ID   DUT_VACCW               Reviewed;         147 AA.
AC   P17374; Q80HY0;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   Name=DUT; OrderedLocusNames=VACWR041; ORFNames=F2L;
OS   Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain
OS   WR)).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Vaccinia virus.
OX   NCBI_TaxID=10254;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2219701; DOI=10.1016/0042-6822(90)90338-r;
RA   Roseman N.A., Slabaugh M.B.;
RT   "The vaccinia virus HindIII F fragment: nucleotide sequence of the left 6.2
RT   kb.";
RL   Virology 178:410-418(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2657744; DOI=10.1073/pnas.86.11.4152;
RA   Slabaugh M.B., Roseman N.A.;
RT   "Retroviral protease-like gene in the vaccinia virus genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:4152-4155(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J.,
RA   Wohlhueter R.;
RT   "Sequencing of the coding region of Vaccinia-WR to an average 9-fold
RT   redundancy and an error rate of 0.16/10kb.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: Was originally thought to be a protease-like protein
CC       (pseudoprotease). {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA48238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M34368; AAA48246.1; -; mRNA.
DR   EMBL; M25392; AAA48238.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY243312; AAO89320.1; -; Genomic_DNA.
DR   PIR; A32907; PRVZWR.
DR   RefSeq; YP_232923.1; NC_006998.1.
DR   SMR; P17374; -.
DR   DIP; DIP-2156N; -.
DR   MINT; P17374; -.
DR   DNASU; 3707498; -.
DR   GeneID; 3707498; -.
DR   KEGG; vg:3707498; -.
DR   Proteomes; UP000000344; 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   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..147
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182942"
SQ   SEQUENCE   147 AA;  16405 MW;  7578ED4F409BF1F2 CRC64;
     MFNMNINSPV RFVKETNRAK SPTRQSPYAA GYDLYSAYDY TIPPGERQLI KTDISMSMPK
     FCYGRIAPRS GLSLKGIDIG GGVIDEDYRG NIGVILINNG KCTFNVNTGD RIAQLIYQRI
     YYPELEEVQS LDSTNRGDQG FGSTGLR