Figure 3From: Proteomic identification of OsCYP2, a rice cyclophilin that confers salt tolerance in rice (Oryza sativa L.) seedlings when overexpressedMultiple alignment of OsCYP2 with amino acid sequences of some plant cyclophilins. (A) Multiple sequence alignment of OsCYP2 with cyclophilins of various plant species by the Jalview multiple alignment editor. Seven residues (His-61, Arg-62, Phe-67, Gln-118, Phe-120, Trp-128 and His-33) associated with PPIase catalysis are marked by filled triangle (â–²). Three of these, His-61, Arg-62 and Phe-120, are extremely important for PPIase activity of OsCYP2. The residue Trp-128 is a binding site of OsCYP2 with cyclosporin A (CsA). (B) Dendrogram showing phylogenetic distance among plant cyclophilins according to average distance using percentage identity.Back to article page