(data stored in SCRATCH9089 zone)

SWISSPROT: UNG_PASMU

ID   UNG_PASMU               Reviewed;         222 AA.
AC   P57807;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=PM0065;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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}.
DR   EMBL; AE004439; AAK02149.1; -; Genomic_DNA.
DR   RefSeq; WP_005718925.1; NC_002663.1.
DR   SMR; P57807; -.
DR   PRIDE; P57807; -.
DR   EnsemblBacteria; AAK02149; AAK02149; PM0065.
DR   GeneID; 29389599; -.
DR   KEGG; pmu:PM0065; -.
DR   eggNOG; ENOG4105D5S; Bacteria.
DR   eggNOG; COG0692; LUCA.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; WFGNKHF; -.
DR   BioCyc; PMUL272843:G1FZ8-69-MONOMER; -.
DR   Proteomes; UP000000809; 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; 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; P57807.
DR   SWISS-2DPAGE; P57807.
KW   Cytoplasm; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT   CHAIN           1..222
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176124"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  24906 MW;  3F9320277FE93367 CRC64;
     MKTWKDVIGT EKTQPYFKHI LDQVHQARAS GKIVYPPPQE VFSAFQLTEF EAVKVVIIGQ
     DPYHGPNQAH GLAFSVKPGV VPPPSLMNMY KELTQDIEGF QIPNHGYLVP WAEQGVLLLN
     TVLTVEQGKA HSHASFGWET FTDRVIAALN AQREKLVFLL WGSHAQKKGQ FIDRQKHCVF
     TAPHPSPLSA HRGFLGCRHF SKTNAYLMAQ GLSPIQWQLA SL
//

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