A0A1A8W0E9 · A0A1A8W0E9_9APIC

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 site306Nucleophile; for N-glycosylase activity
Site325Important for catalytic activity
Binding site374[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site381[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site384[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site390[4Fe-4S] cluster (UniProtKB | ChEBI)

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
      NTH1
    • ORF names
      POVCU1_028810
      , POVCU2_0031370

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)

Accessions

  • Primary accession
    A0A1A8W0E9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region23-61Disordered
Compositional bias98-118Basic and acidic residues
Region98-138Disordered
Domain224-372HhH-GPD

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    410
  • Mass (Da)
    47,215
  • Last updated
    2016-10-05 v1
  • Checksum
    CB6E766E9E2636F3
MEKQSKYFNKSLAKKIQIKYEDGLNSSPSSVSRVQAQNAEAQSNHLQNRDTQKSYEQNGCTWKSGVNDVRVKKEKTEEGGKSGDISLLAGKVELEQSWEEKEDKKGQIEKQHSDKVHTVKQPNKRRKKNDYGADRKTFEGERMYKQRDGYDGINGQMGIIKGAQEKSENNEELKKEHFLLTYNKIKEMRKEIVAPVDKYGCHMLGERTGDLKTYRFQTLISCLLSSRTKDEVTATVMDKLKKHGLTVENILHTSEEELRKMIYGVGFYNVKAKQILQICRILKEKYNSDIPNSYDELIKLPGIGEKIAQLVLQIALNKHEGIAVDIHVHRIANRLNWVYTKNELSTQVKLKNYVQKELWSELNTLLVGFGQVICKGKKPNCEKCTLTNDCQYYKDSLVRKVKQKKGNEDN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias98-118Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FLQU01000419
EMBL· GenBank· DDBJ
SBS85421.1
EMBL· GenBank· DDBJ
Genomic DNA
FLQV01000531
EMBL· GenBank· DDBJ
SBS94792.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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