A0A0F7S9R7 · A0A0F7S9R7_9BASI
- ProteinLon protease homolog, mitochondrial
- GeneSSCI49150.1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1208 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner.
Catalytic activity
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 640-647 | ATP (UniProtKB | ChEBI) | |||
Active site | 1073 | ||||
Active site | 1116 | ||||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent peptidase activity | |
Molecular Function | sequence-specific DNA binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | single-stranded DNA binding | |
Biological Process | cellular response to oxidative stress | |
Biological Process | chaperone-mediated protein complex assembly | |
Biological Process | mitochondrion organization | |
Biological Process | oxidation-dependent protein catabolic process | |
Biological Process | protein quality control for misfolded or incompletely synthesized proteins |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLon protease homolog, mitochondrial
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Sporisorium
Accessions
- Primary accessionA0A0F7S9R7
Proteomes
Subcellular Location
Interaction
Subunit
Homohexamer or homoheptamer. Organized in a ring with a central cavity.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-21 | Disordered | |||
Compositional bias | 96-123 | Basic and acidic residues | |||
Region | 96-148 | Disordered | |||
Compositional bias | 124-144 | Polar residues | |||
Domain | 155-487 | Lon N-terminal | |||
Region | 232-256 | Disordered | |||
Compositional bias | 241-256 | Basic and acidic residues | |||
Region | 273-296 | Disordered | |||
Region | 335-372 | Disordered | |||
Region | 854-947 | Disordered | |||
Compositional bias | 875-889 | Polar residues | |||
Compositional bias | 897-922 | Polar residues | |||
Domain | 981-1168 | Lon proteolytic | |||
Region | 1179-1208 | Disordered | |||
Sequence similarities
Belongs to the peptidase S16 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,208
- Mass (Da)129,923
- Last updated2015-07-22 v1
- Checksum8576E07F4AE6A3A7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 96-123 | Basic and acidic residues | |||
Compositional bias | 124-144 | Polar residues | |||
Compositional bias | 241-256 | Basic and acidic residues | |||
Compositional bias | 875-889 | Polar residues | |||
Compositional bias | 897-922 | Polar residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CCFA01002904 EMBL· GenBank· DDBJ | CDW98179.1 EMBL· GenBank· DDBJ | Genomic DNA |