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Database: UniProt
Entry: Q1R8F2
LinkDB: Q1R8F2
Original site: Q1R8F2 
ID   UNG_ECOUT               Reviewed;         229 AA.
AC   Q1R8F2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   14-MAY-2014, entry version 53.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=UTI89_C2902;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as
CC       a result of misincorporation of dUMP residues by DNA polymerase or
CC       due to deamination of cytosine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC       double-stranded DNA and polynucleotides, releasing free uracil.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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DR   EMBL; CP000243; ABE08362.1; -; Genomic_DNA.
DR   RefSeq; YP_541893.1; NC_007946.1.
DR   ProteinModelPortal; Q1R8F2; -.
DR   SMR; Q1R8F2; 1-229.
DR   STRING; 364106.UTI89_C2902; -.
DR   EnsemblBacteria; ABE08362; ABE08362; UTI89_C2902.
DR   GeneID; 3992210; -.
DR   KEGG; eci:UTI89_C2902; -.
DR   PATRIC; 18455342; VBIEscCol42261_2901.
DR   eggNOG; COG0692; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; WARQGVM; -.
DR   OrthoDB; EOG6MSS63; -.
DR   BioCyc; ECOL364106:GHPQ-2883-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR002043; Ura_DNA_glycsylse.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair; Glycosidase;
KW   Hydrolase.
FT   CHAIN         1    229       Uracil-DNA glycosylase.
FT                                /FTId=PRO_1000009887.
FT   ACT_SITE     64     64       Proton acceptor (By similarity).
SQ   SEQUENCE   229 AA;  25681 MW;  E94F193824FE6137 CRC64;
     MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI
     LGQDPYHGPG QAHGLAFSVR PGIATPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL
     LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDKQRH
     HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAESE
//
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