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. 2016 Oct 2;291(46):24280–24292. doi: 10.1074/jbc.M116.740506

FIGURE 1.

FIGURE 1.

Overview and alignment of the PFA0210c orthologues from P. falciparum, P. knowlesi (PKH_020910), and P. chabaudi (PCHAS_020730). A, outline of the domains of PFA0210c and its orthologues, indicating the signal sequence (black), the motif that mediates export to the erythrocyte (PEXEL; black rectangle), the non-conserved N-terminal region (dark blue), the START domain (light blue), and the C-terminal extension (gray). Numbers above the outline indicate the position of the amino acid residues at the start and end of the domains. The domain structure among the PFA0210c orthologues is the same, although the length of the non-conserved N-terminal domain, and therefore the length of the entire protein, varies. B, alignment of PFA0210c with its orthologues of P. knowlesi (PKH_020910) and P. chabaudi (PCHAS_020730). The START domain is underlined. Conserved residues in the C terminus that were targeted in the mutagenesis studies are shown in boldface type. The numbers at the end of the sequence indicate the position of the residue at the extreme C terminus; the numbers above the sequence and the italicized numbers below the sequence indicate the position of the last residue of the truncations of the P. falciparum and P. knowlesi protein, respectively, used in this study. Note that the variation in sequence length is determined by variation in the N-terminal portion of the proteins; the length of the sequence from the start of the START domain to the C terminus varies by only two residues between these proteins. Sequences were obtained from PlasmoDB (40) and aligned using Clustal Omega (45).