ID   DUT_EHV4                Reviewed;         326 AA.
AC   Q00030;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   24-JAN-2024, entry version 72.
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=9, B3;
OS   Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC   Varicellovirus equidalpha4; Equid alphaherpesvirus 4.
OX   NCBI_TaxID=10333;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1850013; DOI=10.1128/jvi.65.5.2320-2326.1991;
RA   Whittaker G.R., Riggio M.P., Halliburton I.W., Killington R.A., Allen G.P.,
RA   Meredith D.M.;
RT   "Antigenic and protein sequence homology between VP13/14, a herpes simplex
RT   virus type 1 tegument protein, and gp10, a glycoprotein of equine
RT   herpesvirus 1 and 4.";
RL   J. Virol. 65:2320-2326(1991).
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_04031};
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_04031}.
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DR   EMBL; X17684; CAA35671.1; -; Genomic_DNA.
DR   PIR; S36705; S36705.
DR   SMR; Q00030; -.
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; -; 1.
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; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..326
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182953"
FT   BINDING         218..220
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT   BINDING         321..322
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ   SEQUENCE   326 AA;  35173 MW;  C0825CB752D36D58 CRC64;
     MASATNLADN IVVVECSNGW EARAEADGRL LVLINNHTVE LSAGLGSAGE FYSVLTDVGV
     RVACSSGYAI VLAQISGLPH VGREPGNFSN ITFTGNLANY YTAYGIVDSG YRGVVKAVQF
     ANGVNTVVPP GCMSLGLVLV KLSTETINVT NINLTENGRS PRVNIFYDYF APKRDEDAGY
     DISAQTNATI EPDESYFVEL PIVFSSSNPA VTPCIFGRSS MNRRGLIVLP TRWVTGRTCC
     FFILNINKYP VYITKGQRVA QLVLTEDIDE ALIPTNVNYN TPFPTYSPTG AVKHNPTPIL
     WKFTEAFDHD APSSARSEGG FGSTGL
//