A0A9P5W2Z3 · A0A9P5W2Z3_9FUNG

  • Protein
    Endonuclease III homolog
  • Gene
    NTH1
  • 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.

Caution

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

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

[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 site704Nucleophile; for N-glycosylase activity
Site723Important for catalytic activity
Binding site774[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site781[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site784[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site790[4Fe-4S] cluster (UniProtKB | ChEBI)

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
Molecular Functionphosphoprotein phosphatase 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
      BGX34_003483

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NVP85
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Mortierellomycotina > Mortierellomycetes > Mortierellales > Mortierellaceae > Mortierella

Accessions

  • Primary accession
    A0A9P5W2Z3

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region40-67Disordered
Compositional bias45-67Polar residues
Domain105-174Ubiquitin-like
Domain231-394FCP1 homology
Region522-560Disordered
Compositional bias541-560Basic and acidic residues
Compositional bias857-874Basic and acidic residues
Region857-886Disordered

Sequence similarities

Belongs to the Nth/MutY family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    902
  • Mass (Da)
    100,435
  • Last updated
    2023-09-13 v1
  • Checksum
    E25672DA3CFE5065
MISKSTATTDTALVPETVVTGDQVDGSRLPLLPATVALEGDSRTGPLQDLNSLPSETSFPVSTPSSLPTAATVTETAAAPLLAEQLVPSSSLTQDRMNENNKRVISLTAQWNGKKLPFEVDLDYTVGELKNKLMELTNVEPKRQKLMLVRGKLPEDHVVLSTLQLKNNQTFLMMGTPEANAFKKPEVLPEVLNDLEEDYTPDDDSFASMAQNQRSLRSTIDNCNINIMNTLRPGKRLLVLDLDYTLIDCKALNSPLGDVMRPYLHEFLTDCYRHYDIVIWSQTSWKALEAKVTTIGLLTHPDYKISFVMDITSMFYVISQRDGKPFRHQVKALDIIWEKFPQYSARNTVHIDDLSRNFAMNPKSGLKIGAYKNGAMSRHSDRELYHLARYLVDICESPNFTVLDHKNWKNHRLELILVQAIRSKGFIGLTDLVTPPQVLCTTMSTRSSSRLREARVKAEQTDTIAGSMTRNPQTGTDAAVTTNSKRIPRPTRMIVKSEDGGPDEETLARLQLEADEHRKALAAEKRSKRNSATTTGNAAKRIKSEEQDEPGLDGQAKIKRSKFATKTPVGWETTLNRIREFRLQNLAPVDTMGCERLAEVGDDIPPEVTRFQTLMSLVLSSQTKDTVTSVAIRRLQKELKGGLTIQSVIDVPSEELNRIIAAVGFHNKKTIFMKQVAEICKTKYNGDIPDTAEDLIALPGVGPKMAYLTLQVAWKKNLGIGVDTHVHRIANRLGWVKTEKDGPEGTREALQSWLPKEHWREINYLLVGFGQVLCLPRGPLCSVCPVQDRCPSATGITKQKKKLLAVVKDEKEEPFGEVEIHALHNHHEGSSVQGAEISIKQEATEDVSPYFTNKSKDKVEAEVKEEEQGDAIGHGIKLHGRGSSVDVSNLDAENADIEDLIT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias45-67Polar residues
Compositional bias541-560Basic and acidic residues
Compositional bias857-874Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAAAVA010000184
EMBL· GenBank· DDBJ
KAF9363719.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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