ID A0A673TV42_SURSU Unreviewed; 170 AA.
AC A0A673TV42;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|ARBA:ARBA00070266, ECO:0000256|PIRNR:PIRNR029826};
DE EC=3.6.1.12 {ECO:0000256|ARBA:ARBA00066457, ECO:0000256|PIRNR:PIRNR029826};
OS Suricata suricatta (Meerkat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Herpestidae; Suricata.
OX NCBI_TaxID=37032 {ECO:0000313|Ensembl:ENSSSUP00005015753.1, ECO:0000313|Proteomes:UP000472268};
RN [1] {ECO:0000313|Ensembl:ENSSSUP00005015753.1, ECO:0000313|Proteomes:UP000472268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dudchenko O., Lieberman Aiden E., Tung J., Barreiro L.B.,
RA Clutton-Brock T.H.;
RT "A Chromosome-scale Meerkat (S. suricatta) Genome Assembly.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSUP00005015753.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) 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|ARBA:ARBA00058235,
CC 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|ARBA:ARBA00050236,
CC ECO:0000256|PIRNR:PIRNR029826};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR029826};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|PIRNR:PIRNR029826}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|PIRNR:PIRNR029826}.
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DR RefSeq; XP_029804034.1; XM_029948174.1.
DR AlphaFoldDB; A0A673TV42; -.
DR Ensembl; ENSSSUT00005017970.1; ENSSSUP00005015753.1; ENSSSUG00005010155.1.
DR GeneID; 115298959; -.
DR OMA; FRDERNW; -.
DR OrthoDB; 411123at2759; -.
DR Proteomes; UP000472268; Chromosome 8.
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 FunFam; 1.10.287.1080:FF:000004; dCTP pyrophosphatase 1; 1.
DR Gene3D; 1.10.287.1080; MazG-like; 1.
DR InterPro; IPR052555; dCTP_Pyrophosphatase.
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|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR029826};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR029826};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR029826};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR029826};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472268}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 18473 MW; 5CA5649954348FDA CRC64;
MSRANGVARG DTEGDGSAAA GPFSFSPEPT LEDIRRLHAE FAAERDWGQF HQPRNLLLAL
VGEVGELAEL FQWKPDEALG PQAWPPRERA ALQEELSDVL IYLVALAARC HVDLPQAVLS
KMDINRRRYP AHLSRGSALK YTDLPHGATS EDQAGGPADL ACESTDQAST
//
