ID   DUT_VARV                Reviewed;         147 AA.
AC   P0DSZ8; P33826; Q76Q48;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   Name=DUT; ORFNames=C6L, E2L, F2L;
OS   Variola virus.
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus.
OX   NCBI_TaxID=10255;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bangladesh-1975;
RX   PubMed=8264798; DOI=10.1038/366748a0;
RA   Massung R.F., Esposito J.J., Liu L.I., Qi J., Utterback T.R., Knight J.C.,
RA   Aubin L., Yuran T.E., Parsons J.M., Loparev V.N., Selivanov N.A.,
RA   Cavallaro K.F., Kerlavage A.R., Mahy B.W.J., Venter J.C.;
RT   "Potential virulence determinants in terminal regions of variola smallpox
RT   virus genome.";
RL   Nature 366:748-751(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Congo-1965, Garcia-1966, and Somalia-1977;
RA   Massung R.F., Loparev V.N., Knight J.C., Chizhikov V.E., Parsons J.M.,
RA   Totmenin A.V., Shchelkunov S.N., Esposito J.J.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Garcia-1966;
RX   PubMed=10639322; DOI=10.1006/viro.1999.0086;
RA   Shchelkunov S.N., Totmenin A.V., Loparev V.N., Safronov P.F., Gutorov V.V.,
RA   Chizhikov V.E., Knight J.C., Parsons J.M., Massung R.F., Esposito J.J.;
RT   "Alastrim smallpox variola minor virus genome DNA sequences.";
RL   Virology 266:361-386(2000).
CC   -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it produces
CC       dUMP, the immediate precursor of thymidine nucleotides and it decreases
CC       the intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; L22579; AAA60774.1; -; Genomic_DNA.
DR   EMBL; U18340; AAA69437.1; -; Genomic_DNA.
DR   EMBL; U18337; AAA69331.1; -; Genomic_DNA.
DR   EMBL; U18338; AAA69372.1; -; Genomic_DNA.
DR   EMBL; Y16780; CAB54626.1; -; Genomic_DNA.
DR   PIR; H72153; H72153.
DR   PIR; T28464; T28464.
DR   RefSeq; NP_042070.1; NC_001611.1.
DR   SMR; P0DSZ8; -.
DR   GeneID; 1486386; -.
DR   KEGG; vg:1486386; -.
DR   Proteomes; UP000111493; Genome.
DR   Proteomes; UP000119805; Genome.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   InterPro; IPR008181; dUTPase.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   PANTHER; PTHR11241; PTHR11241; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; SSF51283; 1.
DR   TIGRFAMs; TIGR00576; dut; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..147
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000448104"
SQ   SEQUENCE   147 AA;  16465 MW;  D918ED4F482ECDA1 CRC64;
     MFNMNINSPV RFVKETNRAK SPTRQSPYAA GYDLYSAYDY TIPPGERQLI KTDISMSMPK
     FCYGRIAPRS GLSLKGIDIG GGVIDEDYRG NIGVILINNG KYTFNVNTGD RIAQLIYQRI
     YYPELKEVQS LDSTDRGDQG FGSTGLR