ID   UNG_FRATT               Reviewed;         220 AA.
AC   Q5NEP2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=FTT_1578c;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46211.1; -; Genomic_DNA.
DR   RefSeq; WP_003018069.1; NZ_CP010290.1.
DR   RefSeq; YP_170500.1; NC_006570.2.
DR   AlphaFoldDB; Q5NEP2; -.
DR   SMR; Q5NEP2; -.
DR   STRING; 177416.FTT_1578c; -.
DR   DNASU; 3192316; -.
DR   EnsemblBacteria; CAG46211; CAG46211; FTT_1578c.
DR   KEGG; ftu:FTT_1578c; -.
DR   eggNOG; COG0692; Bacteria.
DR   OMA; PDNGYLM; -.
DR   Proteomes; UP000001174; 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; Reference proteome.
FT   CHAIN           1..220
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176096"
FT   ACT_SITE        60
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-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