The domain within your query sequence starts at position 301 and ends at position 498; the E-value for the LON_substr_bdg domain shown below is 2.6e-27.
DVPIFVCAMAFPTVPCPLHVFEPRYRLMIRRCMETGTKRFGMCLSAENAGISEYGCMLEI KDVRTFPDGSSVVDAIGISRFRVLSHRHRDGYNTADIEYLEDEKVEGPEFEELTALHESV YQQSVSWFASLQDHMKKQILSHFGSMPDREPEPQSNSSGPAWSWWILAVLPLERKAQLAI LGMASLKERLLAIRRILV
LON_substr_bdg |
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PFAM accession number: | PF02190 |
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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. |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry LON_substr_bdg