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Database: UniProt
Entry: A0A165IXF2_EXIGL
LinkDB: A0A165IXF2_EXIGL
Original site: A0A165IXF2_EXIGL 
ID   A0A165IXF2_EXIGL        Unreviewed;       143 AA.
AC   A0A165IXF2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000256|RuleBase:RU367024};
DE            Short=dUTPase {ECO:0000256|RuleBase:RU367024};
DE            EC=3.6.1.23 {ECO:0000256|RuleBase:RU367024};
DE   AltName: Full=dUTP pyrophosphatase {ECO:0000256|RuleBase:RU367024};
GN   ORFNames=EXIGLDRAFT_835325 {ECO:0000313|EMBL:KZV94014.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV94014.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZV94014.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZV94014.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- FUNCTION: Involved in nucleotide metabolism via production of dUMP, the
CC       immediate precursor of thymidine nucleotides, and decreases the
CC       intracellular concentration of dUTP so that uracil cannot be
CC       incorporated into DNA. {ECO:0000256|RuleBase:RU367024}.
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:0000256|RuleBase:RU367024};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU367024};
CC   -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP
CC       route): step 2/2. {ECO:0000256|ARBA:ARBA00005142,
CC       ECO:0000256|RuleBase:RU367024}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233,
CC       ECO:0000256|RuleBase:RU367024}.
CC   -!- SIMILARITY: Belongs to the dUTPase family.
CC       {ECO:0000256|ARBA:ARBA00006581, ECO:0000256|RuleBase:RU367024}.
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DR   EMBL; KV425980; KZV94014.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165IXF2; -.
DR   STRING; 1314781.A0A165IXF2; -.
DR   InParanoid; A0A165IXF2; -.
DR   OrthoDB; 1343066at2759; -.
DR   UniPathway; UPA00610; UER00666.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046081; P:dUTP catabolic process; IEA:UniProtKB-UniRule.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367024};
KW   Magnesium {ECO:0000256|RuleBase:RU367024};
KW   Metal-binding {ECO:0000256|RuleBase:RU367024};
KW   Nucleotide metabolism {ECO:0000256|RuleBase:RU367024};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266}.
FT   DOMAIN          15..142
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   143 AA;  14990 MW;  90E00114B328FCBA CRC64;
     MSVAPLLIKK LSPKARAPTR GSALAAGYDL YSAEDKVVPA HGKALIDTQL QIAVPADTYG
     RVAPRSGLAS KHMIDTGAGV IDADYRGTVF VLLFNHSDND FPVKEGDRVA QLVLEKIATP
     EVVEVEDLDA TLRGSGGFGS TGA
//
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