Fig. 5

Only amino-acid neutral for function diverge among mammalian ERKs. a Ratio of non-synonymous rate (Ka) over synonymous rate (Ks) for all available erk1 and erk2 pairs of mammalian gene sequences (37 pairs). Multiple sequence alignment was generated and Ka/Ks values were then computed at each codon. Abscissa: distance from start ATG codon. The 5′ end of the sequences (first exon) could not be analyzed because some sequences were incomplete. b Still images were generated for 3D PDB structure 4QTB (Human ERK1) displaying the following highlighted positions: amino-acids interacting with substrates forming the DEJL(KIM) motif are colored in blue, light blue for docking groove and darker blue for acidic patch; amino-acids interacting with substrates via the DEF domain (FXFP) are colored in green; the threonine and tyrosine phosphorylated upon activation by MEK are colored in white and the “face of the kinase” is circled by a dashed white line. Amino-acids that diverge among at least 5 % of 49 mammalian ERK1s are colored in yellow (17 amino-acids). i) front-side of the kinase where ATP-transfer occurs in the catalytic cleft between the two lobes ii) left-side of the kinase iii) back-side of the kinase iv) right-side of the kinase