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. Author manuscript; available in PMC: 2022 Feb 1.
Published in final edited form as: Crit Rev Biochem Mol Biol. 2020 Dec 27;56(1):54–87. doi: 10.1080/10409238.2020.1856768

Figure 2. Multiple sequence alignment of dsRNA binding domains of ADARs.

Figure 2.

Sequences of the dsRBDs for the indicated proteins were obtained from UniProt database using the accession numbers described for Figure 1. Domain boundaries were adjusted based on structural data. The final figure was produced using ESPript 3 (Robert and Gouet, 2014). Sequences that are identical are shown in a red-filled box, while those meet consensus (> 70%, <100%) are boxed with consensus residues in red font. The residues important for dsRNA binding (Masliah, Barraud, and Allain, 2013) and the secondary structure elements (conserved αβββα fold) are shown below. The conserved GPxH motif and di-alanine residues (AA) as well as the aromatic residues that reside within the hydrophobic core (HC) of the dsRBD are indicated above the alignment.