Protein fold recognition using sequence profile searches frequently allows prediction of the structure and biochemical mechanisms of proteins with an important biological function but unknown biochemical activity. In this present, we describe such predictions resulting from an analysis of the dimerization and autoproteolysis. We employ sequence profile analysis to show that the human glycosylasparaginase (1apy), Flvobacteria glycosylasparaginase (2gaw), proteasome (1ryp), penicillin acylase (1pnk), and glutamine phosphoribosylpyrophosphate amidotransferase (1ecf) belong to autoproteolysis and possess dimerization or oligomerization. Using sequence profile searches, we show that several previously undetected protein families contain dimer fold. This allows us to predict the catalytic activity for a wide range of biologically important, but biochemically uncharacterized proteins from eukaryotes and bacteria.
