UNG_MYCLE
ID UNG_MYCLE Reviewed; 227 AA.
AC Q9CBS3;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; OrderedLocusNames=ML1675;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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}.
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DR EMBL; AL583923; CAC30628.1; -; Genomic_DNA.
DR PIR; E87118; E87118.
DR RefSeq; NP_302149.1; NC_002677.1.
DR RefSeq; WP_010908470.1; NC_002677.1.
DR AlphaFoldDB; Q9CBS3; -.
DR SMR; Q9CBS3; -.
DR STRING; 272631.ML1675; -.
DR EnsemblBacteria; CAC30628; CAC30628; CAC30628.
DR KEGG; mle:ML1675; -.
DR PATRIC; fig|272631.5.peg.3167; -.
DR Leproma; ML1675; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_1_11; -.
DR OMA; WEAVTEQ; -.
DR Proteomes; UP000000806; 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..227
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176118"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 24655 MW; F54B7F0AE1CE43BF CRC64;
MTARPLSELV EQGWAAALEP VVDQVAEMGR FLRAEIAAGR RYLPAGHSVL RAFTYPFDNV
RVLIVGQDPY PTPGHAVGLS FSVAPDVRPL PRSLANVFDE YTADLGYPLP VCGDLTPWAQ
RGVLLLNRVL TVRPSNPASH RGKGWEVITE CAIRALAARS EPMVAILWGR DAATLKPLLT
VDNCVVIESP HPSPLSASRG FFGSRPFSRT NEILVGMGAG PINWRLP