| UniProt functional annotation for A6MH22 | |||
| UniProt code: A6MH22. |
| Organism: | Chikungunya virus (CHIKV). | |
| Taxonomy: | Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes; Martellivirales; Togaviridae; Alphavirus. | |
| Function: | Inactive precursor of the viral replicase, which is activated by cleavages carried out by the viral protease nsP2. {ECO:0000256|ARBA:ARBA00002589}. | |
| Catalytic activity: | Reaction=4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + H2O = ADP-D-ribose + H(+) + L-aspartyl-[protein]; Xref=Rhea:RHEA:54428, Rhea:RHEA- COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29961, ChEBI:CHEBI:57967, ChEBI:CHEBI:138102; Evidence={ECO:0000256|ARBA:ARBA00000002}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54429; Evidence={ECO:0000256|ARBA:ARBA00000002}; | |
| Catalytic activity: | Reaction=5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + H2O = ADP-D-ribose + H(+) + L-glutamyl-[protein]; Xref=Rhea:RHEA:58248, Rhea:RHEA- COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:57967, ChEBI:CHEBI:142540; Evidence={ECO:0000256|ARBA:ARBA00000461}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58249; Evidence={ECO:0000256|ARBA:ARBA00000461}; | |
| Catalytic activity: | Reaction=ADP-D-ribose 1''-phosphate + H2O = ADP-D-ribose + phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84; Evidence={ECO:0000256|ARBA:ARBA00001508}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25030; Evidence={ECO:0000256|ARBA:ARBA00001508}; | |
| Catalytic activity: | Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000256|ARBA:ARBA00001556}; | |
| Catalytic activity: | Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:11128, Rhea:RHEA-COMP:14647, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:83400, ChEBI:CHEBI:140626; EC=2.7.7.19; Evidence={ECO:0000256|ARBA:ARBA00000310}; | |
| Catalytic activity: | Reaction=GTP + S-adenosyl-L-methionine = N(7)-methyl-GTP + S-adenosyl- L-homocysteine; Xref=Rhea:RHEA:46948, ChEBI:CHEBI:37565, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:87133; Evidence={ECO:0000256|ARBA:ARBA00023718}; | |
| Catalytic activity: | Reaction=[nsP1 protein]-L-histidine + N(7)-methyl-GTP = [nsP1 protein]- N(tele)-(N(7)-methylguanosine 5'-phospho)-L-histidine + diphosphate; Xref=Rhea:RHEA:54792, Rhea:RHEA-COMP:13994, Rhea:RHEA-COMP:13995, ChEBI:CHEBI:29979, ChEBI:CHEBI:33019, ChEBI:CHEBI:87133, ChEBI:CHEBI:138334; Evidence={ECO:0000256|ARBA:ARBA00023734}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54793; Evidence={ECO:0000256|ARBA:ARBA00023734}; | |
| Catalytic activity: | Reaction=[nsP1 protein]-N(tele)-(N(7)-methylguanosine 5'-phospho)-L- histidine + a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) = [nsP1 protein]-L-histidine + a 5'-end (N(7)-methyl 5'- triphosphoguanosine)-(purine-ribonucleoside) in mRNA; Xref=Rhea:RHEA:54800, Rhea:RHEA-COMP:12925, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13994, Rhea:RHEA-COMP:13995, ChEBI:CHEBI:15378, ChEBI:CHEBI:29979, ChEBI:CHEBI:133968, ChEBI:CHEBI:138276, ChEBI:CHEBI:138334; Evidence={ECO:0000256|ARBA:ARBA00023699}; | |
| Catalytic activity: | Reaction=a 5'-end triphospho-(purine-ribonucleoside) in mRNA + H2O = a 5'-end diphospho-(purine-ribonucleoside) in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:11008, Rhea:RHEA-COMP:13929, Rhea:RHEA-COMP:13942, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:138276, ChEBI:CHEBI:138288; EC=3.1.3.33; Evidence={ECO:0000256|ARBA:ARBA00023738}; | |
| Catalytic activity: | Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'- diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000256|ARBA:ARBA00001491}; | |
| Cofactor: | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00001946}; | |
| Cofactor: | Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|ARBA:ARBA00001936}; | |
| Subcellular location: | Cell membrane {ECO:0000256|ARBA:ARBA00004342}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004342}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004342}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004594}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004594}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004284}. Host cell membrane {ECO:0000256|ARBA:ARBA00004112}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004112}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004112}. Host cell projection, host filopodium {ECO:0000256|ARBA:ARBA00004490}. Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Host cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004615}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004615}. Host cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004350}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004350}. Host nucleus {ECO:0000256|ARBA:ARBA00004147}. Membrane {ECO:0000256|ARBA:ARBA00004423, ECO:0000256|ARBA:ARBA00004635}; Lipid- anchor {ECO:0000256|ARBA:ARBA00004423, ECO:0000256|ARBA:ARBA00004635}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004423}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. | |
Annotations taken from UniProtKB at the EBI.