A0A7K9T4I1 · A0A7K9T4I1_9PICI
- Proteinexodeoxyribonuclease III
- GeneApex1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids194 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends.
Catalytic activity
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 | 14 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 89 | |||||
Sequence: Y | ||||||
Active site | 128 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 128 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 130 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 130 | Transition state stabilizer | ||||
Sequence: N | ||||||
Site | 159 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 184 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 185 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 185 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 185 | Interaction with DNA substrate | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
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 | lyase 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 nameexodeoxyribonuclease III
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Coraciimorphae > Piciformes > Galbulidae > Galbula
Accessions
- Primary accessionA0A7K9T4I1
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-185 | Endonuclease/exonuclease/phosphatase | ||||
Sequence: WVQEEAPDVLCLQETKCGAQAVPQELRDLPELPHQYWASPEDKPGYSGVGLLARHKPLNVTYGIGEEEHDREGRVVTAEFPSLYVVAAYVPNAGRRLVRLAYRQRWDQAFRSYLTRLDAHKPIALCGDLNVAYQDMPHAYTFWTYLGGARERNVGWRLDYLVISKRLEGALCDSKIRSQVMGSDH |
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Family and domain databases
Sequence
- Sequence statusFragment
- Length194
- Mass (Da)22,025
- Last updated2021-04-07 v1
- ChecksumFBA4B13E2297DFF6
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: W | ||||||
Non-terminal residue | 194 | |||||
Sequence: L |
Keywords
- Technical term