Figure 1

a) Sequence-structure alignment of the ORFan R843 and the template human acyl protein thioesterase 1 (PDB code: 1fj2, Chain: A). The predicted secondary structure (H: helix and E: β-strand) of R843 is shown above its sequence. The observed secondary structure of 1fj2A is shown below its sequence. Identical residues are marked in black with blue background. The secondary structural elements of 1fj2 are represented as α and β and are numbered from A-F and 3–8 respectively. The conserved catalytic residues, S, D and H are shown as stars and highlighted with bold black letters in magenta background. The conserved pentapeptide sequence G-X-S-X-G with active site serine is shown in green color. The conserved PROSITE signature pattern of carboxylesterases is shown in grey boxes. The residues probably forming the oxyanion hole are marked in bold black letters in yellow background. b) Ribbon diagram of predicted model of ORFan R843. The model was generated from INUB and refined using Nest [53]. α-helices and β-sheets are colored in blue and yellow. The remaining secondary structure is in white color. α-helices and β-strands of the canonical fold are numbered alphabetically from A to F and numerically from 3 to 8 respectively (the canonical strands 1 and 2 are missing). The residues forming the catalytic triad (Ser200, Asp261 and His292) are represented in ball-and-sticks. The figure is drawn using MOLSCRIPT program [54].