ID   DUT_FRG3G               Reviewed;         164 AA.
AC   Q6GZR2;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 77.
DE   RecName: Full=Putative deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
GN   ORFNames=FV3-063R;
OS   Frog virus 3 (isolate Goorha) (FV-3).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Alphairidovirinae; Ranavirus; Frog virus 3.
OX   NCBI_TaxID=654924;
OH   NCBI_TaxID=30343; Dryophytes versicolor (chameleon treefrog).
OH   NCBI_TaxID=8404; Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OH   NCBI_TaxID=45438; Lithobates sylvaticus (Wood frog) (Rana sylvatica).
OH   NCBI_TaxID=8316; Notophthalmus viridescens (Eastern newt) (Triturus viridescens).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15165820; DOI=10.1016/j.virol.2004.02.019;
RA   Tan W.G., Barkman T.J., Gregory Chinchar V., Essani K.;
RT   "Comparative genomic analyses of frog virus 3, type species of the genus
RT   Ranavirus (family Iridoviridae).";
RL   Virology 323:70-84(2004).
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}.
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; AY548484; AAT09723.1; -; Genomic_DNA.
DR   RefSeq; YP_031642.1; NC_005946.1.
DR   SMR; Q6GZR2; -.
DR   GeneID; 2947763; -.
DR   KEGG; vg:2947763; -.
DR   Proteomes; UP000008770; Segment.
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   Acetylation; Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism;
KW   Reference proteome.
FT   CHAIN           1..164
FT                   /note="Putative deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_0000410587"
FT   BINDING         65..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         79..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         138..139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         71
FT                   /note="N6-acetyllysine; by host"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   164 AA;  17435 MW;  1E78DC1098330934 CRC64;
     MHGNSLQYVK LSEHASGLIR GSAGAAGYDL AAAHPVVVPS FGRALVKTDL AVKMPPGLYG
     RVAPRSGLAL KKFIDVGAGV VDPDYRGNLG VILFNFGCDP FRVKRGDRIA QLVLERYESP
     PILEVDSLDS TDRGDAGYGS TGVGNWHSAL WEGFSSGDLK ESFV
//