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. 2018 Nov 22;8:17254. doi: 10.1038/s41598-018-35545-7

Figure 1.

Figure 1

Comparison of AtDGAT3 sequence with that of other DGAT3s. The AtDGAT3 amino acid sequence (GenBank accession number AEE32272) was aligned, using Clustal Omega with (A) five plant DGAT3 protein sequences [Theobroma cacao (EOX95446), Arachis hypogaea (AAX62735 and AGT57760), Ricinus communis (EEF43203), Vernicia fordii (AGL81309)] and with (B) homologues to the thioredoxin-like [2Fe-2S] ferredoxin class: a ferredoxin from Bacillus megaterium (CbiW, CAA04306), a NADH-ubiquinone oxidoreductase subunit from Paracoccus denitrificans (NuoE or NQO2, AAA25588), the [FeFe]-hydrogenase gamma subunit from Thermotoga maritima (Tma or HydC, AAC02684)]. Multiple sequence alignments were edited using the BioEdit program and the BLOSUM62 similarity matrix for shading with a threshold of 75%. Identical residues are highlighted in black and homologous residues are shaded in grey. Conserved motifs are boxed: the two polylysine motifs in blue, a polyserine-rich region in purple and the thioredoxin-like ferredoxin domain in red with its conserved cysteine residues in yellow and highlighted with red asterisks. Putative catalytic motifs identified in A. hypogea DGAT3s by homology with motifs found in GPATs or DGAT1s are boxed in green. The putative catalytic histidine from the first GPAT-like motif, absent in the truncated forms of AtDGAT3, is yellow.