Multiple alignment of the catalytic core of 44 Protein Phosphatase sequences: H, human; B, bovine; Rb, rabbit; Rt, rat; M, mouse; P, pig; D.m, Drosophila melanogaster; S.c, Saccharomyces cerevisiae; S.p, Schizosaccharomyces pombe.. Reference numbers for the first publication of each complete sequence are shown in square brackets. Numbers in parentheses refer to 1. (A. E. McPartlin, H. M. Barker and P. T. W. Cohen, in preparation) and 2. (M. X. Chen, Y.H. Chen and P. T. W. Cohen, in preparation).
Secondary structure prediction histograms and summary secondary structure prediction obtained by combining the prediction histograms with an analysis of residue conservation patterns (see text). The sequences are divided into four groups or sub-families according to similarity. These sub-families are delineated by horizontal lines. The shading is based upon a physico-chemical property scoring scheme [17]. Shading was calculated allowing up to two gaps at each position, and ignoring the 10%least frequently represented amino acids at each position.
White on black positions are identical residues in all sequences,or where residues are identical within a sub-family (e.g. at position 28, C is conserved in the PP2A sub-family, but not within other sub-families). Light shading shows positions where residue physico-chemical properties are conserved within a sub-family. Italic text indicates positions where a sub-family does not have highly conserved physico-chemical properties. The line marked conservation shows positions that share physico-chemical properties across all sequences on a scale of 0-10 (10 = +) calculated according to Zvelebil et al. [17]. The helix, beta and loop histograms plot the frequencies of each state predicted by the three secondary structure and two turn prediction algorithms (see text). The helix, strand and loop summary lines show the positions of predicted secondary structures obtained by combining the information from the histograms with a consideration of residue conservation patterns (see text). Black shading on these summaries indicates the positions of the conserved hydrophobic residues.