UNG_CAMJE
ID UNG_CAMJE Reviewed; 231 AA.
AC Q9PJ40; Q0PC51;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Cj0086c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(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: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; AL111168; CAL34257.1; -; Genomic_DNA.
DR PIR; F81424; F81424.
DR RefSeq; WP_002851931.1; NC_002163.1.
DR RefSeq; YP_002343546.1; NC_002163.1.
DR AlphaFoldDB; Q9PJ40; -.
DR SMR; Q9PJ40; -.
DR IntAct; Q9PJ40; 22.
DR STRING; 192222.Cj0086c; -.
DR PaxDb; Q9PJ40; -.
DR PRIDE; Q9PJ40; -.
DR EnsemblBacteria; CAL34257; CAL34257; Cj0086c.
DR GeneID; 904411; -.
DR KEGG; cje:Cj0086c; -.
DR PATRIC; fig|192222.6.peg.84; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_1_1_7; -.
DR OMA; PDNGYLM; -.
DR Proteomes; UP000000799; 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..231
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176077"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ SEQUENCE 231 AA; 26341 MW; C3514FCA0C38199A CRC64;
MEEITINIDK IKINDDWKEF LRDEFQKKYF LEIKKQYLNA INQNIIIYPP ANLIFNAFNL
CPLKEIKIII LGQDPYHQPN QAMGLSFSVP KNVKIPPSLN NIFKELQNDL NITPAKSGDL
SSWAKQGVLL LNSILSVEAN KAASHSSWGW QEFSDAIIHK LSNEKSGLVF MLWGNYAKNK
EILIDNTKHL ILKAAHPSPL ARTGFLGCKH FSKANEFLKK VGKIPIDWKI V