A0A346DKW0 · A0A346DKW0_VACCO

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.

1993100200300400500600700800900
TypeIDPosition(s)Description
Binding site471-478ATP (UniProtKB | ChEBI)
Active site893
Active site936

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
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

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > Ericales > Ericaceae > Vaccinioideae > Vaccinieae > Vaccinium

Accessions

  • Primary accession
    A0A346DKW0

Subcellular Location

Keywords

Interaction

Subunit

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

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain105-316Lon N-terminal
Domain803-987Lon proteolytic

Sequence similarities

Belongs to the peptidase S16 family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    993
  • Mass (Da)
    109,510
  • Last updated
    2018-11-07 v1
  • Checksum
    D48EBD17741FCEF9
MLKALSSSCLRGRFQATPSALPSNLRRHGTQLESPWSRVLGSLRGRKNPSLCQRLFFCSDSTDGSETVEAAAEAKRVEVEGEEADSKTSSAIVPTVARPEDYLTVLALPLPHRPLFPGFYMPIYVKDPKLLAALVESRKRQAPYAGAFLLKDEPGTDPSAASGSDADKNIYELKGKELFNRLNEVGTLAQITSIQGDQVVLIGHRRLRITELVSEDPLTVKVDHLKDKPYDKDDDVVKATSFEVISTLRDVLKTSSLWRDHVQTYTQHIGDFNYSRLADFGAAISGANKSQCQQVLEELDVYKRLKLTLELVKKEMEISKIQESIAKAIEEKISGEQRRYLLNEQLKAIKKELGLEADDKTALSAKFRERIEPNKDKCPPHVLQVIEEELTKLQLLEASSSEFNVTRNYLDWLTALPWGNYSDENFDVLRAQKILDEDHYGLTDVKERILEFIAVGKLRGTSQGKIICLSGPPGVGKTSIGRSIARALNRKFYRFSVGGLSDVAEIKGHRRTYIGAMPGKMVQCLKNVGTANPLVLIDEIDKLGRGHAGDPASAMLELLDPEQNANFLDHYLDVPIDLSKVLFVCTANVVEMIPNPLLDRMEVVSIAGYITDEKMHIARDYLEKTTREACGIKPEQVEVTDAALLALIESYCREAGVRNLQKQIEKIYRKIALQLVRKGALTEHPTAGDHVVVLDEAKIESVTDLGETEVGGETQVVADPADCSSNEMASDTTVEVDPMQKDLPVDQSQPVTDQHTDLQVSIESHEKKETDAGKAVEKVLIDASNLSDFVGKPVFHAERIYDQTPAGVVMGLAWTAMGGSTLYIETTLVEQSEGKGALHVTGQLGDVMKESTQIAHTVARAILLEKDPENTFFANSKLHLHVPAGATPKDGPSAGCTMITSLLSLALKKPVKKDIAMTGEVTLTGKILPIGGVKEKTIAARRSDVKTIIFPSANRRDFDELAPNVKDGLEVHFVDDYNQIFDVAFADEQHTEN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MF972079
EMBL· GenBank· DDBJ
AXM90738.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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