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Comparative Analysis of AfPiwi and Eukaryotic Argonaute Proteins

Sequence alignment and structure-based comparison of AfPiwi with Piwi and Ago subfamily proteins across eukaryotes. The figure highlights key residues in guide strand coordination and putative slicer catalytic sites. Invariant, switch, and conserved residues are color-coded to illustrate evolutionary relationships.

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Comparative Analysis of AfPiwi and Eukaryotic Argonaute Proteins

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  1. Supplementary Figure 2. Sequence alignment of AfPiwi with PIWI domains of eukaryotic Argonaute proteins from the Piwi and Ago subfamilies, together with a structure-based alignment of AfPiwi and PfAgo. Residues coordinating the 5’phosphate of theguide strand (Fig. 2) are indicated by red arrows. Blue arrows denote putative slicer catalytic site residues. Colour coding of invariant residues as follows: Red: invariant in all eukaryote Argonaute sequences and AfPiwi. Blue: Switch residues: residues which are invariant within the Ago and Piwi subfamilies of eukaryotic Argonaute proteins, but differ between these two subfamilies. The equivalent residue in AfPiwi is conserved with one of these eukaryotic Argonaute subfamilies. Magenta: highly conserved in all eukaryote Argonaute sequences and AfPiwi. Orange: invariant in all eukaryote Argonaute sequences only.

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