Protein alignments of N-terminal regions of CM1 domain proteins. (A) An alignment of Cnn-C homologues from different Drosophila species. The alignment was performed in JalView keeping Drosophilamelanogaster at the top with the closest related species in order below. Only the N-terminal regions of the proteins were used in the alignment (∼1–255 aa). Potential phosphorylation patches are highlighted in yellow, with the proportion of S/T residues present in the D. melanogaster sequence indicated in brackets. The CM1 domain is highlighted in purple. Red boxes and green arrows indicate α-helices and β-sheets based on predictions from JPred. (B) An alignment of the N-terminal region of Cnn-C with the equivalent N-terminal regions of its homologues in non-Drosophila species. Phosphorylation sites that promote binding to γ-TuRCs identified either in this study (Drosophila Cnn-C, T27 and S186) or other studies (S. cerevisiae SPC110 S36, S60, T64, T68 and S91, C. elegans SPD-5, T178, T198; human CDK5RAP2, S140) are indicated. Note that only the originally identified CM1 domain sequence (yellow) is conserved between homologues. The position of the CM1 helix (blue) and CM1 coiled-coil (CC) region (brown) recently identified in SPC110 are indicated, as is the γ-TuNA sequence from human CDK5RAP2 (green).
