The predicted secondary structures for the merlin proteins of various species. The region with a predicted β-sheet structure is shaded in grey, while the region with an α-helix structure is shaded in black. These predicted secondary structures correspond to the crystal structural data , which are shown above the alignment with the α-helix region indicated with a thick black bar and the β-sheet region with a thin black bar. The predicted α-helical domain in the central-to-C-terminal region of merlin is marked with an open bar. Asterisks denote known domains of the merlin protein with numbers pointing to the end of truncated Drosophila merlin protein discussed in the text. "+" denotes the beginning and the end of the predicted α-helical domain. The positions of specific residues in the FERM domain discussed in the text are denoted by black dots below the aligned sequences.