A0A0L0T4E5 · A0A0L0T4E5_ALLM3
- ProteinLon protease homolog, mitochondrial
- GenePIM1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids914 (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.
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
- Strain
- Taxonomic lineageEukaryota > Fungi > Fungi incertae sedis > Blastocladiomycota > Blastocladiomycetes > Blastocladiales > Blastocladiaceae > Allomyces
Accessions
- Primary accessionA0A0L0T4E5
Proteomes
Organism-specific databases
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 domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-294 | Lon N-terminal | ||||
Sequence: CFALPITRRPLFPGFYKTVVIKDPEVIRAIKDLAESRQPYVAAVLLKDEEADTDRIQSLDEIHQVGVFSQITNVYHTSPTGPGDDAPSLTAILYPHRRVRISGLVNDSDSPSTTAAATTAAPVSTTESDAVTKPATAPDAAVAADADKPETASEPTGSPQSYLRSKYNVSVVHAETLHDEPYKKGNQLVRAITAEIVNVFKDIASLNPLFREQISAFSVSQASTTIFDDPSKLADFAAAVSGGSDSEELQGVLESLVIEERLQKALYVLKKEL | ||||||
Region | 124-185 | Disordered | ||||
Sequence: GLVNDSDSPSTTAAATTAAPVSTTESDAVTKPATAPDAAVAADADKPETASEPTGSPQSYLR | ||||||
Compositional bias | 126-153 | Polar residues | ||||
Sequence: VNDSDSPSTTAAATTAAPVSTTESDAVT | ||||||
Domain | 685-872 | Lon proteolytic | ||||
Sequence: HPPAGVVMGLAWTAMGGSSLYIESVLEAPLTTESKPALTKTGQLGDVMKESSMLPVNGSRAEGAGQCASDRPETVPKSTHTESPPPPAPPDGPSAGITMATSLISLAANTPIPPHIAMTGELTLSGKVLKIGGLKEKTIAAKRSGITTILFPAANTADWAELPDFVKDGIEGRPVEWYSEVFDACFGE | ||||||
Region | 738-780 | Disordered | ||||
Sequence: LPVNGSRAEGAGQCASDRPETVPKSTHTESPPPPAPPDGPSAG | ||||||
Compositional bias | 763-777 | Pro residues | ||||
Sequence: THTESPPPPAPPDGP |
Sequence similarities
Belongs to the peptidase S16 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length914
- Mass (Da)99,018
- Last updated2015-11-11 v1
- Checksum84BD12726D749E88
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 126-153 | Polar residues | ||||
Sequence: VNDSDSPSTTAAATTAAPVSTTESDAVT | ||||||
Compositional bias | 763-777 | Pro residues | ||||
Sequence: THTESPPPPAPPDGP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
GG745361 EMBL· GenBank· DDBJ | KNE69688.1 EMBL· GenBank· DDBJ | Genomic DNA |