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Database: UniProt
Entry: A0A1Y1I8E0_KLENI
LinkDB: A0A1Y1I8E0_KLENI
Original site: A0A1Y1I8E0_KLENI 
ID   A0A1Y1I8E0_KLENI        Unreviewed;       156 AA.
AC   A0A1Y1I8E0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=dCTP pyrophosphatase 1 {ECO:0000256|PIRNR:PIRNR029826};
DE            EC=3.6.1.12 {ECO:0000256|PIRNR:PIRNR029826};
GN   ORFNames=KFL_001860150 {ECO:0000313|EMBL:GAQ84368.1};
OS   Klebsormidium nitens (Green alga) (Ulothrix nitens).
OC   Eukaryota; Viridiplantae; Streptophyta; Klebsormidiophyceae;
OC   Klebsormidiales; Klebsormidiaceae; Klebsormidium.
OX   NCBI_TaxID=105231 {ECO:0000313|EMBL:GAQ84368.1, ECO:0000313|Proteomes:UP000054558};
RN   [1] {ECO:0000313|EMBL:GAQ84368.1, ECO:0000313|Proteomes:UP000054558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2285 {ECO:0000313|EMBL:GAQ84368.1,
RC   ECO:0000313|Proteomes:UP000054558};
RX   PubMed=24865297; DOI=10.1038/ncomms4978;
RA   Hori K., Maruyama F., Fujisawa T., Togashi T., Yamamoto N., Seo M.,
RA   Sato S., Yamada T., Mori H., Tajima N., Moriyama T., Ikeuchi M.,
RA   Watanabe M., Wada H., Kobayashi K., Saito M., Masuda T.,
RA   Sasaki-Sekimoto Y., Mashiguchi K., Awai K., Shimojima M., Masuda S.,
RA   Iwai M., Nobusawa T., Narise T., Kondo S., Saito H., Sato R., Murakawa M.,
RA   Ihara Y., Oshima-Yamada Y., Ohtaka K., Satoh M., Sonobe K., Ishii M.,
RA   Ohtani R., Kanamori-Sato M., Honoki R., Miyazaki D., Mochizuki H.,
RA   Umetsu J., Higashi K., Shibata D., Kamiya Y., Sato N., Nakamura Y.,
RA   Tabata S., Ida S., Kurokawa K., Ohta H.;
RT   "Klebsormidium flaccidum genome reveals primary factors for plant
RT   terrestrial adaptation.";
RL   Nat. Commun. 5:3978-3978(2014).
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; DF237135; GAQ84368.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1I8E0; -.
DR   STRING; 105231.A0A1Y1I8E0; -.
DR   OrthoDB; 5485883at2759; -.
DR   Proteomes; UP000054558; 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:SF24; 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:UP000054558}.
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   156 AA;  17051 MW;  BB9B3BCA04BF5649 CRC64;
     MDQGAAAREI LPEATSPQTA APPAGDPLLP VTLGELQELQ ASFAKDRDWD QFHSPRNLLL
     ALVGEVGELS ELFQWRGEVP RGLPGWTPPE REHLGEELAD VLLYLVRLAD VCGVDLGRAA
     LRKLEKNAQK YPVDACRGSS QKYTAYQEAE AEGSKS
//
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