The domain within your query sequence starts at position 18 and ends at position 46; the E-value for the A1_Propeptide domain shown below is 1.5e-18.
LIRVPLKKMKSIRETMKEQGVLKDFLKNH
A1_Propeptide |
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PFAM accession number: | PF07966 |
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Interpro abstract (IPR012848): | This entry represents the N-terminal domain of the aspartic peptidases. Aspartic peptidase, also known as aspartyl proteases ([intenz:3.4.23.-]) are a widely distributed family of proteolytic enzymes [ (PUBMED:6795036) (PUBMED:2194475) (PUBMED:1851433) ] known to exist in vertebrates, fungi, plants, retroviruses and some plant viruses. Aspartate proteases of eukaryotes are monomeric enzymes which consist of two domains. Each domain contains an active site centred on a catalytic aspartyl residue. The two domains most probably evolved from the duplication of an ancestral gene encoding a primordial domain. Currently known eukaryotic aspartyl proteases are:
Most retroviruses and some plant viruses, such as badnaviruses, encode for an aspartyl protease which is an homodimer of a chain of about 95 to 125 amino acids. In most retroviruses, the protease is encoded as a segment of a polyprotein which is cleaved during the maturation process of the virus. It is generally part of the pol polyprotein and, more rarely, of the gag polyprotein. |
GO process: | proteolysis (GO:0006508) |
GO function: | aspartic-type endopeptidase activity (GO:0004190) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry A1_Propeptide