Conclusions
Here we have collected and analyzed the percentage identity, amino acid composition and logo motifs, and the dN/dS ratio in the largest and functionally important ribosome multidomain bacterial S1 protein. The collected and structured data were integrated into the server, which can be accessed athttp://oka.protres.ru:4200. In this comparative analysis of 1333 S1 protein sequences that have been identified in 24 different phyla, we demonstrate how such phyla can be independently/dependently formed during evolution in accordance with the change in the number of structural RNA-binding S1 domains, the presence of a conserved RNA binding site in each individual domain, as well as the specificity of the amino acid composition and the ratio of non-synonymous and synonymous substitutions. Based on the obtained data, the study of the evolutionary relationships for the bacterial phyla will suggest that for the bacterial ribosomal S1 proteins, the evolutionary development of proteins evolved from multirepeat assemblies to single repeat. At the same time, it is more likely that the terminal S1 domains are “cut off”, while the more conservative central ones are preserved.