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. Author manuscript; available in PMC: 2020 Jun 1.
Published in final edited form as: Comp Biochem Physiol Part D Genomics Proteomics. 2019 Mar 7;30:262–282. doi: 10.1016/j.cbd.2019.03.002

Figure 4.

Figure 4.

Alignment of Cancer borealis and related allatostatin C receptors. (A) MAFFT alignment of the putative C. borealis allatostatin C receptor (Canbo-AST-CR; deduced from GEFB01019215) and Drosophila melanogaster allatostatin C receptor 2, isoform F (Drome-AST-CR2-F; Accession No. ALI30485). (B) MAFFT alignment of Canbo-AST-CR and the extant portion of Neocaridina denticulata allatostatin receptor 1 (Neode-ASTR1; Accession No. AIY69136). In the line immediately below each sequence grouping, “*” indicates identical amino acid residues, while “:” and “” denote amino acids that are similar in structure between sequences. In this figure, rhodopsin family seven-transmembrane receptor domains identified by Pfam analyses are highlighted in black. In A, the residue that varies between the transcriptome derived Canbo-AST-CR sequence and that deduced from the cloned transcript MH729784, i.e., Arg76 to Gly, is shown in red font.