plosone-phylo
Figure 1
Domain structure, phylogeny and conservation of critical catalytic features of ciliate PI4Ks.A, Domain structure of Tetrahymena PI4Ks. The RING domain predicted in PI4K2 has been removed (see Table S1 and Methods). Domain boundaries, e-values and further details are given in Table S1. B, Unrooted neighbor-joining tree of catalytic domains from 28 ciliate, 2 yeast (Stt4, Pik1) and 2 mammalian (PI4Ka and PI4Kb) type III PI4Ks. Bootstrap values from 1000 replicates higher than 70% are indicated near the corresponding branches. Type III?, III? and ciliate-specific III-like PI4Ks are color coded (blue, green and red, respectively). Circles and triangles represent Tetrahymena and Paramecium PI4Ks, respectively. Bar indicates number of amino acid substitutions per site. C, Sequence alignment of the catalytic kinase domains from type III ciliate, mammalian and yeast PI4Ks. The position of prominent catalytic features is indicated by arrows and numbered residues refer to human PI4KIII? sequence [58]. All ciliate PI4Ks have conserved catalytic motifs and they bear key residues: the K1792 residue (IFK motif), the catalytic motifs DRH1901-N1904 and HID1917 and the E1933 and K1937 residues in the activation loop [58]. Significant conservation was also observed in the G-loop (G1836 in human PI4KIII?). The TtPI4K1 and PtStt4 G-loop (highlighted in red) could not be properly aligned due to a unique 5aa insertion in both PI4Ks. Also, alignment of the activation loop and the E1933 and K1937 residues was distorted due to unique insertions in all type III-like ciliate PI4Ks (highlighted in grey). PtPI4K21 apparently lacks a portion of the activation loop.
Figure 1
Domain structure, phylogeny and conservation of critical catalytic features of ciliate PI4Ks.A, Domain structure of Tetrahymena PI4Ks. The RING domain predicted in PI4K2 has been removed (see Table S1 and Methods). Domain boundaries, e-values and further details are given in Table S1. B, Unrooted neighbor-joining tree of catalytic domains from 28 ciliate, 2 yeast (Stt4, Pik1) and 2 mammalian (PI4Ka and PI4Kb) type III PI4Ks. Bootstrap values from 1000 replicates higher than 70% are indicated near the corresponding branches. Type III?, III? and ciliate-specific III-like PI4Ks are color coded (blue, green and red, respectively). Circles and triangles represent Tetrahymena and Paramecium PI4Ks, respectively. Bar indicates number of amino acid substitutions per site. C, Sequence alignment of the catalytic kinase domains from type III ciliate, mammalian and yeast PI4Ks. The position of prominent catalytic features is indicated by arrows and numbered residues refer to human PI4KIII? sequence [58]. All ciliate PI4Ks have conserved catalytic motifs and they bear key residues: the K1792 residue (IFK motif), the catalytic motifs DRH1901-N1904 and HID1917 and the E1933 and K1937 residues in the activation loop [58]. Significant conservation was also observed in the G-loop (G1836 in human PI4KIII?). The TtPI4K1 and PtStt4 G-loop (highlighted in red) could not be properly aligned due to a unique 5aa insertion in both PI4Ks. Also, alignment of the activation loop and the E1933 and K1937 residues was distorted due to unique insertions in all type III-like ciliate PI4Ks (highlighted in grey). PtPI4K21 apparently lacks a portion of the activation loop.