Fig. 6

The essential amino acid residues in neoculin group members have been conserved. a Amino acid sequence alignment of neoculin group members from C. latifolia and C. capitulata fruits. In each alignment, the residues that are shared with only NBS or only NAS are shown in blue and red, respectively. The residues that are not consistent with NBS or NAS are shown in pink, and those that are consistent with only C_9931_c0_g1_i1 (Ser17) are shown in light green. His-11 and Cys residues are highlighted in dark red and dark green, respectively. Arg-48, Tyr-65, Val-72, and Phe-94 are highlighted in pale green. Mannose-binding sites (MBS, QxDxNxVxY) are indicated by a dagger (†), and conserved residues are highlighted in yellow. MBS residues that are conserved in all sequences are indicated by a double dagger (‡). MBS residues in L_307_c0_g2_i1, L_307_c0_g1_i1, and C_9931_c0_g1_i1 are shown in boxes. The predicted proteins were divided into nine regions—N-Pro, N-term, MBS1, inter1, MBS2, inter2, MBS3, C-term, and C-Pro—based on the regions removed after signal-peptide cleavage, the N- or C-terminal regions, the regions of MBS 1 to 3, and the regions between the MBSs. b Amino acid residue substitutions in proteins from the neoculin group. The region from inter2 to C-term is the primary region of sequence diversity in the neoculin group. The values shown in the heatmap are amino acid substitution rates (%) of neoculin group. The NBA sequence was used as the reference