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P39615 (UNG_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uracil-DNA glycosylase

Short name=UDG
EC=3.2.2.27
Gene names
Name:ung
Synonyms:ywdG
Ordered Locus Names:BSU37970
ORF Names:ipa-57d
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine By similarity. HAMAP-Rule MF_00148

Catalytic activity

Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil. HAMAP-Rule MF_00148

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00148.

Sequence similarities

Belongs to the uracil-DNA glycosylase family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbase-excision repair

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionuracil DNA N-glycosylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Uracil-DNA glycosylase HAMAP-Rule MF_00148
PRO_0000176067

Sites

Active site651Proton acceptor By similarity

Secondary structure

........................................... 225
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39615 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 649052A9C2904F9C

FASTA22526,047
        10         20         30         40         50         60 
MKQLLQDSWW NQLKEEFEKP YYQELREMLK REYAEQTIYP DSRDIFNALH YTSYDDVKVV 

        70         80         90        100        110        120 
ILGQDPYHGP GQAQGLSFSV KPGVKQPPSL KNIFLELQQD IGCSIPNHGS LVSWAKQGVL 

       130        140        150        160        170        180 
LLNTVLTVRR GQANSHKGKG WERLTDRIID VLSERERPVI FILWGRHAQM KKERIDTSKH 

       190        200        210        220 
FIIESTHPSP FSARNGFFGS RPFSRANAYL EKMGEAPIDW CIKDL 

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis genome project: cloning and sequencing of the 97 kb region from 325 degrees to 333 degrees."
Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F., Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E., Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.
Mol. Microbiol. 10:371-384(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73124 Genomic DNA. Translation: CAA51613.1.
AL009126 Genomic DNA. Translation: CAB15823.1.
PIRS39712.
RefSeqNP_391676.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZOQX-ray1.45A1-225[»]
3ZORX-ray2.95A1-225[»]
ProteinModelPortalP39615.
SMRP39615. Positions 1-224.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU37970.

Proteomic databases

PaxDbP39615.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15823; CAB15823; BSU37970.
GeneID937265.
KEGGbsu:BSU37970.
PATRIC18979638. VBIBacSub10457_3981.

Organism-specific databases

GenoListBSU37970. [Micado]

Phylogenomic databases

eggNOGCOG0692.
HOGENOMHOG000229528.
KOK03648.
OMAAGKEIYP.
OrthoDBEOG6MSS63.
ProtClustDBPRK05254.

Enzyme and pathway databases

BioCycBSUB:BSU37970-MONOMER.

Family and domain databases

Gene3D3.40.470.10. 1 hit.
HAMAPMF_00148. UDG.
InterProIPR018085. Ura-DNA_Glyclase_AS.
IPR002043. Ura_DNA_glycsylse.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERPTHR11264. PTHR11264. 1 hit.
PfamPF03167. UDG. 1 hit.
[Graphical view]
SMARTSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMSSF52141. SSF52141. 1 hit.
TIGRFAMsTIGR00628. ung. 1 hit.
PROSITEPS00130. U_DNA_GLYCOSYLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUNG_BACSU
AccessionPrimary (citable) accession number: P39615
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 19, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList