Related: None; Repeats: 1; Topology: Undefined; Example: P08282; Scope: Eukaryota Bacteria Archaea Viruses; Mimivirus Comments: None; XX # Revision 1.1 2021/09/30 // AC PRU01332; DC Domain; TR PROSITE; PS51988; HERPESVIRUS_UL32; 1; level=0 XX Names: Herpesviridae UL32 packaging protein family Function: The Herpesviridae UL32 family proteins form homopentameric rings with a positively charged central channel that binds double-stranded DNA. XX CC -!- FUNCTION: Plays a role in efficient localization of neo- CC synthesized capsids to nuclear replication compartments, thereby CC controlling cleavage and packaging of virus genomic DNA. CC -!- SIMILARITY: Belongs to the herpesviridae UL32 protein family. XX GO GO:0042025; C:host cell nucleus GO GO:0030430; C:host cell cytoplasm GO GO:0019031; C:viral envelope case ( and and and ) or ( and and and ) or ( and and and ) GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger KW Host cytoplasm KW Host nucleus XX FT From: PS51988 case FT REGION 67..151 FT /note="Zinc finger #1" end case case FT REGION 220..483 FT /note="Zinc finger #3" end case case FT REGION 328..405 FT /note="Zinc finger #2" end case FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 145 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 221 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 328 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 331 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 398 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 405 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 445 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] FT BINDING 483 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 430-620; Related: None; Repeats: 1; Topology: Undefined; Example: Q66671; Scope: Viruses; Herpesviridae Comments: None; XX # Revision 1.3 2022/11/19 // AC PRU01333; DC Domain; TR PROSITE; PS51989; COV_NSP2_N; 1; level=0 XX Names: Coronavirus (CoV) Nsp2 N-terminal domain Function: The Nsp2 N-terminal domain contains ten alpha-helices and fourteen beta-sheets with three zinc fingers (ZnFs), belonging to the C2H2, C4, and C2HC types, respectively. The three zinc fingers are not involved in binding nucleic acids directly but may play other unknown functions. The interaction of Nsp2 and nucleic acid is mainly dependent on a large positively charged region on the electrostatic surface of the Nsp2 N-terminal domain. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX case or or GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51989 FT DOMAIN from..to FT /note="CoV Nsp2 N-terminal #" FT REGION 18..44 FT /note="C2H2" FT Group: 1 FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 42 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 44 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT REGION 132..153 FT /note="C4" FT Group: 2 FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 135 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 151 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 153 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT REGION 176..213 FT /note="C2HC" FT Group: 3 FT BINDING 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 188 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: H FT BINDING 213 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C XX Chop: Nter=0; Cter=0; Size: 230-290; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6U7; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.3 2022/11/19 // AC PRU01334; DC Domain; TR PROSITE; PS51990; COV_NSP2_M; 1; level=0 XX Names: Coronavirus (CoV) Nsp2 middle domain Function: Nsp2 has been implicated in processes ranging from translation repression to endosomal transport, ribosome biogenesis, and actin filament binding. Nsp2 in SARS-CoV-2 and other coronaviruses have been observed to localize to endosomes and replication-transcription complexes (RTC). Nsp2 may be involved in binding nucleic acids and regulating intracellular signaling pathways. It contains an N-terminal, a middle and a C-terminal domain. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX FT From: PS51990 FT DOMAIN from..to FT /note="CoV Nsp2 middle #" XX Chop: Nter=0; Cter=0; Size: 180-400; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6W5; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2021/12/09 // AC PRU01335; DC Domain; TR PROSITE; PS51991; COV_NSP2_C; 1; level=0 XX Names: Coronavirus (CoV) Nsp2 C-terminal domain Function: Nsp2 has been implicated in processes ranging from translation repression to endosomal transport, ribosome biogenesis, and actin filament binding. Nsp2 in SARS-CoV-2 and other coronaviruses have been observed to localize to endosomes and replication-transcription complexes (RTC). Nsp2 may be involved in binding nucleic acids and regulating intracellular signaling pathways. It contains an N-terminal, a middle and a C-terminal domain. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX FT From: PS51991 FT DOMAIN from..to FT /note="CoV Nsp2 C-terminal #" XX Chop: Nter=0; Cter=0; Size: 100-140; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6W4; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.1 2021/12/09 // AC PRU01336; DC Domain; TR PROSITE; PS51992; COV_NSP3_Y; 1; level=0 XX Names: Coronavirus (CoV) Nsp3 Y domain Function: The Y domains including Y1 and CoV-Y may form higher-order oligomeric complexes and play a role in pore formation in double-membrane vesicles (DMVs) that serve as the central hubs for viral RNA replication. Specific membrane binding might be a conserved activity of the Y domain. XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX case or GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc KW Zinc-finger XX end case FT From: PS51992 FT DOMAIN from..to FT /note="CoV Nsp3 Y #" FT REGION 92..to FT /note="CoV-Y #" FT REGION from..91 FT /note="Y1 #" FT REGION 92..186 FT /note="Y2 #" FT REGION 187..268 FT /note="Y3 #" FT REGION 269..to FT /note="Y4 #" FT REGION 5..18 FT /note="ZF1 #" FT Group: 1 FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 15 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT REGION 51..61 FT /note="ZF2 #" FT Group: 2 FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 54 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 58 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 61 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C XX Chop: Nter=0; Cter=0; Size: 340-374; Related: None; Repeats: 1; Topology: Undefined; Example: P0DTD1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.2 2023/04/06 // AC PRU01337; DC Domain; TR PROSITE; PS51993; COV_3ECTO; 1; level=0 XX Names: Coronavirus 3Ecto domain Function: The CoV 3Ecto domain is glycosylated and predicted to be located on the lumenal side of the membrane. It has been shown that interaction of the 3Ecto domain with the large lumenal loop of Nsp4 is essential for the endoplasmic reticulum (ER) rearrangements and double-membrane vesicles (DMVs) formation occurring in cells infected by SARS-CoV or mouse hepatitis virus (MHV). XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX case KW Disulfide bond end case ** case ** KW Glycoprotein ** end case XX FT From: PS51993 FT DOMAIN from..to FT /note="3Ecto #" FT DISULFID 17..44 FT Tag: disulf; Condition: C-x*-C FT DISULFID 35..41 FT Tag: disulf; Condition: C-x*-C ** case ** FT CARBOHYD 26 ** FT /note="N-linked (GlcNAc...) asparagine; by host" ** FT Tag: glycosylation; Condition: N ** end case ** case ** FT CARBOHYD 29 ** FT /note="N-linked (GlcNAc...) asparagine; by host" ** FT Tag: glycosylation; Condition: N ** end case XX Chop: Nter=0; Cter=0; Size: 75-89; Related: None; Repeats: 1; Topology: Undefined; Example: P0DTD1; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.7 2023/03/31 // AC PRU01338; DC Domain; TR PROSITE; PS51994; BCOV_NSP3E_G2M; 1; level=0 XX Names: Betacoronavirus Nsp3e group 2-specific marker (G2M) domain Betacoronavirus-specific marker (BetaSM) Function: Nsp3e is unique to Betacoronaviruses and consists of a nucleic acid- binding domain (NAB) and the so-called group 2-specific marker (G2M) or Betacoronavirus-specific marker (BetaSM). XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX FT From: PS51994 FT DOMAIN from..to FT /note="G2M #" XX Chop: Nter=0; Cter=0; Size: 100-160; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6U5; Scope: Viruses; Betacoronavirus Comments: None; XX # Revision 1.2 2022/01/13 // AC PRU01339; DC Domain; TR PROSITE; PS51995; ATLF; 1; level=0 XX Names: Anthrax toxin lethal factor (ATLF)-like domain Function: The ATLF-like domain acts either as a metalloprotease domain, forming the M34 family of metalloendopeptidases, (ATLF domain IV, PPEP-1 and 2) or as an anthrax protective antigen-binding domain (PABD) (ATLF domain I and EF and Certhrax PABD). XX case CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit. CC -!- SIMILARITY: Belongs to the peptidase M34 family. XX GO GO:0008237; F:metallopeptidase activity GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc KW Hydrolase KW Protease KW Metalloprotease end case XX FT From: PS51995 FT DOMAIN from..to FT /note="ATLF-like #" FT ACT_SITE 111 FT /note="Proton acceptor" FT Group: 1; Condition: E FT BINDING 110 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 114 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 147 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: Y FT BINDING 154 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 180-230; Related: None; Repeats: 1; Topology: Undefined; Example: Q183R7; Scope: Bacteria; Bacillota Comments: None; XX # Revision 1.4 2023/01/13 // AC PRU01340; DC Domain; TR PROSITE; PS51996; TR_MART; 1; level=0 XX Names: Toxin-related mono-ADP-ribosyltransferase (TR mART) core domain Function: Most known mARTs transfer ADP-ribose onto arginine residues. Some enzymatically inactive mART domains, for example, the N-terminal domains of C2 and VIP2 toxins, have acquired a new, protein-binding function. XX DR PROSITE; PS01291; ART; 0-1; trigger=no XX case GO GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity XX KW Transferase KW NAD end case XX FT From: PS51996 FT DOMAIN from..to FT /note="TR mART core #" FT ACT_SITE 89 FT Group: 1; Condition: R FT ACT_SITE 116 FT Group: 1; Condition: S FT ACT_SITE 157 FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 170-260; Related: None; Repeats: 1; Topology: Undefined; Example: P21454; Scope: Eukaryota; Euteleostomi Bacteria Viruses Comments: None; XX # Revision 1.2 2022/05/02 // AC PRU01341; DC Domain; TR PROSITE; PS51997; UPF1_CH_RICH; 1; level=0 XX Names: UPF1 cysteine-histidine-rich (CH-rich) domain Function: In its N-terminal region, Upf1 has a conserved cysteine-histidine- rich (CH-rich) domain, while centrally it possesses the seven conserved motifs characteristic of eukaryotic group I RNA helicases. The Upf1 CH-rich domain has a cis-inhibitory effect on the ATPase activity and is also the region that binds Upf2. XX case or or GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc KW Zinc-finger end case XX FT From: PS51997 FT DOMAIN from..to FT /note="Upf1 CH-rich #" FT REGION 9..41 FT /note="C3H" FT Group: 1 FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 31 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: C FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: H FT REGION 23..51 FT /note="CC/SHH/C" FT Group: 2 FT BINDING 23 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: C FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CS] FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: H FT BINDING 51 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [HC] FT REGION 69..99 FT /note="C4" FT Group: 3 FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 95 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#3" FT Group: 3; Condition: C XX Chop: Nter=0; Cter=0; Size: 150-340; Related: None; Repeats: 1; Topology: Undefined; Example: Q09820; Scope: Eukaryota Comments: None; XX # Revision 1.3 2022/11/19 // AC PRU01342; DC Domain; TR PROSITE; PS51998; DEK_C; 1; level=0 XX Names: DEK C-terminal (DEK-C) domain Function: The DEK-C domain is able to bind DNA and induce protein-protein interactions, but its function remains unknown. XX FT From: PS51998 FT DOMAIN from..to FT /note="DEK-C #" XX Chop: Nter=0; Cter=0; Size: 50-60; Related: None; Repeats: 1; Topology: Undefined; Example: Q76I79; Scope: Eukaryota Comments: None; XX # Revision 1.1 2022/04/28 // AC PRU01343; DC Domain; TR PROSITE; PS51999; ZF_GRF; 1; level=0 XX Names: Zinc finger GRF-type Function: GRF-ZFs are nucleic acid interaction modules and in several cases these motifs have been shown to enhance enzymatic activity. XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS51999 case and and and FT ZN_FING from..to FT /note="GRF-type #" else case and and and FT ZN_FING from..to FT /note="GRF-type #; atypical" else FT ZN_FING from..to FT /note="GRF-type #; degenerate" end case FT BINDING 1 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 3 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 38 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 35-65; Related: None; Repeats: 1; Topology: Undefined; Example: Q6DCD7; Scope: Eukaryota Comments: None; XX # Revision 1.2 2022/11/19 // AC PRU01344; DC Domain; TR PROSITE; PS52000; COV_NSP12_IF; 1; level=0 XX Names: Coronavirus Nsp12 Interface domain Function: The coronavirus Nsp12 subunit contains an N-terminal NiRAN domain, an interface domain, composed of three helices and five beta strands, and a C-terminal polymerase domain, which resembles a right hand, comprising the fingers, palm and thumb subdomains. XX DE AltName: Full=ORF1ab polyprotein; XX CC -!- SIMILARITY: Belongs to the coronaviruses polyprotein 1ab family. XX case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case XX FT From: PS52000 FT DOMAIN from..to FT /note="Nsp12 Interface #" FT BINDING 30 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [HC] FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 41 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 90-110; Related: None; Repeats: 1; Topology: Undefined; Example: P0C6X6; Scope: Viruses; Orthocoronavirinae Comments: None; XX # Revision 1.2 2022/11/19 // AC PRU01345; DC Domain; TR PROSITE; PS52001; AD; 1; level=0 XX Names: AD domain Function: The AD domain, which may function in RNA-binding based on its predicted anticodon-binding fold, is found in the Hezron/Gemin6/Lsm12 protein family. XX FT From: PS52001 FT DOMAIN from..to FT /note="AD #" XX Chop: Nter=0; Cter=0; Size: 90-110; Related: None; Repeats: 1; Topology: Undefined; Example: P38828; Scope: Eukaryota Comments: None; XX # Revision 1.1 2022/06/22 // AC PRU01346; DC Domain; TR PROSITE; PS52002; SM; 1; level=0 XX Names: Sm domain Function: The Sm domain is responsible for both protein oligomerization and specific RNA binding. XX GO GO:0003723; F:RNA binding XX KW RNA-binding XX FT From: PS52002 FT DOMAIN from..to FT /note="Sm #" XX Chop: Nter=0; Cter=0; Size: 55-105; Related: None; Repeats: 1; Topology: Undefined; Example: B7V207; Scope: Bacteria Eukaryota Archaea Comments: None; XX # Revision 1.1 2022/06/24 // AC PRU01347; DC Domain; TR PROSITE; PS52003; OCA; 1; level=0 XX Names: OCA domain Function: The 23 amino acid OCA domain binds to class II POU domain-containing transcription factors and a DNA octamer motif in a bivalent manner. XX CC -!