ID   DUT_VZVD                Reviewed;         396 AA.
AC   P09254;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   04-NOV-2026, entry version 85.
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=ORF8;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC   Varicellovirus humanalpha3; Human herpesvirus 3.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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 = dUMP + diphosphate + 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; X04370; CAA27891.1; -; Genomic_DNA.
DR   PIR; H27212; WZBE8.
DR   AlphaFoldDB; P09254; -.
DR   SMR; P09254; -.
DR   Proteomes; UP000002602; Segment.
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; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..396
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182956"
FT   BINDING         280..282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT   BINDING         380..381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ   SEQUENCE   396 AA;  44819 MW;  ECD0B8109DA3923D CRC64;
     MNEAVIDPIL ETAVNTGDMF CSQTIPNRCL KDTILIEVQP ECADTLQCVL DDKVSRHQPL
     LLRNHKKLEL PSEKSVTRGG FYMQQLELLV KSAPPNEYAL LLIQCKDTAL ADEDNFFVAN
     GVIDAGYRGV ISALLYYRPG VTVILPGHLT IYLFPVKLRQ SRLLPKNVLK HLDPIFKSIQ
     VQPLSNSPSN YEKPVIPEFA DISTVQQGQP LHRDSAEYHI DVPLTYKHII NPKRQEDAGY
     DICVPYNLYL KRNEFIKIVL PIIRDWDLQH PSINAYIFGR SSKSRSGIIV CPTAWPAGEH
     CKFYVYNLTG DDIRIKTGDR LAQVLLIDHN TQIHLKHNVL SNIAFPYAIR GKCGIPGVQW
     YFTKTLDLIA TPSERGTRGF GSTDKETNDV DFLLKH
//