Author: Rawlings, Neil D.
Title: A large and accurate collection of peptidase cleavages in the MEROPS database Document date: 2009_11_2
ID: 0rq0wdpq_39
Snippet: Cytochrome C Where it is possible to suggest a cause why a cleavage site is not conserved this is indicated in Table 4 by the letters a-h. Included in category d, where insertions and or deletions occur in the homologous cleavage sites, is 50S ribosomal protein L7Ae (UniProt accession P12743). There are N-terminal extensions to most homologues so that the known methionyl aminopeptidase 2-cleavage site is not aligned. Five of these sequences may b.....
Document: Cytochrome C Where it is possible to suggest a cause why a cleavage site is not conserved this is indicated in Table 4 by the letters a-h. Included in category d, where insertions and or deletions occur in the homologous cleavage sites, is 50S ribosomal protein L7Ae (UniProt accession P12743). There are N-terminal extensions to most homologues so that the known methionyl aminopeptidase 2-cleavage site is not aligned. Five of these sequences may be derived from erroneous gene builds (point b). The UniRef50 database entry for 60S ribosomal protein L10 (P27635) includes a wide range of species (the cleavage is known in the human protein) and the peptidase performing the cleavage (granzyme B) is not present in Paracoccidiodes brasiliensis, where the substrate cleavage is also not conserved. The replacements that are reported as atypical in hemoglobin subunit alpha (P69905) by Schistosoma cathepsin D (A01.009) (34) are the rarest naturally occurring amino acids, tryptophan and cysteine, and despite there being 109 known cleavages for this peptidase, this may still not be enough to properly exclude these rare amino acids. On the other hand, this is the cleavage of a host protein by a parasite peptidase and the specificity may have adapted to limit the availability of hosts.
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