W8NRU5 · W8NRU5_9EURY

  • Protein
    N-glycosylase/DNA lyase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site, active site.

126220406080100120140160180200220240260
TypeIDPosition(s)Description
Binding site438-oxoguanine (UniProtKB | ChEBI)
Binding site718-oxoguanine (UniProtKB | ChEBI)
Binding site828-oxoguanine (UniProtKB | ChEBI)
Active site163Schiff-base intermediate with DNA
Binding site1678-oxoguanine (UniProtKB | ChEBI)
Binding site1938-oxoguanine (UniProtKB | ChEBI)
Active site195
Binding site2298-oxoguanine (UniProtKB | ChEBI)
Binding site2338-oxoguanine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Functionoxidized base lesion DNA N-glycosylase activity
Biological Processbase-excision repair

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    N-glycosylase/DNA lyase
  • Alternative names
    • 8-oxoguanine DNA glycosylase
      (EC:3.2.2.-
      ) . EC:3.2.2.- (UniProtKB | ENZYME | Rhea)
    • AGOG
    • DNA-(apurinic or apyrimidinic site) lyase
      (AP lyase
      ) (EC:4.2.99.18
      ) . EC:4.2.99.18 (UniProtKB | ENZYME | Rhea)

Gene names

    • ORF names
      BD01_0321

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 30-1
  • Taxonomic lineage
    Archaea > Euryarchaeota > Thermococci > Thermococcales > Thermococcaceae > Thermococcus

Accessions

  • Primary accession
    W8NRU5

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Domain

Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).

Sequence similarities

Belongs to the archaeal N-glycosylase/DNA lyase (AGOG) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    262
  • Mass (Da)
    30,575
  • Last updated
    2014-05-14 v1
  • Checksum
    429DC1B0EC244D48
MTLDRFVRVKYREDNEKVNRLVEILRELGIDCARTIEEKVDLQFDALKNLQKNLKDDELFIKLVIANALVSYQLSGKGEDWWWEFSRHFSENPPRDIAEAYAQFLPNSKTNRRLVAGKLKRIERVEPFLESLSMDELRDYYFNGMERLRDDLAKVMNAKRSAKTIVFAVKMFGYAGRIAFSAFVPYPMAIEIPDDVRINAYTKHFTTEPPVSFWNRIAEKTEIPPLHIDSILWPVLGGKGEVLNRLKRHCPRAELVLELRGL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP007264
EMBL· GenBank· DDBJ
AHL21948.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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