A0A7J6D6H2 · A0A7J6D6H2_9TELE
- Proteinexodeoxyribonuclease III
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids341 (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 | 92 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 120 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 195 | |||||
Sequence: Y | ||||||
Active site | 234 | Proton donor/acceptor | ||||
Sequence: D | ||||||
Binding site | 234 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Site | 236 | Transition state stabilizer | ||||
Sequence: N | ||||||
Site | 306 | Important for catalytic activity | ||||
Sequence: D | ||||||
Binding site | 331 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 332 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 332 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 332 | 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 | 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 > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Cyprinidae > Acrossocheilinae > Onychostoma
Accessions
- Primary accessionA0A7J6D6H2
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-17 | |||||
Sequence: MHFVLSSSRILCVRVCA | ||||||
Chain | PRO_5029646966 | 18-341 | exodeoxyribonuclease III | |||
Sequence: VSFLRVCGLKTTVSMPKRAKKNEEAVDGETGNGAEPAKKEKKGKEPEAPILYEDPQDKMTSKDGRASNMKITSWNVDGLRAWVKKKGLDWVRKEDPDVLCLQETKCAEKALPSEITDMPEYPHKFWAGSEDKEGYSGVAMLCKNEPLNVTYGIGKEEHDKEGRVITAEFPSFFLVTAYVPNASRGLVRLDYRKTWDVDFQAYLSGLDQRKPLVLCGDLNVAHQEIDLKNPKGNRKNAGFTPEEREGFTKLLEAGFTDSFRELYPEQANAYTFWTYMMNSRAKNVGWRLDYFLLSSALLPGLCDSKIRNTAMGSDHCPITLYLAV |
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 34-81 | Basic and acidic residues | ||||
Sequence: KRAKKNEEAVDGETGNGAEPAKKEKKGKEPEAPILYEDPQDKMTSKDG | ||||||
Region | 34-83 | Disordered | ||||
Sequence: KRAKKNEEAVDGETGNGAEPAKKEKKGKEPEAPILYEDPQDKMTSKDGRA | ||||||
Domain | 90-332 | Endonuclease/exonuclease/phosphatase | ||||
Sequence: SWNVDGLRAWVKKKGLDWVRKEDPDVLCLQETKCAEKALPSEITDMPEYPHKFWAGSEDKEGYSGVAMLCKNEPLNVTYGIGKEEHDKEGRVITAEFPSFFLVTAYVPNASRGLVRLDYRKTWDVDFQAYLSGLDQRKPLVLCGDLNVAHQEIDLKNPKGNRKNAGFTPEEREGFTKLLEAGFTDSFRELYPEQANAYTFWTYMMNSRAKNVGWRLDYFLLSSALLPGLCDSKIRNTAMGSDH |
Sequence similarities
Belongs to the DNA repair enzymes AP/ExoA family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length341
- Mass (Da)38,432
- Last updated2021-04-07 v1
- ChecksumD2A76870E7335361
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 34-81 | Basic and acidic residues | ||||
Sequence: KRAKKNEEAVDGETGNGAEPAKKEKKGKEPEAPILYEDPQDKMTSKDG |
Keywords
- Technical term