Fig. 9

Sequence characteristics of DGAT3. a C. reinhardtii DGAT3 predicted amino acid sequence. Putative catalytic sites are underlined. Highlighted are the cysteines predicted to participate in 2Fe-2S binding (in gray) and the residues potentially involved in dimerization (in black). The bolded italicized residues correspond to the 91 amino acids modeled on the thioredoxin-like 2Fe-2S ferredoxin from Aquifex aeolicus. b Sequence logo of the DGAT3 family. The sequences within the DGAT3 clade of Fig. 8 were aligned, and the MSA was trimmed using BMGE to eliminate gaps (see Methods). The y axes show the logo bits; error bars are shown on each position. Underlined is the putative acyltransferase catalytic site that is most conserved amongst the members of the clade. c Comparison of C. reinhardtii DGAT1 partial sequence published by Boyle et al. [9], DGAT2 (DGTT4) and DGAT3 sequences. Highlighted in gray are the hydrophobic regions obtained by Kyte & Dolittle hydrophobicity scale analysis using a window size of 9. Underlined regions indicate transmembrane segments predicted by TM-HMM analysis. Residues highlighted in black show well established and/or putative conserved catalytic motifs