ID A0A2C9UNU4_MANES Unreviewed; 131 AA.
AC A0A2C9UNU4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|PIRNR:PIRNR029826};
DE EC=3.6.1.12 {ECO:0000256|PIRNR:PIRNR029826};
GN ORFNames=MANES_13G053600 {ECO:0000313|EMBL:OAY32890.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY32890.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY32890.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY32890.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM004399; OAY32890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C9UNU4; -.
DR STRING; 3983.A0A2C9UNU4; -.
DR EnsemblPlants; OAY32890; OAY32890; MANES_13G053600.
DR Gramene; OAY32890; OAY32890; MANES_13G053600.
DR OMA; THYANGV; -.
DR OrthoDB; 5485883at2759; -.
DR Proteomes; UP000091857; Chromosome lg13.
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; PTHR14552; -; 1.
DR PANTHER; PTHR14552:SF25; DCTP PYROPHOSPHATASE 1; 1.
DR Pfam; PF12643; MazG-like; 1.
DR PIRSF; PIRSF029826; UCP029826_pph; 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:UP000091857}.
SQ SEQUENCE 131 AA; 14723 MW; F6924316CAD6A809 CRC64;
MTGVSDGESV SLDLLKKKMA EFAQERDWDR FHSPRNLLLA LVGEVGELSE IFQWKGEVPK
GLPDWKEEEK IHLGEELSDV LLYLVRLSDI CGIDLGKAAL RKVELNAIKY PVGMCKGSSK
KYNSNNDNDT L
//
