S8C4N0 · S8C4N0_DACHA

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

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.

111491002003004005006007008009001,0001,100
TypeIDPosition(s)Description
Binding site626-633ATP (UniProtKB | ChEBI)
Active site1007
Active site1050

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
      H072_3347

Organism names

Accessions

  • Primary accession
    S8C4N0

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.

TypeIDPosition(s)Description
Region1-67Disordered
Compositional bias16-67Polar residues
Region89-176Disordered
Compositional bias91-122Basic and acidic residues
Compositional bias123-171Polar residues
Domain184-473Lon N-terminal
Region289-353Disordered
Compositional bias296-313Polar residues
Compositional bias838-870Basic and acidic residues
Region838-874Disordered
Domain915-1101Lon proteolytic
Region1116-1135Disordered

Sequence similarities

Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,149
  • Mass (Da)
    126,094
  • Last updated
    2013-10-16 v1
  • Checksum
    A48FA2DA09FF0436
MLYGRAAGRALRQPRPSACQSASSLSTRLLRSSSRLYSTARRQPLGSNLSRRDASAPTFSNDASSIQPWSLYAPPFRLHSRTFTSSSIRLKEDASKPDEPVVNKEEPPKEEVEEELAEKKSGSGSKKTSSNDPKGTAGSSGASSSGSPPPSNPSDGSSSSNNNNSTKKPHLLSKPQVPEIYPQVMAIPIAKRPLFPGFYKAVTIRDPSVTAAIQEMLKRGQPYVGVFLFKDENMDADTISSADEVHDVGVFAQITSVFPVSGEEHSLTAVLYPHRRIKLSRLLPPKEKAPAAATITEVESKTTSTSGLEEDSTAAQIVTPPKDADGNPPEPKGDVVASFEETSSDIEPPKQASVASTPTFATAFLQKYNVSLVDVENLTELPHDRKSPVIKAVTSEIVSVFKDIANMNPLFRDQISTFQMSQSAGNVIEEPAKLADFAAAVASAEVKELQEVLETLDVESRLHKALVVLKKELMNAELQSKIAKDVEQKIQKRQREYWLMEQMKGIRRELGIESDGKDKLIEKFKEKGNKLAMPEAVKKVFDEELNKLTHLEAVASEFNVTRNYLDWLTQIPWGQRSAENYSIKNAMKVLDEDHHGLKDVKDRILEFIAVGKLRGGVEGKILCFVGPPGVGKTSIGKSIARAVQREFYRFSVGGLTDVAEIKGHRRTYVGALPGRIIQALKKCQTENPLILIDEVDKIGRGHQGDPASALLELLDPEQNNAFLDHYMDVPVDLSKVLFVCTANMSDTIPRPLLDRMEMIELSGYVADEKMAIAERYLAPQAKTLSGLEKVDVDLTKEAIEELIKSYCRESGVRNLKKHIEKVYRKAALKIVQNIGEEEELSEEKALTEEGKEAQKETTEKAEEIADPKSDAKPTTAEVPRAALEVPDSVHVSINKENLKDYVGPPVYTSDRLYETTPPGVTMGLAWTQLGGSALYVESILESALDSESRPGLERTGNLQNVMKESTAIAYSFAKSFMVKKFPENKFLEKARVHLHCPEGAVPKDGPSAGVTMATSLLSLALDVPVSPTVAMTGELTVTGKVLRIGGLREKTVAAKRSGASTVIFPSDNMSDWLELPENIKEGIEGRPVSWYADVFDIVFPGIDPVRANGLWREQLKKKSKGSGEERESLEVDMDESDVNESKIIGSRFV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias16-67Polar residues
Compositional bias91-122Basic and acidic residues
Compositional bias123-171Polar residues
Compositional bias296-313Polar residues
Compositional bias838-870Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AQGS01000104
EMBL· GenBank· DDBJ
EPS42672.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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