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Database: UniProt
Entry: Q8FF08
LinkDB: Q8FF08
Original site: Q8FF08 
ID   UNG_ECOL6               Reviewed;         228 AA.
AC   Q8FF08;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   14-MAY-2014, entry version 76.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=c3105;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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DR   EMBL; AE014075; AAN81554.1; -; Genomic_DNA.
DR   RefSeq; NP_754986.1; NC_004431.1.
DR   ProteinModelPortal; Q8FF08; -.
DR   SMR; Q8FF08; 3-228.
DR   STRING; 199310.c3105; -.
DR   EnsemblBacteria; AAN81554; AAN81554; c3105.
DR   GeneID; 1038816; -.
DR   KEGG; ecc:c3105; -.
DR   PATRIC; 18284058; VBIEscCol75197_2929.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; VEEMADW; -.
DR   OrthoDB; EOG6MSS63; -.
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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    228       Uracil-DNA glycosylase.
FT                                /FTId=PRO_0000176092.
FT   ACT_SITE     64     64       Proton acceptor (By similarity).
SQ   SEQUENCE   228 AA;  25535 MW;  3F19383AD8BA4470 CRC64;
     MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI
     LGQDPYHGPG QAHGLAFSVR PGIATPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL
     LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDXQRH
     HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAES
//
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