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Figure 2 | Biology Direct

Figure 2

From: Prokaryotic homologs of Argonaute proteins are predicted to function as key components of a novel system of defense against mobile genetic elements

Figure 2

Prokaryotic PIWI-domains: predicted active nucleases and apparently inactivated forms. The multiple sequence alignment includes the core motifs of PIWI domains encompassing the amino acid residues that comprise the (D/E)-(D/E)XK active site. The sequences are denoted by their GI numbers and species names. The positions of the first and the last residues of the aligned region in the corresponding protein are indicated for each sequence. The numbers within the alignment represent poorly conserved inserts that are not shown. The catalytic residues of the D-RD-EXK active site are shown in reverse shading and shown underneath the secondary structure, which corresponds to the solved structure for Pf-Ago (PDB: 1Z25); 'H' indicates α-helix, 'E' indicates extended conformation (β-strand). Sequence identifiers for pAgos that are not associated with other proteins in putative operons are highlighted in bold. The coloring is based on the consensus shown underneath the alignment; 'h' indicates hydrophobic residues (WFYMLIVACTH), 'p' indicates polar residues (EDKRNQHTS), 's' indicates small residues (ACDGNPSTV).

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