ID   DUT_HHV11               Reviewed;         371 AA.
AC   P10234; Q09I84;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=UL50;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nonneuroinvasive mutant HF10;
RX   PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA   Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT   "Determination and analysis of the DNA sequence of highly attenuated herpes
RT   simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL   Microbes Infect. 9:142-149(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17 syn+;
RA   Cunningham C., Davison A.J.;
RT   "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; X14112; CAA32301.1; -; Genomic_DNA.
DR   EMBL; DQ889502; ABI63511.1; -; Genomic_DNA.
DR   EMBL; FJ593289; ACM62274.1; -; Genomic_DNA.
DR   PIR; E30089; WMBEY0.
DR   RefSeq; YP_009137126.1; NC_001806.2.
DR   BioGRID; 971447; 1.
DR   DIP; DIP-62052N; -.
DR   IntAct; P10234; 1.
DR   PRIDE; P10234; -.
DR   DNASU; 2703421; -.
DR   GeneID; 2703421; -.
DR   KEGG; vg:2703421; -.
DR   Proteomes; UP000009294; Genome.
DR   Proteomes; UP000180652; 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; 1.
DR   SUPFAM; SSF51283; SSF51283; 2.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..371
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182952"
FT   REGION          350..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         260..262
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
FT   BINDING         366..367
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ   SEQUENCE   371 AA;  39128 MW;  5FFA2556AD2F7158 CRC64;
     MSQWGSGAIL VQPDSLGRGY DGDWHTAVAT RGGGVVQLNL VNRRAVAFMP KVSGDSGWAV
     GRVSLDLRMA MPADFCAIIH APALASPGHH VILGLIDSGY RGTVMAVVVA PKRTREFAPG
     TLRVDVTFLD ILATPPALTE PISLRQFPQL APPPPTGAGI REDPWLEGAL GAPSVTTALP
     ARRRGRSLVY AGELTPVQTE HGDGVREAIA FLPKREEDAG FDIVVRRPVT VPANGTTVVQ
     PSLRMLHADA GPAACYVLGR SSLNARGLLV VPTRWLPGHV CAFVVYNLTG VPVTLEAGAK
     VAQLLVAGAD ALPWIPPDNF HGTKALRNYP RGVPDSTAEP RNPPLLVFTN EFDAEAPPSE
     RGTGGFGSTG I