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Database: UniProt
Entry: V7I2G7_9CLOT
LinkDB: V7I2G7_9CLOT
Original site: V7I2G7_9CLOT 
ID   V7I2G7_9CLOT            Unreviewed;       209 AA.
AC   V7I2G7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   ORFNames=T472_0217030 {ECO:0000313|EMBL:ETA79384.1};
OS   Youngiibacter fragilis 232.1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Youngiibacter.
OX   NCBI_TaxID=994573 {ECO:0000313|EMBL:ETA79384.1, ECO:0000313|Proteomes:UP000017747};
RN   [1] {ECO:0000313|EMBL:ETA79384.1, ECO:0000313|Proteomes:UP000017747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=232.1 {ECO:0000313|EMBL:ETA79384.1,
RC   ECO:0000313|Proteomes:UP000017747};
RX   PubMed=24459265;
RA   Wawrik C.B., Callaghan A.V., Stamps B.W., Wawrik B.;
RT   "Genome Sequence of Youngiibacter fragilis, the Type Strain of the Genus
RT   Youngiibacter.";
RL   Genome Announc. 2:e01183-13(2014).
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:ETA79384.1}.
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DR   EMBL; AXUN02000215; ETA79384.1; -; Genomic_DNA.
DR   AlphaFoldDB; V7I2G7; -.
DR   STRING; 994573.T472_0217030; -.
DR   PATRIC; fig|994573.3.peg.3227; -.
DR   eggNOG; COG0756; Bacteria.
DR   OrthoDB; 9809956at2; -.
DR   Proteomes; UP000017747; 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:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   Aminotransferase {ECO:0000313|EMBL:ETA79384.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017747};
KW   Transferase {ECO:0000313|EMBL:ETA79384.1}.
FT   DOMAIN          15..97
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   209 AA;  22741 MW;  79A0F0B96A522D62 CRC64;
     MDKVQVYIEI MENGAVPAYA NFNDAGADVF ASCDIAIRPM ESVVIPLNIR VALPDDIEMQ
     VRPRSGLSLK TDLRIPNSPG TVDAGYRDIV GIIAQNTYNI ANLPYEVFSN PSITDVIASE
     YEILKLNSHI KDHVLTADPA HDHILEAISC ISPLIIDKRG NPYGTIYIEK GMKIAQLVFN
     EYRSAEFIVV DSVASIGTDR GGGFGSTGI
//
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