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Database: UniProt
Entry: G3IKR0_CRIGR
LinkDB: G3IKR0_CRIGR
Original site: G3IKR0_CRIGR 
ID   G3IKR0_CRIGR            Unreviewed;       157 AA.
AC   G3IKR0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|PIRNR:PIRNR029826};
DE            EC=3.6.1.12 {ECO:0000256|PIRNR:PIRNR029826};
GN   ORFNames=I79_024463 {ECO:0000313|EMBL:EGW13607.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW13607.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
CC   -!- FUNCTION: Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the
CC       corresponding nucleoside monophosphates. Has a strong preference for
CC       dCTP and its analogs including 5-iodo-dCTP and 5-methyl-dCTP for which
CC       it may even have a higher efficiency. May protect DNA or RNA against
CC       the incorporation of these genotoxic nucleotide analogs through their
CC       catabolism. {ECO:0000256|PIRNR:PIRNR029826}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCTP + H2O = dCMP + diphosphate + H(+); Xref=Rhea:RHEA:22636,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57566, ChEBI:CHEBI:61481; EC=3.6.1.12;
CC         Evidence={ECO:0000256|PIRNR:PIRNR029826};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRNR:PIRNR029826};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|PIRNR:PIRNR029826}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|PIRNR:PIRNR029826}.
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DR   EMBL; JH003722; EGW13607.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3IKR0; -.
DR   STRING; 10029.G3IKR0; -.
DR   PaxDb; 10029-XP_007612395-1; -.
DR   eggNOG; ENOG502S210; Eukaryota.
DR   InParanoid; G3IKR0; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0047840; F:dCTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006253; P:dCTP catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042262; P:DNA protection; IEA:UniProtKB-UniRule.
DR   CDD; cd11537; NTP-PPase_RS21-C6_like; 1.
DR   Gene3D; 1.10.287.1080; MazG-like; 1.
DR   InterPro; IPR025984; DCTPP.
DR   PANTHER; PTHR46523; DCTP PYROPHOSPHATASE 1; 1.
DR   PANTHER; PTHR46523:SF1; DCTP PYROPHOSPHATASE 1; 1.
DR   Pfam; PF12643; MazG-like; 1.
DR   SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR029826};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR029826};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR029826};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR029826};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075}.
SQ   SEQUENCE   157 AA;  17569 MW;  1B1E6461C187E611 CRC64;
     MRGKKTLLLP AADSASTLED IRRLHAEFAA ERDWEQFHQP RNLLLALVGE VGELAELFQW
     KSDAESSPQA WPPKERAALQ EELSDVLIYL VALAARCHVD LPQAVLSKMD TNRQRYPVHL
     SRGSARKYTD LPHGTISENQ AVEAVDPTSE LKNQAST
//
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