Skip to main content
Fig. 1 | BMC Plant Biology

Fig. 1

From: Cloning and characterization of KoOsmotin from mangrove plant Kandelia obovata under cold stress

Fig. 1

Sequence alignment of KoOsmotin and other well-studied plant PR-5 proteins. Only the complete published sequences were used. Identical and similar amino acids among PR-5 proteins were colored dark and light gray, respectively. A cleavage site in KoOsmotin was indicated by a red arrowhead on the N-terminus. Predicted α-helix and β-strand were indicated above the sequences in dark boxes and in white wide arrows, respectively. Conserved positions containing five amino acids of the central cleft were labeled by red triangles. The sixteen conserved cysteine residues, possibly involved in the formation of disulfide-bridges in PR-5 proteins, were highlighted by yellow shadows. The N- and C-terminal elongations, predicted as signal peptide responsible for extracellular secretion and for vacuolar location, respectively, were indicated with blue lines. Sequences boxed in red dotted line showed the thaumatin motif G-x-G/F-x-C-x-T/S-G/A-D-C-x-G/Q-x-x-x-C, which was family signature in PR-5 proteins. The domain II and domain III in the 3D structures were indicated by green and orange boxes under the sequences, respectively

Back to article page