ID   DUT_YMTV5               Reviewed;         143 AA.
AC   Q6TUZ4;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
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=17L;
OS   Yaba monkey tumor virus (strain VR587) (YMTV).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC   Chitovirales; Poxviridae; Chordopoxvirinae; Yatapoxvirus.
OX   NCBI_TaxID=928314;
OH   NCBI_TaxID=9538; Erythrocebus patas (Red guenon) (Cercopithecus patas).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9539; Macaca (macaques).
OH   NCBI_TaxID=9557; Papio hamadryas (Hamadryas baboon).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14645589; DOI=10.1128/jvi.77.24.13335-13347.2003;
RA   Brunetti C.R., Amano H., Ueda Y., Qin J., Miyamura T., Suzuki T., Li X.,
RA   Barrett J.W., McFadden G.;
RT   "Complete genomic sequence and comparative analysis of the tumorigenic
RT   poxvirus Yaba monkey tumor virus.";
RL   J. Virol. 77:13335-13347(2003).
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; AY386371; AAR07375.1; -; Genomic_DNA.
DR   RefSeq; NP_938274.1; NC_005179.1.
DR   SMR; Q6TUZ4; -.
DR   PRIDE; Q6TUZ4; -.
DR   GeneID; 2943676; -.
DR   KEGG; vg:2943676; -.
DR   Proteomes; UP000008596; 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;
KW   Reference proteome.
FT   CHAIN           1..143
FT                   /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT                   /id="PRO_0000182951"
SQ   SEQUENCE   143 AA;  15658 MW;  A67BB9059654C8DF CRC64;
     MSKFIVYVKK SSEFATIPTR SSKKSAGYDL YSAYDYLVRP KSRVLVKTDI CLSIPDECYG
     RIASRSGLSL NNSIDIGGGV IDGDYRGVIG VIFINNGNSP HYIKRGDRIA QIVFERLANV
     EIKEISNLDC TCRGDCGFGS SGI