A0A0L8RMQ0 · A0A0L8RMQ0_SACEU
- ProteinLon protease homolog, mitochondrial
- GenePIM1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1142 (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
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionA0A0L8RMQ0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-19 | Mitochondrion | ||||
Sequence: MLRARTAKTLGTVARTTRA | ||||||
Chain | PRO_5023425500 | 89-1142 | Lon protease homolog, mitochondrial | |||
Sequence: AAYSYRSILAKDDSAKKDEDDKIVPEEKDKDNEVEPTRDDETTTNKSPESEVSKNSKSSASGSGQSSSSRSDTGDGNPKQKPPKPEVPEVYPQMLALPIARRPLFPGFYKAVVISDERVMKAIKEMLDRQQPYIGAFMLKNSEEDTDVITSKDEVYDVGVLAQITSAFPSKDEKTGTETMTALLYPHRRIKIDELFPPNEEKEKLKEQAKEKDVETVVTEAAEIKEDQAENANAGGAPKLEDIVVEKIPDSELQQQQQHKKIEASEEEPDELDDAQEGDDVNPTEFLKDYNVSLVNVLNLEDEPFDRKSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEDELQDILSSLNIEHRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQREYYLMEQLKGIKRELGIDDGRDKLIDTYKERVKSLKLPESVQKIFDDEITKLSTLETSMSEFGVIRNYLDWLTSIPWGKHSQEQYSIPRAKKILDEDHYGMIDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSIARALNRKFFRFSVGGMTDVAEIKGHRRTYIGALPGRVVQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEDKVKIAEQYLVPSAKKSAGLENSHVDMTEDAITALMKYYCRESGVRNLKKHIEKIYRKAALQVVKKLSIEDSPTSSDTQKDTAKSKETASSEDKTSKNVESSSKMSKDIDSKKTSDDIEALKTSDKINVSISQDNLKDYVGPPVYTTDRLYETTPPGVVMGLAWTNMGGCSLYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFSKMYLAQKFPENRFFEKASIHLHCPEGATPKDGPSAGVTMASSFLSLALNKSIEPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGLEPLAADWYNDIFQKLFKDVDTKQGNSVWKAEFEILDAKKDKD |
Interaction
Subunit
Homoheptamer. Organized in a ring with a central cavity. Oligomerization is independent of its proteolytic activity and the autocatalytic maturation of its subunits.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 102-135 | Basic and acidic residues | ||||
Sequence: SAKKDEDDKIVPEEKDKDNEVEPTRDDETTTNKS | ||||||
Region | 102-176 | Disordered | ||||
Sequence: SAKKDEDDKIVPEEKDKDNEVEPTRDDETTTNKSPESEVSKNSKSSASGSGQSSSSRSDTGDGNPKQKPPKPEVP | ||||||
Compositional bias | 136-164 | Polar residues | ||||
Sequence: PESEVSKNSKSSASGSGQSSSSRSDTGDG | ||||||
Domain | 182-485 | Lon N-terminal | ||||
Sequence: MLALPIARRPLFPGFYKAVVISDERVMKAIKEMLDRQQPYIGAFMLKNSEEDTDVITSKDEVYDVGVLAQITSAFPSKDEKTGTETMTALLYPHRRIKIDELFPPNEEKEKLKEQAKEKDVETVVTEAAEIKEDQAENANAGGAPKLEDIVVEKIPDSELQQQQQHKKIEASEEEPDELDDAQEGDDVNPTEFLKDYNVSLVNVLNLEDEPFDRKSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEDELQDILSSLNIEHRLEKSLLVLKKEL | ||||||
Compositional bias | 340-354 | Basic and acidic residues | ||||
Sequence: ELQQQQQHKKIEASE | ||||||
Region | 340-371 | Disordered | ||||
Sequence: ELQQQQQHKKIEASEEEPDELDDAQEGDDVNP | ||||||
Region | 849-896 | Disordered | ||||
Sequence: EDSPTSSDTQKDTAKSKETASSEDKTSKNVESSSKMSKDIDSKKTSDD | ||||||
Compositional bias | 859-896 | Basic and acidic residues | ||||
Sequence: KDTAKSKETASSEDKTSKNVESSSKMSKDIDSKKTSDD | ||||||
Domain | 932-1118 | Lon proteolytic | ||||
Sequence: TTPPGVVMGLAWTNMGGCSLYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFSKMYLAQKFPENRFFEKASIHLHCPEGATPKDGPSAGVTMASSFLSLALNKSIEPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGLEPLAADWYNDIFQKLFKD |
Sequence similarities
Belongs to the peptidase S16 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,142
- Mass (Da)127,910
- Last updated2015-11-11 v1
- Checksum1036445BB1EEAF22
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 102-135 | Basic and acidic residues | ||||
Sequence: SAKKDEDDKIVPEEKDKDNEVEPTRDDETTTNKS | ||||||
Compositional bias | 136-164 | Polar residues | ||||
Sequence: PESEVSKNSKSSASGSGQSSSSRSDTGDG | ||||||
Compositional bias | 340-354 | Basic and acidic residues | ||||
Sequence: ELQQQQQHKKIEASE | ||||||
Compositional bias | 859-896 | Basic and acidic residues | ||||
Sequence: KDTAKSKETASSEDKTSKNVESSSKMSKDIDSKKTSDD |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JMCK01000002 EMBL· GenBank· DDBJ | KOH00824.1 EMBL· GenBank· DDBJ | Genomic DNA |