UniProt ID: A0A8M3AMJ3 |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'- deoxyribonucleoside + H(+) + triphosphate; Xref=Rhea:RHEA:46148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:18274, ChEBI:CHEBI:61560; Evidence={ECO:0000256|ARBA:ARBA00001432}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947}; SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}. SIMILARITY: Belongs to the SAMHD1 family. {ECO:0000256|ARBA:ARBA00005776}. |
UniProt ID: Q502K2 |
FUNCTION: Protein that acts both as a host restriction factor involved in defense response to virus and as a regulator of DNA end resection at stalled replication forks. Has deoxynucleoside triphosphate (dNTPase) activity, which is required to restrict infection by viruses: dNTPase activity reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur, blocking early-stage virus replication in dendritic and other myeloid cells. Functions during S phase at stalled DNA replication forks to promote the resection of gapped or reversed forks: acts by stimulating the exonuclease activity of MRE11, activating the ATR-CHK1 pathway and allowing the forks to restart replication. Its ability to promote degradation of nascent DNA at stalled replication forks is required to prevent induction of type I interferons, thereby preventing chronic inflammation. Ability to promote DNA end resection at stalled replication forks is independent of dNTPase activity. {ECO:0000250|UniProtKB:Q9Y3Z3}. CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'- deoxyribonucleoside + H(+) + triphosphate; Xref=Rhea:RHEA:46148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:18274, ChEBI:CHEBI:61560; Evidence={ECO:0000250|UniProtKB:Q9Y3Z3}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9Y3Z3}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y3Z3}; ACTIVITY REGULATION: Allosterically activated and regulated via the combined actions of GTP and dNTPs (dATP, dGTP, dTTP and dCTP): Allosteric site 1 binds GTP, while allosteric site 2 binds dNTP. Allosteric activation promotes the formation of highly active homotetramers. {ECO:0000250|UniProtKB:Q9Y3Z3}. SUBUNIT: Homodimer; in absence of GTP and dNTP. Homotetramer; in GTP- and dNTP-bound form (By similarity). Interacts with rbbp8/CtIP (By similarity). {ECO:0000250|UniProtKB:Q6INN8, ECO:0000250|UniProtKB:Q9Y3Z3}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}. Chromosome {ECO:0000250|UniProtKB:Q9Y3Z3}. Note=Localizes to sites of DNA double-strand breaks in response to DNA damage. {ECO:0000250|UniProtKB:Q9Y3Z3}. SIMILARITY: Belongs to the SAMHD1 family. {ECO:0000305}. SEQUENCE CAUTION: Sequence=AAH95665.1; Type=Erroneous initiation; Evidence={ECO:0000305}; |
UniProt ID: F1R861 |
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'- deoxyribonucleoside + H(+) + triphosphate; Xref=Rhea:RHEA:46148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18036, ChEBI:CHEBI:18274, ChEBI:CHEBI:61560; Evidence={ECO:0000256|ARBA:ARBA00001432}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|ARBA:ARBA00001947}; SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}. SIMILARITY: Belongs to the SAMHD1 family. {ECO:0000256|ARBA:ARBA00005776}. |
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