ID A0A427YNR5_9TREE Unreviewed; 260 AA.
AC A0A427YNR5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 Name=DUT1 {ECO:0000313|EMBL:RSH92772.1};
GN ORFNames=EHS25_008218 {ECO:0000313|EMBL:RSH92772.1};
OS Saitozyma podzolica.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Trimorphomycetaceae; Saitozyma.
OX NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH92772.1, ECO:0000313|Proteomes:UP000279259};
RN [1] {ECO:0000313|EMBL:RSH92772.1, ECO:0000313|Proteomes:UP000279259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH92772.1,
RC ECO:0000313|Proteomes:UP000279259};
RA Aliyu H., Gorte O., Ochsenreither K.;
RT "Genome sequence of Saitozyma podzolica DSM 27192.";
RL Submitted (NOV-2018) 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:RSH92772.1}.
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DR EMBL; RSCD01000005; RSH92772.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A427YNR5; -.
DR STRING; 1890683.A0A427YNR5; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000279259; 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; -; 2.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
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; 2.
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:UP000279259}.
FT DOMAIN 147..221
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 260 AA; 27727 MW; 902A987CC5597B69 CRC64;
MSALQDFTVE FQVKLLSERG TVPTLGSEFA AGMDLYSAEH KVVPARGKAL VDLQLSVADQ
ETAGITTVAW RGIQWRGWLE GEKHSLRGLG ENSGGKDERM SEMSLTSKTR GALHSCEGQN
VRSRITPGNG GSRRSPAACW SNRVEALASK HGIQTGAGVI DSDYRGPLMV LLFNHSDVDF
EINPKDRIAQ LILERISVPI LKQVDTLDET ARGQGGFGST GGFGSAAKKQ KLENGGAVET
VQAAAEAVVE AVQNGVDGKH
//
