Fig. 4

Eu-KAI2 proteins have highly conserved structure. Alignment illustrating conservation of primary protein structure in D14/KAI2 proteins. The 265 core positions (numbered) are shown in the alignment, for the whole family (top row), for eu-KAI2 proteins (middle row) and for eu-D14 proteins (bottom row). Positions where the same amino acid is present in >50% of sequences in the clade are denoted by corresponding letter; other positions are denoted by a dash. The colouring of each conserved residue indicates the degree of conservation; pale blue >50%, light blue >70%, mid-blue >90%, dark blue >99%, purple =100%. Structural features are annotated below the alignment. The catalytic triad is indicated by *. MAX2-interacting residues are indicated by m. Predicted alpha helices (based on the crystal structure of AtKAI2 (Protein Data Bank (PDB) code 4HRX1A) are shown by grey bars, predicted beta strands by grey bars with an arrow. The discrete positions in the polypeptide chain where insertions (or deletions) can be tolerated are illustrated with red arrow heads. Residues that are characteristic of eu-KAI2 proteins are underlined in yellow; residues characteristic of eu-D14 are underlined in orange (see Fig. 5)