A0A6P3Y3E9 · A0A6P3Y3E9_DINQU

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.

Caution

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

Cofactor

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

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 Functionendonuclease activity
Molecular Functionmetal ion binding
Molecular Functionoxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
Biological Processbase-excision repair, AP site formation

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
      LOC106749924
    • Synonyms
      NTH1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Ponerinae > Ponerini > Dinoponera

Accessions

  • Primary accession
    A0A6P3Y3E9

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region16-50Disordered
Compositional bias17-48Polar residues
Domain188-338HhH-GPD

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    368
  • Mass (Da)
    41,373
  • Last updated
    2020-12-02 v1
  • Checksum
    3AF5EAF34CB68170
MSKRLKLGALSAARTLRSGKTVATKESSGETSPYFAGKKSTSTKTSTKKRAPIKIEYETAEDKTSVKSTKVISAVQVKSENAEESADARTIKTEEREIKCEEAKQTKDAKDIMVEKSESVGHEMDSENVKDEKQSRWIPPNWETILENVKEMRKYNTAPVDEMGCHKCVDPSASPPVSRYQSLVALMLSSQTKDQVTHAAMQRLITYGCKPNLIAQTSDDVLGKLIYPVGFWKRKVEYIKRTSVILLNKYNGDIPRTIKELCELPGVGSKMAHLCMQIAWGEVSGIGVDTHVHRISNRLGWVRKPTKIPEETRNELEDWLPKHLWSQVNHLLVGFGQEICLPRFPKCSECFNKDICPYGKKNGGKVKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias17-48Polar residues

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

Disclaimer

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