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B5QZ48 (MUG_SALEP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
G/U mismatch-specific DNA glycosylase

EC=3.2.2.28
Alternative name(s):
Double-strand-specific uracil glycosylase
Mismatch-specific uracil DNA-glycosylase
Short name=MUG
Gene names
Name:mug
Ordered Locus Names:SEN3055
OrganismSalmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]
Taxonomic identifier550537 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length168 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Excises ethenocytosine and uracil, which can arise by alkylation or deamination of cytosine, respectively, from the corresponding mispairs with guanine in ds-DNA. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells By similarity. HAMAP-Rule MF_01956

Catalytic activity

Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil. HAMAP-Rule MF_01956

Subunit structure

Binds DNA as a monomer By similarity. HAMAP-Rule MF_01956

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01956.

Sequence similarities

Belongs to the TDG/mug DNA glycosylase family.

Ontologies

Keywords
   Biological processDNA damage
DNA excision
DNA repair
   Cellular componentCytoplasm
   LigandDNA-binding
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrolase activity, hydrolyzing N-glycosyl compounds

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168G/U mismatch-specific DNA glycosylase HAMAP-Rule MF_01956
PRO_1000188964

Sequences

Sequence LengthMass (Da)Tools
B5QZ48 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: A946974A29B16FF5

FASTA16818,650
        10         20         30         40         50         60 
MVKDILAPGL RVVFCGINPG LSSANTGFPF AHPANRFWKV IHLAGFTDRQ LKPEEAEKLL 

        70         80         90        100        110        120 
DFRCGVTKLV DRPTVQATEV KLHELRSGGR NLIEKIEDYQ PAALAVLGKQ AFEQGFSQRG 

       130        140        150        160 
IAWGKQKIAI GATMVWVLPN PSGLNRIKTE KLVEAYRELD QALIMRGL 

« Hide

References

[1]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P125109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM933172 Genomic DNA. Translation: CAR34631.1.
RefSeqYP_002245121.1. NC_011294.1.

3D structure databases

ProteinModelPortalB5QZ48.
SMRB5QZ48. Positions 1-165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING550537.SEN3055.

Proteomic databases

PRIDEB5QZ48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR34631; CAR34631; SEN3055.
PATRIC32336718. VBISalEnt14964_3113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3663.
HOGENOMHOG000264684.
OMAETGCGIT.
OrthoDBEOG68H872.

Enzyme and pathway databases

BioCycSENT550537:GJFI-3095-MONOMER.

Family and domain databases

Gene3D3.40.470.10. 1 hit.
HAMAPMF_01956. MUG.
InterProIPR023502. DNA_glyclase_G/T-mismatch_bac.
IPR015637. DNA_glycosylase_G/T-mismatch.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERPTHR12159. PTHR12159. 1 hit.
PfamPF03167. UDG. 1 hit.
[Graphical view]
SMARTSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMSSF52141. SSF52141. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMUG_SALEP
AccessionPrimary (citable) accession number: B5QZ48
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: November 4, 2008
Last modified: June 11, 2014
This is version 37 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