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. Author manuscript; available in PMC: 2019 Mar 3.
Published in final edited form as: Nature. 2018 Sep 3;561(7722):248–252. doi: 10.1038/s41586-018-0471-x

Figure 10 |. Multiple alignment of Arabidopsis thaliana LRR-RK cytoplasmic domain illustrating the conservation (a) or non-conservation (b) of Tyr-VIa, and conservation of Tyr-VIa in representative members of the 20 groups of animal receptor tyrosine kinases.

Figure 10 |

a, b, Clustal Omega multiple alignments were visualized using JalView v2.10.2b2. The alignment is coloured by percentage identity. Magenta, Tyr-VIa. Protein IDs for the sequences used for the alignment are in Supplementary Table 1. Arrows indicate the LRR-RKs reported in this study. c, In silico alignments of BAK1CD and EGFRCD structures. A selected overlapping region of the BAK1 (3UIM.pdb) and EGFR (2JIT.pdb) cytoplasmic domain structures is presented, highlighting BAK1-Y403 and EGFR-Y827. d, 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).