A0A078GEW8 · A0A078GEW8_BRANA

  • Protein
    Endonuclease III homolog
  • Gene
    BnaC03g17500D
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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 site275Nucleophile; for N-glycosylase activity
Site294Important for catalytic activity
Binding site350[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site357[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site360[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site366[4Fe-4S] cluster (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchloroplast nucleoid
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 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
      BnaC03g17500D
    • Synonyms
      NTH1
    • ORF names
      DARMORV10_C03P20720.1
      , GSBRNA2T00024445001

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • cv. Darmor-bzh
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Brassiceae > Brassica

Accessions

  • Primary accession
    A0A078GEW8

Proteomes

Genome annotation databases

Subcellular Location

PTM/Processing

Proteomic databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias28-42Polar residues
Region28-65Disordered
Domain192-348HhH-GPD

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    389
  • Mass (Da)
    42,743
  • Last updated
    2014-10-29 v1
  • Checksum
    3CFA22323E76EBA2
MILVNRAVSTTLDNVAWFSRVRTMNRKIHSTVSSSSKANSVRIQHSRSEDSDPETANGASGSSETLVYTRKKRLKQEALEPLEKKSQQLCGLPDIEEFAFKKNTRSSKRSTTETNISVASASTAGMSTETIITPTSTKTAGSPPENWVQVLEGIRQMRSSGDAPVDSMGCDKAGSFLPPLERRFAVLLGSLLSSQTKDQVNNAAIHRLHQNGLLTPEAIDKADESTIKELIYPVGFYARKATYMKKVAKICLEKYNGDIPSSLDDLLALPGIGPKMAHLILHIAWNDVQGICVDTHVHRICNRLGWVSRPATKQKTSSPEETRVALQQWLPKEEWVAINPLLVGFGQTICTPLRPRCEACSVARLCPAAFKEASSPSSKLKKSKQSKEL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias28-42Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HG994367
EMBL· GenBank· DDBJ
CAF1699695.1
EMBL· GenBank· DDBJ
Genomic DNA
LK032152
EMBL· GenBank· DDBJ
CDY23941.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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