ID   DUT_VZVO                Reviewed;         396 AA.
AC   Q4JQW7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
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 Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=341980;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC   Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA   Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT   "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT   its parental virus.";
RL   J. Virol. 76:11447-11459(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC   Oka varicella vaccine Varivax (V-Oka-Merk);
RX   PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA   Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA   Vassilev V.;
RT   "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL   J. Virol. 82:11023-11044(2008).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ008354; AAY57626.1; -; Genomic_DNA.
DR   EMBL; DQ008355; AAY57697.1; -; Genomic_DNA.
DR   IntAct; Q4JQW7; 8.
DR   MINT; Q4JQW7; -.
DR   PRIDE; Q4JQW7; -.
DR   Proteomes; UP000002603; Genome.
DR   Proteomes; UP000008504; Genome.
DR   Proteomes; UP000008505; Genome.
DR   Proteomes; UP000008506; 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; -; 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; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..396
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000385168"
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;  44809 MW;  FD8E18ECACFC91F3 CRC64;
     MNEAVIDPIL ETAVNTGDMF CSQTIPNRCL KDTILIEVQP ECADTLQCVL DDKVSRHQPL
     LLRNHKKLEL PSEKSVTRGG FYMQQLELLV KSAPPNEYAL LLIQCKDTAL ADEDNFFVAN
     GVIDAGYRGV ISALLYYRPG VTVILPGHLT IYLFPVKLRQ SRLLPKNVLK HLDPIFKSIQ
     VQPLSNSPSN YEKPVISEFA DISTVQQGQP LHRDSAEYHI DVPLTYKHII NPKRQEDAGY
     DICVPYNLYL KRNEFIKIVL PIIRDWDLQH PSINAYIFGR SSKSRSGIIV CPTAWPAGEH
     CKFYVYNLTG DDIRIKTGDR LAQVLLIDHN TQIHLKHNVL SNIAFPYAIR GKCGIPGVQW
     YFTKTLDLIA TPSERGTRGF GSTDKETNDV DFLLKH