UNG_UREPA
ID UNG_UREPA Reviewed; 212 AA.
AC Q9PPU2;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; OrderedLocusNames=UU548;
OS Ureaplasma parvum serovar 3 (strain ATCC 700970).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=273119;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700970;
RX PubMed=11048724; DOI=10.1038/35037619;
RA Glass J.I., Lefkowitz E.J., Glass J.S., Heiner C.R., Chen E.Y.,
RA Cassell G.H.;
RT "The complete sequence of the mucosal pathogen Ureaplasma urealyticum.";
RL Nature 407:757-762(2000).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF222894; AAF30961.1; -; Genomic_DNA.
DR RefSeq; WP_006688756.1; NC_002162.1.
DR AlphaFoldDB; Q9PPU2; -.
DR SMR; Q9PPU2; -.
DR STRING; 273119.UU548; -.
DR EnsemblBacteria; AAF30961; AAF30961; UU548.
DR GeneID; 29672495; -.
DR KEGG; uur:UU548; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_2_14; -.
DR OMA; PDNGYLM; -.
DR Proteomes; UP000000423; 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..212
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176160"
FT ACT_SITE 59
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 212 AA; 24807 MW; 26A66F0F2C07B1DE CRC64;
MKWKEFIINE TKQSYLKNII KKINNIENHQ VVFPLKKQRF RCFDFFDIEQ TKVVILGQDP
YHTPKIANGL CFSVDLGNNL PGSLINIFKA LEYDLQIKRT NPDLSDWAKQ GVLLLNTVLT
VNAHQPNSHK NFGYEELIKN VFNELRKQKH VVYLLWGKQA MSYINLIDQK QNLILCASHP
SPLSAHRGFL TCKHFSKCND YLIKHLRTPI KW