LONFound in ATP-dependent protease La (LON) |
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SMART accession number: | SM00464 |
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Description: | N-terminal domain of the ATP-dependent protease La (LON), present also in other bacterial ORFs. |
Interpro abstract (IPR003111): | This signature defines the N-terminal substrate-binding domain of the archael, bacterial and eukaryotic lon proteases, which are ATP-dependent serine peptidases belonging to the MEROPS peptidase family S16 (lon protease family, clan SF). In the eukaryotes the majority of the proteins are located in the mitochondrial matrix [(PUBMED:8248235), (PUBMED:9620272)]. In yeast, Pim1, is located in the mitochondrial matrix, is required for mitochondrial function, is constitutively expressed but is increased after thermal stress, suggesting that Pim1 may play a role in the heat shock response [(PUBMED:8276800)]. This structure of this domain has been determined [(PUBMED:16199667), (PUBMED:19191354), (PUBMED:20834233)]. This domain also occurs in proteins which lack the peptidase domain, such as the SPBC14F5.10c gene product from Schizosaccharomyces pombe; these proteins are uncharacterized. |
Family alignment: |
There are 17617 LON domains in 17613 proteins in SMART's nrdb database.
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- Evolution (species in which this domain is found)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)