ID H2NQN5_PONAB Unreviewed; 170 AA.
AC H2NQN5; A0A2J8TKF3; A0A663DC05;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|PIRNR:PIRNR029826};
DE EC=3.6.1.12 {ECO:0000256|PIRNR:PIRNR029826};
GN Name=DCTPP1 {ECO:0000313|Ensembl:ENSPPYP00000008220.2};
GN ORFNames=CR201_G0034458 {ECO:0000313|EMBL:PNJ33519.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000008220.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000008220.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ33519.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ33519.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000008220.2}
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; NDHI03003494; PNJ33519.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000008220; -.
DR Ensembl; ENSPPYT00000008558.3; ENSPPYP00000008220.2; ENSPPYG00000007273.3.
DR eggNOG; ENOG502S210; Eukaryota.
DR GeneTree; ENSGT00390000017709; -.
DR HOGENOM; CLU_110454_0_1_1; -.
DR OMA; HFQWLTE; -.
DR OrthoDB; 5485883at2759; -.
DR TreeFam; TF300237; -.
DR Proteomes; UP000001595; Chromosome 16.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0047840; F:dCTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032556; F:pyrimidine deoxyribonucleotide binding; IEA:Ensembl.
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:UP000001595}.
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 170 AA; 18725 MW; 38A622864B70820B CRC64;
MSVAGGEIRG DTGGEDTAAP GRFSFSPEPT LEDIRRLHAE FAAERDWEQF HQPRNLLLAL
VGEVGELAEL FQWKTDGEPG PQGWSPRERT ALQEELSDVL IYLVALAARC RVDLPLAVLS
KMDINRRRYP AHLARSSSRK YTELPHGAIS EDQAVGPADI PCDSTAQTST
//
