Fig. 1.

AfrLEA6 is predicted to have three distinct regions. (A) The N-terminal SMP repeats (purple) exhibit alpha-helical propensity. The C-terminal domain (green) exhibits fuzzy self-interactions. These two domains are linked by an intrinsically disordered spacer enriched in proline, glycine, and aromatic residues (blue). I-Tasser structural prediction of AfrLEA6 is based on hierarchical stability of known crystal structures, thus associating this structure with a possible conformation in the dried state. (B) SmartEMBLE identifies two N-terminal SMP domains in AfrLEA6 (purple). (C) The protein is overall negatively charged, with alternating charges (green) at the C terminus promoting interactions with other proteins or itself.