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
//