ID   DCTP1_BOVIN             Reviewed;         169 AA.
AC   Q32KY6;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=dCTP pyrophosphatase 1 {ECO:0000305};
DE            EC=3.6.1.12 {ECO:0000250|UniProtKB:Q9QY93};
DE   AltName: Full=Deoxycytidine-triphosphatase 1;
DE            Short=dCTPase 1;
GN   Name=DCTPP1 {ECO:0000250|UniProtKB:Q9QY93};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q9H773}.
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:0000250|UniProtKB:Q9QY93};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q9QY93};
CC       Note=Probably binds two or three Mg(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:Q9QY93};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9QY93}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9H773}. Note=May also localize to mitochondrion
CC       and nucleus. {ECO:0000250|UniProtKB:Q9H773}.
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DR   EMBL; BC109855; AAI09856.1; -; mRNA.
DR   RefSeq; NP_001033291.1; NM_001038202.2.
DR   AlphaFoldDB; Q32KY6; -.
DR   SMR; Q32KY6; -.
DR   STRING; 9913.ENSBTAP00000014406; -.
DR   PaxDb; Q32KY6; -.
DR   PRIDE; Q32KY6; -.
DR   GeneID; 614103; -.
DR   KEGG; bta:614103; -.
DR   CTD; 79077; -.
DR   eggNOG; ENOG502S210; Eukaryota.
DR   InParanoid; Q32KY6; -.
DR   OrthoDB; 1472354at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0047840; F:dCTP diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006253; P:dCTP catabolic process; ISS:UniProtKB.
DR   GO; GO:0042262; P:DNA protection; ISS:UniProtKB.
DR   GO; GO:0009143; P:nucleoside triphosphate catabolic process; ISS:UniProtKB.
DR   CDD; cd11537; NTP-PPase_RS21-C6_like; 1.
DR   InterPro; IPR025984; DCTPP.
DR   Pfam; PF12643; MazG-like; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..169
FT                   /note="dCTP pyrophosphatase 1"
FT                   /id="PRO_0000291768"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          143..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         46..50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         62
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         65
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         97
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QY93"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H773"
SQ   SEQUENCE   169 AA;  18626 MW;  E5074A541A98A01A CRC64;
     MSASEEMLGG ARGESTTATG PFSFSSEPTL EDIRRLHAEF AAERDWEQFH QPRNLLLALV
     GEVGELAELF QWKPDEEPGP QAWSPRERAA LQEELSDILI YLVALAARCR VDLPQAVLCK
     MDTNRRRYPV HLSRGSACKY TDLPHGATSE NQAMGPADPA SESTGQVST