The domain within your query sequence starts at position 232 and ends at position 302; the E-value for the Peptidase_M54 domain shown below is 2e-16.
DYSIFDNYYIPEITSVLLLRSCKTLTHEIGHILGLRHCQWLACLMQGSNHLEESDRRPLN VCPICLRKLQS
Peptidase_M54 |
 |
|---|
| PFAM accession number: | PF07998 |
|---|---|
| Interpro abstract (IPR012962): | Peptidase family M54 (archaemetzincin or archaelysin) is a zinc-dependent aminopeptidase that contains the consensus zinc-binding sequence HEXXHXXGXXH/D and a conserved Met residue at the active site, and is thus classified as a metzincin. Archaemetzincins, first identified in archaea, are also found in bacteria and eukaryotes, including two human members, archaemetzincin-1 and -2 (AMZ1 and AMZ2). AMZ1 is mainly found in the liver and heart while AMZ2 is primarily expressed in testis and heart; both have been reported to be aminopeptidases, degrading synthetic substrates and peptides. The peptidase M54 family contains an extended metzincin concensus sequence of HEXXHXXGX3CX4CXMX17CXXC such that a second zinc ion is bound to four cysteines, thus resembling a zinc finger. Phylogenetic analysis of this family reveals a complex evolutionary process involving a series of lateral gene transfer, gene loss and genetic duplication events [ (PUBMED:15972818) (PUBMED:20597090) (PUBMED:20561058) ]. Archaemetzincin (from Mycococcus xanthus) seem to have evolved into a zinc-binding transcription factor fulfilling only a structural role [ (PUBMED:15972818) (PUBMED:20597090) (PUBMED:16879646) ]. The structure of archaemetzincin from Methanopyrus kandleri has been resolved [ (PUBMED:20597090) ]. |
| GO process: | proteolysis (GO:0006508) |
| GO function: | peptidase activity (GO:0008233) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M54