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Database: UniProt
Entry: A0A1R3GC72_COCAP
LinkDB: A0A1R3GC72_COCAP
Original site: A0A1R3GC72_COCAP 
ID   A0A1R3GC72_COCAP        Unreviewed;       103 AA.
AC   A0A1R3GC72;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|PIRNR:PIRNR029826};
DE            EC=3.6.1.12 {ECO:0000256|PIRNR:PIRNR029826};
GN   ORFNames=CCACVL1_27097 {ECO:0000313|EMBL:OMO55672.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO55672.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO55672.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO55672.1};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT   "Corchorus capsularis genome sequencing.";
RL   Submitted (SEP-2013) 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:OMO55672.1}.
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DR   EMBL; AWWV01014591; OMO55672.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3GC72; -.
DR   STRING; 210143.A0A1R3GC72; -.
DR   EnsemblPlants; OMO55672; OMO55672; CCACVL1_27097.
DR   Gramene; OMO55672; OMO55672; CCACVL1_27097.
DR   OMA; PAKVCKE; -.
DR   OrthoDB; 5485883at2759; -.
DR   Proteomes; UP000188268; 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; 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, ECO:0000313|EMBL:OMO55672.1};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR029826};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR029826};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188268}.
SQ   SEQUENCE   103 AA;  11577 MW;  8DA36CEFF073AEB7 CRC64;
     MANFAKERDW DQFHSPRNLL LALVGEVGEL SEIFQWKGEV PKGLPDWKEE EKVHLGEELS
     DVLLYLVRLS DICGIDLGKA ALRKVELNAI KYPASNNNNN GTA
//
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