(data stored in ACNUC30630 zone)

SWISSPROT: UNG_TROW8

ID   UNG_TROW8               Reviewed;         230 AA.
AC   P67079; Q83FW3; Q83NR7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 85.
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=TW179;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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}.
DR   EMBL; BX251410; CAD66858.1; -; Genomic_DNA.
DR   RefSeq; WP_011096139.1; NC_004551.1.
DR   SMR; P67079; -.
DR   EnsemblBacteria; CAD66858; CAD66858; TW179.
DR   GeneID; 29578598; -.
DR   KEGG; tws:TW179; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; WFGNKHF; -.
DR   BioCyc; GCF_000196075:G1EE9-202-MONOMER; -.
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; 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;
DR   PRODOM; P67079.
DR   SWISS-2DPAGE; P67079.
KW   Cytoplasm; DNA damage; DNA repair; Hydrolase.
FT   CHAIN           1..230
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176159"
FT   ACT_SITE        71
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   230 AA;  25457 MW;  DAE798B4CC2ECE30 CRC64;
     MGYLHVLAQR GVIHATWVSA LEPVSSNLAA MGDCLRSLRS KGESFLPAPR NILRAFRYPF
     DSVRVLIVGQ DPYPTQGHPI GLSFAVDHKV RPLPGSLQNI YTEYRSDLNL DPPQHGDISL
     WSERGVMLLN RTLTVRPGIP SSHRGLGWEE ITQTAVRALA ARDVPLIAIL WGRHAQELKS
     VLQSDRVAIL ESVHPSPMSA TRGFFGSKPF SKANDLLRDL GSAPIDWRLT
//

If you have problems or comments...

PBIL Back to PBIL home page