ID V5LPI3_9PHYC Unreviewed; 148 AA.
AC V5LPI3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN ORFNames=EhV18_00422 {ECO:0000313|EMBL:AHA54468.1};
OS Emiliania huxleyi virus 18.
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC Algavirales; Phycodnaviridae; Coccolithovirus.
OX NCBI_TaxID=1421424 {ECO:0000313|EMBL:AHA54468.1, ECO:0000313|Proteomes:UP000257831};
RN [1] {ECO:0000313|EMBL:AHA54468.1, ECO:0000313|Proteomes:UP000257831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhV-18 {ECO:0000313|EMBL:AHA54468.1,
RC ECO:0000313|Proteomes:UP000257831};
RA Nissimov J.I., Kimmance S.A., Napier J.A., Allen M.J.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC the intracellular concentration of dUTP so that uracil cannot be
CC incorporated into DNA. {ECO:0000256|ARBA:ARBA00003495}.
CC -!- SIMILARITY: Belongs to the dUTPase family.
CC {ECO:0000256|ARBA:ARBA00006581}.
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DR EMBL; KF481685; AHA54468.1; -; Genomic_DNA.
DR Proteomes; UP000257831; Genome.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR NCBIfam; TIGR00576; dut; 1.
DR PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR Pfam; PF00692; dUTPase; 1.
DR SUPFAM; SSF51283; dUTPase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AHA54468.1}.
FT DOMAIN 16..147
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 148 AA; 15907 MW; DD7449AC12EA3A5F CRC64;
MSPATTNLYV SRLTDDAKLP TKGTPLSAGY DLYSSEYVKI PPFCKKMVST GVAMTVPEGT
YGRVAPRSGL AHKNSIDVLA GVIDRGYTGE VKVILMNLSN DTHEFPKHTR IAQLVLEKIE
NAEVKEVVDL TTTIKSDRGA GGFGSTGM
//
