Extended Data Fig. 10: The conservation of Tyr-VIa in the A. thaliana LRR-RK cytoplasmic domain and in representative members of the 20 groups of animal-receptor tyrosine kinases.
From: Phosphocode-dependent functional dichotomy of a common co-receptor in plant signalling
a, b, Clustal Omega multiple alignments of A. thaliana LRR-RK cytoplasmic domain, visualized using JalView v2.10.2b2, illustrate the conservation (a) and non-conservation (b) of Tyr-VIa. The alignment is coloured by percentage identity. Magenta, Tyr-VIa. Protein IDs of the sequences used for the alignment are in Supplementary Table 1. Arrows indicate the LRR-RKs reported in this study. c, The conservation of Tyr-VIa in representative members of the 20 groups of animal receptor tyrosine kinases. Clustal Omega multiple alignments were visualized using JalView v2.10.2b2. The alignment is coloured by percentage identity. Red, position analogous to BAK1 Y403. Protein IDs used for the alignments: EGFR (P00533), AXL (P30530), DDR15 (Q08345), EphA1 (P21709), FGFR2 (P21802), HGFR (P08581), INSR (P06213), PTK7 (Q13308), LTK (P29376), MUSK (O15146), PGFRB (P09619), RET (P07949), RYK (P34925), TIE1 (P35590), NTRK1 (P04629), VGFR1 (P17948), ROR1 (Q01973), ROS (P08922), LMR1 (Q6ZMQ8), STYK1 (Q6J9G0). d, In silico alignments of the structures of BAK1CD and EGFRCD. A selected overlapping region of the BAK1 (PDB ID: 3UIM) and EGFR (PDB ID: 2JIT) cytoplasmic domain structures is presented, highlighting BAK1 Y403 and EGFR Y827.