- SUBCELLULAR LOCATION: Nucleus. XX GO GO:0005634; C:nucleus GO GO:0006355; P:regulation of DNA-templated transcription GO GO:0006351; P:DNA-templated transcription XX KW Nucleus KW Transcription KW Transcription regulation KW Activator XX FT From: PS52003 FT DOMAIN from..to FT /note="OCA #" XX Chop: Nter=0; Cter=0; Size: 20-25; Related: None; Repeats: 1; Topology: Undefined; Example: Q64693; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.2 2022/07/11 // AC PRU01348; DC Domain; TR PROSITE; PS52004; KS3_2; 1; level=0 XX Names: Ketosynthase family 3 (KS3) domain Function: Ketoacyl synthases (KSs) (more officially 3-oxoacyl synthases and also known as beta-ketoacyl synthases) are the condensing enzymes that catalyze the reaction of acyl-coenzyme A (acyl-CoA) or acyl-acyl carrier protein (acyl-ACP) with malonyl-CoA, malonyl-ACP, or occasionally other substrates. XX case DR PROSITE; PS00606; KS3_1; 1; trigger=no XX KW Transferase end case XX FT From: PS52004 FT DOMAIN from..to FT /note="Ketosynthase family 3 (KS3) #" FT ACT_SITE 171 FT /note="For beta-ketoacyl synthase #1 activity" FT Group: 1; Condition: C FT ACT_SITE 307 FT /note="For beta-ketoacyl synthase #1 activity" FT Group: 1; Condition: H FT ACT_SITE 347 FT /note="For beta-ketoacyl synthase #1 activity" FT Group: 1; Condition: [HN] XX Chop: Nter=0; Cter=0; Size: 240-550; Related: None; Repeats: 1; Topology: Undefined; Example: P9WQE4; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.2 2023/02/28 // AC PRU01349; DC Domain; TR PROSITE; PS52005; CBM56; 1-3; level=0 XX Names: CBM56 (carbohydrate binding type-56) domain Function: The CBM family 56 (CBM56) domain is an ~95-amino acid module, which selectively binds insoluble beta-1,3-glucans, probably by binding domains in the polysaccharide with triple-helical quaternary structure. XX GO GO:0030246; F:carbohydrate binding XX FT From: PS52005 FT DOMAIN from..to FT /note="CBM56 #" XX Chop: Nter=0; Cter=0; Size: 80-100; Related: none; Repeats: 1-3; Topology: Undefined; Example: Q9KG76; Scope: Bacteria Viruses; Faustovirus Comments: None XX # Revision 1.2 2022/09/15 // AC PRU01350; DC Domain; TR PROSITE; PS52006; GH64; 1; level=0 XX Names: Glycosyl hydrolases family 64 (GH64) domain Function: All reported GH family 64 (GH64) members are laminaripentaose- producing "inverting" beta-1,3-glucanases. Two strictly conserved catalytic residues, a Glu and an Asp, act as an acid catalyst and a base catalyst, respectively. XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 64 family. XX GO GO:0030246; F:carbohydrate binding XX case KW Glycosidase KW Hydrolase end case XX FT From: PS52006 FT DOMAIN from..to FT /note="GH64 #" FT ACT_SITE 128 FT /note="Proton donor" FT Group: 1; Condition: E FT ACT_SITE 144 FT /note="Proton acceptor" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 305-375; Related: None; Repeats: 1; Topology: Undefined; Example: Q59146; Scope: Bacteria; Micrococcales Comments: None; XX # Revision 1.1 2022/09/16 // AC PRU01351; DC Domain; TR PROSITE; PS52007; PADR1; 1; level=0 XX Names: PADR1 zinc-binding domain Function: The PADR1 zinc-binding domain is involved in protein-protein interactions that orchestrate PARP-1 activation and are critical to the DNA- dependent stimulation of PARP-1. It relays the DNA binding signal from the first two zinc fingers to the catalytic C terminus by helping to establish the active form of the enzyme. XX CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus. Chromosome. CC Note=Localizes to sites of DNA damage. CC -!- SIMILARITY: Belongs to the ARTD/PARP family. XX GO GO:0005730; C:nucleolus GO GO:0070212; P:protein poly-ADP-ribosylation case GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW ADP-ribosylation KW Nucleus XX FT From: PS52007 FT DOMAIN from..to FT /note="PADR1 zinc-binding #" FT REGION 66..108 FT /note="Zinc ribbon #" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 74 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 87 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 130-155; Related: None; Repeats: 1; Topology: Undefined; Example: Q9N4H4; Scope: Eukaryota Comments: None; XX # Revision 1.2 2022/11/19 // AC PRU01352; DC Domain; TR PROSITE; PS52008; GH81; 1; level=0 XX Names: Glycosyl hydrolases family 81 (GH81) domain Function: The GH family 81 (GH81) includes proteins with endo-beta-1,3- glucanase widely distributed in plants, fungi, bacteria, archaea and viruses. XX case DE + RecName: EC=2.1.1.-; end case CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 81 family. XX case GO GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity XX KW Carbohydrate metabolism KW Hydrolase KW Polysaccharide degradation KW Glycosidase end case XX FT From: PS52008 FT DOMAIN from..to FT /note="GH81 #" FT REGION from..224 FT /note="beta-sandwich subdomain #" FT REGION 225..322 FT /note="alpha/beta subdomain #" FT REGION 337..to FT /note="(alpha/beta)6 barrel subdomain #" FT ACT_SITE 443 FT Group: 1; Condition: D FT ACT_SITE 518 FT Group: 1; Condition: E FT ACT_SITE 522 FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 647-729; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KG76; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.1 2022/10/11 // AC PRU01353; DC Domain; TR PROSITE; PS52009; GH84; 1; level=0 XX Names: Glycosyl hydrolases family 84 (GH84) domain Function: Family 84 glycoside hydrolases (GH84) cleave the glycosidic linkage of N-acetylglucosaminides by a two-step catalytic mechanism that involves a pair of aspartate residues as catalytic residues, D1 as the polarizing residue and Asp175 as the general acid/base catalyst. XX case DE + RecName: EC=3.2.1.-; end case XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family. XX case KW Glycosidase KW Hydrolase end case FT From: PS52009 FT DOMAIN from..to FT /note="GH84 #" ** FT ACT_SITE 116 ** FT Group: 1; Condition: D FT ACT_SITE 117 FT /note="Proton donor" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 268-282; Related: None; Repeats: 1; Topology: Undefined; Example: Q89ZI2; Scope: Bacteria Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.1 2022/11/21 // AC PRU01354; DC Domain; TR PROSITE; PS52010; COLLECTRIN_LIKE; 1; level=0 XX Names: Collectrin-like domain Function: The collectrin-like domain mediates homodimerization. It consists of a small extracellular neck subdomain, which adopts a ferredoxin-like fold, a long linker, and a single transmembrane (TM) helix. XX CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. XX GO GO:0005886; C:plasma membrane XX KW Cell membrane KW Membrane KW Transmembrane KW Transmembrane helix XX FT From: PS52010 FT DOMAIN from..to FT /note="Collectrin-like #" FT TRANSMEM 122..142 FT /note="Helical" XX Chop: Nter=0; Cter=0; Size: 192-202; Related: None; Repeats: 1; Topology: Undefined; Example: Q9HBJ8; Scope: Eukaryota; Eutheria Comments: None; XX # Revision 1.1 2022/10/24 // AC PRU01355; DC Domain; TR PROSITE; PS52011; PEPTIDASE_M2; 1; level=0 XX Names: Peptidase family M2 domain Function: Members of the M2 family of peptidases, related to mammalian angiotensin converting enzyme (EC 3.4.15.1, ACE, peptidyl-dipeptidase A), play important roles in regulating a number of physiological processes. XX case CC -!- COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case CC -!- SIMILARITY: Belongs to the peptidase M2 family. XX case () and ( or or ) GO GO:0008237; F:metallopeptidase activity end case case () GO GO:0008241; F:peptidyl-dipeptidase activity GO GO:0004180; F:carboxypeptidase activity XX KW Carboxypeptidase KW Hydrolase KW Protease end case case () and ( or or ) KW Metalloprotease end case case ( or or ) KW Metal-binding end case case KW Zinc end case case KW Disulfide bond end case XX FT From: PS52011 FT DOMAIN from..to FT /note="Peptidase M2 #" FT ACT_SITE 350 FT /note="Proton acceptor #1" FT Group: 1; Condition: E FT ACT_SITE 479 FT /note="Proton donor #1" FT Group: 1; Condition: H FT BINDING 349 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 353 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 377 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 2; Condition: E FT BINDING 152 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#1" FT Group: 3; Condition: R FT BINDING 451 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#1" FT Group: 3; Condition: W FT BINDING 455 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#1" FT Group: 3; Condition: [RK] case and FT BINDING 190 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#2" FT Group: 4; Condition: Y FT BINDING 488 FT /ligand="chloride" FT /ligand_id="ChEBI:CHEBI:17996" FT /ligand_label="#2" FT Group: 4; Condition: R end case FT DISULFID 115..123 FT Tag: disulf; Condition: C-x*-C FT DISULFID 318..336 FT Tag: disulf; Condition: C-x*-C FT DISULFID 504..522 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 580-591; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q56NL1; Scope: Eukaryota; Metazoa Comments: None; XX # Revision 1.1 2022/12/05 // AC PRU01356; DC Domain; TR PROSITE; PS52012; CFEM; 1; level=0 XX Names: CFEM) domain Function: Common in Fungal Extracellular Membrane (CFEM) proteins, characterized by a distinctive pattern of eight cysteine residues of conserved interspacing, are widespread among fungi. The CFEM domain adopts a helical-basket fold that consists of six alpha-helices, and is uniquely stabilized by four disulfide bonds formed by its eight signature cysteines. XX GO GO:0005576; C:extracellular region case GO GO:0046872; F:metal ion binding XX KW Heme KW Iron KW Metal-binding end case case KW Disulfide bond end case FT From: PS52012 FT DOMAIN from..to FT /note="CFEM #" FT DISULFID 29..69 FT Tag: disulf; Condition: C-x*-C FT DISULFID 33..64 FT Tag: disulf; Condition: C-x*-C FT DISULFID 43..50 FT Tag: disulf; Condition: C-x*-C FT DISULFID 52..85 FT Tag: disulf; Condition: C-x*-C FT BINDING 47 FT /ligand="heme" FT /ligand_id="ChEBI:CHEBI:30413" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT Tag: heme; Condition: D XX Chop: Nter=0; Cter=0; Size: 107-119; Related: None; Repeats: 1-4; Topology: Undefined; Example: Q4WMA6; Scope: Eukaryota; Ascomycota Comments: None; XX # Revision 1.1 2022/11/10 // AC PRU01357; DC Domain; TR PROSITE; PS52013; ZF_C6H2; 1; level=0 XX Names: Zinc finger C6H2-type Function: The C6H2-type zinc finger is essential for the normal processing function of MetAP1 and may be important for the proper functional alignment of MetAP1 on the ribosomes. It is a protein-protein interaction domain. XX case ( and and and ) or ( and and and ) CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase type 1 subfamily. XX case ( and and and ) or ( and and and ) GO GO:0046872; F:metal ion binding XX KW Zinc KW Metal-binding end case KW Zinc-finger XX FT From: PS52013 case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="C6H2-type #" else case ( and and and ) and ( and and and ) FT ZN_FING from..to FT /note="C6H2-type #; atypical" else FT ZN_FING from..to FT /note="C6H2-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 19 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 37 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] FT BINDING 49 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT Group: 2; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 53-59; Related: None; Repeats: 1; Topology: Undefined; Example: Q5RBF3; Scope: Eukaryota Comments: None; XX # Revision 1.1 2022/12/15 // AC PRU01358; DC Domain; TR PROSITE; PS52014; SAMD1_WH; 1; level=0 XX Names: SAMD1-like winged helix (WH) domain Function: The SAMD1-like winged helix (WH) domain forms a group of WH domains with shared sequence homology found in the transcriptional regulators SAMD1, KAT6A, -B and ZMYND11. XX GO GO:0005634; C:nucleus GO GO:0045892; P:negative regulation of DNA-templated transcription XX KW Nucleus KW Chromatin regulator XX FT From: PS52014 FT DOMAIN from..to FT /note="SAMD1-like winged helix (WH) #" XX Chop: Nter=0; Cter=0; Size: 70-80; Related: None; Repeats: 1; Topology: Undefined; Example: Q15326; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.1 2023/01/12 // AC PRU01359; DC Domain; TR PROSITE; PS52015; TONB_CTD; 1; level=0 XX Names: TonB C-terminal domain Function: The TonB protein plays an essential role in the energy transduction system to drive active transport across the outer membrane (OM) using the proton-motive force of the cytoplasmic membrane of Gram-negative bacteria. The C-terminal domain (CTD) of TonB protein is known to interact with the conserved TonB box motif of TonB-dependent OM transporters, which likely induces structural changes in the OM transporters. XX CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane CC protein; Periplasmic side. CC -!- SIMILARITY: Belongs to the TonB family. XX GO GO:0055085; P:transmembrane transport GO GO:0015031; P:protein transport GO GO:0031992; F:energy transducer activity GO GO:0030288; C:outer membrane-bounded periplasmic space XX KW Cell inner membrane KW Cell membrane KW Membrane KW Protein transport KW Transmembrane KW Transmembrane helix KW Transport XX FT From: PS52015 FT DOMAIN from..to FT /note="TonB C-terminal #" XX Chop: Nter=0; Cter=0; Size: 85-95; Related: None; Repeats: 1; Topology: Undefined; Example: O52042; Scope: Bacteria; Pseudomonadota Comments: None; XX # Revision 1.1 2023/01/27 // AC PRU01360; DC Domain; TR PROSITE; PS52016; TONB_DEPENDENT_REC_3; 1; level=0 XX Names: TonB-dependent receptor proteins Function: TonB-dependent receptors (TBDRs) are transport proteins found at the outer membrane (OM) to allow Gram-negative bacteria to uptake scarce resources from competitive environments with very high affinity. All of them share the same basic architecture, a C-terminal membrane-embedded 22-strand antiparallel beta-barrel domain that is sealed by a conserved N-terminal globular 'plug' domain (also called 'cork' or 'hatch'). XX CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the TonB-dependent receptor family. XX DR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 0-1; trigger=yes DR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1; trigger=yes XX GO GO:0009279; C:cell outer membrane XX KW Cell outer membrane KW Membrane KW Transmembrane KW Transmembrane beta strand KW Transport XX FT From: PS52016 FT DOMAIN from..119 FT /note="TBDR plug #" FT DOMAIN 124..to FT /note="TBDR beta-barrel #" XX Chop: Nter=0; Cter=0; Size: 80-1001; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KVI9; Scope: Bacteria Comments: None; XX # Revision 1.3 2023/02/03 // AC PRU01362; DC Domain; TR PROSITE; PS52018; DART; 1; level=0 XX Names: DNA ADP-ribosyl transferase (DarT) domain Function: The bacterial DNA ADP-ribosyl transferase (DarT) protein is a toxin that has been shown to transfer ADP-ribose from NAD(+) onto thymidine bases present in single-stranded DNA (ssDNA) specifically at the four-base motif TNTC, and to have no activity on RNA or protein targets. XX case CC -!- CATALYTIC ACTIVITY: Reaction=a thymidine in DNA + NAD(+) = an N- CC (ADP-alpha-D-ribosyl)-thymidine in DNA + H(+) + nicotinamide; CC Xref=Rhea:RHEA:71651, Rhea:RHEA-COMP:13556, Rhea:RHEA-COMP:18051, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:137386, ChEBI:CHEBI:191199; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71652; end case CC -!- SIMILARITY: Belongs to the DarT ADP-ribosyltransferase family. XX GO GO:0003677; F:DNA binding case GO GO:0016779; F:nucleotidyltransferase activity GO GO:0016757; F:glycosyltransferase activity XX KW Glycosyltransferase KW Nucleotidyltransferase KW Transferase end case KW DNA-binding KW Toxin-antitoxin system XX FT From: PS52018 FT DOMAIN from..to FT /note="DarT" FT BINDING 5..7 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Group: 1 case FT BINDING 14 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: G FT BINDING 22 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Condition: L end case FT ACT_SITE 44 FT /note="Proton acceptor" FT Group: 1; Condition: R FT BINDING 44 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT Group: 1 FT ACT_SITE 141 FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 192-205; Related: None; Repeats: 1; Topology: Undefined; Example: A0A0B0SG80; Scope: Bacteria Comments: None; XX # Revision 1.1 2023/02/21 // AC PRU01363; DC Domain; TR PROSITE; PS52019; PKS_MFAS_DH; 1; level=0 XX Names: Polyketide and metazoan fatty acid synthase dehydratase (PKS/mFAS DH) domain Function: Dehydratase domains catalyze formation of an alpha,beta-double bond in the nascent polyketide intermediate. XX FT From: PS52019 FT DOMAIN from..to FT /note="PKS/mFAS DH #" FT REGION from..132 FT /note="N-terminal hotdog fold #" FT REGION 149..to FT /note="C-terminal hotdog fold #" FT ACT_SITE 33 FT /note="Proton acceptor; for dehydratase activity #" FT Group: 1; Condition: H FT ACT_SITE 210 FT /note="Proton donor; for dehydratase activity #" FT Group: 1; Condition: D XX Chop: Nter=0; Cter=0; Size: 261-345; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q54FQ1; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.1 2023/03/03 // AC PRU01364; DC Domain; TR PROSITE; PS52020; CRESS_DNA_REP; 1; level=0 XX Names: CRESS-DNA virus replication initiator protein (Rep) endonuclease domain Function: The Rep endonuclease domain is characterized by rolling circle replication (RCR) motifs I through III, which are important for RCR initiation and termination. Motif I, UUTU (U denotes hydrophobic residues), is thought to be involved in the recognition of the origin of replication. Motif II, HU(H/Q), is involved in the coordination of divalent metal ions, Mg(2+) or Mn(2+), which are essential for endonuclease activity at the origin of replication. Motif III (YxxK, where x is any amino acid) is involved in dsDNA cleavage and subsequent covalent attachment of the Rep through the catalytic tyrosine residue to the 5' end of the cleaved product. XX case CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Divalent metal cations, possibly Mg(2+) or Mn(2+). end case CC -!