A0A6P6LLB9 · A0A6P6LLB9_CARAU
- Proteinexodeoxyribonuclease III
- GeneLOC113059822
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids308 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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 | 59 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 87 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 162 | |||||
Sequence: Y | ||||||
Active site | 201 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 201 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 203 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 203 | Transition state stabilizer | ||||
Sequence: N | ||||||
Site | 273 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 298 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 299 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 299 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 299 | 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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Cyprinidae > Cyprininae > Carassius
Accessions
- Primary accessionA0A6P6LLB9
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-48 | Basic and acidic residues | ||||
Sequence: MPKRAKKNEEAVEGETGNEPAKKEKKGKEPEAPILYEDPPDKTSSKDG | ||||||
Region | 1-50 | Disordered | ||||
Sequence: MPKRAKKNEEAVEGETGNEPAKKEKKGKEPEAPILYEDPPDKTSSKDGRA | ||||||
Domain | 57-299 | Endonuclease/exonuclease/phosphatase | ||||
Sequence: SWNVDGLRAWVKKKGLDWVRKEDPDVLCLQETKCAEKALPSEITDMPEYPHKYWAGSEEKEGYSGVAMLCKTEPLRVTYGIGKEEHGKEGRVITAEFPSFFLVTAYVPNASRGLVRLDYRKTWDVDFRAYLSVLDQRKPLVLCGDLNVAHQEIDLKNPKGNRKNAGFTPEEREGFTKLLEAGFTDSFRELYPEQANAYTFWTYMMNARAKNVGWRLDYFLLSSALLPGLCDSKIRNTAMGSDH |
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length308
- Mass (Da)34,903
- Last updated2020-12-02 v1
- ChecksumBFCA45A72091A57E
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6P6LLA1 | A0A6P6LLA1_CARAU | LOC113059822 | 341 | ||
A0A6P6LLA5 | A0A6P6LLA5_CARAU | LOC113059822 | 339 | ||
A0A6P6LI19 | A0A6P6LI19_CARAU | LOC113059822 | 310 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-48 | Basic and acidic residues | ||||
Sequence: MPKRAKKNEEAVEGETGNEPAKKEKKGKEPEAPILYEDPPDKTSSKDG |
Keywords
- Technical term