Fig. 4: Rcr3 is highly polymorphic in Solanaceae.

a The evolutionary history of Rcr3 was inferred using the Maximum Likelihood method based on the Whelan and Goldman model. The bootstrap consensus tree inferred from 1000 replicates is taken to represent the evolutionary history. Shown are percentage bootstrap values. b Summary of variant residues in the protease domain. Columns with conserved residues or a single substitution are not shown. Highlighted are residues that are polymorphic within a genus (red) polymorphic within solanaceous plants but putatively fixed within a genus (gray), and putatively fixed only within Nicotiana (green). The residue position is indicated on top (e.g., first residue is pos. 130) with the residues relevant for Avr2 binding highlighted in red and residues associated with HR in green. *, resurrected NbRcr3a* is not included in the annotation of Nicotiana-specific sites (green). c Position of polymorphic residues in the 3D model of Rcr3. SlRcr3 was modelled on 1s4v and amino acid polymorphism were analysed by ConSurf and scores were used to color the structure using PyMol. Highlighted are the catalytic Cys residue (yellow) and substrate-binding groove (yellow dash line), as well as some of the most polymorphic residues (white numbers).