- SUBCELLULAR LOCATION: Host nucleus. XX GO GO:0006260; P:DNA replication GO GO:0003677; F:DNA binding GO GO:0042025; C:host cell nucleus case GO GO:0046872; F:metal ion binding end case case GO GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters GO GO:0016779; F:nucleotidyltransferase activity end case XX KW DNA-binding KW Host nucleus KW DNA replication KW Nucleotide-binding case KW Endonuclease KW Hydrolase KW Nuclease KW Covalent protein-DNA linkage KW Nucleotidyltransferase KW Transferase end case case KW Metal-binding end case XX FT From: PS52020 FT DOMAIN from..to FT /note="CRESS-DNA virus Rep endonuclease #" FT MOTIF 8..11 FT /note="RCR-1" FT Condition: [FWILMVACGTSYPH](2)-T-[FWILMVACGTSYPH] FT MOTIF 47..49 FT /note="RCR-2" FT Condition: H-[FWILMVACGTSYPH]-[HQ] FT MOTIF 87..90 FT /note="RCR-3" FT Condition: Y-x(2)-K FT ACT_SITE 87 FT /note="For DNA cleavage activity" FT Tag: act_site; Condition: Y FT BINDING 39 FT /ligand="a divalent metal cation #1" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: E FT BINDING 47 FT /ligand="a divalent metal cation #1" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: H FT BINDING 49 FT /ligand="a divalent metal cation #1" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: H FT BINDING 91 FT /ligand="a divalent metal cation #1" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: [DEN] XX Chop: Nter=0; Cter=0; Size: 94-130; Related: None; Repeats: 1; Topology: Undefined; Example: D4N3P2; Scope: Viruses; Cressdnaviricota Bacteria; Candidatus Phytoplasma asteris Comments: None; XX # Revision 1.1 2023/03/17 // AC PRU01366; DC Domain; TR PROSITE; PS52022; PV_NS1_NUC; 1; level=0 XX Names: Parvovirus (PV) NS1 nuclease (NS1-Nuc) domain profile Parvovirus (PV) NS1 origin of replication binding (OBD) domain Parvovirus (PV) NS1 DNA-specific binding domain Function: The PV NS1-Nuc domain plays an important role in the "rolling hairpin" replication of the single-stranded parvoviral DNA genome, recognizing origin of replication sequences in double-stranded DNA, and cleaving (i.e., nicking) single-stranded DNA at a nearby site known as the terminal resolution site (trs). Since the DNA encountered by NS1 is double- stranded, it is assumed that binding of NS1 to its target sequences in dsDNA induces strand separation nearby, allowing for the endonuclease activity of NS1 to cleave at the trs site. XX case CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=CHEBI:60240; end case CC -!- SUBCELLULAR LOCATION: Host nucleus. XX GO GO:0006260; P:DNA replication GO GO:0003677; F:DNA binding GO GO:0042025; C:host cell nucleus case GO GO:0046872; F:metal ion binding end case case GO GO:0004519; F:endonuclease activity end case XX KW DNA-binding KW Host nucleus KW DNA replication KW Nucleotide-binding case KW Endonuclease KW Hydrolase KW Nuclease KW Covalent protein-DNA linkage end case case KW Metal-binding end case XX FT From: PS52022 FT DOMAIN from..to FT /note="PV NS1-Nuc #" FT MOTIF 100..102 FT /note="RCR-2" FT Condition: H-[FWILMVACGTSYPH]-H FT MOTIF 175..179 FT /note="RCR-3" FT Condition: Y-x(3)-K FT ACT_SITE 175 FT /note="For nuclease activity" FT Tag: act_site; Condition: Y FT BINDING 93 FT /ligand="a divalent metal cation #1" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: [ED] FT BINDING 100 FT /ligand="a divalent metal cation #1" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: H FT BINDING 102 FT /ligand="a divalent metal cation #1" FT /ligand_id="ChEBI:CHEBI:60240" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 69-253; Related: None; Repeats: 1; Topology: Undefined; Example: P07300; Scope: Viruses Comments: None; XX # Revision 1.1 2023/05/05 // AC PRU01368; DC Domain; TR PROSITE; PS52024; GL_AHV; 1; level=0 XX Names: Alphaherpesvirus glycoprotein L (gL) domain Function: Two glycoprotein complexes are conserved throughout the three herpesvirus subfamilies: the trimeric glycoprotein B (gB) that functions as a membrane fusogen and the heterodimeric glycoprotein H/glycoprotein L (gH/gL), the role of which is less clearly defined. The intrinsic structural plasticity of gH/gL enables it to function as a signal integration machine that can accept diverse regulatory inputs and convert them into a "trigger" signal that activates the fusogenic ability of gB. XX DE + AltName: Full=Envelope glycoprotein L; DE Short=gL; XX CC -!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is CC required for the fusion of viral and plasma membranes leading to CC virus entry into the host cell. Acts as a functional inhibitor of CC gH and maintains gH in an inhibited form. Upon binding to host CC integrins, gL dissociates from gH leading to activation of the CC viral fusion glycoproteins gB and gH. CC -!- SUBUNIT: Interacts with glycoprotein H (gH); this interaction is CC necessary for the correct processing and cell surface expression CC of gH. The heterodimer gH/gL seems to interact with gB trimers CC during fusion. CC -!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane CC protein; Extracellular side. Host cell membrane; Peripheral CC membrane protein; Extracellular side. Host Golgi apparatus, host CC trans-Golgi network. Note=gL associates with the extravirion CC surface through its binding to gH. During virion morphogenesis, CC this protein probably accumulates in the host trans-Golgi where CC secondary envelopment occurs. CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L (gL) family. CC Alphaherpesvirinae gL subfamily. XX GO GO:0044177; C:host cell Golgi apparatus GO GO:0055036; C:virion membrane GO GO:0016020; C:membrane GO GO:0046718; P:viral entry into host cell GO GO:0020002; C:host cell plasma membrane GO GO:0019064; P:fusion of virus membrane with host plasma membrane GO GO:0019031; C:viral envelope XX KW Fusion of virus membrane with host cell membrane KW Fusion of virus membrane with host membrane KW Glycoprotein KW Host Golgi apparatus KW Host cell membrane KW Host membrane KW Membrane KW Viral envelope protein KW Viral penetration into host cytoplasm KW Virion KW Virus entry into host cell case KW Disulfide bond end case XX FT From: PS52024 FT DOMAIN from..to FT /note="gL alphaherpesvirus-type #" FT DISULFID 22..53 FT Tag: disulf; Condition: C-x*-C FT DISULFID 126..138 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 107-179; Related: None; Repeats: 1; Topology: Undefined; Example: P52510; Scope: Viruses; Alphaherpesvirinae Comments: None; XX # Revision 1.1 2023/06/09 // AC PRU01369; DC Domain; TR PROSITE; PS52025; GL_BHV; 1; level=0 XX Names: Betaherpesvirus glycoprotein L (gL) domain Function: Two glycoprotein complexes are conserved throughout the three herpesvirus subfamilies: the trimeric glycoprotein B (gB) that functions as a membrane fusogen and the heterodimeric glycoprotein H/glycoprotein L (gH/gL), the role of which is less clearly defined. The intrinsic structural plasticity of gH/gL enables it to function as a signal integration machine that can accept diverse regulatory inputs and convert them into a "trigger" signal that activates the fusogenic ability of gB. XX DE + AltName: Full=Envelope glycoprotein L; DE Short=gL; XX CC -!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane CC protein; Extracellular side. Host cell membrane; Peripheral CC membrane protein; Extracellular side. Host Golgi apparatus, host CC trans-Golgi network. Note=gL associates with the extravirion CC surface through its binding to gH. During virion morphogenesis, CC this protein probably accumulates in the host trans-Golgi where CC secondary envelopment occurs. CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L (gL) family. CC Betaherpesvirinae gL subfamily. XX GO GO:0046718; P:viral entry into host cell GO GO:0019064; P:fusion of virus membrane with host plasma membrane GO GO:0019031; C:viral envelope GO GO:0055036; C:virion membrane GO GO:0044177; C:host cell Golgi apparatus GO GO:0020002; C:host cell plasma membrane GO GO:0016020; C:membrane XX KW Fusion of virus membrane with host cell membrane KW Fusion of virus membrane with host membrane KW Glycoprotein KW Host Golgi apparatus KW Host cell membrane KW Host membrane KW Membrane KW Viral envelope protein KW Viral penetration into host cytoplasm KW Virion KW Virus entry into host cell case KW Disulfide bond end case XX FT From: PS52025 FT DOMAIN from..to FT /note="gL betaherpesvirus-type #" FT DISULFID 5 FT /note="Interchain" FT Tag: disulf; Condition: C FT DISULFID 12 FT /note="Interchain" FT Tag: disulf; Condition: C FT DISULFID 102 FT /note="Interchain" FT Tag: disulf; Condition: C FT DISULFID 112..117 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 201-214; Related: None; Repeats: 1; Topology: Undefined; Example: O92277; Scope: Viruses; Betaherpesvirinae Comments: None; XX # Revision 1.1 2023/06/09 // AC PRU01370; DC Domain; TR PROSITE; PS52026; GL_GHV; 1; level=0 XX Names: Gammaherpesvirus glycoprotein L (gL) domain Function: Two glycoprotein complexes are conserved throughout the three herpesvirus subfamilies: the trimeric glycoprotein B (gB) that functions as a membrane fusogen and the heterodimeric glycoprotein H/glycoprotein L (gH/gL), the role of which is less clearly defined. The intrinsic structural plasticity of gH/gL enables it to function as a signal integration machine that can accept diverse regulatory inputs and convert them into a "trigger" signal that activates the fusogenic ability of gB. XX DE + AltName: Full=Envelope glycoprotein L; DE Short=gL; XX CC -!- SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane CC protein; Extracellular side. Host cell membrane; Peripheral CC membrane protein; Extracellular side. Host Golgi apparatus, host CC trans-Golgi network. Note=gL associates with the extravirion CC surface through its binding to gH. During virion morphogenesis, CC this protein probably accumulates in the host trans-Golgi where CC secondary envelopment occurs. CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L (gL) family. CC Gammaherpesvirinae gL subfamily. XX GO GO:0046718; P:viral entry into host cell GO GO:0016020; C:membrane GO GO:0019031; C:viral envelope GO GO:0020002; C:host cell plasma membrane GO GO:0055036; C:virion membrane GO GO:0044177; C:host cell Golgi apparatus GO GO:0019064; P:fusion of virus membrane with host plasma membrane XX KW Fusion of virus membrane with host cell membrane KW Fusion of virus membrane with host membrane KW Glycoprotein KW Host Golgi apparatus KW Host cell membrane KW Host membrane KW Membrane KW Viral envelope protein KW Viral penetration into host cytoplasm KW Virion KW Virus entry into host cell case KW Disulfide bond end case XX FT From: PS52026 FT DOMAIN from..to FT /note="gL gammaherpesvirus-type #" FT DISULFID 3..31 FT Tag: disulf; Condition: C-x*-C FT DISULFID 4..52 FT Tag: disulf; Condition: C-x*-C XX Chop: Nter=0; Cter=0; Size: 108-118; Related: None; Repeats: 1; Topology: Undefined; Example: P03212; Scope: Viruses; Gammaherpesvirinae Comments: None; XX # Revision 1.2 2023/07/11 // AC PRU01371; DC Domain; TR PROSITE; PS52027; ZF_C2HC_C3H; 1; level=0 XX Names: Zinc finger C2HC/C3H-type Function: The C2HC/C3H-type zinc finger has first been identified in four copies in Zfp474, a protein exclusively found in testis and ovary and thought to function as a germ cell specific transcription factor that plays important roles in spermatid differentiation and oocyte development. XX case ( and and and ) CC -!- COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; XX GO GO:0008270; F:zinc ion binding GO GO:0046872; F:metal ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS52027 case ( and and and ) FT ZN_FING from..to FT /note="C2HC/C3H-type #" else case ( and and and ) FT ZN_FING from..to FT /note="C2HC/C3H-type #; atypical" else FT ZN_FING from..to FT /note="C2HC/C3H-type #; degenerate" end case FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 25-35; Related: None; Repeats: 1-6; Topology: Undefined; Example: Q6V5K9; Scope: Eukaryota Comments: None; XX # Revision 1.1 2023/06/02 // AC PRU01372; DC Domain; TR PROSITE; PS52028; SMCR; 1; level=0 XX Names: Streptococcal M proteins C repeat Function: M proteins belong to a family of fibrous streptococcal surface proteins which represent major virulence factors due to their antiphagocytic activities. The C repeats are present in all M proteins, although the number of repeat sequences varies from two (M6) to four (M12). The conserved repetitive C units are responsible for several biological activities of M and M-like proteins. XX CC -!- SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. CC -!- SIMILARITY: Belongs to the M protein family. XX GO GO:0005576; C:extracellular region XX KW Cell wall KW Peptidoglycan-anchor KW Secreted XX FT From: PS52028 FT REPEAT from..to FT /note="C #" XX Chop: Nter=0; Cter=0; Size: 35-36; Related: None; Repeats: 2-4; Topology: Undefined; Example: P16947; Scope: Bacteria; Streptococcus Comments: None; XX # Revision 1.1 2023/06/29 // AC PRU01373; DC Domain; TR PROSITE; PS52029; LD_TPASE; 1; level=0 XX Names: L,D-transpeptidase (L,D-TPase) catalytic domain Function: Members of the L,D-transpeptidase family can also display L,D- carboxypeptidase and L,D-endopeptidase activities. XX CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. XX GO GO:0071555; P:cell wall organization GO GO:0008360; P:regulation of cell shape XX KW Cell shape KW Cell wall biogenesis/degradation KW Peptidoglycan synthesis XX FT From: PS52029 FT DOMAIN from..to FT /note="L,D-TPase catalytic #" FT ACT_SITE 83 FT /note="Proton donor/acceptor" FT Group: 1; Condition: H FT ACT_SITE 99 FT /note="Nucleophile" FT Group: 1; Condition: C XX Chop: Nter=0; Cter=0; Size: 108-181; Related: None; Repeats: 1; Topology: Undefined; Example: C0SP99; Scope: Bacteria Comments: None; XX # Revision 1.1 2023/06/23 // AC PRU01374; DC Domain; TR PROSITE; PS52030; SMDRR; 1; level=0 XX Names: Streptococcal M proteins D repeat Function: M proteins belong to a family of fibrous streptococcal surface proteins which represent major virulence factors due to their antiphagocytic activities. All M proteins share a common framework that includes a conserved signal peptide, a hypervariable amino terminus, a less variable central domain, and a highly conserved C-terminus. A number of repeat sequences (A, B, C and D repeats) follow the hypervariable region. Sequence conservation increases from the A repeats to D repeats. XX CC -!- SUBCELLULAR LOCATION: Secreted, cell wall; Peptidoglycan-anchor. CC -!- SIMILARITY: Belongs to the M protein family. XX GO GO:0005576; C:extracellular region XX KW Cell wall KW Peptidoglycan-anchor KW Secreted XX FT From: PS52030 FT REPEAT from..6 FT /note="D #" FT REPEAT 7..12 FT /note="D #" FT REPEAT 15..20 FT /note="D #" FT REPEAT 22..to FT /note="D #" XX Chop: Nter=0; Cter=0; Size: 27-27; Related: None; Repeats: 1; Topology: Undefined; Example: Q5X9Q9; Scope: Bacteria; Streptococcus Comments: None; XX # Revision 1.1 2023/07/05 // AC PRU01375; DC Domain; TR PROSITE; PS52031; GG_LECTIN; 1; level=0 XX Names: GG-type lectin domain Function: The GG domain, with two well-conserved glycine residues, is present in eukaryotic FAM3 superfamily (FAM3A, FAM3B, FAM3C and FAM3D), POMGnT1 (protein O-linked mannose beta-1,2-N-acetylglucosaminyltransferase), TEM2 proteins as well as phage gp35 proteins. The GG domain is a lectin with carbohydrate-binding activity. XX GO GO:0030246; F:carbohydrate binding XX KW Lectin XX FT From: PS52031 FT DOMAIN from..to FT /note="GG-type lectin #" XX Chop: Nter=0; Cter=0; Size: 135-172; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q9D309; Scope: Eukaryota; Euteleostomi Viruses; Tequatrovirus Comments: None; XX # Revision 1.1 2023/07/13 // AC PRU01376; DC Domain; TR PROSITE; PS52032; MARR_BRCT_CHROMO; 1; level=0 XX Names: MarR-like, BRCT and chromo domains module Function: The N-terminus of the BAF155/SMARCC1 and BAF170/SMARCC2 subunits contain a putative DNA-binding MarR-like domain, a chromo domain and a BRCT domain that are interconnected to each other to form a distinct module. This N-terminal module could participate in an interaction involving both protein and nucleic acid components. XX CC -!