A0A8H7PL34 · A0A8H7PL34_9FUNG

  • Protein
    Endonuclease III homolog
  • Gene
    NTH1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

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
      INT44_000336

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • WA0000051536
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mucoromycotina > Umbelopsidomycetes > Umbelopsidales > Umbelopsidaceae > Umbelopsis

Accessions

  • Primary accession
    A0A8H7PL34

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region45-70Disordered
Domain122-282HhH-GPD
Compositional bias322-337Basic and acidic residues
Region322-345Disordered

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    345
  • Mass (Da)
    38,317
  • Last updated
    2022-01-19 v1
  • Checksum
    D3DDDD1059955D1E
MAGRRQSSRLSKQTLSTVSEPKLKIKRELLSNYAYNDNQVHSASHVSESAQVIKHSRPKSTKANKSTNLAGPPNDWKTVYEVIKEYRKIALAPVDTMGCERLSEETVDEKTSRYQTLTSLMLSSQTKDAITAAAMRNLQLKIPGGLTLDNVIACDKDLLHECIKSVGFHTRKTDYIKATAAILKEKYNGDIPDTIEGLISLPGVGPKMGYLTLQCAWDKNIGIGVDVHVHRISNRLGWVKTVNGSPEDTRKACIAYFEALEAWLPKEYWKEINPLLVGFGQITCLPRGPRCNACPVNDLCPSAKLTSTIKKQRLSVTVQESLDDKSDTSKKVVKQEEATTDPLSW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias322-337Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEPRA010000014
EMBL· GenBank· DDBJ
KAG2175858.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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