Additional file 1: of Classification of the human THAP protein family identifies an evolutionarily conserved coiled coil region

Figure S1. Amino acids are represented as (a) a, d (hydrophobic); e, g (charged); b, c, f (polar) (b) Hydrophobic (Grey circles), Charged (textured circles), Polar (white circles). Figure S2. The color coding in Jalview [47] is described in the legend for Fig. 1. Figure S3. (a) The Multiple Sequence alignment was generated using CLUSTAL OMEGA, which represents conserved amino acid residues by an asterisk (*) mark and similarly charged amino acid residues by a colon (:). The most conserved region in all twelve THAP proteins is the amino terminal THAP domain, highlighted in grey. No conservation is found when the predicted alpha helical regions of (b) sTHAP with mTHAP (c) sTHAP with lTHAP (d) mTHAP with lTHAP protein groups are aligned with each other. The Multiple Sequence Alignments for Figures S3b, c and d were generated using CLUSTAL OMEGA and visualized using Jalview. The color coding in Jalview is described in the legend for Fig. 1. Figure S4. Protein models generated for (a) Full length THAP protein (b) Corresponding predicted alpha helical region. I TASSER results were viewed using VMD, selecting Ribbon model for secondary structure of proteins with alpha helix (purple), 310 helix (blue), Π- helix (red), beta sheet (yellow), turn (cyan) and coils (white). Figure S5. Superposition of THAP7 (green), THAP8 (blue), THAP11 (red). Figure S6. The reported crystal structure of THAP11 (yellow) is overlapped (using PyMOL) with the structure of the helical region of THAP11 (cyan) predicted using I TASSER. Table S1. Leucine content in THAP proteins and their predicted alpha helical regions. Table S2. LOGICOIL and Multicoil predicts higher order oligomer formation. Table S3. NLSmapper predicts NLS in THAP0, THAP1, THAP2, THAP4, THAP5, THAP9. The predicted NLS regions in THAP1 and THAP9 overlap with the predicted coiled coil regions of the respective proteins. (DOCX 2200 kb)