ID A0A1R0H8H5_9FUNG Unreviewed; 152 AA.
AC A0A1R0H8H5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=AYI68_g335 {ECO:0000313|EMBL:OLY85465.1};
OS Smittium mucronatum.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133383 {ECO:0000313|EMBL:OLY85465.1, ECO:0000313|Proteomes:UP000187455};
RN [1] {ECO:0000313|EMBL:OLY85465.1, ECO:0000313|Proteomes:UP000187455}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ALG-7-W6 {ECO:0000313|EMBL:OLY85465.1,
RC ECO:0000313|Proteomes:UP000187455};
RX PubMed=27343289; DOI=10.1093/molbev/msw126;
RA Wang Y., White M.M., Kvist S., Moncalvo J.M.;
RT "Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First
RT Horizontally Transferred Ubiquitin Gene from a Mosquito Host.";
RL Mol. Biol. Evol. 33:2544-2554(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}.
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:OLY85465.1}.
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DR EMBL; LSSL01000100; OLY85465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R0H8H5; -.
DR STRING; 133383.A0A1R0H8H5; -.
DR UniPathway; UPA00610; UER00666.
DR Proteomes; UP000187455; 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:UP000187455}.
FT DOMAIN 16..145
FT /note="dUTPase-like"
FT /evidence="ECO:0000259|Pfam:PF00692"
SQ SEQUENCE 152 AA; 16076 MW; 7B2F168D41578CCA CRC64;
MAQESFQVIL DSPLAKLPVR ATPGSAGYDL HSSEKVVIPK KGGRHAVDTG LKLKIPEGTY
GRVAGRSGLA MKFCIDTTAG VIDSDYRGIL KVALINNGEK DFEINVGDRI AQLILERIVT
PDVVAVESFD EEMTQRGTGG FGSTGGISAS VI
//