A0AAD5E030 · A0AAD5E030_UMBRA

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

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

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentnucleus
Molecular Function4 iron, 4 sulfur cluster binding
Molecular FunctionDNA binding
Molecular FunctionDNA-(apurinic or apyrimidinic site) endonuclease activity
Molecular Functionlyase 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
      NTH1
    • ORF names
      K450DRAFT_180761

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • AG
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Umbelopsidomycetes > Umbelopsidales > Umbelopsidaceae > Umbelopsis

Accessions

  • Primary accession
    A0AAD5E030

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-20Polar residues
Region1-22Disordered
Compositional bias40-73Polar residues
Region40-74Disordered
Domain122-278HhH-GPD

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    341
  • Mass (Da)
    37,740
  • Last updated
    2024-05-29 v1
  • Checksum
    DB279601B0730D5D
MAGRRQSSRLSKQTLSTVSEPKSKIKRDLLSTYAYSDNQVHSASHVSESSQVIKHARPKSTKVSKSTNPAGPPNDWKSVYEVIKEYRKIALAPVDTMGCERLSEETVDEKTSRYQTLTSLMLSSQTKDAITAAAMRNLQSQIPGGLTLDNVIACDKDLLHECIKSVGFHTRKTDYIKATAAILKEKYNGDIPDTIEGLISLPGVGPKMGYLTLQCAWNKNIGIGVDVHVHRISNRLGWVKTVNGSPEDTRKACIALEAWLPKEYWKEINPLFVGFGQITCLPRGPRCNACPVNDLCPSAKLTSTIKKRRLSITVQEALDNKSDTSKKVVKEEEVIADPLSW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-20Polar residues
Compositional bias40-73Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MU620980
EMBL· GenBank· DDBJ
KAI8575458.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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