I2FQ94 · I2FQ94_USTHO
- ProteinDNA-(apurinic or apyrimidinic site) endonuclease
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids362 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
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 | 104 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 132 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 205 | |||||
Sequence: Y | ||||||
Active site | 244 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 244 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 246 | Transition state stabilizer | ||||
Sequence: N | ||||||
Site | 324 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 350 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 351 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 351 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 351 | Interaction with DNA substrate | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | nuclease activity | |
Biological Process | DNA repair |
Keywords
- 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 > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Ustilago
Accessions
- Primary accessionI2FQ94
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Polar residues | ||||
Sequence: MATRRSSSRTATFAASQEVAKVA | ||||||
Region | 1-92 | Disordered | ||||
Sequence: MATRRSSSRTATFAASQEVAKVASASPSPAKPKRKATDSASSVAQKNGARKSRKKAVADSDSPSAPKSEDTTADPSLPKNIKMPATLSYPRP | ||||||
Domain | 114-351 | Endonuclease/exonuclease/phosphatase | ||||
Sequence: KGMMRYIEAEDADIIVLSETKVNDVPMHPGLTKIYKHQYWGIGKKKGYTGLAILSKIEPIKAVYGLPGLKYQDTKGRIVTLEFENTFLVGTYAVNAGEGLKTMATKQAWNTAFATYLAWLDSKKPVIWCGDFNVVQDERDLAGASKKWNKTPGYTAIECDAHRELIQGTATPTSKPLVDVWRQKHPDAVGHYTFYGWRGFCRAKGIGWRLDSFILSERIASKALECEIRHECFGASDH |
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length362
- Mass (Da)39,736
- Last updated2012-07-11 v1
- ChecksumD329B4ACCE96D3A0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Polar residues | ||||
Sequence: MATRRSSSRTATFAASQEVAKVA |