ID   DUT_EBVA8               Reviewed;         278 AA.
AC   Q07275; Q1HVG9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000255|HAMAP-Rule:MF_04031};
DE            Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_04031};
DE            EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_04031};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_04031};
GN   Name=DUT {ECO:0000255|HAMAP-Rule:MF_04031}; ORFNames=BLLF3;
OS   Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=82830;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8393237; DOI=10.1006/viro.1993.1409;
RA   Lees J.F., Arrand J.E., Pepper S.V., Stewart J.P., Mackett M., Arrand J.R.;
RT   "The Epstein-Barr virus candidate vaccine antigen gp340/220 is highly
RT   conserved between virus types A and B.";
RL   Virology 195:578-586(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA   Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT   "The genome of Epstein-Barr virus type 2 strain AG876.";
RL   Virology 350:164-170(2006).
CC   -!- FUNCTION: Involved in nucleotide metabolism: produces dUMP, the
CC       immediate precursor of thymidine nucleotides and decreases the
CC       intracellular concentration of dUTP to avoid uracil incorporation into
CC       viral DNA. {ECO:0000255|HAMAP-Rule:MF_04031}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04031};
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_04031}.
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DR   EMBL; L07923; AAA02786.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; DQ279927; ABB89239.1; -; Genomic_DNA.
DR   RefSeq; YP_001129459.1; NC_009334.1.
DR   SMR; Q07275; -.
DR   PRIDE; Q07275; -.
DR   GeneID; 5176172; -.
DR   KEGG; vg:5176172; -.
DR   Proteomes; UP000007639; Genome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046080; P:dUTP metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07557; trimeric_dUTPase; 2.
DR   Gene3D; 2.70.40.10; -; 2.
DR   HAMAP; MF_04031; HSV_DUT; 1.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   InterPro; IPR034745; HSV_DUT.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..278
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182963"
FT   BINDING         171..173
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT   BINDING         273..274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT   CONFLICT        245
FT                   /note="S -> T (in Ref. 1; AAA02786)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  30892 MW;  05073FAB4B863531 CRC64;
     MEACPHIRYA FQNDKLLLQQ ASVGRLTLVN KTTILLRPMK TTTVDLGLYA RPPEGHGLML
     WGSTSRPVTS HVGIIDPGYT GELRLILQNQ RRYNSTLRPS ELKIHLAAFR YATPQMEEDK
     GPINHPQYPG DVGLDVSLPK DLALFPHQTV SVTLTVPPPS IPHHRPTIFG RSGLAMQGIL
     VKPCRWRRGG VDVSLTNFSD QTVFLNKYRR FCQLVYLHKH HLTSFYSPHS DAGVLGPRSL
     FRWASCAFEE VPGLAMGDSG LSEALEGRQG RGFGSSGQ