The domain within your query sequence starts at position 12 and ends at position 220; the E-value for the LON_substr_bdg domain shown below is 1e-24.

RLPLLLTHESVLLPGSTMRTSVDTARNLQLVRSRLLKGTSLQSTILGVIPNTPDPASDTQ
DLPPLHRIGTAALAVQVVGSNWPKPHYTLLITGLCRFQIVQVLKEKPYPVAEVEQLDRLE
EFPNICKSREELGELSEQFYRYAVQLVEMLDMSVPAVAKLRRLLDNLPREALPDILTSII
RTSNKEKLQILDAVSLEDRFKMTIPLLVR

LON_substr_bdg

LON_substr_bdg
PFAM accession number:PF02190
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