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Fig. 1 | BMC Structural Biology

Fig. 1

From: Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region

Fig. 1

Multiple sequence alignment of leucine-rich alpha helical regions of human THAP proteins. The leucine rich alpha helical regions in human THAP proteins align with each other within THAP protein groups. a Helical region corresponds to residues143–188 (THAP1), 135–178 (THAP2), 189–224 (THAP3) and 148–193 (THAP6) (b) Helical region corresponds to residues 237–281 (THAP7), 180–209 (THAP8) and 254–310 (THAP11) (c) Helical region corresponds to residues 150–180 (THAP0), 362–398 (THAP4), 331–372 (THAP5) and 145–182 (THAP9). Boundaries of each protein are labelled. The Multiple Sequence Alignments were generated using CLUSTAL OMEGA and visualized using Jalview [47]. The color coding in Jalview is as follows; If each column has more than 60% hydrophobic amino acid residues, it is represented by blue, red represents more than 60% positively charged amino acid residues combined or more than 80% of either of the positively charged amino acid residues, more than 60% of negatively charged amino acid residues are represented by magenta, around 50 to 60% of polar amino acid residues are represented by green, Cysteine amino acid is pink colored, Glycine amino acid is orange colored, Proline amino acid is represented by yellow, more than 60% of aromatic amino acid residues are colored cyan and unconserved amino acid residues are represented as white

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