A0A194Q6J6 · A0A194Q6J6_PAPXU
- ProteinDNA-(apurinic or apyrimidinic site) endonuclease
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids651 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
Cofactor
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 | 396 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 424 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Active site | 497 | ||||
Active site | 536 | Proton donor/acceptor | |||
Binding site | 536 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 538 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Site | 538 | Transition state stabilizer | |||
Site | 608 | Important for catalytic activity | |||
Binding site | 633 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Active site | 634 | Proton acceptor | |||
Binding site | 634 | Mg2+ 1 (UniProtKB | ChEBI) | |||
Site | 634 | Interaction with DNA substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | DNA-(apurinic or apyrimidinic site) endonuclease activity | |
Molecular Function | double-stranded DNA 3'-5' DNA exonuclease activity | |
Molecular Function | endonuclease activity | |
Molecular Function | metal ion binding | |
Molecular Function | phosphoric diester hydrolase activity | |
Biological Process | base-excision repair |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-(apurinic or apyrimidinic site) endonuclease
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Lepidoptera > Glossata > Ditrysia > Papilionoidea > Papilionidae > Papilioninae > Papilio
Accessions
- Primary accessionA0A194Q6J6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-369 | Disordered | |||
Compositional bias | 8-92 | Basic and acidic residues | |||
Compositional bias | 112-195 | Basic and acidic residues | |||
Compositional bias | 203-233 | Basic and acidic residues | |||
Compositional bias | 243-316 | Basic and acidic residues | |||
Compositional bias | 331-369 | Basic and acidic residues | |||
Domain | 394-634 | Endonuclease/exonuclease/phosphatase | |||
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length651
- Mass (Da)73,106
- Last updated2016-10-05 v1
- Checksum863FC8F0ECAD36A3
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 8-92 | Basic and acidic residues | |||
Compositional bias | 112-195 | Basic and acidic residues | |||
Compositional bias | 203-233 | Basic and acidic residues | |||
Compositional bias | 243-316 | Basic and acidic residues | |||
Compositional bias | 331-369 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KQ459439 EMBL· GenBank· DDBJ | KPJ00999.1 EMBL· GenBank· DDBJ | Genomic DNA |