ID   UNG_COREF               Reviewed;         238 AA.
AC   Q8FPQ4;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=CE1436;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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; BA000035; BAC18246.1; -; Genomic_DNA.
DR   RefSeq; WP_006769398.1; NZ_GG700686.1.
DR   AlphaFoldDB; Q8FPQ4; -.
DR   SMR; Q8FPQ4; -.
DR   STRING; 196164.23493275; -.
DR   EnsemblBacteria; BAC18246; BAC18246; BAC18246.
DR   KEGG; cef:CE1436; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_1_11; -.
DR   OMA; WEAVTEQ; -.
DR   OrthoDB; 1260295at2; -.
DR   Proteomes; UP000001409; 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..238
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176087"
FT   ACT_SITE        81
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   238 AA;  26326 MW;  870163EE5DA2A59E CRC64;
     MPVDEQPTTP EAVQWRTIED LPIHPSWRKV LEPVMDQIRD LGQFLTAETQ AGRGFLPPEP
     DIFRAFSYPF EEVKVLILGQ DPYPTPGHSM GLCFSTQPGV RPLPRSLVNI FKEMATDLGV
     SINATDGDLR PWSRQGVMLL NRVLTVQPGN SNSHKGRGWE AVTEAAITAL GQRDQPLVAI
     LWGRQAQAVQ KFLGDTPCIT SAHPSPLSAS RGFFGSRPFS TTNRMLDDLG ATPVDWRL