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W6QMY0 · W6QMY0_PENRF

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

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

Features

Showing features for binding site, active site.

111161002003004005006007008009001,0001,100
Type
IDPosition(s)Description
Binding site614-621ATP (UniProtKB | ChEBI)
Active site995
Active site1038

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
    • Synonyms
      PIM1
    • ORF names
      PROQFM164_S06g000262

Organism names

  • Taxonomic identifier
  • Strain
    • FM164
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    W6QMY0

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer or homoheptamer. Organized in a ring with a central cavity.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region48-193Disordered
Compositional bias58-72Basic and acidic residues
Compositional bias82-105Basic and acidic residues
Compositional bias112-141Basic and acidic residues
Domain203-461Lon N-terminal
Region302-327Disordered
Region835-864Disordered
Compositional bias839-854Basic and acidic residues
Domain903-1089Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,116
  • Mass (Da)
    123,039
  • Last updated
    2014-04-16 v1
  • MD5 Checksum
    DC07F21BD6A0BF90E6107CA58845755F
MLRGQTLPWRAVLHQTPRPLLRRPFLASPRYNATFRSTLISARFGASLPSSSRAFSASSIRRREKPPPEDPKEESEEKEEDETSHDDKGTERAPEPRKKGADSGKHVPSADQVAPARRKDRSSDKERGVEEEVKKEANASDSKGNSNDTPSPIPPSDGPADSKPSGASSGGHGGNDDSGKKGKKASGEKALQKPAVPDVYPQVMAIPIAKRPLFPGFYKAITIRDPNVAAAIQDMMKRGQPYVGAFLFKDDNADGDVIEKLDDVYDTGVFAQITAAYPLRGESSGVTAVLYPHRRIKISSLLPPGEHTKAATPPPAPTSEDKTTEKRGDVVASFEEGAPEPTPKDHYEPTSFLKKYPVSLVNVENLTEEPFDKKNPIIRAVTSEIVNVCKEIATLNPLFRDQISAFYTDQFPGNLSDEPAKLADFAAAVSAGELHEMQEVLETMNIEERLPKALVVLKKELMNAQLQSKITKDVEAKIQKRQREYWLMEQMKGIKRELGIESDGKDKLVEKFKEKAEKLAMPEVVKKVFDEEINKLAHLEPAASEFNVTRNYLDWLTQIPWGQKSVENFGVKNAVSVLDEDHYGLKDVKDRILEFIAVGKLRGTVEGKILCLVGPPGVGKTSIGKSIARALNRQYYRFSVGGLTDVAEIKGHRRTYVGALPGRIIQALKKCQTENPLILIDEVDKIGRGHQGDPSSALLELLDPEQNNSFLDHYMDVPVDLSKVLFVCTANVTDTIPRPLLDRMELIELSGYVADEKMAIAEKYLAPAARELTGLKDVDVNLERDAIEELIKSYCRESGVRNLKKQIEKVYRKAAFKIVQDLGEDVLPEEAALTEAGKAAQEESKEHEPADPAQVPVEPEKSTTEIPRLALKVPDTVHLSIGKGTLKDYVGPPVFTSDRLYDQFPPGVTMGLAWTSMGGAALYVECILENALNHNSRPGLEITGNLQNVMKESTHIAYSFAKSVMARQFPENRFFEKAKVHLHCPEGAVPKDGPSAGITMASALLSLALNHSLEPTVAMTGELTVTGKVLRIGGLREKTVAARRAGATKVLFPADNTSDWLELPENIKEGIEGHPVNWYSEVFDLLFPTLDQEAARTVWQKALAKPKKESHEVEEE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias58-72Basic and acidic residues
Compositional bias82-105Basic and acidic residues
Compositional bias112-141Basic and acidic residues
Compositional bias839-854Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HG792020
EMBL· GenBank· DDBJ
CDM37301.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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