Figure 1

Comparison of the primary structures of plant Rhilphs, related α-proteobacterial phosphatases and human PP1α as a prototype of "conventional" eukaryotic PPP phosphatases. Amino acid residues conserved in at least all but one Rhilphs and α-proteobacterial phosphatases are shown in white and shaded in black. Residues conserved in at least two thirds of the sequences are shown in white and shaded in dark grey. Residues conserved in at least half of the sequences are shown in black and shaded in light grey. Following substitutions were considered as conserved residues: Ile/Leu, Phe/Tyr, Asp/Glu, Asn/Gln, Arg/Lys and Ser/Thr. Catalytic site residues that interact with metal ions are indicated by asterisks according to [20]. SAPNY motif in PP1, conserved in most eukaryotic PPP phosphatases, is double underlined. Solanum tuberosum sequence is translation of the EST entries BQ516856, BQ516857 and BI435517. Physcomitrella patens sequence is translation of the EST entry BQ039171. Other accession numbers are indicated in Table 1.