ID   DUT_EHV2                Reviewed;         289 AA.
AC   Q66656;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
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}; OrderedLocusNames=54;
OS   Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX   NCBI_TaxID=82831;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA   Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus 2.";
RL   J. Mol. Biol. 249:520-528(1995).
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; U20824; AAC13842.1; -; Genomic_DNA.
DR   PIR; S55649; S55649.
DR   RefSeq; NP_042651.1; NC_001650.2.
DR   SMR; Q66656; -.
DR   GeneID; 1461064; -.
DR   KEGG; vg:1461064; -.
DR   Proteomes; UP000007083; 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   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; IPR034745; HSV_DUT.
DR   Pfam; PF00692; dUTPase; 2.
DR   SUPFAM; SSF51283; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..289
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000406053"
FT   BINDING         176..178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT   BINDING         283..284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ   SEQUENCE   289 AA;  32958 MW;  6FCEB405630FA996 CRC64;
     MTLRKQRQEI YYEFTSSSFE ITSPPESSKI TLTNLYPILV RPYVPAVIPL GIRIIYGNKG
     QGFILAGSSQ KKVFCHTGLI DPGYRGEIKL IVLNTTKYNV TLFAGELRVS LFSFFFSTPI
     IYDYDLLNRP QYSDDAGYDL YLQEDLMLFP QASTTVTIDS RVPTTTKFFK PVVFGRSGLA
     TRGVVVDVVK WTHSPLTLKI YNFTDNTLRY SAGTRICQVV FVHRRHFPSK LKHFFTYINL
     NSKTSFYWAN VSFVDCQNDA YRSLVTLPCQ EDTDRGYRGD SGFGSSGMR