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Database: UniProt
Entry: Q14G45
LinkDB: Q14G45
Original site: Q14G45 
ID   UNG_FRAT1               Reviewed;         220 AA.
AC   Q14G45;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   01-OCT-2014, entry version 54.
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=FTF1578c;
OS   Francisella tularensis subsp. tularensis (strain FSC 198).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=393115;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSC 198;
RX   PubMed=17406676; DOI=10.1371/journal.pone.0000352;
RA   Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J.,
RA   Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E.,
RA   Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.;
RT   "Genome sequencing shows that European isolates of Francisella
RT   tularensis subspecies tularensis are almost identical to US laboratory
RT   strain Schu S4.";
RL   PLoS ONE 2:E352-E352(2007).
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}.
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DR   EMBL; AM286280; CAL09594.1; -; Genomic_DNA.
DR   RefSeq; YP_667632.1; NC_008245.1.
DR   ProteinModelPortal; Q14G45; -.
DR   SMR; Q14G45; 2-216.
DR   STRING; 393115.FTF1578c; -.
DR   EnsemblBacteria; CAL09594; CAL09594; FTF1578c.
DR   GeneID; 4198983; -.
DR   KEGG; ftf:FTF1578c; -.
DR   PATRIC; 17962367; VBIFraTul133500_1823.
DR   eggNOG; COG0692; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; WARQGVM; -.
DR   OrthoDB; EOG6MSS63; -.
DR   BioCyc; FTUL393115:GJUT-1617-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    220       Uracil-DNA glycosylase.
FT                                /FTId=PRO_1000009888.
FT   ACT_SITE     60     60       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00148}.
SQ   SEQUENCE   220 AA;  25298 MW;  35DDC501CA0A1AF7 CRC64;
     MTWSDILAEE KQKPYFKQIL DFLACESAKG KVIFPTKENI FNAFKYTELD NLKVVILGQD
     PYHNYNQAHG LAFSVQKGVD IPPSLQNIYK ELARSIPEFK TPNHGYLVDW AKQGVFLLNT
     TLTVEAHKAN SHKDIGWETF TDTVINKISE NKHNVVFMLW GSHARKKKVL IDSSRHLILE
     STHPSPLSAH RGFLGCNHFV DCNKYLIEKK DQKIDWNLLC
//
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