A8NAI8 · A8NAI8_COPC7
- ProteinDNA-(apurinic or apyrimidinic site) endonuclease 2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids609 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Probably binds two magnesium or manganese ions per subunit.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 7 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 42 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Active site | 158 | ||||
Active site | 200 | Proton donor/acceptor | |||
Binding site | 200 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 202 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Site | 202 | Transition state stabilizer | |||
Site | 288 | Important for catalytic activity | |||
Binding site | 313 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Active site | 314 | Proton acceptor | |||
Binding site | 314 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Site | 314 | Interaction with DNA substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | double-stranded DNA 3'-5' DNA exonuclease activity | |
Molecular Function | lyase activity | |
Molecular Function | phosphoric diester hydrolase activity | |
Molecular Function | zinc ion binding | |
Biological Process | base-excision repair |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameDNA-(apurinic or apyrimidinic site) endonuclease 2
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Agaricales > Agaricineae > Psathyrellaceae > Coprinopsis
Accessions
- Primary accessionA8NAI8
Proteomes
Organism-specific databases
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 373-402 | Polar residues | |||
Region | 373-596 | Disordered | |||
Compositional bias | 420-460 | Polar residues | |||
Compositional bias | 469-506 | Polar residues | |||
Compositional bias | 507-531 | Basic and acidic residues | |||
Compositional bias | 539-567 | Polar residues | |||
Domain | 574-609 | GRF-type | |||
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length609
- Mass (Da)67,423
- Last updated2008-01-15 v1
- ChecksumC2B6F8636C6ADB01
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 373-402 | Polar residues | |||
Compositional bias | 420-460 | Polar residues | |||
Compositional bias | 469-506 | Polar residues | |||
Compositional bias | 507-531 | Basic and acidic residues | |||
Compositional bias | 539-567 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AACS02000007 EMBL· GenBank· DDBJ | EAU90023.1 EMBL· GenBank· DDBJ | Genomic DNA |