Skip to main content
. 2014 Sep 2;9(9):e105834. doi: 10.1371/journal.pone.0105834

Figure 1. Homology comparison of the amino acid sequences of AhDGAT1 with DGAT1s from other plant species.

Figure 1

Identical amino acid residues are highlighted in black. A putative acyl-CoA binding motif is underlined and designated as block ‘I’. The AS11 tandem repeat is underlined and designated as block ‘II’. The putative catalytic active site is underlined and designated as block ‘III’. The phosphopantetheine attachment site is underlined and designated as block ‘IV’. The SnRK1 target site is designated as block ‘V’. The putative thiolase acyl-enzyme intermediate signature is underlined and designated as block ‘VI’; the dot shows the invariant proline. The putative fatty acid protein signature is underlined and designated as block ‘VII’; the dot shows the tyrosine phosphorylation site. The DAG/phorbol ester binding signature motif is underlined and designated as block ‘VIII’; the dot shows the conserved phenylalanine. The putative C-terminal ER retrieval motifs is underlined and designated as block ‘IX’. The N-glycosylation sites are boxed. Amino acids denoted with triangle represent leucine (L) residues forma putative leucine zipper motif.