ID   UNG_FRASN               Reviewed;         225 AA.
AC   A8LD98;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   01-MAY-2013, entry version 34.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=Franean1_4601;
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Frankineae; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec;
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(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 (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; CP000820; ABW13972.1; -; Genomic_DNA.
DR   RefSeq; YP_001508878.1; NC_009921.1.
DR   ProteinModelPortal; A8LD98; -.
DR   SMR; A8LD98; 3-225.
DR   STRING; 298653.Franean1_4601; -.
DR   EnsemblBacteria; ABW13972; ABW13972; Franean1_4601.
DR   GeneID; 5672946; -.
DR   KEGG; fre:Franean1_4601; -.
DR   PATRIC; 21942329; VBIFraSp51419_4770.
DR   eggNOG; COG0692; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; KGWEEVT; -.
DR   ProtClustDB; PRK05254; -.
DR   BioCyc; FSP298653:GHPI-4645-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:HAMAP.
DR   GO; GO:0006284; P:base-excision repair; IEA: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; UDNA_glycsylseSF; 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_1000096582.
FT   ACT_SITE     68     68       Proton acceptor (By similarity).
SQ   SEQUENCE   225 AA;  24587 MW;  32589D3689426243 CRC64;
     MPAQPLRDIL EPGWAKALEP MADRIAAMGD FLRAEIAAGR SYLPAGQHVL RAFQQPFDDV
     RVLIVGQDPY PTPGMAIGYS FAVAPEVRRL PGSLENIFQE LCADLSVPRP TNGDLTPWTR
     QGVLLLNRVL TTAPRQPGAH RGKGWEEVTE QAIRALAARG TPLVAILWGA DARSLRPFLS
     PAPTIESAHP SPRSADRGFF GSRPFSRANN HLLEQGAQPV DWHLP
//