Fig. 3

Biophysical features of drought stress responsive RBPome and domain conservation across species. Density of (a) protein length (number of amino acids), b isoelectric point (pI) and c hydrophobicity (gravy) were analyzed for RBPome responsive to drought stress with proteins linked to RNA biology (red), RBPome responsive to drought stress with proteins whose RNA biology is unknown (blue), RBP repertoire linked to RNA biology (black), RBP repertoire with unknown RNA biology (orange) [41] and input proteome from controls that are used as input or background (N = 5630) (green). Significances of differences between RBP subsets in (a-c) was tested using the Kolmogorov-Smirnov test. Compared to the reference data set, all the four subsets are significantly different number of amino acids (a), pI (b) and hydrophobicity (c) (p < 0.01), with the exception of number of amino acids in the RBP repertoire with unknown RBP biology. d Log₂ enrichment of amino acid residues in the RBPome responsive to drought stress, determined using the composition profiler (http://www.cprofiler.org/). The significance of enrichment or depletion was tested by a two-sample T-test and amino acids that are significantly enriched or depleted (p ≤ 0.01) are marked with asterisks. e-f Domain copy numbers of the cold shock domain-containing protein 3 (e), the pentatricopeptide repeat-containing protein (f) and the ACT-like tyrosine kinase (g). The motifs and copy number assignments were performed using the ScanProsite (http://prosite.expasy.org/)