D6WW40 · D6WW40_TRICA

Function

function

Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.

Features

Showing features for active site, site, binding site.

TypeIDPosition(s)Description
Active site187Nucleophile; for N-glycosylase activity
Site206Important for catalytic activity
Binding site255[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site262[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site265[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site271[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular FunctionDNA binding
Molecular FunctionDNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Functionendonuclease activity
Molecular Functionmetal ion binding
Molecular Functionoxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
Biological Processbase-excision repair, AP site formation
Biological Processnucleotide-excision repair

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Endonuclease III homolog
  • EC number
  • Alternative names
    • Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase
      (DNA glycosylase/AP lyase
      )

Gene names

    • Name
      NTH1
    • Synonyms
      AUGUSTUS-3.0.2_05819
    • ORF names
      TcasGA2_TC005819

Organism names

  • Taxonomic identifier
  • Strain
    • Georgia GA2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Coleoptera > Polyphaga > Cucujiformia > Tenebrionidae > Tenebrionidae incertae sedis > Tribolium

Accessions

  • Primary accession
    D6WW40

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-58Disordered
Compositional bias15-58Basic and acidic residues
Domain105-253HhH-GPD

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    283
  • Mass (Da)
    31,999
  • Last updated
    2016-05-11 v2
  • Checksum
    B0452AFFA01FBE5A
MEPSTSQVNKPDLSRFKMAPKRQLSHKSRDTKPDTQTKRGKRDHITIGSEIADKGPPDWEKTLTNIREMRKNYDAPVDSMGCHKCTEESATPEVFRYQALLALMLSSQTKDQVVFSAMQKLHKYGCNVDNILATSDEKLGELIYPVGFWKTKVKHIKKASEILKNEYNGDIPRTVEDLCKLPGVGPKMANLCMKTAWNEVTGIGVDTHVHRISNRIGWVKTKTPEETKKSLERWLPRDLWDEIGALLVGFGQQTCKPVKPQCGTCLNNSVCPFGTKEVKKNKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias15-58Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KQ971361
EMBL· GenBank· DDBJ
EFA08192.2
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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