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Database: UniProt
Entry: A0A396Q1D5_9CLOT
LinkDB: A0A396Q1D5_9CLOT
Original site: A0A396Q1D5_9CLOT 
ID   A0A396Q1D5_9CLOT        Unreviewed;       144 AA.
AC   A0A396Q1D5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   ORFNames=DXB18_03515 {ECO:0000313|EMBL:RHV68384.1};
OS   Clostridium sp. OM02-18AC.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=2292311 {ECO:0000313|EMBL:RHV68384.1, ECO:0000313|Proteomes:UP000266676};
RN   [1] {ECO:0000313|EMBL:RHV68384.1, ECO:0000313|Proteomes:UP000266676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OM02-18AC {ECO:0000313|EMBL:RHV68384.1,
RC   ECO:0000313|Proteomes:UP000266676};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000878};
CC   -!- SIMILARITY: Belongs to the dUTPase family.
CC       {ECO:0000256|ARBA:ARBA00006581}.
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:RHV68384.1}.
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DR   EMBL; QULW01000003; RHV68384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A396Q1D5; -.
DR   Proteomes; UP000266676; Unassembled WGS sequence.
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:InterPro.
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; 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:0000313|EMBL:RHV68384.1};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}.
FT   DOMAIN          27..140
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
FT   REGION          124..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   144 AA;  16627 MW;  5613797FF2139E1C CRC64;
     MQKIRIKYFQ EDMEKLTYID GKSDWIDLRA AEDIEMKAGE FKLIPLGIAM ELPKGYEAHV
     VPRSSTYKNF GIIQANHMGV IDESYCGDND QWFFPAYALR DTKISKGDRI CQFRIMEHQP
     AIEFEETDSL DHEDRGGIGS TGRR
//
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