- SIMILARITY: Belongs to the SMARCC family. XX GO GO:0000785; C:chromatin GO GO:0006338; P:chromatin remodeling GO GO:0016514; C:SWI/SNF complex XX KW Chromatin regulator XX FT From: PS52032 FT REGION from..to FT /note="MarR-like, BRCT and chromo domains module #" FT DOMAIN 11..137 FT /note="MarR-like #" FT DOMAIN 141..184 FT /note="BRCT #1; N-terminus" FT DOMAIN 190..218 FT /note="Chromo #" FT DOMAIN 234..258 FT /note="BRCT #1; C-terminus" XX Chop: Nter=0; Cter=0; Size: 274-275; Related: None; Repeats: 1; Topology: Undefined; Example: P97496; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.3 2023/07/27 // AC PRU01377; DC Domain; TR PROSITE; PS52033; CYSTATIN_LXN; 1; level=0 XX Names: Latexin (LXN)-type cystatin domain Function: The LXN-type cystatin domains are packed against each other through the helices and linked by a connecting segment encompassing a third alpha- helix. The two domains are arranged so that there is a cleft in this part of the structure that can accommodate a peptide chain. XX CC -!- SIMILARITY: Belongs to the protease inhibitor I47 (latexin) CC family. XX GO GO:0008191; F:metalloendopeptidase inhibitor activity XX KW Protease inhibitor XX FT From: PS52033 FT DOMAIN from..to FT /note="Cystatin LXN-type #" XX Chop: Nter=0; Cter=0; Size: 97-116; Related: None; Repeats: 2; Topology: Undefined; Example: Q64361; Scope: Eukaryota; Euteleostomi Comments: None; XX # Revision 1.1 2023/07/28 // AC PRU01378; DC Domain; TR PROSITE; PS52034; PEPTIDASE_M32; 1; level=0 XX Names: Peptidase family M32 domain Function: The M32 family of Zn-dependent metallocarboxypeptidases (MCPs) contains a group of hydrolases, which although being broadly distributed among prokaryotic organisms, are only present in a few eukaryotes including some green algae and trypanosomatids. XX case and DE + AltName: EC=3.4.17.19; end case XX case and CC -!- CATALYTIC ACTIVITY: Reaction=Release of a C-terminal amino acid CC with broad specificity, except for -Pro.; EC=3.4.17.19; end case case CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=CHEBI:60240; CC Note=Binds 1 divalent metal cation per subunit. end case CC -!- SIMILARITY: Belongs to the peptidase M32 family. XX case and GO GO:0004181; F:metallocarboxypeptidase activity GO GO:0006508; P:proteolysis XX KW Carboxypeptidase KW Hydrolase KW Metalloprotease KW Protease end case case KW Metal-binding end case XX FT From: PS52034 FT DOMAIN from..to FT /note="Peptidase M32 #" FT MOTIF 232..234 FT /note="HPF #" FT Condition: H-P-F FT MOTIF 241..245 FT /note="DXRXT #" FT Condition: D-x-R-x-T FT MOTIF 262..266 FT /note="HEXXH #" FT Condition: H-E-x(2)-H FT MOTIF 291..294 FT /note="HES/GQ #" FT Condition: H-E-[SG]-Q FT MOTIF 344..349 FT /note="I/NRXXA/SD #" FT Condition: [IN]-R-x(2)-[AS]-D FT MOTIF 399..406 FT /note="GXXQDXHW #" FT Condition: G-x(2)-Q-D-x-H-W FT ACT_SITE 263 FT /note="Proton donor/acceptor" FT Tag: act_site; Condition: E FT BINDING 262 FT /ligand="a divalent metal cation #" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 266 FT /ligand="a divalent metal cation #" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 292 FT /ligand="a divalent metal cation #" FT /ligand_id="ChEBI:CHEBI:60240" FT /ligand_note="catalytic" FT Group: 1; Condition: E XX Chop: Nter=0; Cter=0; Size: 494-504; Related: None; Repeats: 1; Topology: Undefined; Example: P50848; Scope: Bacteria Archaea; Pyrococcus Comments: None; XX # Revision 1.2 2023/08/08 // AC PRU01379; DC Domain; TR PROSITE; PS52035; PEPTIDASE_M14; 1; level=0 XX Names: Peptidase family M14 domain Function: M14 metallocarboxypeptidases are a diverse and important class of peptidases that catalyze the removal of the C-terminal residue from polypeptides by means of a coordinated Zn(2+) cofactor. XX case CC -!- COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case CC -!- SIMILARITY: Belongs to the peptidase M14 family. XX case GO GO:0008270; F:zinc ion binding end case case and GO GO:0004181; F:metallocarboxypeptidase activity GO GO:0006508; P:proteolysis XX KW Carboxypeptidase KW Hydrolase KW Metalloprotease KW Protease end case case KW Metal-binding KW Zinc end case XX FT From: PS52035 FT DOMAIN from..to FT /note="Peptidase M14 #" FT ACT_SITE 256 FT /note="Proton donor/acceptor" FT Tag: act_site; Condition: E FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 65 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: E FT BINDING 182 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 234-454; Related: None; Repeats: 1-3; Topology: Undefined; Example: Q09M02; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.2 2023/08/29 // AC PRU01380; DC Domain; TR PROSITE; PS52036; ZF_RG_N; 1; level=0 XX Names: Zinc finger reverse gyrase N-terminal-type Function: Reverse gyrase (RG) is an ATP-dependent topoisomerase that is only found in archaeal and bacterial hyperthermophiles (above 80 degre C) and thermophiles (65-80 degre C). RGs share a modular structure with an N- terminal cysteine-rich region (a zinc finger) preceding a helicase domain that is followed by a C-terminal topoisomerase domain. The helicase domain is subdivided into H1 and H2 domains that are flexibly linked. Some RG topoisomerase domains also include a cysteine-rich region that has been proposed to form a second zinc finger. The two zinc-finger motifs are found to be important to the structure stability maintenance of RG at high temperature. The N-terminal zinc finger firmly attaches the H1 domain to the topoisomerase domain and may contribute to double-strand DNA (dsDNA) binding. XX case ( and and and ) CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; XX GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS52036 case ( and and and ) FT ZN_FING from..to FT /note="RG N-terminal-type #" else case ( and and and ) FT ZN_FING from..to FT /note="RG N-terminal-type #; atypical" else FT ZN_FING from..to FT /note="RG N-terminal-type #; degenerate" end case FT BINDING 11 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 32 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 37-47; Related: None; Repeats: 1; Topology: Undefined; Example: P0DW67; Scope: Archaea Bacteria Comments: None; XX # Revision 1.1 2023/09/13 // AC PRU01381; DC Domain; TR PROSITE; PS52037; ZF_RG_C; 1; level=0 XX Names: Zinc finger reverse gyrase C-terminal-type Function: Reverse gyrase (RG) is an ATP-dependent topoisomerase that is only found in archaeal and bacterial hyperthermophiles (above 80 degre C) and thermophiles (65-80 degre C). The RG C-terminal-type zinc finger is inserted into the Toprim domain at the base of the DNA-binding site and protrudes from the surface of the topoisomerase domain. XX case ( and and and ) CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; XX GO GO:0046872; F:metal ion binding GO GO:0008270; F:zinc ion binding XX KW Metal-binding KW Zinc end case KW Zinc-finger XX FT From: PS52037 case ( and and and ) FT ZN_FING from..to FT /note="RG C-terminal-type #" else case ( and and and ) FT ZN_FING from..to FT /note="RG C-terminal-type #; atypical" else FT ZN_FING from..to FT /note="RG C-terminal-type #; degenerate" end case FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 18 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT Group: 1; Condition: [CH] XX Chop: Nter=0; Cter=0; Size: 28-30; Related: None; Repeats: 1; Topology: Undefined; Example: O29238; Scope: Archaea Bacteria Comments: None; XX # Revision 1.1 2023/09/13 // AC PRU01382; DC Domain; TR PROSITE; PS52038; TOPO_IB_2; 1; level=0 XX Names: Topoisomerase (Topo) IB-type catalytic domain Function: The RKKRH/N "catalytic pentad", conserved in all members of the topo IB family, catalyzes the attack of the active site tyrosine nucleophile on the scissile phosphodiester. XX case DE + AltName: EC=5.6.2.1; XX CC -!- CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single- CC stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; CC -!- SIMILARITY: Belongs to the type IB topoisomerase family. XX DR PROSITE; PS00176; TOPO_IB_1; 1; trigger=no XX GO GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity GO GO:0006265; P:DNA topological change end case GO GO:0003677; F:DNA binding XX KW DNA-binding case KW Isomerase KW Topoisomerase end case XX FT From: PS52038 FT DOMAIN from..to FT /note="Topo IB-type catalytic #" FT ACT_SITE 262 FT /note="O-(3'-phospho-DNA)-tyrosine intermediate" FT Tag: act_site; Condition: Y XX Chop: Nter=0; Cter=0; Size: 238-475; Related: None; Repeats: 1; Topology: Undefined; Example: Q8R4U6; Scope: Eukaryota Viruses; Nucleocytoviricota Comments: None; XX # Revision 1.1 2023/09/19 // AC PRU01383; DC Domain; TR PROSITE; PS52039; TOPO_IA_2; 1; level=0 XX Names: Topoisomerase (Topo) IA-type catalytic domain Function: Topo IA form a transient 5'-phospho-tyrosine covalent intermediate and release a free 3'-OH strand. The Topo IA-type catalytic domain consisting of subdomains III, II and IV exhibits a typical toroidal shape with a central hole able to accommodate single-strand or double-strand DNA. XX CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. XX case DR PROSITE; PS00396; TOPO_IA_1; 1; trigger=no end case XX GO GO:0003677; F:DNA binding case GO GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity XX KW Isomerase KW Topoisomerase end case KW DNA-binding XX FT From: PS52039 FT DOMAIN from..to FT /note="Topo IA-type catalytic #" FT ACT_SITE 158 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT Tag: act_site; Condition: Y XX Chop: Nter=0; Cter=0; Size: 269-889; Related: None; Repeats: 1; Topology: Undefined; Example: Q9NG98; Scope: Bacteria Archaea Eukaryota Viruses; Mimivirus bradfordmassiliense Comments: None; XX # Revision 1.1 2023/09/28 // AC PRU01384; DC Domain; TR PROSITE; PS52040; TOPO_IIA; 1; level=0 XX Names: Topoisomerase (Topo) IIA-type catalytic domain Function: Type IIA enzymes include topoisomerase II (topo II) encoded by both eukaryotes and viruses, and DNA gyrase and topoisomerase IV (topo IV) encoded by bacteria. The Topo IIA-type catalytic domain containing the active site tyrosine involved in the covalent complex with DNA is located on the C- terminal region of eukaryal enzymes or on the A-subunit of bacterial enzymes (GyrA or ParC for gyrase and Topo IV respectively). XX case DE + AltName: EC=5.6.2.2; CC -!- CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and CC rejoining of double-stranded DNA.; EC=5.6.2.2; end case XX GO GO:0003677; F:DNA binding case GO GO:0006265; P:DNA topological change XX KW Isomerase KW Topoisomerase end case KW DNA-binding XX FT From: PS52040 FT DOMAIN from..to FT /note="Topo IIA-type catalytic #" FT ACT_SITE 93 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT Tag: act_site; Condition: Y XX Chop: Nter=0; Cter=0; Size: 60-890; Related: None; Repeats: 1; Topology: Undefined; Example: P0C1U9; Scope: Bacteria Eukaryota Viruses Archaea; Haloferacaceae Comments: None; XX # Revision 1.1 2023/10/05 // AC PRU01385; DC Domain; TR PROSITE; PS52041; TOPO_IIB; 1; level=0 XX Names: Topoisomerase (Topo) IIB-type catalytic domain Function: DNA cleavage by topo VI generates two-nucleotide 5'-protruding ends. XX case DE + AltName: EC=5.6.2.2; CC -!- CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and CC rejoining of double-stranded DNA.; EC=5.6.2.2; end case CC -!- SIMILARITY: Belongs to the TOP6A family. XX GO GO:0003677; F:DNA binding case GO GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity XX KW Isomerase KW Topoisomerase end case KW DNA-binding XX FT From: PS52041 FT DOMAIN from..to FT /note="Topo IIA-type catalytic #" FT ACT_SITE 95 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" FT Tag: act_site; Condition: Y XX Chop: Nter=0; Cter=0; Size: 92-151; Related: None; Repeats: 1; Topology: Undefined; Example: Q9M4A2; Scope: Archaea Eukaryota Comments: None; XX # Revision 1.1 2023/10/13 // AC PRU01386; DC Domain; TR PROSITE; PS52042; GLOBIN_CP_ADGB; 1; level=0 XX Names: Androglobin (Adgb) circularly permuted globin domain Function: Adgb has a unique modular architecture, possessing an N-terminal calpain-like domain, an internal, circular permuted globin domain, and an IQ calmodulin-binding motif. XX DE + AltName: Full=Androglobin; XX CC -!- DOMAIN: The globin domain is circularly permuted. The globin CC domain, which normally consists of eight consecutive alpha-helices CC from A (N-terminal) to H (C-terminal), is circularly permutated CC and split into two parts. The part containing helices A and B is CC shifted C-terminally and is separated from the main globin CC sequence (helices C-H) by a potential calmodulin-binding IQ CC domain. CC -!- SIMILARITY: In the central section; belongs to the globin family. XX DR PROSITE; PS50096; IQ; 1; trigger=yes XX GO GO:0020037; F:heme binding XX case KW Iron KW Metal-binding end case KW Heme XX FT From: PS52042 FT REGION from..131 FT /note="Globin domain; C-terminal part" FT REGION 179..to FT /note="Globin domain; N-terminal part" FT BINDING 30 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="distal binding residue" FT Group: 1; Condition: [QH] FT BINDING 62 FT /ligand="heme b" FT /ligand_id="ChEBI:CHEBI:60344" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="proximal binding residue" FT Group: 1; Condition: H XX Chop: Nter=0; Cter=0; Size: 206-206; Related: None; Repeats: 1; Topology: Undefined; Example: G3UZ78; Scope: Eukaryota; Euarchontoglires Comments: None; XX # Revision 1.1 2023/12/06 // AC PRU01700; DC Domain; TR Metamotif; -; XX Names: ABC transporter superfamily ATP binding cassette superfamily Function: Uses the hydrolysis of ATP to energize diverse biological systems XX CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. XX DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1; trigger=no DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1; trigger=yes XX GO GO:0043190; C:ATP-binding cassette (ABC) transporter complex GO GO:0006810; P:transport GO GO:0005524; F:ATP binding XX case ( or ) and defined and KW Cell inner membrane KW Membrane end case XX Chop: Nter=0; Cter=0; Size: 200-2438; Related: None; Repeats: 1-2; Topology: Not cytoplasmic; Example: P02915; P60752; P13569; Scope: Eukaryota Bacteria Archaea Plastid Viruses Comments: Contains ABC cassette but lost transport capability in UvrA subfamily. XX # Revision 1.20 2016/09/26 // AC PRU10001; DC Domain; TR PROSITE; PS00061; ADH_SHORT; 1; level=0 XX Names: Short-chain dehydrogenases/reductases family Function: Undefined XX FT From: PS00061 FT ACT_SITE 3 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P48814; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.7 2022/04/07 // AC PRU10002; DC Domain; TR PROSITE; PS00064; L_LDH; 1; level=0 XX Names: L-lactate dehydrogenase active site Function: Undefined XX DE + AltName: Full=L-lactate dehydrogenase; DE EC=1.1.1.27; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; CC Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; XX FT From: PS00064 FT ACT_SITE 4 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9PW06; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2019/11/22 // AC PRU10003; DC Domain; TR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1; level=0 XX Names: Hydroxymethylglutaryl-coenzyme A reductases Function: Undefined XX DE + AltName: Full=Hydroxymethylglutaryl-CoA reductase; DE AltName: Full=NADPH; DE EC=1.1.1.34; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3- CC methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; XX FT From: PS01192 FT ACT_SITE 7 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P00347; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10004; DC Domain; TR PROSITE; PS00068; MDH; 1; level=0 XX Names: Malate dehydrogenase active site Function: Undefined XX DE + AltName: Full=Malate dehydrogenase; DE EC=1.1.1.37; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate; CC Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, CC ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37; XX FT From: PS00068 FT ACT_SITE 5 FT /note="Proton relay" FT BINDING 6 FT /ligand="substrate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5U907; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2022/05/14 // AC PRU10005; DC Domain; TR PROSITE; PS00069; G6P_DEHYDROGENASE; 1; level=0 XX Names: Glucose-6-phosphate dehydrogenase active site Function: Undefined XX DE + RecName: EC=1.1.1.