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. 1999 Apr;119(4):1261–1270. doi: 10.1104/pp.119.4.1261

Figure 3.

Figure 3

Optimal alignment of PPOs from several plant species. Accession nos.: apricot, no. AF020786; apple, no. P43309 (Boss et al., 1995); grape, no. P43311 (Dry and Robinson, 1994); fava bean, no. 418754 (Cary et al., 1992); Virginian pokeweed, no. D45385 (Joy et al., 1995); tomato, no. Q08296 (Newmann et al., 1993). A dot refers to identity with apricot. A space denotes a gap introduced for improved alignment. Single underlined amino acid residues correspond to the transit peptide. Domain I of transit peptide is marked by •. Domain II of transit peptide is marked by ⋄. The “n-region” of domain II of transit peptide is shaded in blue. The thylakoid transfer domain of the domain II of transit peptide is shaded in green. Shown as bold letters are the hydrophobic amino acids of thylakoid transfer domain and the precleavage site. The first amino acid residue of the mature protein is shaded in black. Double underlined amino acid residues correspond to the sequence obtained from N-terminal sequencing of the purified protein. Copper domains A and B of the mature protein are shaded in yellow. His residues predicted to be copper-binding ligands are boxed.