A0A8J4Q6I7 · A0A8J4Q6I7_9MYCE

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
      CYY_003663

Organism names

  • Taxonomic identifier
  • Strain
    • QSvi11
  • Taxonomic lineage
    Eukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Polysphondylium

Accessions

  • Primary accession
    A0A8J4Q6I7

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias65-111Polar residues
Region65-134Disordered
Compositional bias112-134Basic and acidic residues
Region146-174Disordered
Domain229-378HhH-GPD
Region407-446Disordered

Sequence similarities

Belongs to the Nth/MutY family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    446
  • Mass (Da)
    50,513
  • Last updated
    2022-05-25 v1
  • Checksum
    1EC2597C0E13E1F4
MNRFFKSLQNRYCSIVNIKVNLTHSDLFRSSPSSSLSPRSPFFTKPSFSLILNQNMTSKIITRSMSSDAKGVKHSNNNQSDTDNKVNVDKNNNKSTTTTTTTTSSPSKTKTKVVTSKEKEITEDDKKLSSTKNTKKRKVIEIEYEEDSNKKKEKEEESESESESESDLEVDDKNKESLARIHWKQVWDKIGVMRAEQEAPVDWAGASSFDDHSIDAPTRRFHILVGCLLSSQTKDQITHAAMVRLKKHGLTVENVIKTPNETLSKLIHPVGFYQRKAVYLKNIASILKSKYKSDVPDQFDQLMDLPGLGPKMTHLILQIAFDKVEGIAIDVHMHRIMNRMKWVHNTNTPEETRKELESWLPKDRWRDVNHLIVGFGQTVCLPTTPKCQNCTINDLCPTGIANMKANARKESKKQSKVKVKSKSISSAKKSKSTSSTKPPNKKKSKS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias65-111Polar residues
Compositional bias112-134Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJWJ01000118
EMBL· GenBank· DDBJ
KAF2075011.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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