A0A6P4CL16 · A0A6P4CL16_ARADU
- ProteinEndonuclease III homolog
- GeneLOC107476774
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids378 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 262 | Nucleophile; for N-glycosylase activity | ||||
Sequence: K | ||||||
Site | 281 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 337 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 344 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 347 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 353 | [4Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast nucleoid | |
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
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > dalbergioids sensu lato > Dalbergieae > Pterocarpus clade > Arachis
Accessions
- Primary accessionA0A6P4CL16
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 25-49 | Polar residues | ||||
Sequence: TTPSLPSNSNTDTPTSDSSSHAASV | ||||||
Region | 25-88 | Disordered | ||||
Sequence: TTPSLPSNSNTDTPTSDSSSHAASVSKARVFVRRSKRPKTTLVALQQKELEPPTRDHDKSSGLP | ||||||
Compositional bias | 74-88 | Basic and acidic residues | ||||
Sequence: LEPPTRDHDKSSGLP | ||||||
Domain | 179-335 | HhH-GPD | ||||
Sequence: LSSQTKDHVTHGAIQRLLENGLLTPDAINNADEETIKKMLYPVGFYTRKATNLKKIANICLMKYDGDIPSTIEQLLLLPGIGPKMAHLVMNVGWNNVQGICVDTHVHRICNRLGWVSRPSTKQKTLTPEETREALQRWLPREEWVPINPLLVGFGQT | ||||||
Region | 357-378 | Disordered | ||||
Sequence: FKEASNSSPSSKPKKSGPNKKR |
Sequence similarities
Belongs to the Nth/MutY family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length378
- Mass (Da)41,660
- Last updated2020-12-02 v1
- ChecksumFFBC50B4CA5EA287
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 25-49 | Polar residues | ||||
Sequence: TTPSLPSNSNTDTPTSDSSSHAASV | ||||||
Compositional bias | 74-88 | Basic and acidic residues | ||||
Sequence: LEPPTRDHDKSSGLP |
Keywords
- Technical term