-; XX FT From: PS00069 FT BINDING 6 FT /ligand="substrate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q00612; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2022/05/14 // AC PRU10007; DC Domain; TR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1; level=0 XX Names: Aldehyde dehydrogenases glutamic acid active site Function: Undefined XX FT From: PS00687 FT ACT_SITE 2 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9K9B2; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10008; DC Domain; TR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1; level=0 XX Names: Aldehyde dehydrogenases cysteine active site Function: Undefined XX FT From: PS00070 FT ACT_SITE 7 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9K9B2; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2023/07/04 // AC PRU10009; DC Domain; TR PROSITE; PS00071; GAPDH; 1; level=0 XX Names: Glyceraldehyde 3-phosphate dehydrogenase active site Function: Undefined XX DE + AltName: Full=Glyceraldehyde-3-phosphate dehydrogenase; DE AltName: Full=phosphorylating; DE EC=1.2.1.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3- CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12; XX FT From: PS00071 FT ACT_SITE 3 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P09124; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10010; DC Domain; TR PROSITE; PS01224; ARGC; 1; level=0 XX Names: N-acetyl-gamma-glutamyl-phosphate reductase active site Function: Undefined XX FT From: PS01224 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P57156; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10011; DC Domain; TR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1; level=0 XX Names: Glu / Leu / Phe / Val dehydrogenases active site Function: Undefined XX DE + AltName: Full=Glutamate dehydrogenase (NAD(P)(+)); DE EC=1.4.1.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3; XX FT From: PS00074 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q43314; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10012; DC Domain; TR PROSITE; PS00436; PEROXIDASE_2; 1; level=0 XX Names: Peroxidases active site Function: Undefined XX DE + AltName: Full=NAD(P)H oxidase; DE EC=1.6.3.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1; XX FT From: PS00436 FT ACT_SITE 7 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P20010; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10013; DC Domain; TR PROSITE; PS00438; CATALASE_2; 1; level=0 XX Names: Catalase proximal active site Function: Undefined XX DE + AltName: Full=Catalase; DE EC=1.11.1.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; XX FT From: PS00438 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q96528; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10014; DC Domain; TR PROSITE; PS00368; RIBORED_SMALL; 1; level=0 XX Names: Ribonucleotide reductase small subunit Function: Undefined XX DE + AltName: Full=Ribonucleoside-diphosphate reductase; DE EC=1.17.4.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; XX FT From: PS00368 FT BINDING 2 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT BINDING 4 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT ACT_SITE 7 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P26713; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.8 2022/11/19 // AC PRU10015; DC Domain; TR PROSITE; PS01230; TRMA_1; 1; level=0 XX Names: RNA methyltransferase trmA family Function: Undefined XX FT From: PS01230 FT ACT_SITE 10 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q97R12; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10016; DC Domain; TR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1; level=0 XX Names: Thymidylate synthase active site Function: Undefined XX FT From: PS00091 FT ACT_SITE 7 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P54081; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.4 2019/11/22 // AC PRU10017; DC Domain; TR PROSITE; PS00374; MGMT; 1; level=0 XX Names: Methylated-DNA--protein-cysteine methyltransferase active site Function: Undefined XX DE + AltName: Full=Methylated-DNA--[protein]-cysteine S-methyltransferase; DE EC=2.1.1.63; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] CC = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein]; CC Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a CC thymidine in DNA + S-methyl-L-cysteinyl-[protein]; CC Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132, CC Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387; CC EC=2.1.1.63; XX FT From: PS00374 FT ACT_SITE 3 FT /note="Nucleophile; methyl group acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q4J9C6; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10018; DC Domain; TR PROSITE; PS00094; C5_MTASE_1; 1; level=0 XX Names: C-5 cytosine-specific DNA methylases active site Function: Undefined XX DE + AltName: Full=DNA (cytosine-5-)-methyltransferase; DE EC=2.1.1.37; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5- CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37; XX FT From: PS00094 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P25262; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10019; DC Domain; TR PROSITE; PS00958; TRANSALDOLASE_2; 1; level=0 XX Names: Transaldolase active site Function: Undefined XX DE + AltName: Full=Transaldolase; DE EC=2.2.1.2; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = CC beta-D-fructose 6-phosphate + D-erythrose 4-phosphate; CC Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483, CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2; XX FT From: PS00958 FT ACT_SITE 3 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q57TP8; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10020; DC Domain; TR PROSITE; PS00099; THIOLASE_3; 1; level=0 XX Names: Thiolases active site Function: Undefined XX DE + AltName: Full=Acetyl-CoA C-acetyltransferase; DE EC=2.3.1.9; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; XX FT From: PS00099 FT ACT_SITE 6 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8X8J4; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10021; DC Domain; TR PROSITE; PS00100; CAT; 1; level=0 XX Names: Chloramphenicol acetyltransferase active site Function: Undefined XX DE + AltName: Full=Chloramphenicol O-acetyltransferase; DE EC=2.3.1.28; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + chloramphenicol = chloramphenicol 3-acetate + CC CoA; Xref=Rhea:RHEA:18421, ChEBI:CHEBI:16730, ChEBI:CHEBI:17698, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.28; XX FT From: PS00100 FT ACT_SITE 4 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P00485; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10022; DC Domain; TR PROSITE; PS00606; KS3_1; 1; level=0 XX Names: Ketosynthase family 3 (KS3) active site Function: Undefined XX DE + AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I; DE EC=2.3.1.41; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP] CC + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623, CC Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479, CC ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651; XX FT From: PS00606 FT ACT_SITE 7 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P0A954; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2022/08/10 // AC PRU10023; DC Domain; TR PROSITE; PS00441; CHALCONE_SYNTH; 1; level=0 XX Names: Chalcone and stilbene synthases active site Function: Undefined XX DE + AltName: Full=Naringenin-chalcone synthase; DE EC=2.3.1.74; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'- CC tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74; XX FT From: PS00441 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9FSC0; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10024; DC Domain; TR PROSITE; PS00547; TRANSGLUTAMINASES; 1; level=0 XX Names: Transglutaminases active site Function: Undefined XX DE + AltName: Full=Protein-glutamine gamma-glutamyltransferase; DE EC=2.3.2.13; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L- CC lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, CC ChEBI:CHEBI:138370; EC=2.3.2.13; XX FT From: PS00547 FT ACT_SITE 3 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P51176; Scope: Eukaryota Comments: None XX # Revision 1.7 2019/11/22 // AC PRU10027; DC Domain; TR PROSITE; PS00108; PROTEIN_KINASE_ST; 1; level=0 XX Names: Serine/Threonine protein kinases active-site Function: Undefined XX DE + AltName: Full=Serine/threonine-protein; DE EC=2.7.11.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; FT From: PS00108 FT ACT_SITE 3 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P00546; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.7 2023/11/22 // AC PRU10028; DC Domain; TR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1; level=0 XX Names: Tyrosine protein kinases specific active-site Function: Undefined XX DE + AltName: Full=Receptor protein-tyrosine kinase; DE EC=2.7.10.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; XX FT From: PS00109 FT ACT_SITE 4 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P15054; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10029; DC Domain; TR PROSITE; PS00112; GUANIDO_KINASE; 1; level=0 XX Names: ATP:guanido phosphotransferases active site Function: Undefined XX DE + AltName: Full=Creatine kinase; DE EC=2.7.3.2; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + creatine = ADP + H(+) + N-phosphocreatine; CC Xref=Rhea:RHEA:17157, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57947, ChEBI:CHEBI:58092, ChEBI:CHEBI:456216; EC=2.7.3.2; XX FT From: PS00112 FT ACT_SITE 1 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q95V58; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10030; DC Domain; TR PROSITE; PS00469; NDPK; 1; level=0 XX Names: Nucleoside diphosphate kinase (NDPK) active site Function: There is a single histidine residue involved in the catalytic mechanism, conserved in all known active NDPK enzymes. XX DE + AltName: Full=Nucleoside-diphosphate kinase; DE EC=2.7.4.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; XX FT From: PS00469 FT ACT_SITE 2 FT /note="Pros-phosphohistidine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P81766; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.6 2023/12/20 // AC PRU10031; DC Domain; TR PROSITE; PS00900; RNA_POL_PHAGE_1; 1; level=0 XX Names: Bacteriophage-type RNA polymerase family active site Function: Undefined XX DE + AltName: Full=DNA-directed RNA polymerase; DE EC=2.7.7.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.6; XX FT From: PS00900 FT ACT_SITE 3 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P69243; Scope: Eukaryota Viruses Comments: None XX # Revision 1.7 2021/06/03 // AC PRU10032; DC Domain; TR PROSITE; PS00489; RNA_POL_PHAGE_2; 1; level=0 XX Names: Bacteriophage-type RNA polymerase family active site Function: Undefined XX DE + AltName: Full=DNA-directed RNA polymerase; DE EC=2.7.7.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.6; XX FT From: PS00489 FT ACT_SITE 3 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P69243; Scope: Eukaryota Viruses Comments: None XX # Revision 1.7 2021/06/03 // AC PRU10033; DC Domain; TR PROSITE; PS00117; GAL_P_UDP_TRANSF_I; 1; level=0 XX Names: Galactose-1-phosphate uridyl transferase family 1 active site Function: Undefined XX DE + AltName: Full=UDP-glucose--hexose-1-phosphate uridylyltransferase; DE EC=2.7.7.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D- CC glucose 1-phosphate + UDP-alpha-D-galactose; Xref=Rhea:RHEA:13989, CC ChEBI:CHEBI:58336, ChEBI:CHEBI:58601, ChEBI:CHEBI:58885, CC ChEBI:CHEBI:66914; EC=2.7.7.12; XX FT From: PS00117 FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT ACT_SITE 9 FT /note="Tele-UMP-histidine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P31764; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.8 2022/11/19 // AC PRU10034; DC Domain; TR PROSITE; PS01274; COA_TRANSF_2; 1; level=0 XX Names: Coenzyme A transferases Function: Undefined XX DE + AltName: Full=3-oxoacid CoA-transferase; DE EC=2.8.3.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 3-oxo acid + succinyl-CoA = a 3-oxoacyl-CoA + succinate; CC Xref=Rhea:RHEA:24564, ChEBI:CHEBI:30031, ChEBI:CHEBI:35973, CC ChEBI:CHEBI:57292, ChEBI:CHEBI:90726; EC=2.8.3.5; XX FT From: PS01274 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q59091; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10035; DC Domain; TR PROSITE; PS00118; PA2_HIS; 1; level=0 XX Names: Phospholipase A2 histidine active site Function: Undefined XX DE + AltName: Full=Phospholipase A(2); DE EC=3.1.1.4; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; XX FT From: PS00118 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P45881; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10036; DC Domain; TR PROSITE; PS00119; PA2_ASP; 1; level=0 XX Names: Phospholipase A2 aspartic acid active site Function: Undefined XX DE + AltName: Full=Phospholipase A(2); DE EC=3.1.1.4; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; XX FT From: PS00119 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P45881; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10037; DC Domain; TR PROSITE; PS00120; LIPASE_SER; 1; level=0 XX Names: Lipases, serine active site Function: Undefined XX FT From: PS00120 FT ACT_SITE 7 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8VBX1; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10038; DC Domain; TR PROSITE; PS01174; LIPASE_GDXG_SER; 1; level=0 XX Names: Lipolytic enzymes "G-D-X-G" family, putative serine active site Function: Undefined XX FT From: PS01174 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q05469; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10039; DC Domain; TR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1; level=0 XX Names: Carboxylesterases type-B serine active site Function: Undefined XX DE + AltName: Full=Carboxylesterase; DE EC=3.1.1.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); CC Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; XX FT From: PS00122 FT ACT_SITE 7 FT /note="Acyl-ester intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8VCT4; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10040; DC Domain; TR PROSITE; PS00503; PECTINESTERASE_2; 1; level=0 XX Names: Pectinesterase Function: Undefined XX FT From: PS00503 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O04886; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10041; DC Domain; TR PROSITE; PS01328; 4HBCOA_THIOESTERASE; 1; level=0 XX Names: 4-hydroxybenzoyl-CoA thioesterase family active site Function: Undefined XX DE + AltName: Full=4-hydroxybenzoyl-CoA thioesterase; DE EC=3.1.2.23; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=4-hydroxybenzoyl-CoA + H2O = 4-hydroxybenzoate + CoA + H(+); CC Xref=Rhea:RHEA:11948, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17879, ChEBI:CHEBI:57287, ChEBI:CHEBI:57356; EC=3.1.2.23; XX FT From: PS01328 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P44679; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10042; DC Domain; TR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1; level=0 XX Names: Alkaline phosphatase active site Function: Undefined XX DE + AltName: Full=Alkaline phosphatase; DE EC=3.1.3.