*2.2. Structures, Physiochemical Properties and Subcellular Localizations of CsLEA Proteins*

Most proteins within the same family exhibited similar structures and properties (Table S1). Over one third of the CsLEA proteins were classified as unstable proteins with an instability index value higher than 40. Furthermore, this property varied significantly among the proteins within the Dehydrin subfamily, ranging from 3.83 to 56.11. All the proteins in the LEA\_5 subfamily showed instability index values greater than 47 and were considered as the most unstable and/or potentially disordered proteins [29–31]. The GRAVY (grand average of hydropathicity index) values of more than 90% CsLEA proteins were below 0, stressing that CsLEA proteins are likely to have low hydrophobicity features. CsLEA\_2 subfamily proteins were the most hydrophobic proteins, while Cs\_LEA5 proteins

were the highest hydrophilic proteins. These results are consistent with previous studies [28,32] and reinforce the structural disordered properties of LEA proteins by which they are capable of interacting with other molecules and mitigating the collision of enzymes during plant stress conditions [11]

**Figure 1.** Phylogenetic analysis of *C. songorica* LEA proteins. Full-length amino acid sequences of the 44 CsLEA proteins were analyzed using the unrooted method in the ClustalW software.
