A0A0L0T4E5 · A0A0L0T4E5_ALLM3

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.

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.

1914100200300400500600700800900
TypeIDPosition(s)Description
Binding site447-454ATP (UniProtKB | ChEBI)
Active site778
Active site821

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
      AMAG_20018

Organism names

Accessions

  • Primary accession
    A0A0L0T4E5

Proteomes

Organism-specific databases

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 domain, region, compositional bias.

TypeIDPosition(s)Description
Domain22-294Lon N-terminal
Region124-185Disordered
Compositional bias126-153Polar residues
Domain685-872Lon proteolytic
Region738-780Disordered
Compositional bias763-777Pro residues

Sequence similarities

Belongs to the peptidase S16 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    914
  • Mass (Da)
    99,018
  • Last updated
    2015-11-11 v1
  • Checksum
    84BD12726D749E88
MATRATRAICRRLPRQTRTRRCFALPITRRPLFPGFYKTVVIKDPEVIRAIKDLAESRQPYVAAVLLKDEEADTDRIQSLDEIHQVGVFSQITNVYHTSPTGPGDDAPSLTAILYPHRRVRISGLVNDSDSPSTTAAATTAAPVSTTESDAVTKPATAPDAAVAADADKPETASEPTGSPQSYLRSKYNVSVVHAETLHDEPYKKGNQLVRAITAEIVNVFKDIASLNPLFREQISAFSVSQASTTIFDDPSKLADFAAAVSGGSDSEELQGVLESLVIEERLQKALYVLKKELVNAQLQSKISKEVESKIQKRQREYYLMEQLKGIKKELGMESDGKDKLLEKFKERIQYATLPATVATVIEEEMQKLGHLDPASSEFNVTRNYLDWLTCLPWGKYSQEVLDVEHAQQCLDEDHYGLKDVKERILEFIAVGKLKGTVEGKIMCLSGPPVVGKTSIGKSIARALGREFYRFSVGGLSDVAEIKGHRRTYVGAMPGKLVQALKKVQTENPLVLIDEIDKLGRGLQGDPASALLELLDPEQNSSFLDHYLDVPLDLSKVLFVCTANVLDTIPGPLLDRMEVIQLSGYVADEKVAIAEKYLAPQARIASDTKCSMQQQLDRAIEDLIRYYCRESGVRNLKKHIEKIYRKAAFKVVSAGANAEPLQITPANLKDYVGNPPFSGERLFEHPPAGVVMGLAWTAMGGSSLYIESVLEAPLTTESKPALTKTGQLGDVMKESSMLPVNGSRAEGAGQCASDRPETVPKSTHTESPPPPAPPDGPSAGITMATSLISLAANTPIPPHIAMTGELTLSGKVLKIGGLKEKTIAAKRSGITTILFPAANTADWAELPDFVKDGIEGRPVEWYSEVFDACFGEAVARGEFAKNAWPIVSAATATAVLADMPGTAAGSPPASIGGA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias126-153Polar residues
Compositional bias763-777Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GG745361
EMBL· GenBank· DDBJ
KNE69688.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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