Figure 6
From: Organization and molecular evolution of a disease-resistance gene cluster in coffee trees
Alignment of the predicted amino acid sequences from SH3 -CNL members. The coiled-coil, NBS and LRR domains are highlighted in lilac, blue and green, respectively. The motif EDVID [79] as well as the motifs P-loop/kinase 1, RNBS-A, kinase II, RNBS-B, RNBS-C, hydrophobic domain in NBS domain are underlined. The first sequence is shown in full, while for other proteins only amino acids that differ from the first one are indicated. A 8 bp deletions in B2_Ea and an 1 bp insertion in A2_Ea modifying the reading frame were disregarded. The xxLxLxx motif in the LRR domain is boxed, where L is any aliphatic amino acid and x is any amino acid. Gaps introduced at alignment are indicated by dashes, while asterisks indicate the presence of stop codons. NBS probe used in Southern hybridization is highlighted by a frame. The tryptophan residue (W), specific to the non-TIR-NBS-LRR class of plant disease R gene, located at the end of the kinase 2 motif [20], is highlighted in yellow.