ID A0A0A1UZ96_9HYPO Unreviewed; 177 AA.
AC A0A0A1UZ96;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=X797_003808 {ECO:0000313|EMBL:EXV02686.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV02686.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXV02686.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV02686.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXV02686.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JELW01000004; EXV02686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1UZ96; -.
DR HOGENOM; CLU_068508_2_1_1; -.
DR OrthoDB; 1343066at2759; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000030151; 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}.
FT DOMAIN 41..169
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 177 AA; 18510 MW; 8E4302E300406057 CRC64;
MSAAPDSVAA ATTSPPAKRV KTDLSTMEAP PALQVKKLSD KARLPTRGSA FAAGYDIYAS
KDTTVPARGK VLVDTDISIA VPAGTYGRIA PRSGLASKHF IDTGAGVIDA DYRGQVKVLL
FNHAETDFEI KEGDRIAQLV IERIYTPEVV EVQELEESVR GAGGFGSTGG FANGTAA
//
