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.