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate; CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; XX FT From: PS00123 FT ACT_SITE 3 FT /note="Phosphoserine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P35483; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10043; DC Domain; TR PROSITE; PS00124; FBPASE; 1; level=0 XX Names: Fructose-1-6-bisphosphatase active site Function: Undefined XX DE + AltName: Full=Fructose-bisphosphatase; DE EC=3.1.3.11; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6- CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; XX FT From: PS00124 FT ACT_SITE 2 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9MA79; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10044; DC Domain; TR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1; level=0 XX Names: Tyrosine specific protein phosphatases active site Function: Undefined XX DE + AltName: Full=Protein-tyrosine-phosphatase; DE EC=3.1.3.48; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620; EC=3.1.3.48; XX FT From: PS00383 FT ACT_SITE 3 FT /note="Phosphocysteine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5BIP9; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10045; DC Domain; TR PROSITE; PS00530; RNASE_T2_1; 1; level=0 XX Names: Ribonuclease T2 family histidine active site 1 Function: Undefined XX DE + AltName: Full=Ribonuclease T(2); DE EC=4.6.1.19; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'- CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA- CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, CC ChEBI:CHEBI:173118; EC=4.6.1.19; XX FT From: PS00530 FT ACT_SITE 3 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O80322; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2021/08/23 // AC PRU10046; DC Domain; TR PROSITE; PS00531; RNASE_T2_2; 1; level=0 XX Names: Ribonuclease T2 family histidine active site 2 Function: Undefined XX DE + AltName: Full=Ribonuclease T(2); DE EC=4.6.1.19; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'- CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA- CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284, CC ChEBI:CHEBI:173118; EC=4.6.1.19; XX FT From: PS00531 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P81296; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.7 2021/08/23 // AC PRU10047; DC Domain; TR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1; level=0 XX Names: DNA/RNA non-specific endonucleases active site Function: Undefined XX DE + AltName: Full=Serratia marcescens nuclease; DE EC=3.1.30.2; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphomononucleotide and 5'- CC phosphooligonucleotide end-products.; EC=3.1.30.2; XX FT From: PS01070 FT ACT_SITE 4 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P08466; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10048; DC Domain; TR PROSITE; PS01123; TNASE_1; 1; level=0 XX Names: Thermonuclease family Function: Undefined XX DE + AltName: Full=Micrococcal nuclease; DE EC=3.1.31.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'- CC phosphooligonucleotide end-products.; EC=3.1.31.1; XX FT From: PS01123 FT ACT_SITE 7 FT ACT_SITE 12 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5HHM4; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10049; DC Domain; TR PROSITE; PS01284; TNASE_2; 1; level=0 XX Names: Thermonuclease family Function: Undefined XX DE + AltName: Full=Micrococcal nuclease; DE EC=3.1.31.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'- CC phosphooligonucleotide end-products.; EC=3.1.31.1; XX FT From: PS01284 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5HHM4; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10050; DC Domain; TR PROSITE; PS00679; BETA_AMYLASE_2; 1; level=0 XX Names: Beta-amylase active site 2 Function: Undefined XX DE + AltName: Full=Beta-amylase; DE EC=3.2.1.2; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-alpha-D-glucosidic linkages in CC polysaccharides so as to remove successive maltose units from the CC non-reducing ends of the chains.; EC=3.2.1.2; XX FT From: PS00679 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P16098; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10051; DC Domain; TR PROSITE; PS00820; GLUCOAMYLASE; 1; level=0 XX Names: Glucoamylase active site region Function: Undefined XX DE + AltName: Full=Glucan 1,4-alpha-glucosidase; DE EC=3.2.1.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues CC successively from non-reducing ends of the chains with release of CC beta-D-glucose.; EC=3.2.1.3; XX FT From: PS00820 FT ACT_SITE 3 FT /note="Proton acceptor" FT ACT_SITE 5 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P23176; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10052; DC Domain; TR PROSITE; PS00502; POLYGALACTURONASE; 1; level=0 XX Names: Polygalacturonase active site Function: Undefined XX FT From: PS00502 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q00446; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10053; DC Domain; TR PROSITE; PS01095; GH18_1; 1; level=0 XX Names: Glycosyl hydrolases family 18 (GH18) active site Function: Undefined XX DE + AltName: Full=Chitinase; DE EC=3.2.1.14; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; XX FT From: PS01095 FT ACT_SITE 8 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q95M17; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.7 2019/11/22 // AC PRU10054; DC Domain; TR PROSITE; PS00385; ALPHA_L_FUCOSIDASE; 1; level=0 XX Names: Alpha-L-fucosidase putative active site Function: Undefined XX DE + AltName: Full=Alpha-L-fucosidase; DE EC=3.2.1.51; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose; CC Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51; XX FT From: PS00385 FT SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P49713; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10055; DC Domain; TR PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1; level=0 XX Names: Glycosyl hydrolases family 1 active site Function: Undefined XX DE + RecName: EC=3.2.1.-; XX FT From: PS00572 FT ACT_SITE 5 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P50977; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10056; DC Domain; TR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1; level=0 XX Names: Glycosyl hydrolases family 6 Function: Undefined XX DE + RecName: EC=3.2.1.-; XX FT From: PS00655 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P26414; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10057; DC Domain; TR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1; level=0 XX Names: Glycosyl hydrolases family 6 Function: Undefined XX DE + RecName: EC=3.2.1.-; XX FT From: PS00656 FT ACT_SITE 7 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P33682; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10058; DC Domain; TR PROSITE; PS00812; GLYCOSYL_HYDROL_F8; 1; level=0 XX Names: Glycosyl hydrolases family 8 Function: Undefined XX DE + RecName: EC=3.2.1.-; XX FT From: PS00812 FT ACT_SITE 3 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P27032; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10059; DC Domain; TR PROSITE; PS00592; GH9_2; 1; level=0 XX Names: Glycosyl hydrolases family 9 (GH9) active site H Function: Three conserved regions in these enzymes are centered on conserved residues which have been shown to be important for the catalytic activity. The second region contains an active site histidine. XX DE + RecName: EC=3.2.1.-; XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family. XX GO GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds XX KW Carbohydrate metabolism KW Glycosidase KW Hydrolase KW Polysaccharide degradation XX FT From: PS00592 FT ACT_SITE 15 FT Condition: H XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P28622; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10060; DC Domain; TR PROSITE; PS00698; GH9_3; 1; level=0 XX Names: Glycosyl hydrolases family 9 (GH9) active site Function: Three conserved regions in these enzymes are centered on conserved residues which have been shown to be important for the catalytic activity. The third one contains two catalytically important residues: an aspartate and a glutamate. XX DE + RecName: EC=3.2.1.-; XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family. XX GO GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds XX KW Carbohydrate metabolism KW Glycosidase KW Hydrolase KW Polysaccharide degradation XX FT From: PS00698 FT ACT_SITE 2 FT Condition: D FT ACT_SITE 4 FT Condition: E XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P28622; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10061; DC Domain; TR PROSITE; PS00591; GH10_1; 1; level=0 XX Names: Glycosyl hydrolases family 10 active site Function: Undefined XX FT From: PS00591 FT ACT_SITE 7 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O60206; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.4 2019/11/22 // AC PRU10062; DC Domain; TR PROSITE; PS00776; GH11_1; 1; level=0 XX Names: Glycosyl hydrolases family 11 active site Function: Undefined XX DE + AltName: Full=Endo-1,4-beta-xylanase; DE EC=3.2.1.8; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; XX FT From: PS00776 FT ACT_SITE 3 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P55334; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2019/11/22 // AC PRU10063; DC Domain; TR PROSITE; PS00777; GH11_2; 1; level=0 XX Names: Glycosyl hydrolases family 11 active site Function: Undefined XX DE + AltName: Full=Endo-1,4-beta-xylanase; DE EC=3.2.1.8; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.; CC EC=3.2.1.8; XX FT From: PS00777 FT ACT_SITE 2 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P55334; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2019/11/22 // AC PRU10064; DC Domain; TR PROSITE; PS01034; GH16_1; 1; level=0 XX Names: Glycosyl hydrolases family 16 active sites Function: Undefined XX DE + RecName: EC=3.2.1.-; XX FT From: PS01034 FT ACT_SITE 1 FT /note="Nucleophile" FT ACT_SITE 5 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P07883; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10065; DC Domain; TR PROSITE; PS00953; GLYCOSYL_HYDROL_F25_1; 1; level=0 XX Names: Glycosyl hydrolases family 25 active site Function: Undefined XX DE + AltName: Full=Lysozyme; DE EC=3.2.1.17; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and CC between N-acetyl-D-glucosamine residues in chitodextrins.; CC EC=3.2.1.17; XX FT From: PS00953 FT ACT_SITE 1 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P19385; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.8 2019/11/22 // AC PRU10066; DC Domain; TR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1; level=0 XX Names: Glycosyl hydrolases family 31 active site Function: Undefined XX DE + AltName: Full=Glucan 1,4-alpha-glucosidase; DE EC=3.2.1.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues CC successively from non-reducing ends of the chains with release of CC beta-D-glucose.; EC=3.2.1.3; XX FT From: PS00129 FT ACT_SITE 4 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9BE70; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10067; DC Domain; TR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1; level=0 XX Names: Glycosyl hydrolases family 32 active site Function: Undefined XX DE + AltName: Full=Beta-fructofuranosidase; DE EC=3.2.1.26; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside CC residues in beta-D-fructofuranosides.; EC=3.2.1.26; XX FT From: PS00609 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P10594; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10068; DC Domain; TR PROSITE; PS01027; GLYCOSYL_HYDROL_F39; 1; level=0 XX Names: Glycosyl hydrolases family 39 active site Function: Undefined XX DE + AltName: Full=Xylan 1,4-beta-xylosidase; DE EC=3.2.1.37; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-D-xylans, to remove successive D- CC xylose residues from the non-reducing termini.; EC=3.2.1.37; XX FT From: PS01027 FT ACT_SITE 6 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9ZFM2; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10069; DC Domain; TR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1; level=0 XX Names: Glycosyl hydrolases family 45 active site Function: Undefined XX DE + AltName: Full=Cellulase; DE EC=3.2.1.4; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; XX FT From: PS01140 FT ACT_SITE 6 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P43317; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10070; DC Domain; TR PROSITE; PS60000; CHITOSANASE_46_80; 1; level=0 XX Names: Chitosanases families 46 and 80 active sites Function: Undefined XX DE + AltName: Full=Chitosanase; DE EC=3.2.1.132; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Endohydrolysis of beta-(1->4)-linkages between D-glucosamine CC residues in a partly acetylated chitosan.; EC=3.2.1.132; XX FT From: PS60000 FT ACT_SITE 1 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P48846; Scope: Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10071; DC Domain; TR PROSITE; PS00922; TRANSGLYCOSYLASE; 1; level=0 XX Names: Prokaryotic transglycosylases Function: Undefined XX FT From: PS00922 FT ACT_SITE 2 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P0AEZ8; Scope: Bacteria Viruses Comments: None XX # Revision 1.4 2019/11/22 // AC PRU10072; DC Domain; TR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1; level=0 XX Names: Uracil-DNA glycosylase Function: Undefined XX FT From: PS00130 FT ACT_SITE 7 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5LA67; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10073; DC Domain; TR PROSITE; PS00869; RENAL_DIPEPTIDASE_1; 1; level=0 TR PROSITE; PS51365; RENAL_DIPEPTIDASE_2; 1; level=0 XX Names: Renal dipeptidase family microsomal dipeptidase membrane dipeptidase Function: Renal dipeptidase (rDP) (EC 3.4.13.19) and related enzymes are zinc-dependent metalloenzymes which hydrolyze a wide range of dipeptides. XX case or or not DE + AltName: Full=dipeptidase; DE EC=3.4.13.19; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=an L-aminoacyl-L-amino acid + H2O = 2 an L-alpha-amino acid; CC Xref=Rhea:RHEA:48940, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, CC ChEBI:CHEBI:77460; EC=3.4.13.19; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; end case case and and CC -!- SUBUNIT: Homodimer; disulfide-linked. end case CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Peptidase M19 family. XX case or GO GO:0016805; F:dipeptidase activity GO GO:0016787; F:hydrolase activity GO GO:0046872; F:metal ion binding GO GO:0008237; F:metallopeptidase activity GO GO:0008233; F:peptidase activity GO GO:0008270; F:zinc ion binding XX KW Dipeptidase KW Hydrolase KW Metal-binding KW Metalloprotease KW Protease KW Zinc end case case KW Disulfide bond end case XX FT From: PS51365 FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: H FT BINDING 22 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: D FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" FT Group: 1; Condition: E FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: E FT BINDING 198 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: Y FT BINDING 219 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#2" FT /ligand_note="catalytic" FT Group: 2; Condition: H FT BINDING 152 FT /ligand="substrate" FT Condition: H FT BINDING 230 FT /ligand="substrate" FT Condition: R FT BINDING 290 FT /ligand="substrate" FT Condition: D FT DISULFID 71..154 FT Tag: disulf; Group: 3; Condition: C-x*-C FT DISULFID 226..258 FT Tag: disulf; Group: 4; Condition: C-x*-C FT DISULFID 365 FT /note="Interchain" FT Tag: disulf; Condition: C-x*-C FT From: PS00869 case not FT BINDING 2 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="#1" FT /ligand_note="catalytic" end case XX Chop: Nter=0; Cter=1; Size: 260-380; Related: None; Repeats: 1; Topology: Undefined; Example: Q3SZM7; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.13 2022/11/19 // AC PRU10074; DC Domain; TR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1; level=0 XX Names: Serine carboxypeptidases, serine active site Function: Undefined XX DE + AltName: Full=Carboxypeptidase C; DE EC=3.4.16.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of a C-terminal amino acid with broad specificity.; CC EC=3.4.16.5; XX FT From: PS00131 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9HB40; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10075; DC Domain; TR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1; level=0 XX Names: Serine carboxypeptidases, histidine active site Function: Undefined XX DE + AltName: Full=Carboxypeptidase C; DE EC=3.4.16.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of a C-terminal amino acid with broad specificity.; CC EC=3.4.16.5; XX FT From: PS00560 FT ACT_SITE 7 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P37891; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10076; DC Domain; TR PROSITE; PS01333; PYRASE_GLU; 1; level=0 XX Names: Pyrrolidone-carboxylate peptidase glutamic acid active site Function: Undefined XX DE + AltName: Full=Pyroglutamyl-peptidase I; DE EC=3.4.19.