ID W5M4C3_LEPOC Unreviewed; 151 AA.
AC W5M4C3;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|PIRNR:PIRNR029826};
DE EC=3.6.1.12 {ECO:0000256|PIRNR:PIRNR029826};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000003231.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000003231.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AHAT01038728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015201629.1; XM_015346143.1.
DR AlphaFoldDB; W5M4C3; -.
DR STRING; 7918.ENSLOCP00000003231; -.
DR Ensembl; ENSLOCT00000003238.1; ENSLOCP00000003231.1; ENSLOCG00000002747.1.
DR GeneID; 102682302; -.
DR KEGG; loc:102682302; -.
DR CTD; 79077; -.
DR eggNOG; ENOG502S210; Eukaryota.
DR GeneTree; ENSGT00390000017709; -.
DR HOGENOM; CLU_110454_0_1_1; -.
DR InParanoid; W5M4C3; -.
DR OMA; HFQWLTE; -.
DR OrthoDB; 5485883at2759; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000002747; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047840; F:dCTP diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006253; P:dCTP catabolic process; IBA:GO_Central.
DR GO; GO:0042262; P:DNA protection; IBA:GO_Central.
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:UP000018468}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 151 AA; 17183 MW; B8C26C02514FDD47 CRC64;
MAESSVKAQE VSEAPAAQQN GLPAPERFSF SPTPTLEDIR RLQAEFTDER NWEQYHQPRN
LLLAMVGEVG EVSELFQWKG EVAEGLPSWT EREREQLSHE LSDVLIYLVE LAEKCHVDLP
KAVLAKMAIN RSKYPASKVH GLAKKYTEYQ D
//
