A0A0L8RMQ0 · A0A0L8RMQ0_SACEU

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Hydrolysis of proteins in presence of ATP.
    EC:3.4.21.53 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site, active site.

111421002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Binding site637-644ATP (UniProtKB | ChEBI)
Active site1024
Active site1067

GO annotations

AspectTerm
Cellular Componentmitochondrial matrix
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionsequence-specific DNA binding
Molecular Functionserine-type endopeptidase activity
Molecular Functionsingle-stranded DNA binding
Biological Processcellular response to oxidative stress
Biological Processchaperone-mediated protein complex assembly
Biological Processmitochondrion organization
Biological Processoxidation-dependent protein catabolic process
Biological Processprotein quality control for misfolded or incompletely synthesized proteins

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lon protease homolog, mitochondrial
  • EC number

Gene names

    • Name
      PIM1
    • ORF names
      DI49_0159

Organism names

  • Taxonomic identifier
  • Strain
    • FM1318
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces

Accessions

  • Primary accession
    A0A0L8RMQ0

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-19Mitochondrion
ChainPRO_502342550089-1142Lon protease homolog, mitochondrial

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.

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias102-135Basic and acidic residues
Region102-176Disordered
Compositional bias136-164Polar residues
Domain182-485Lon N-terminal
Compositional bias340-354Basic and acidic residues
Region340-371Disordered
Region849-896Disordered
Compositional bias859-896Basic and acidic residues
Domain932-1118Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,142
  • Mass (Da)
    127,910
  • Last updated
    2015-11-11 v1
  • Checksum
    1036445BB1EEAF22
MLRARTAKTLGTVARTTRAIQYYRSVVKAAALPQKRFASTLNVHDVANVKPNHIIKTPAWQEFQHQLKTSRYTEQLTQLEDQFARDTLAAYSYRSILAKDDSAKKDEDDKIVPEEKDKDNEVEPTRDDETTTNKSPESEVSKNSKSSASGSGQSSSSRSDTGDGNPKQKPPKPEVPEVYPQMLALPIARRPLFPGFYKAVVISDERVMKAIKEMLDRQQPYIGAFMLKNSEEDTDVITSKDEVYDVGVLAQITSAFPSKDEKTGTETMTALLYPHRRIKIDELFPPNEEKEKLKEQAKEKDVETVVTEAAEIKEDQAENANAGGAPKLEDIVVEKIPDSELQQQQQHKKIEASEEEPDELDDAQEGDDVNPTEFLKDYNVSLVNVLNLEDEPFDRKSPVINALTSEILKVFKEISQLNTMFREQIATFSASIQSATTNIFEEPARLADFAAAVSAGEEDELQDILSSLNIEHRLEKSLLVLKKELMNAELQNKISKDVETKIQKRQREYYLMEQLKGIKRELGIDDGRDKLIDTYKERVKSLKLPESVQKIFDDEITKLSTLETSMSEFGVIRNYLDWLTSIPWGKHSQEQYSIPRAKKILDEDHYGMIDVKDRILEFIAVGKLLGKVDGKIICFVGPPGVGKTSIGKSIARALNRKFFRFSVGGMTDVAEIKGHRRTYIGALPGRVVQALKKCQTQNPLILIDEIDKIGHGGIHGDPSAALLEVLDPEQNNSFLDNYLDIPIDLSKVLFVCTANSLETIPRPLLDRMEVIELTGYVAEDKVKIAEQYLVPSAKKSAGLENSHVDMTEDAITALMKYYCRESGVRNLKKHIEKIYRKAALQVVKKLSIEDSPTSSDTQKDTAKSKETASSEDKTSKNVESSSKMSKDIDSKKTSDDIEALKTSDKINVSISQDNLKDYVGPPVYTTDRLYETTPPGVVMGLAWTNMGGCSLYVESVLEQPLHNCKHPTFERTGQLGDVMKESSRLAYSFSKMYLAQKFPENRFFEKASIHLHCPEGATPKDGPSAGVTMASSFLSLALNKSIEPTVAMTGELTLTGKVLRIGGLREKAVAAKRSGAKTIIFPKDNLNDWEELPDNVKEGLEPLAADWYNDIFQKLFKDVDTKQGNSVWKAEFEILDAKKDKD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias102-135Basic and acidic residues
Compositional bias136-164Polar residues
Compositional bias340-354Basic and acidic residues
Compositional bias859-896Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JMCK01000002
EMBL· GenBank· DDBJ
KOH00824.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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