Additional file 18: of Refining a steroidogenic model: an analysis of RNA-seq datasets from insect prothoracic glands

Abstract

Figure S2. Bombyx mori adenylate cyclases and 3′, 5′ cyclic nucleotide phosphodiesterases. A: Secondary structure and multiple sequence alignment of the C1 and C2 domains of Bm ACs based on sequence similarities with mammalian ACs [48, 49]. Secondary structure prediction of BmAC1L was carried out using Swiss model protein structure homology-modelling server [116] and is shown on top of each alignment. Arrows indicate β-sheets and cylinders indicate α-helixes. Forskolin interacting residues are highlighted in green based on data from mammalian ACs [48, 49]. ATP binding residues are highlighted in blue based on data from mammalian adenylate cyclases [48, 49]. Boxed residues indicate the change of Serine to Alanine in BmAC8L and BmAC5L that probably confers insensitivity to forskolin [50]. The name of each adenylate cyclase is based on sequence similarity of each protein to the human adenylate cyclases (i.e. BmAC1L: Bombyx mori Adenylate Cyclase 1 (human adenylate cyclase 1)-Like). B: Graphical representation of the Pfam domains of Bm ACs. Pfam domains were visualized via HMMER https://www.ebi.ac.uk/Tools/hmmer/search/phmmer [128]. The length of each protein and the location of transmembrane domains is indicated. C: Secondary structure and multiple sequence alignment of the catalytic domain of Bm PDEs based on sequence similarities with mammalian PDEs [52–54]. Secondary structure prediction of BmPDE1L was carried out using Swiss model protein structure homology-modelling server [116] and is shown on top of each alignment. Cylinders indicate α-helixes. IBMX interacting residues are highlighted in blue [55]. Residues contacting the AMP ligand or otherwise involved in the catalytic mechanism are highlighted in orange based on sequence similarities with mammalian phosphodiesterases [52–54]. The name of each phosphodiesterase is based on sequence similarity of each protein to the human phosphodiesterases (i.e. BmPDE4L: Bombyx mori PhospoDiEsterase 4 (human phosphodiesterase 4)-Like). D: Graphical representation of the Pfam domains of Bm PDEs. Pfam domains were visualized via HMMER https://www.ebi.ac.uk/Tools/hmmer/search/phmmer [128]. The length of each protein is indicated. (TIFF 450352 kb)