GenomeNet

Database: UniProt
Entry: C3P2F8
LinkDB: C3P2F8
Original site: C3P2F8 
ID   UNG_BACAA               Reviewed;         225 AA.
AC   C3P2F8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   29-OCT-2014, entry version 34.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN   Name=ung {ECO:0000255|HAMAP-Rule:MF_00148};
GN   OrderedLocusNames=BAA_5675;
OS   Bacillus anthracis (strain A0248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=592021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A0248;
RA   Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G.,
RA   Sims D., Brettin T.;
RT   "Genome sequence of Bacillus anthracis A0248.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC       double-stranded DNA and polynucleotides, releasing free uracil.
CC       {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001598; ACQ46314.1; -; Genomic_DNA.
DR   RefSeq; YP_002869611.1; NC_012659.1.
DR   ProteinModelPortal; C3P2F8; -.
DR   SMR; C3P2F8; 1-224.
DR   STRING; 592021.BAA_5675; -.
DR   EnsemblBacteria; ACQ46314; ACQ46314; BAA_5675.
DR   GeneID; 7849258; -.
DR   KEGG; bai:BAA_5675; -.
DR   PATRIC; 18777267; VBIBacAnt132916_5916.
DR   eggNOG; COG0692; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; WARQGVM; -.
DR   OrthoDB; EOG6MSS63; -.
DR   BioCyc; BANT592021:GJAQ-5616-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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    225       Uracil-DNA glycosylase.
FT                                /FTId=PRO_1000199762.
FT   ACT_SITE     65     65       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00148}.
SQ   SEQUENCE   225 AA;  25918 MW;  8FDC19B5D4D20F75 CRC64;
     MKHVLKNDWG PLLAPEFEKE YYRELDVFLK EEYSTHVVYP KIEDIFNALE YTSYENTKVV
     ILGQDPYHGP NQAHGLSFSV QPGVKTPPSL LNMYKELRDE YGYDIPNNGY LVKWAEQGVL
     LLNTVLTVRQ GEANSHKGKG WEHFTDRVIE LLNEREKPVI FILWGRHAQA KKKLITNPNH
     QIIESVHPSP LSARRGFFGS KPYSKVNTIL ANMGEGEIDW EIPNL
//
DBGET integrated database retrieval system