ID   438L_IIV6               Reviewed;         296 AA.
AC   Q91F87;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Probable deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE            Short=dUTPase;
DE            EC=3.6.1.23;
DE   AltName: Full=dUTP pyrophosphatase;
GN   ORFNames=IIV6-438L;
OS   Invertebrate iridescent virus 6 (IIV-6) (Chilo iridescent virus).
OC   Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes;
OC   Pimascovirales; Iridoviridae; Betairidovirinae; Iridovirus.
OX   NCBI_TaxID=176652;
OH   NCBI_TaxID=6997; Acheta domesticus (House cricket).
OH   NCBI_TaxID=168631; Chilo suppressalis (Asiatic rice borer moth).
OH   NCBI_TaxID=6999; Gryllus bimaculatus (Two-spotted cricket).
OH   NCBI_TaxID=58607; Gryllus campestris.
OH   NCBI_TaxID=7108; Spodoptera frugiperda (Fall armyworm).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11448171; DOI=10.1006/viro.2001.0963;
RA   Jakob N.J., Mueller K., Bahr U., Darai G.;
RT   "Analysis of the first complete DNA sequence of an invertebrate iridovirus:
RT   coding strategy of the genome of Chilo iridescent virus.";
RL   Virology 286:182-196(2001).
RN   [2]
RP   GENOME REANNOTATION.
RX   PubMed=17239238; DOI=10.1186/1743-422x-4-11;
RA   Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.;
RT   "Comparative genomic analysis of the family Iridoviridae: re-annotating and
RT   defining the core set of iridovirus genes.";
RL   Virol. J. 4:11-11(2007).
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   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2.
CC   -!- SIMILARITY: Belongs to the dUTPase family. {ECO:0000305}.
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DR   EMBL; AF303741; AAK82298.1; -; Genomic_DNA.
DR   RefSeq; NP_149901.1; NC_003038.1.
DR   SMR; Q91F87; -.
DR   GeneID; 1733373; -.
DR   KEGG; vg:1733373; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000001359; 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:UniProtKB-UniPathway.
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   Coiled coil; Hydrolase; Nucleotide metabolism; Reference proteome.
FT   CHAIN           1..296
FT                   /note="Probable deoxyuridine 5'-triphosphate
FT                   nucleotidohydrolase"
FT                   /id="PRO_0000376921"
FT   COILED          66..102
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   296 AA;  33257 MW;  7F4CDD5D131C62B6 CRC64;
     MDKKPTIAIL KNEIDKLKSS FDTEKDEKDT KINHILSVVE GLSKSLSLYI EDNDKETTNE
     EVNIDEIDKN IVKNLEDKVN CLEQDVQYLK NELKKKDADW QQKLDLIVHQ FTKQYDSLKS
     SLLISQKETS VFQSVQNNSN LPNNSNLPIE TPILQIKFAA LTEYAQKPKR GSEFSAGIDL
     RSAYEYLVPA NGNKLIKTDW KIQYPDGYFG KICSRSGLSL NHNLEVGAGI VDADYREGVS
     VVLNNLSPRD FHVAPGDRIA QLVCTPYITP EIVFCKPSDI PDTVRGKNGF GSTGIN