A0A8J4Q6I7 · A0A8J4Q6I7_9MYCE
- ProteinEndonuclease III homolog
- GeneNTH1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids446 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Catalytic activity
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Cofactor
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Cellular Component | nucleus | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | lyase activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity | |
Biological Process | base-excision repair, AP site formation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEndonuclease III homolog
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Amoebozoa > Evosea > Eumycetozoa > Dictyostelia > Dictyosteliales > Dictyosteliaceae > Polysphondylium
Accessions
- Primary accessionA0A8J4Q6I7
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 65-111 | Polar residues | ||||
Sequence: MSSDAKGVKHSNNNQSDTDNKVNVDKNNNKSTTTTTTTTSSPSKTKT | ||||||
Region | 65-134 | Disordered | ||||
Sequence: MSSDAKGVKHSNNNQSDTDNKVNVDKNNNKSTTTTTTTTSSPSKTKTKVVTSKEKEITEDDKKLSSTKNT | ||||||
Compositional bias | 112-134 | Basic and acidic residues | ||||
Sequence: KVVTSKEKEITEDDKKLSSTKNT | ||||||
Region | 146-174 | Disordered | ||||
Sequence: EDSNKKKEKEEESESESESESDLEVDDKN | ||||||
Domain | 229-378 | HhH-GPD | ||||
Sequence: LSSQTKDQITHAAMVRLKKHGLTVENVIKTPNETLSKLIHPVGFYQRKAVYLKNIASILKSKYKSDVPDQFDQLMDLPGLGPKMTHLILQIAFDKVEGIAIDVHMHRIMNRMKWVHNTNTPEETRKELESWLPKDRWRDVNHLIVGFGQT | ||||||
Region | 407-446 | Disordered | ||||
Sequence: ARKESKKQSKVKVKSKSISSAKKSKSTSSTKPPNKKKSKS |
Sequence similarities
Belongs to the Nth/MutY family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length446
- Mass (Da)50,513
- Last updated2022-05-25 v1
- Checksum1EC2597C0E13E1F4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 65-111 | Polar residues | ||||
Sequence: MSSDAKGVKHSNNNQSDTDNKVNVDKNNNKSTTTTTTTTSSPSKTKT | ||||||
Compositional bias | 112-134 | Basic and acidic residues | ||||
Sequence: KVVTSKEKEITEDDKKLSSTKNT |
Keywords
- Technical term