ID   UNG_SINSX               Reviewed;         217 AA.
AC   P29950;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
DE   Flags: Fragment;
GN   Name=ung;
OS   Sinorhizobium sp.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=42445;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC510;
RX   PubMed=2211521; DOI=10.1128/jb.172.10.5980-5990.1990;
RA   Crouzet J., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F.,
RA   Thibaut D., Debussche L.;
RT   "Genetic and sequence analysis of an 8.7-kilobase Pseudomonas denitrificans
RT   fragment carrying eight genes involved in transformation of precorrin-2 to
RT   cobyrinic acid.";
RL   J. Bacteriol. 172:5980-5990(1990).
RN   [2]
RP   IDENTIFICATION, AND IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA   Aasland R.;
RL   Unpublished observations (FEB-1993).
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:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from Pseudomonas
CC       denitrificans, but similarity searches show that the sequence is much
CC       closer to Sinorhizobium. The entry's taxonomy has been changed.
CC       {ECO:0000305}.
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DR   EMBL; M59301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; I36145; I36145.
DR   AlphaFoldDB; P29950; -.
DR   SMR; P29950; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
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..217
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176128"
FT   ACT_SITE        51
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   217 AA;  24315 MW;  C6C38B5491881AC4 CRC64;
     EFASAYMADL KQFLVAQKNE GRQIFPRGPE YFRALDLTPL DKVRVVILGQ DPYHGDGQAH
     GLCFSVRPGV RTPPSLVNIY KELNTDLGIP PARHGFLESW ARQGVLLLNS VLTVRARERA
     SHQGHGWEKF TDAIIRAVNE AEHPVVFMLW GSYAQKKAAF VDRSRHLVLR APHPSPLSAH
     SGFLGCRHFS QANAFLESKG FDPIDWRLPE NPAADIN