G2XFZ8 · G2XFZ8_VERDV

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.

111101002003004005006007008009001,0001,100
Type
IDPosition(s)Description
Binding site618-625ATP (UniProtKB | ChEBI)
Active site994
Active site1037

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 Processmitochondrial protein catabolic process
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
      VDAG_08977

Organism names

Accessions

  • Primary accession
    G2XFZ8

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
Region69-176Disordered
Compositional bias74-115Basic and acidic residues
Domain186-465Lon N-terminal
Region834-868Disordered
Compositional bias835-861Basic and acidic residues
Domain902-1088Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,110
  • Mass (Da)
    120,940
  • Last updated
    2011-11-16 v1
  • MD5 Checksum
    61805B9AF009D80C6F6F726A198200F2
MVLRTTLPRRLTLVPQNAARRLRTQPARRLWTTNPAWQSSAAAPAVVSQSRRVPTSCSSNARPHTLAAFSTSSRALKEDKDKDQGFFDRSVESLSEDEKKANLENQRDLEDELAEASKGPASGSAADAAAKSEGAADGKAGSAAGGSSGSSGDGSGSGSGDGGRRGRKSAERSLQKPVVPDVYPQVLAIPIAKRPLFPGFYKAITIKDPNVAAAITEMIKRGQPYVGAFLFKDENADEDVIRNPDDVYDTGVFAQITSAFPMHGEQGSLTAILYPHRRIRLSSLLPPNAKEGDAATKVNEAKVDPVAATPEPIPQKPVEDDVQTDKKGDVVASFEESAVSPAKPDAVAEKYEPTAFLKRYDVSLVNVENLTEEPYDPKSAVIRAVTNEIVNVFKEVATMNSLFRDQISTFSMSQSTGNVTSEPAKLADFAAAVSSGEQGELQEVLSSLNVEERMQKALIVLKKELMNAQLQSKITKDVESKITKRQREYWLMEQMKGIRRELGLESDGKDKLVEKFKEKADKLAMPDAVRKVFDDEINKLAHLEPAASEFNVTRNYLDWLTQIPWGQRSAENFGIKNAMSVLDEDHYGLKDVKDRILEFIAVGKLRGTVEGKILCFVGPPGVGKTSIGKSIARALNRQYYRFSVGGLTDVAEIKGHRRTYVGALPGRIIQALKKCQTENPLILIDEIDKIGRGYQGDPSSALLELLDPEQNSSFLDHYMDVPVDLSKVLFVCTANMTDTIPRPLLDRMELIQLSGYVADEKMAIAERYLAPAAKEAAGLQNADVTLSEEAIEELIKSYARESGVRNLKKQIEKVYRKSALKIVQDVGEEVLPESEALTSDGKEALEASEKKAEEAADADPVTTEKPRVPLNVPESVHVTINKANLTDYVGPPVFTSDRLYEVNPAGVAMGLAWTQMGGAAMYIESILQSALKPSSRPSFEVTGNLQSVMKESSTIAYSFAKSLMARDFPGNNFFDKAKLHLHVPDGAVSKDGPSAGITMATSLLSLALEAKVDPTVAMTGELTLTGKVLRIGGLREKTVAARRAGCKMIIFPKDNMSDWLELPENIKNGIEGKPVGWYSDVFNLIFPDVDLEKANTSKVADEEKPADKSN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias74-115Basic and acidic residues
Compositional bias835-861Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DS572718
EMBL· GenBank· DDBJ
EGY18817.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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