Skip to main content
. 2002 May 14;99(10):6749–6754. doi: 10.1073/pnas.102167299

Figure 3.

Figure 3

Sequence analysis of GbpC and -D. Residues are shaded black if they are identical to the consensus for each position in the alignment, and shaded gray if they are similar to the consensus. (A) Alignment of the Ras sequences from GbpC, the Drosophila CG5483 protein (D.m., GenBank accession no. AAF55793), a human protein encoded by the KIAA1790 cDNA (H.s., BAB47419), and human H-Ras (P01112). Key residues involved in GTP hydrolysis are highlighted and marked with an asterisk. (B) Alignment of the protein kinase sequences from GbpC, transforming growth factor β-activated protein kinase 1 (Tak1, O43318), a RAF homolog from Arabidopsis thaliana (Ctr1, A45178), and mixed lineage kinase 1 (Mlk1, AAG44591). The twelve nearly invariant protein kinase residues (41) are highlighted and indicated with an asterisk. For positions that show a conserved residue in >90% of Tyr kinases, but not Ser/Thr kinases (42), the preferred amino acid is indicated above the alignment. (C) Alignment of the RasGEF catalytic domains from GbpC and -D with those from human Sos-1 (Q07889) and Saccharomyces cerevisiae cdc25 (P04821). The bar above the alignment in C indicates the helical hairpin involved in nucleotide exchange. (D) Alignment of the DEP domain from GbpC with mouse dishevelled protein (Dv1, P51141), mouse pleckstrin (Plk., AAG29513), and C. elegans Egl-10 (Egl10, P49809). Residues implicated in forming a β-hairpin arm and electric dipole are highlighted and indicated by asterisks.