ID   DUT_ALHV1               Reviewed;         298 AA.
AC   O36404;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, 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   Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX   NCBI_TaxID=654901;
OH   NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA   Ensser A., Pflanz R., Fleckenstein B.;
RT   "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL   J. Virol. 71:6517-6525(1997).
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; AF005370; AAC58101.1; -; Genomic_DNA.
DR   PIR; T03149; T03149.
DR   RefSeq; NP_065553.1; NC_002531.1.
DR   SMR; O36404; -.
DR   GeneID; 911778; -.
DR   KEGG; vg:911778; -.
DR   Proteomes; UP000000941; 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..298
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000405754"
FT   BINDING         180..182
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04031"
SQ   SEQUENCE   298 AA;  33095 MW;  125F96A07A4B18FA CRC64;
     MSRTLSMRRR QRLEMYYKKV PSVFTVTSNQ EESTLQLVNN KPVVIEPFRS SVVPLGVYLR
     CLPGYACMLL ANTYRNVTFH PGLIDPTYMG ELKLICNNRT DAYVVVPAGR LKVTVLAFTF
     LSPILTGPSV LSPPQYTDDA GYDLCLDQLV MVLPLKAFTF QLALTCPIQS KNFTPVVLGR
     SGLAAKGLSI TPCKWKGDVL RLSMFNHTSE TIILPEGSRL CQVVFMHNDH LPTIKPRILA
     AFLFQHRLMD MPFCQSRVSF IDIQKDPCTS TSTLFQDSTG NSISDATRGS KGLGSSGI