FIG. 7.

HAD domain conservation with other cyclins. (A) Primary sequence comparisons. Members of the C-type and H-type cyclin subfamilies are indicated on the left. Identical residues or conserved substitutions are boxed. The asterisks indicate the conserved KERQK motif. (B) Secondary structure comparison. The primary sequence of each cyclin is presented as indicated. The KERQK motif in Ume3p and the human cyclin C (HsCycC) is in bold face type. The hydrophobic heptad repeats are indicated by the reverse lettering. The secondary structure predictions for each region are indicated below the primary sequence. H = α-helix, spaces indicate no helix, β-sheet, or coiled-coil predicted. Only the consensus of five algorithms (NNPREDICT, PHD, SIMPA, PREDATOR, DSC) is presented. The LxCxE motif that directs HsCycD1 binding to Rb is in bold face type (see text for details).