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. 2000 Jun 6;97(12):6328–6333. doi: 10.1073/pnas.97.12.6328

Figure 2.

Figure 2

Sequence alignment of the Maf protein from B. subtilis (Upper) and homologous proteins from 18 selected archaea, prokaryotes, and eukaryotes. The sequence of Mj0226 from M. jannaschii is shown (Lower); gaps in its sequence indicate regions with larger deviations between the Maf and Mj0226 structures, preventing meaningful structure-based alignment. Conserved residues are highlighted (blue, basic; red, acidic; yellow, hydrophobic; magenta, all others), secondary structure elements observed in the Maf crystal structure are indicated (Upper), and selected conserved residues in Maf are numbered.