3.4.22.44	amyloid-beta + H2O	-	
3.4.22.44	additional information	interaction between purified recombinant NIa-Pro and VPg domains, overview	
3.4.22.44	additional information	the enzyme interacts with proteins EIF3G, FBPA1, FK506BP, GTPBP, MSRB1, and MTL	
3.4.22.44	nuclear inclusion protein a + H2O	-	
3.4.22.44	nuclear inclusion protein a + H2O	identification of cleavage site	
3.4.22.44	nuclear inclusion protein a + H2O	analysis of cleavage sites, specific for its own polypeptide chain, no cleavage of other potyvirus NIa proteins	
3.4.22.44	nuclear inclusion protein a + H2O	the nuclear inclusion protein of potyviruses has two domains, the Vpg domain of 22 kDa and the C-terminal domain of 27 kDa which has proteolytic activity. The first cleavage at Ser223-Gly224 produces a 25 kDa protein. TuMV cleaves itself in cis, removing a 20 amino aicd peptide from the C-terminus. A second cleavage is very slow and occurs between Thr207-Ser208, resulting in a 24 kDa protein	
3.4.22.44	P-sG polyprotein + H2O	-