ID   UNG_FRATF               Reviewed;         220 AA.
AC   A7NAN4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 70.
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}; OrderedLocusNames=FTA_0561;
OS   Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=458234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FTNF002-00 / FTA;
RX   PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA   Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA   Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA   Lion C., Dempsey M.P.;
RT   "Complete genome sequence of Francisella tularensis subspecies holarctica
RT   FTNF002-00.";
RL   PLoS ONE 4:E7041-E7041(2009).
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; CP000803; ABU61037.1; -; Genomic_DNA.
DR   RefSeq; WP_003014844.1; NC_009749.1.
DR   AlphaFoldDB; A7NAN4; -.
DR   SMR; A7NAN4; -.
DR   KEGG; fta:FTA_0561; -.
DR   HOGENOM; CLU_032162_3_1_6; -.
DR   OMA; PDNGYLM; -.
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"
FT                   /id="PRO_1000009889"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   220 AA;  25426 MW;  204AC321D9BD1310 CRC64;
     MTWSDILAEE KQKPYFKQIL DFLACESAKG KVIFPTKENI FNAFKYTELD NLKVVILGQD
     PYHNYNQAHG LAFSVQKWVD IPPSLQNIYK ELARSIPKFK TPNHGYLVDW AKQGVFLLNT
     TLTVEAHKAN SHKDIGWETF TDTVINKISE NKHNVVFMLW GSHARKKKVL IDSSRHLILE
     STHPSPLSAH RGFLGCNHFV DCNKYLIEKK DQKIDWNLLC