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. 2016 Dec 12;173(2):1031–1044. doi: 10.1104/pp.16.01671

Figure 4.

Figure 4.

Multiple sequence alignment of the amino acid sequences for SbCCR1 and several related enzymes. Included in the alignment are a CCR1 from P. hybrida, CCR2s from M. truncatula and sorghum, a dihydroflavonol reductase from V. vinifera, and five CCRs or CCR-like enzymes from sorghum. Mining of sorghum proteomic data using the sequence of SbCCR1 as a query revealed four additional CCR candidates. Among the four additional candidates, high CCR activity could only be confirmed for SbCCR2. Residues that are completely conserved among all enzymes in the alignment are marked with asterisks. Residues highlighted in yellow are in β-strands, while those in red are in α-helices. Residues involved in binding of substrates or cosubstrates are in boldface and underlined. The CCR signature sequence NWYCY is outlined in a box. The N and C termini of CCR candidates from sorghum were truncated to closely match the experimentally observed termini of SbCCR1. The colon (:) and the period (.) indicate conservation of strongly similar properties and conservation of weakly similar properties, respectively.