ID   DUT_CAMPS               Reviewed;         147 AA.
AC   Q775Z7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 68.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   Name=OPG046; Synonyms=DUT; OrderedLocusNames=CMP37L;
OS   Camelpox virus (strain CMS).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Orthopoxvirus; Camelpox virus.
OX   NCBI_TaxID=203172;
OH   NCBI_TaxID=9836; Camelus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11907336; DOI=10.1099/0022-1317-83-4-855;
RA   Gubser C., Smith G.L.;
RT   "The sequence of camelpox virus shows it is most closely related to variola
RT   virus, the cause of smallpox.";
RL   J. Gen. Virol. 83:855-872(2002).
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. {ECO:0000250|UniProtKB:P17374}.
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:0000250|UniProtKB:P17374};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10249;
CC         Evidence={ECO:0000250|UniProtKB:P17374};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000250|UniProtKB:P17374}.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; AY009089; AAG37494.1; -; Genomic_DNA.
DR   SMR; Q775Z7; -.
DR   Proteomes; UP000107153; 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   NCBIfam; TIGR00576; dut; 1.
DR   PANTHER; PTHR11241; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   PANTHER; PTHR11241:SF0; DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
PE   3: Inferred from homology;
KW   Early protein; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism.
FT   CHAIN           1..147
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182945"
FT   BINDING         24
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P17374"
FT   BINDING         68..70
FT                   /ligand="dUTP"
FT                   /ligand_id="ChEBI:CHEBI:61555"
FT                   /evidence="ECO:0000250|UniProtKB:P17374"
FT   BINDING         82..85
FT                   /ligand="dUTP"
FT                   /ligand_id="ChEBI:CHEBI:61555"
FT                   /evidence="ECO:0000250|UniProtKB:P17374"
FT   BINDING         88
FT                   /ligand="dUTP"
FT                   /ligand_id="ChEBI:CHEBI:61555"
FT                   /evidence="ECO:0000250|UniProtKB:P17374"
FT   BINDING         93
FT                   /ligand="dUTP"
FT                   /ligand_id="ChEBI:CHEBI:61555"
FT                   /evidence="ECO:0000250|UniProtKB:P17374"
FT   BINDING         95
FT                   /ligand="dUTP"
FT                   /ligand_id="ChEBI:CHEBI:61555"
FT                   /evidence="ECO:0000250|UniProtKB:P17374"
FT   BINDING         111
FT                   /ligand="dUTP"
FT                   /ligand_id="ChEBI:CHEBI:61555"
FT                   /evidence="ECO:0000250|UniProtKB:P17374"
SQ   SEQUENCE   147 AA;  16453 MW;  4E154F0663A253D8 CRC64;
     MFNMNINSPV RFVKETNRAK SPTRQSPYAA GYDLYSAYYY TIPPGERQLI KTDISMSMPK
     FCYGRIAPRS GLSLKGIDIG GGVIDEDYRG NIGVILINNG KCTFNVNTGD RIAQLIYQRI
     YYPELKEVQS LDSTDRGDQG FGSTGLR
//