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. 2010 Jun 4;10(6):5668–5682. doi: 10.3390/s100605668

Figure 2.

Figure 2.

Alignment of the PAS and kinase domains from selected PAS kinase orthologs. (A) Schematic of PAS kinase homologs. Regions of similarity are boxed in grey, with non-homologous regions indicated by gaps between the grey boxes. Alignment of the PAS (B) and kinase (C) domains from selected PAS kinase orthologs. Secondary structure elements (α-helical and β-sheet) were derived from the published NMR structure of the PAS domain [27] as well as amino acid alignment of the kinase domain with the published structure of microtubule-associate protein/microtubule affinity regulating kinase 2 (MARK2) [33], and are shown above the amino acids in green and purple respectively. Amino acid sequences were aligned using the Clustal W program [34]. The degree of amino acid conservation is indicated both by color and “*” (identical residues in all sequences), “:” (highly conserved amino acids), and “.” (weakly conserved amino acids). Red indicates a small hydrophobic or aromatic amino acid (-Y), blue indicates acidic, magenta is basic, and green is hydroxyl plus amine plus basic (-Q), all other amino acids are grey.