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal pyroglutamyl group from a CC polypeptide, the second amino acid generally not being Pro.; CC EC=3.4.19.3; XX FT From: PS01333 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P65678; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10077; DC Domain; TR PROSITE; PS01334; PYRASE_CYS; 1; level=0 XX Names: Pyrrolidone-carboxylate peptidase cysteine active site Function: Undefined XX DE + AltName: Full=Pyroglutamyl-peptidase I; DE EC=3.4.19.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal pyroglutamyl group from a CC polypeptide, the second amino acid generally not being Pro.; CC EC=3.4.19.3; XX FT From: PS01334 FT ACT_SITE 10 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P65678; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10078; DC Domain; TR PROSITE; PS00134; TRYPSIN_HIS; 1; level=0 XX Names: Serine proteases, trypsin family, histidine active site Function: Undefined XX DE + AltName: Full=Chymotrypsin; DE EC=3.4.21.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|- CC Xaa.; EC=3.4.21.1; XX FT From: PS00134 FT ACT_SITE 5 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P09582; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10079; DC Domain; TR PROSITE; PS00135; TRYPSIN_SER; 1; level=0 XX Names: Serine proteases, trypsin family, serine active site Function: Undefined XX DE + AltName: Full=Chymotrypsin; DE EC=3.4.21.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|- CC Xaa.; EC=3.4.21.1; XX FT From: PS00135 FT ACT_SITE 5 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P04187; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10080; DC Domain; TR PROSITE; PS00136; SUBTILASE_ASP; 1; level=0 XX Names: Serine proteases, subtilase family, aspartic acid active site Function: Undefined XX DE + AltName: Full=Subtilisin-like protease; DE EC=3.4.-.-; XX FT From: PS00136 FT ACT_SITE 5 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P29120; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10081; DC Domain; TR PROSITE; PS00137; SUBTILASE_HIS; 1; level=0 XX Names: Serine proteases, subtilase family, histidine active site Function: Undefined XX DE + AltName: Full=Subtilisin-like protease; DE EC=3.4.-.-; XX FT From: PS00137 FT ACT_SITE 1 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P58099; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10082; DC Domain; TR PROSITE; PS00138; SUBTILASE_SER; 1; level=0 XX Names: Serine proteases, subtilase family, serine active site Function: Undefined XX DE + AltName: Full=Subtilisin-like protease; DE EC=3.4.-.-; XX FT From: PS00138 FT ACT_SITE 3 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P08594; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10083; DC Domain; TR PROSITE; PS00673; V8_SER; 1; level=0 XX Names: Serine proteases, V8 family, serine active site Function: Undefined XX DE + AltName: Full=Glutamyl endopeptidase; DE EC=3.4.21.19; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.; EC=3.4.21.19; XX FT From: PS00673 FT ACT_SITE 4 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5HH35; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10084; DC Domain; TR PROSITE; PS00708; PRO_ENDOPEP_SER; 1; level=0 XX Names: Prolyl endopeptidase family serine active site Function: Undefined XX DE + AltName: Full=Dipeptidyl-peptidase IV; DE EC=3.4.14.5; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a CC polypeptide, preferentially when Yaa is Pro, provided Zaa is neither CC Pro nor hydroxyproline.; EC=3.4.14.5; XX FT From: PS00708 FT ACT_SITE 5 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9XTA2; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10085; DC Domain; TR PROSITE; PS00381; CLP_PROTEASE_SER; 1; level=0 XX Names: Endopeptidase Clp serine active site Function: Undefined XX DE + AltName: Full=Endopeptidase Clp; DE EC=3.4.21.92; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins to small peptides in the presence of CC ATP and magnesium. alpha-casein is the usual test substrate. In the CC absence of ATP, only oligopeptides shorter than five residues are CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr- CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also CC occurs).; EC=3.4.21.92; XX FT From: PS00381 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9K709; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.8 2022/04/28 // AC PRU10086; DC Domain; TR PROSITE; PS00382; CLP_PROTEASE_HIS; 1; level=0 XX Names: Endopeptidase Clp histidine active site Function: Undefined XX DE + AltName: Full=Endopeptidase Clp; DE EC=3.4.21.92; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins to small peptides in the presence of CC ATP and magnesium. alpha-casein is the usual test substrate. In the CC absence of ATP, only oligopeptides shorter than five residues are CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr- CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also CC occurs).; EC=3.4.21.92; XX FT From: PS00382 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q81PL4; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2022/04/28 // AC PRU10087; DC Domain; TR PROSITE; PS01046; LON_SER; 1; level=0 XX Names: ATP-dependent serine proteases, lon family, serine active site Function: Undefined XX DE + AltName: Full=Endopeptidase La; DE EC=3.4.21.53; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53; XX FT From: PS01046 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P57549; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10088; DC Domain; TR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1; level=0 XX Names: Eukaryotic thiol (cysteine) proteases cysteine active site Function: Undefined XX CC -!- SIMILARITY: Belongs to the peptidase C1 family. XX GO GO:0004197; F:cysteine-type endopeptidase activity GO GO:0006508; P:proteolysis XX KW Hydrolase KW Protease KW Thiol protease XX FT From: PS00139 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P00786; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10089; DC Domain; TR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1; level=0 XX Names: Eukaryotic thiol (cysteine) proteases histidine active site Function: Undefined XX CC -!- SIMILARITY: Belongs to the peptidase C1 family. XX GO GO:0004197; F:cysteine-type endopeptidase activity GO GO:0006508; P:proteolysis XX KW Hydrolase KW Protease KW Thiol protease XX FT From: PS00639 FT ACT_SITE 3 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9R014; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10090; DC Domain; TR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1; level=0 XX Names: Eukaryotic thiol (cysteine) proteases asparagine active site Function: Undefined XX CC -!- SIMILARITY: Belongs to the peptidase C1 family. XX GO GO:0004197; F:cysteine-type endopeptidase activity GO GO:0006508; P:proteolysis XX KW Hydrolase KW Protease KW Thiol protease XX FT From: PS00640 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O97397; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10091; DC Domain; TR PROSITE; PS00140; UCH_1; 1; level=0 XX Names: Ubiquitin carboxyl-terminal hydrolase family 1 cysteine active-site Function: Undefined XX DE + AltName: Full=Ubiquitin thiolesterase; DE EC=3.4.19.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; XX FT From: PS00140 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9GM50; Scope: Eukaryota Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10092; DC Domain; TR PROSITE; PS00972; USP_1; 1; level=0 XX Names: Ubiquitin specific protease (USP) domain Function: Undefined XX DE + AltName: Full=Ubiquitin carboxyl-terminal hydrolase; DE EC=3.4.19.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; XX FT From: PS00972 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P54578; Scope: Eukaryota Viruses Comments: None XX # Revision 1.8 2019/11/22 // AC PRU10093; DC Domain; TR PROSITE; PS00973; USP_2; 1; level=0 XX Names: Ubiquitin specific protease (USP) domain Function: Undefined XX DE + AltName: Full=Ubiquitin carboxyl-terminal hydrolase; DE EC=3.4.19.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; XX FT From: PS00973 FT ACT_SITE 8 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9UUD6; Scope: Eukaryota Viruses Comments: None XX # Revision 1.7 2019/11/22 // AC PRU10094; DC Domain; TR PROSITE; PS00141; ASP_PROTEASE; 1; level=0 XX Names: Eukaryotic and viral aspartyl proteases active site Function: Undefined XX DE + AltName: Full=Pepsin A; DE EC=3.4.23.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage: hydrophobic, preferably aromatic, CC residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His- CC 5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu- CC 17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the CC B chain of insulin.; EC=3.4.23.1; XX FT From: PS00141 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P56817; Scope: Eukaryota Viruses Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10095; DC Domain; TR PROSITE; PS00142; ZINC_PROTEASE; 1; level=0 XX Names: Neutral zinc metallopeptidases, zinc-binding region Function: Undefined XX FT From: PS00142 FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT ACT_SITE 5 FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q56H28; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.8 2022/11/19 // AC PRU10096; DC Domain; TR PROSITE; PS00143; INSULINASE; 1; level=0 XX Names: Insulinase family, zinc-binding region Function: Undefined XX DE + AltName: Full=Pitrilysin; DE EC=3.4.24.55; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 CC bonds of oxidized insulin B chain. Also acts on other substrates of CC Mw less than 7 kDa such as insulin and glucagon.; EC=3.4.24.55; XX FT From: PS00143 FT BINDING 4 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT ACT_SITE 7 FT /note="Proton acceptor" FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P27508; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.7 2022/11/19 // AC PRU10097; DC Domain; TR Metamotif; -; PS00501~(PS00760){,1}~PS00761 XX Names: Signal peptidases I serine active sites Function: Signal peptidases (SPases) (also known as leader peptidases) remove the signal peptides from secretory proteins. XX DE + AltName: Full=Signal peptidase I; DE EC=3.4.21.89; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences CC from secreted and periplasmic proteins.; EC=3.4.21.89; XX DR PROSITE; PS00501; SPASE_I_1; 1; trigger=no DR PROSITE; PS00760; SPASE_I_2; 0-1; trigger=no DR PROSITE; PS00761; SPASE_I_3; 1; trigger=no XX GO GO:0016787; F:hydrolase activity GO GO:0008233; F:peptidase activity XX KW Hydrolase KW Protease XX FT From: PS00501 FT ACT_SITE 3 XX FT From: PS00760 FT ACT_SITE 1 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5HHB9; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.10 2019/11/22 // AC PRU10099; DC Domain; TR PROSITE; PS00144; ASN_GLN_ASE_1; 1; level=0 XX Names: Asparaginase / glutaminase active site Function: Undefined XX FT From: PS00144 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P26900; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10100; DC Domain; TR PROSITE; PS00917; ASN_GLN_ASE_2; 1; level=0 XX Names: Asparaginase / glutaminase active site Function: Undefined XX FT From: PS00917 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9V0T9; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10101; DC Domain; TR PROSITE; PS00146; BETA_LACTAMASE_A; 1; level=0 XX Names: Beta-lactamase class-A active site Function: Undefined XX DE + AltName: Full=Beta-lactamase; DE EC=3.5.2.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid; CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, CC ChEBI:CHEBI:140347; EC=3.5.2.6; XX FT From: PS00146 FT ACT_SITE 4 FT /note="Acyl-ester intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9S424; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10102; DC Domain; TR PROSITE; PS00336; BETA_LACTAMASE_C; 1; level=0 XX Names: Beta-lactamase class-C active site Function: Undefined XX DE + AltName: Full=Beta-lactamase; DE EC=3.5.2.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid; CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, CC ChEBI:CHEBI:140347; EC=3.5.2.6; XX FT From: PS00336 FT ACT_SITE 5 FT /note="Acyl-ester intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P18539; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10103; DC Domain; TR PROSITE; PS00337; BETA_LACTAMASE_D; 1; level=0 XX Names: Beta-lactamase class-D active site Function: Undefined XX DE + AltName: Full=Beta-lactamase; DE EC=3.5.2.6; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid; CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, CC ChEBI:CHEBI:140347; EC=3.5.2.6; XX FT From: PS00337 FT ACT_SITE 2 FT /note="Acyl-ester intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P0A1V9; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10104; DC Domain; TR PROSITE; PS00485; A_DEAMINASE; 1; level=0 XX Names: Adenosine and AMP deaminase Function: Undefined XX DE + AltName: Full=Adenosine deaminase; DE EC=3.5.4.4; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + H(+) + H2O = inosine + NH4(+); CC Xref=Rhea:RHEA:24408, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16335, ChEBI:CHEBI:17596, ChEBI:CHEBI:28938; EC=3.5.4.4; XX FT From: PS00485 FT ACT_SITE 5 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8X661; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10105; DC Domain; TR PROSITE; PS00921; NITRIL_CHT_2; 1; level=0 XX Names: Nitrilases / cyanide hydratase active site Function: Undefined XX DE + AltName: Full=Nitrilase; DE EC=3.5.5.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=a nitrile + 2 H2O = a carboxylate + NH4(+); CC Xref=Rhea:RHEA:21724, ChEBI:CHEBI:15377, ChEBI:CHEBI:18379, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29067; EC=3.5.5.1; XX FT From: PS00921 FT ACT_SITE 3 FT /note="Nucleophile" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P32961; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10106; DC Domain; TR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1; level=0 XX Names: ATP synthase alpha and beta subunits Function: Undefined XX DE + AltName: Full=H(+)-transporting two-sector ATPase; DE EC=7.1.2.2; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate; CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2; XX FT From: PS00152 FT SITE 8 FT /note="Required for activity" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q2LQZ7; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10107; DC Domain; TR PROSITE; PS01205; T4_DEIODINASE; 1; level=0 XX Names: Iodothyronine deiodinases active site Function: Undefined XX FT From: PS01205 FT ACT_SITE 11 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5I3B1; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10108; DC Domain; TR PROSITE; PS00155; CUTINASE_1; 1; level=0 XX Names: Cutinase, serine active site Function: Undefined XX DE + AltName: Full=Cutinase; DE EC=3.1.1.74; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; XX FT From: PS00155 FT ACT_SITE 8 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P63880; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2022/04/28 // AC PRU10109; DC Domain; TR PROSITE; PS00931; CUTINASE_2; 1; level=0 XX Names: Cutinase, aspartate and histidine active sites Function: Undefined XX DE + AltName: Full=Cutinase; DE EC=3.1.1.74; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=cutin + H2O = cutin monomers.; EC=3.1.1.74; XX FT From: PS00931 FT ACT_SITE 8 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P63880; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2022/04/28 // AC PRU10110; DC Domain; TR PROSITE; PS00156; OMPDECASE; 1; level=0 XX Names: Orotidine 5'-phosphate decarboxylase active site Function: Undefined XX DE + AltName: Full=Orotidine-5'-phosphate decarboxylase; DE EC=4.1.1.23; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP; CC Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23; XX FT From: PS00156 FT ACT_SITE 4 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5J2D0; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10111; DC Domain; TR PROSITE; PS00781; PEPCASE_1; 1; level=0 XX Names: Phosphoenolpyruvate carboxylase active site 1 Function: Undefined XX FT From: PS00781 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q93MH3; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10112; DC Domain; TR PROSITE; PS00393; PEPCASE_2; 1; level=0 XX Names: Phosphoenolpyruvate carboxylase active site 2 Function: Undefined XX FT From: PS00393 FT ACT_SITE 9 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8X743; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10113; DC