The domain within your query sequence starts at position 486 and ends at position 695; the E-value for the Lon_C domain shown below is 1.5e-83.



PFAM accession number:PF05362
Interpro abstract (IPR008269):

Lon (also known as endopeptidase La) is a multi-domain ATP- dependent protease found throughout all kingdoms of life. It is involved in protein quality control and several regulatory processes. All Lon proteases contain an ATPase domain belonging to the AAA+ superfamily of molecular machines, and a proteolytic domain with a serine-lysine catalytic dyad in which a lysine assists the catalytic serine in proteolytic cleavage. Lon proteases can be divided into two subfamilies: A type (A-Lons), which have a large multi-lobed N-terminal domain together with the ATPase and protease domains, and B type (B-Lons), which lack an N domain, but have a membrane-anchoring region emerging from the ATPase domain. B-Lons are found in Archaea, in which they are the lone membrane-anchored ATP-dependent protease. The soluble A-Lons are found in all bacteria and in eukaryotic cell organelles, such as mitochondria and peroxisomes, and are needed for recovery from various stress conditions [(PUBMED:14665623), (PUBMED:15456757), (PUBMED:16002085), (PUBMED:20834233), (PUBMED:20222013), (PUBMED:24520911)]. The Lon proteolytic domain forms peptidase family S16 of clan SJ [(PUBMED:16002085)].

The structure of the Lon proteolytic domain consists of six alpha helices and ten beta strands [(PUBMED:14665623), (PUBMED:15456757), (PUBMED:16002085), (PUBMED:20834233), (PUBMED:20222013)].

GO process:proteolysis (GO:0006508)
GO function:serine-type endopeptidase activity (GO:0004252), ATP-dependent peptidase activity (GO:0004176)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Lon_C