ID   UNG2_BACFR              Reviewed;         220 AA.
AC   Q64PM3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Uracil-DNA glycosylase 2 {ECO:0000255|HAMAP-Rule:MF_00148};
DE            Short=UDG 2 {ECO:0000255|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN   Name=ung2 {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=BF3816;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC       result of misincorporation of dUMP residues by DNA polymerase or due to
CC       deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC         DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00148};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000255|HAMAP-Rule:MF_00148}.
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DR   EMBL; AP006841; BAD50558.1; -; Genomic_DNA.
DR   RefSeq; WP_005798174.1; NZ_UYXF01000018.1.
DR   RefSeq; YP_101092.1; NC_006347.1.
DR   AlphaFoldDB; Q64PM3; -.
DR   SMR; Q64PM3; -.
DR   STRING; 295405.BF3816; -.
DR   EnsemblBacteria; BAD50558; BAD50558; BF3816.
DR   GeneID; 66331552; -.
DR   KEGG; bfr:BF3816; -.
DR   PATRIC; fig|295405.11.peg.3664; -.
DR   HOGENOM; CLU_032162_3_0_10; -.
DR   OMA; PDNGYLM; -.
DR   Proteomes; UP000002197; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   CDD; cd10027; UDG-F1-like; 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   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
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; Hydrolase.
FT   CHAIN           1..220
FT                   /note="Uracil-DNA glycosylase 2"
FT                   /id="PRO_0000176062"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   220 AA;  24998 MW;  63BFB3CFD93566B6 CRC64;
     MNVQIEESWK THLEPEFEKD YFRTLTEFVR SEYSQYQIFP PGKLIFNAFN LCPFDKVKVV
     IIGQDPYHGP GQAHGLCFSV NDGVAFPPSL VNIFKEIKED IGTPAPSTGN LTRWAEQGVL
     LLNATLTVRA HQAGSHQRRG WEEFTDAAIR VLAEERENLV FILWGSYAQK KGAFIDRNKH
     LVLSSAHPSP LSAYNGFFGN KHFSKTNEYL KAHGKTEINW