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 07-SEP-2016, entry version 64.
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}.
DR EMBL; AM286280; CAL09594.1; -; Genomic_DNA.
DR RefSeq; WP_003018069.1; NC_008245.1.
DR ProteinModelPortal; Q14G45; -.
DR SMR; Q14G45; 2-216.
DR EnsemblBacteria; CAL09594; CAL09594; FTF1578c.
DR KEGG; ftf:FTF1578c; -.
DR PATRIC; 17962367; VBIFraTul133500_1823.
DR HOGENOM; HOG000229528; -.
DR KO; K03648; -.
DR OMA; IALIPKN; -.
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 CDD; cd10027; UDG_F1; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR018085; Ura-DNA_Glyclase_AS.
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 Cytoplasm; DNA damage; DNA repair; Glycosidase; 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
//
