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Figure 3 | BMC Structural Biology

Figure 3

From: Conformational flexibility and molecular interactions of an archaeal homologue of the Shwachman-Bodian-Diamond syndrome protein

Figure 3

Sequence alignment of SBDS proteins from different species. Sequences of SBDS proteins from M. thermautotrophicus (MthSBDS), Archaeoglobus fulgidus (Aful), Halobacterium marismortui (Hmar), Saccharomyces cerevisiae (Scer), Human, Rat, Chicken, Anopheles gambiae (Agam), Drosophila melanogaster (Dmel), Caenorhabditis elegans (Cele) and Arabidopsis thaliana (Atha) were aligned. Green and orange triangles designate boundaries between domains 1 and 2 and domains 2 and 3, respectively. The secondary structure of mthSBDS (molecule A) is shown on top of the aligned sequences. Positions for which the percentage of 'equivalent' residues, considering their physico-chemical properties, is higher than 70% are colored in red on a white background and framed in blue boxes. If residues are strictly conserved, they are colored in white characters on a red background.

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