A0A6P3Y3E9 · A0A6P3Y3E9_DINQU
- ProteinEndonuclease III homolog
- GeneLOC106749924
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids368 (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 | class I DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | endonuclease 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
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Hymenoptera > Apocrita > Aculeata > Formicoidea > Formicidae > Ponerinae > Ponerini > Dinoponera
Accessions
- Primary accessionA0A6P3Y3E9
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 16-50 | Disordered | ||||
Sequence: LRSGKTVATKESSGETSPYFAGKKSTSTKTSTKKR | ||||||
Compositional bias | 17-48 | Polar residues | ||||
Sequence: RSGKTVATKESSGETSPYFAGKKSTSTKTSTK | ||||||
Domain | 188-338 | HhH-GPD | ||||
Sequence: LSSQTKDQVTHAAMQRLITYGCKPNLIAQTSDDVLGKLIYPVGFWKRKVEYIKRTSVILLNKYNGDIPRTIKELCELPGVGSKMAHLCMQIAWGEVSGIGVDTHVHRISNRLGWVRKPTKIPEETRNELEDWLPKHLWSQVNHLLVGFGQE |
Sequence similarities
Belongs to the Nth/MutY family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length368
- Mass (Da)41,373
- Last updated2020-12-02 v1
- Checksum3AF5EAF34CB68170
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 17-48 | Polar residues | ||||
Sequence: RSGKTVATKESSGETSPYFAGKKSTSTKTSTK |
Keywords
- Technical term