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Database: UniProt
Entry: E2SR35_9FIRM
LinkDB: E2SR35_9FIRM
Original site: E2SR35_9FIRM 
ID   E2SR35_9FIRM            Unreviewed;       170 AA.
AC   E2SR35;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=dUTP diphosphatase {ECO:0000256|ARBA:ARBA00012379};
DE            EC=3.6.1.23 {ECO:0000256|ARBA:ARBA00012379};
GN   Name=dut {ECO:0000313|EMBL:EFP60023.1};
GN   ORFNames=HMPREF0983_03720 {ECO:0000313|EMBL:EFP60023.1};
OS   Erysipelotrichaceae bacterium 3_1_53.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP60023.1, ECO:0000313|Proteomes:UP000006223};
RN   [1] {ECO:0000313|EMBL:EFP60023.1, ECO:0000313|Proteomes:UP000006223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_53 {ECO:0000313|EMBL:EFP60023.1,
RC   ECO:0000313|Proteomes:UP000006223};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA   Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA   Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA   Daigneault M., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL   Submitted (JUL-2010) 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:EFP60023.1}.
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DR   EMBL; ACTJ01000086; EFP60023.1; -; Genomic_DNA.
DR   AlphaFoldDB; E2SR35; -.
DR   STRING; 658659.HMPREF0983_03720; -.
DR   eggNOG; COG0756; Bacteria.
DR   HOGENOM; CLU_068508_0_0_9; -.
DR   Proteomes; UP000006223; 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:EFP60023.1};
KW   Nucleotide metabolism {ECO:0000256|ARBA:ARBA00023080}.
FT   DOMAIN          40..168
FT                   /note="dUTPase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00692"
SQ   SEQUENCE   170 AA;  19424 MW;  7941F0CBCBF1F2D0 CRC64;
     MERMAKFHKV SFQRFEKDWK ETFPKEPVQE IRVLYDNLLL PKRATRGSAG YDFFAPAAFT
     LAPQETIKLP TGIRAEIREG WVLQLFPRSS LGFRYRLQCN NTVGIIDSDY FESDNEGHIF
     IKLMNDSREN KTVTVQAGEG FAQGIFLPFG ICEDDDAQDI RNGGFGSTNK
//
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