ID   G3GNT5_9PHYC            Unreviewed;       148 AA.
AC   G3GNT5;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   ORFNames=ENVG_00035 {ECO:0000313|EMBL:AEO97933.1};
OS   Emiliania huxleyi virus 84.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Algavirales; Phycodnaviridae; Coccolithovirus.
OX   NCBI_TaxID=181216 {ECO:0000313|EMBL:AEO97933.1, ECO:0000313|Proteomes:UP000249003};
RN   [1] {ECO:0000313|EMBL:AEO97933.1, ECO:0000313|Proteomes:UP000249003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=84 {ECO:0000313|EMBL:AEO97933.1,
RC   ECO:0000313|Proteomes:UP000249003};
RG   The Broad Institute Genome Sequencing Platform;
RA   Henn M.R., Allen M., Levin J., Malboeuf C., Casali M., Russ C., Lennon N.,
RA   Chapman S.B., Erlich R., Young S.K., Yandava C., Zeng Q., Alvarado L.,
RA   Anderson S., Berlin A., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA   Green L., Griggs A., Gujja S., Heilman E.R., Heiman D., Hollinger A.,
RA   Howarth C., Larson L., Mehta T., Pearson M., Roberts A., Ryan E., Saif S.,
RA   Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., White J., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Emiliania huxleyi virus 84.";
RL   Submitted (NOV-2010) 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; JF974290; AEO97933.1; -; Genomic_DNA.
DR   Proteomes; UP000249003; 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:AEO97933.1}.
FT   DOMAIN          16..147
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   148 AA;  15988 MW;  679B1D9773FAC036 CRC64;
     MSSTTTNLYV SRLTDDAKLP TKGTTLSAGY DLYSSEDVKI PPWSKQMVST GLAMTVPDGT
     YGRIAPRSGL AHKNSIDVLA GVIDRGYIGE VKVILMNLSN ETQTFPKHTR IAQLVLEKIE
     YAEVKEVVDL TTSVVSDRGT NGFGSTGM
//