Domain; TR PROSITE; PS00505; PEPCK_GTP; 1; level=0 XX Names: Phosphoenolpyruvate carboxykinase (GTP) Function: Undefined XX DE + AltName: Full=Phosphoenolpyruvate carboxykinase; DE AltName: Full=GTP; DE EC=4.1.1.32; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + oxaloacetate = CO2 + GDP + phosphoenolpyruvate; CC Xref=Rhea:RHEA:10388, ChEBI:CHEBI:16452, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58702; EC=4.1.1.32; XX FT From: PS00505 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q6F8P2; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10114; DC Domain; TR PROSITE; PS00157; RUBISCO_LARGE; 1; level=0 XX Names: Ribulose bisphosphate carboxylase large chain active site Function: Undefined XX DE + AltName: Full=Ribulose-bisphosphate carboxylase; DE EC=4.1.1.39; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=2 (2R)-3-phosphoglycerate + 2 H(+) = CO2 + D-ribulose 1,5- CC bisphosphate + H2O; Xref=Rhea:RHEA:23124, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57870, CC ChEBI:CHEBI:58272; EC=4.1.1.39; XX FT From: PS00157 FT MOD_RES 4 FT /note="N6-carboxylysine" FT BINDING 5 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P24671; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.9 2022/11/19 // AC PRU10115; DC Domain; TR PROSITE; PS01062; HMG_COA_LYASE; 1; level=0 XX Names: Hydroxymethylglutaryl-coenzyme A lyase active site Function: Undefined XX DE AltName: Full=Hydroxymethylglutaryl-CoA lyase; DE EC=4.1.3.4; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=(3S)-hydroxy-3-methylglutaryl-CoA = acetoacetate + acetyl-CoA; CC Xref=Rhea:RHEA:24404, ChEBI:CHEBI:13705, ChEBI:CHEBI:43074, CC ChEBI:CHEBI:57288; EC=4.1.3.4; XX FT From: PS01062 FT ACT_SITE 8 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P35914; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10116; DC Domain; TR PROSITE; PS01226; HMG_COA_SYNTHASE; 1; level=0 XX Names: Hydroxymethylglutaryl-coenzyme A synthase active site Function: Undefined XX DE + AltName: Full=Hydroxymethylglutaryl-CoA synthase; DE EC=2.3.3.10; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3- CC methylglutaryl-CoA + CoA + H(+); Xref=Rhea:RHEA:10188, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43074, CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.10; XX FT From: PS01226 FT ACT_SITE 10 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P23228; Scope: Eukaryota Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10117; DC Domain; TR PROSITE; PS00480; CITRATE_SYNTHASE; 1; level=0 XX Names: Citrate synthase Function: Undefined XX DE + AltName: Full=Citrate (Si)-synthase; DE EC=2.3.3.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.3.1; XX FT From: PS00480 FT ACT_SITE 4 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q59136; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10118; DC Domain; TR PROSITE; PS00159; ALDOLASE_KDPG_KHG_1; 1; level=0 XX Names: KDPG and KHG aldolases active site Function: Undefined XX DE + AltName: Full=2-dehydro-3-deoxy-phosphogluconate aldolase; DE EC=4.1.2.14; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=2-dehydro-3-deoxy-6-phospho-D-gluconate = D-glyceraldehyde 3- CC phosphate + pyruvate; Xref=Rhea:RHEA:17089, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:57569, ChEBI:CHEBI:59776; EC=4.1.2.14; XX FT From: PS00159 FT ACT_SITE 7 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P38448; Scope: Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10119; DC Domain; TR PROSITE; PS00161; ISOCITRATE_LYASE; 1; level=0 XX Names: Isocitrate lyase Function: Undefined XX DE + AltName: Full=Isocitrate lyase; DE EC=4.1.3.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=D-threo-isocitrate = glyoxylate + succinate; CC Xref=Rhea:RHEA:13245, ChEBI:CHEBI:15562, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:36655; EC=4.1.3.1; XX FT From: PS00161 FT ACT_SITE 3 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P45456; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.6 2020/06/09 // AC PRU10120; DC Domain; TR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1; level=0 XX Names: Tryptophan synthase alpha chain Function: Undefined XX DE + AltName: Full=Indole-3-glycerol-phosphate lyase; DE EC=4.1.2.8; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = D- CC glyceraldehyde 3-phosphate + indole; Xref=Rhea:RHEA:14081, CC ChEBI:CHEBI:16881, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.1.2.8; XX FT From: PS00167 FT ACT_SITE 2 FT /note="Proton acceptor" FT ACT_SITE 11 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q6FEE6; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10121; DC Domain; TR PROSITE; PS01335; METHYLGLYOXAL_SYNTH; 1; level=0 XX Names: Methylglyoxal synthase active site Function: Undefined XX DE + AltName: Full=Methylglyoxal synthase; DE EC=4.2.3.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; CC Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57642; EC=4.2.3.3; XX FT From: PS01335 FT ACT_SITE 7 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q81ST9; Scope: Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10122; DC Domain; TR PROSITE; PS00488; PAL_HISTIDASE; 1; level=0 XX Names: Phenylalanine and histidine ammonia-lyases Function: Undefined XX DE + AltName: Full=Histidine ammonia-lyase; DE EC=4.3.1.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidine = NH4(+) + trans-urocanate; Xref=Rhea:RHEA:21232, CC ChEBI:CHEBI:17771, ChEBI:CHEBI:28938, ChEBI:CHEBI:57595; EC=4.3.1.3; XX FT From: PS00488 FT MOD_RES 6 FT /note="2,3-didehydroalanine (Ser)" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5NZX8; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10123; DC Domain; TR PROSITE; PS00987; PTPS_1; 1; level=0 XX Names: 6-pyruvoyl tetrahydropterin synthase Function: Undefined XX DE + AltName: Full=6-pyruvoyl tetrahydropterin synthase; DE EC=4.2.3.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8- CC tetrahydropterin + H(+) + triphosphate; Xref=Rhea:RHEA:22048, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:58462, CC ChEBI:CHEBI:136564; EC=4.2.3.12; XX FT From: PS00987 FT ACT_SITE 1 FT /note="Proton acceptor" FT BINDING 5 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O02058; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.8 2022/11/19 // AC PRU10124; DC Domain; TR PROSITE; PS00988; PTPS_2; 1; level=0 XX Names: 6-pyruvoyl tetrahydropterin synthase Function: Undefined XX DE + AltName: Full=6-pyruvoyl tetrahydropterin synthase; DE EC=4.2.3.12; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=7,8-dihydroneopterin 3'-triphosphate = 6-pyruvoyl-5,6,7,8- CC tetrahydropterin + H(+) + triphosphate; Xref=Rhea:RHEA:22048, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:58462, CC ChEBI:CHEBI:136564; EC=4.2.3.12; XX FT From: PS00988 FT ACT_SITE 2 FT /note="Charge relay system" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P80081; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.6 2019/11/22 // AC PRU10125; DC Domain; TR PROSITE; PS01326; DAP_EPIMERASE; 1; level=0 XX Names: Diaminopimelate epimerase Function: Undefined XX FT From: PS01326 FT ACT_SITE 5 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q8YVD0; Scope: Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10126; DC Domain; TR PROSITE; PS00545; ALDOSE_1_EPIMERASE; 1; level=0 XX Names: Aldose 1-epimerase putative active site Function: Undefined XX DE + AltName: Full=Aldose 1-epimerase; DE EC=5.1.3.3; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucose = beta-D-glucose; Xref=Rhea:RHEA:10264, CC ChEBI:CHEBI:15903, ChEBI:CHEBI:17925; EC=5.1.3.3; XX FT From: PS00545 FT ACT_SITE 4 FT /note="Proton donor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q5EA79; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.5 2019/11/22 // AC PRU10130; DC Domain; TR PROSITE; PS00176; TOPO_IB_1; 1; level=0 XX Names: Topoisomerase (Topo) IB-type active site Function: The RKKRH/N "catalytic pentad", conserved in all members of the topo IB family, catalyzes the attack of the active site tyrosine nucleophile on the scissile phosphodiester. XX DE + AltName: Full=DNA topoisomerase; DE EC=5.6.2.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed by CC passage and rejoining.; EC=5.6.2.1; XX FT From: PS00176 FT ACT_SITE 6 FT /note="O-(3'-phospho-DNA)-tyrosine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q76ZS7; Scope: Eukaryota Viruses Comments: None XX # Revision 1.8 2023/09/19 // AC PRU10131; DC Domain; TR PROSITE; PS00396; TOPO_IA_1; 1; level=0 XX Names: Topoisomerase (Topo) IA-type active site Function: Undefined XX DE + AltName: Full=DNA topoisomerase; DE EC=5.6.2.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP-independent breakage of single-stranded DNA, followed by CC passage and rejoining.; EC=5.6.2.1; XX FT From: PS00396 FT ACT_SITE 7 FT /note="O-(5'-phospho-DNA)-tyrosine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KA23; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.8 2023/09/28 // AC PRU10132; DC Domain; TR PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1; level=0 XX Names: Ubiquitin-activating enzyme active site Function: Undefined XX FT From: PS00865 FT ACT_SITE 3 FT /note="Glycyl thioester intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P22314; Scope: Eukaryota Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10133; DC Domain; TR PROSITE; PS00183; UBC_1; 1; level=0 XX Names: Ubiquitin-conjugating (UBC) active site Function: Ubiquitin-conjugating enzymes (EC 2.3.2.23) (UBC or E2 enzymes) catalyze the covalent attachment of ubiquitin to target proteins. XX DE + RecName: EC= 2.3.2.-; XX FT From: PS00183 FT ACT_SITE 8 FT /note="Glycyl thioester intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P25865; Scope: Eukaryota Viruses Comments: None XX # Revision 1.6 2020/04/15 // AC PRU10134; DC Domain; TR PROSITE; PS00513; ADENYLOSUCCIN_SYN_2; 1; level=0 XX Names: Adenylosuccinate synthetase active site Function: Undefined XX FT From: PS00513 FT ACT_SITE 6 XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q39PN9; Scope: Eukaryota Bacteria Archaea Comments: None XX # Revision 1.3 2019/11/22 // AC PRU10135; DC Domain; TR PROSITE; PS00697; DNA_LIGASE_A1; 1; level=0 XX Names: ATP-dependent DNA ligase AMP-binding site Function: Undefined XX DE + AltName: Full=DNA ligase; DE AltName: Full=ATP; DE EC=6.5.1.1; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho- CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + CC diphosphate.; EC=6.5.1.1; XX FT From: PS00697 FT ACT_SITE 3 FT /note="N6-AMP-lysine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: O29632; Scope: Eukaryota Bacteria Archaea Viruses Comments: None XX # Revision 1.8 2022/04/28 // AC PRU10136; DC Domain; TR PROSITE; PS01055; DNA_LIGASE_N1; 1; level=0 XX Names: NAD-dependent DNA ligase Function: Undefined XX DE + AltName: Full=DNA ligase; DE AltName: Full=NAD(+); DE EC=6.5.1.2; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho- CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta- CC nicotinamide D-nucleotide.; EC=6.5.1.2; XX FT From: PS01055 FT ACT_SITE 1 FT /note="N6-AMP-lysine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: Q9ZLM1; Scope: Bacteria Viruses Comments: None XX # Revision 1.7 2022/04/28 // AC PRU10137; DC Domain; TR PROSITE; PS00397; RECOMBINASES_1; 1; level=0 XX Names: Site-specific recombinases active site Function: Undefined XX FT From: PS00397 FT ACT_SITE 5 FT /note="O-(5'-phospho-DNA)-serine intermediate" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P21703; Scope: Bacteria Viruses Comments: None XX # Revision 1.4 2019/11/22 // AC PRU10138; DC Domain; TR PROSITE; PS00014; ER_TARGET; 1; level=0 XX Names: Endoplasmic reticulum targeting sequence Function: Proteins that permanently reside in the lumen of the endoplasmic reticulum (ER) seem to be distinguished from newly synthesized secretory proteins by the presence of the C-terminal sequence Lys-Asp-Glu-Leu (KDEL). XX CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. XX GO GO:0005783; C:endoplasmic reticulum XX KW Endoplasmic reticulum XX FT From: PS00014 FT MOTIF from..to FT /note="Prevents secretion from ER" XX Chop: Nter=0; Cter=0; Size: 4; Related: None; Repeats: 1; Topology: Not cytoplasmic; Example: Q9Y2B0; Scope: Eukaryota Viruses Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU10139; DC Domain; TR PROSITE; PS00920; NITRIL_CHT_1; 1; level=0 XX Names: Nitrilases / cyanide hydratase active site Function: Undefined XX FT From: PS00920 FT ACT_SITE 5 FT /note="Proton acceptor" XX Chop: Nter=0; Cter=0; Size: unlimited; Related: None; Repeats: 1; Topology: Undefined; Example: P32961; Scope: Eukaryota Bacteria Comments: None XX # Revision 1.2 2019/11/22 // AC PRU10140; DC Domain; TR PROSITE; PS60032; GH9_1; 1; level=0 XX Names: Glycosyl hydrolases family 9 (GH9) active site D Function: Three conserved regions in these enzymes are centered on conserved residues which have been shown to be important for the catalytic activity. The first region contains the characteristic DAGD motif, where the C-terminal D acts as the catalytic base that extracts a proton from the nucleophilic water. XX DE + RecName: EC=3.2.1.-; XX CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 9 (cellulase E) family. XX GO GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds XX KW Carbohydrate metabolism KW Glycosidase KW Hydrolase KW Polysaccharide degradation XX FT From: PS60032 FT ACT_SITE 9 FT /note="Nucleophile" FT Condition: D XX Chop: Nter=0; Cter=0; Size: 18-18; Related: None; Repeats: 1; Topology: Undefined; Example: O81416; Scope: Eukaryota Bacteria Comments: None; XX # Revision 1.3 2019/11/22 // AC PRU10141; DC Domain; TR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1; level=0 XX Names: Protein kinases ATP-binding region signature Function: Eukaryotic protein kinases are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common to both serine/threonine and tyrosine protein kinases. XX GO GO:0005524; F:ATP binding GO GO:0000166; F:nucleotide binding XX KW ATP-binding KW Nucleotide-binding XX FT From: PS00107 FT BINDING to FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" XX Chop: Nter=0; Cter=0; Size: 20-40; Related: None; Repeats: 1-2; Topology: Undefined; Example: Q07912; Scope: Eukaryota Bacteria Viruses Comments: None; XX # Revision 1.3 2022/11/19 // AC PRU10142; DC Domain; TR PROSITE; PS00018; EF_HAND_1; 1; level=0 XX Names: EF-hand calcium-binding domain Function: Many calcium-binding proteins belong to the same evolutionary family and share a type of calcium-binding domain known as the EF-hand. XX GO GO:0005509; F:calcium ion binding XX KW Metal-binding KW Calcium XX FT From: PS00018 FT BINDING 1 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT BINDING 3 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT BINDING 5 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT BINDING 7 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" FT BINDING 10 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="#1" XX Chop: Nter=0; Cter=0; Size: 11; Related: None; Repeats: 1-8; Topology: Undefined; Example: P06702; Scope: Eukaryota Bacteria Viruses Comments: None XX # Revision 1.3 2022/11/19 // AC PRU10143; DC Domain; TR PROSITE; PS00430; TONB_DEPENDENT_REC_1; 1; level=0 XX Names: TonB-dependent receptor (TBDR) proteins Function: The C-terminal domain (CTD) of TonB protein has a globular structure of ~100 residues and interacts with a conserved TonB box motif located at the N-terminus of TBDRs, which likely induces structural changes in the outer membrane transporters. XX case KW TonB box XX FT From: PS00430 FT MOTIF 2..to FT /note="TonB box #" end case XX Chop: Nter=0; Cter=0; Size: 24-122; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KVI9; Scope: Bacteria; Pseudomonadota Comments: None; XX # Revision 1.1 2023/01/31 // AC PRU10144; DC Domain; TR PROSITE; PS01156; TONB_DEPENDENT_REC_2; 1; level=0 XX Names: TonB-dependent receptor (TBDR) proteins Function: With the exception of the colicin B, D and M receptors TBDR proteins all also contain, in their C-terminal extremity a short conserved domain that contains two invariant residues. XX case FT From: PS01156 FT MOTIF from..to FT /note="TonB C-terminal box #" end case XX Chop: Nter=0; Cter=0; Size: 18-18; Related: None; Repeats: 1; Topology: Undefined; Example: Q9KVI9; Scope: Bacteria; Pseudomonadota Comments: None; XX # Revision 1.1 2023/01/31 //