ID A0A3R7Q9B9_PENVA Unreviewed; 157 AA.
AC A0A3R7Q9B9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 22-FEB-2023, entry version 11.
DE RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|PIRNR:PIRNR029826};
DE EC=3.6.1.12 {ECO:0000256|PIRNR:PIRNR029826};
GN ORFNames=C7M84_009850 {ECO:0000313|EMBL:ROT71822.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT71822.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT71822.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT71822.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT71822.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT71822.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT71822.1}.
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DR EMBL; QCYY01002241; ROT71822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7Q9B9; -.
DR STRING; 6689.A0A3R7Q9B9; -.
DR EnsemblMetazoa; XM_027363471.1; XP_027219272.1; LOC113811682.
DR OrthoDB; 5485883at2759; -.
DR Proteomes; UP000283509; 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:UP000283509}.
FT REGION 134..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 157 AA; 18125 MW; 9A05A2FF26E58D97 CRC64;
MAQSDPEDRE FKFSSNLSLE EIRSDQHNFC KERNWAQFHP PRNVLLALVG EVGELSELFQ
WRGEVTRGLP DFSAHEKTRV GEELSDILIY LVDLAEQCEI DLPRAVKEKM VKNAEKYPVE
RVIGRSDKYN DYPEYLLQEA PAGEEPQPER EEGDGSE
//
