UNG_NEIG2
ID UNG_NEIG2 Reviewed; 219 AA.
AC B4RLL6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=NGK_1026;
OS Neisseria gonorrhoeae (strain NCCP11945).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=521006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCCP11945;
RX PubMed=18586945; DOI=10.1128/jb.00566-08;
RA Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF29703.1; -; Genomic_DNA.
DR RefSeq; WP_003688628.1; NC_011035.1.
DR AlphaFoldDB; B4RLL6; -.
DR SMR; B4RLL6; -.
DR EnsemblBacteria; ACF29703; ACF29703; NGK_1026.
DR GeneID; 66753125; -.
DR KEGG; ngk:NGK_1026; -.
DR HOGENOM; CLU_032162_3_0_4; -.
DR OMA; PDNGYLM; -.
DR OrthoDB; 1260295at2; -.
DR Proteomes; UP000002564; 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.
FT CHAIN 1..219
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_1000096596"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ SEQUENCE 219 AA; 24688 MW; 8B55F4010567E3E2 CRC64;
MDTWHDALGG EKQQPYFQEI LNAVRQERLS GQIIYPPEAD VFNAFRLTAF DRVKVVILGQ
DPYHGVGQAH GLAFSVRQGV RIPPSLLNIY KELETDIEGF SIPAHGCLTA WAEQGILLLN
TVLTVRAGQA HSHALLGWER FTDTVIRQLA THRKHLVFML WGGYAQQKGR LIDSQNHLIL
TAPHPSPLSA YRGFFGCRHF SQANSYLSQH GIEPINWKL