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. 2019 Apr 16;16(7):906–917. doi: 10.1080/15476286.2019.1600396

Figure 3.

Figure 3.

Comparison of chloroplast-targeted cpSecA from distinct species. Multiple alignment of the amino acid sequences of cpSecA from Prunus persica (ppcpSecA, Prupe.3G002700.1) and its homologues from Oryza sativa (OscpSecA, BAD44978), Pisum sativum (PscpSecA, CAA57798), Spinacia oleracea (SocpSecA, CAA88933) and the cyanobacterium Trichormus variabilis (TvSecA, ABA21744). High-affinity ATP-binding domains (a, b) and low-affinity ATP-binding domains (c, d), conserved among the prokaryotic SecA homologues, are indicated. Arrow marks the cleavage site of the chloroplast transit peptide of PpcpSecA predicted by ChloroP1.1. Sequences were aligned using Clustal Omega. Small and hydrophobic amino acids including the aromatic ones (AVFPMILW) are in red, acidic amino acids (DE) in blue, basic amino acids (RK) in magenta, and polar (STNQ) and aromatic (YH) amino acids together with cystein (C) and glycine (G) in green. (*) indicates positions with a conserved amino acid, (:) conservation between amino acid groups of strongly similar properties, and (.) conservation between amino acids groups of weakly similar properties.