Figure_2_cysDN_phylogeny

Figure 2 of manuscript "Comparative genomics and proteomic analysis of assimilatory sulfate reduction pathways in anaerobic methanotrophic archaea"Files included:Fig2_cysN_ef_clustalo_alignment.faa - ClustalO alignment of protein sequencesFig2_cysN_ef_clustalo_alignment_filtered_for_tree.faa - Filtered protein sequences (416 amino acids) used for phylogeneticsFig2_cysN_ef_clustalo_tree.png - Final Bayesian Phylogeny of CysN and Elongation FactorFig2_cysD_clustalo_alignment.faa - ClustalO alignment of protein sequencesFig2_cysD_clustalo_alignment_filtered_for_tree.faa - Filtered protein sequences (416 amino acids) used for phylogeneticsFig2_cysD_clustalo_tree.png - Final Bayesian Phylogeny of CysN and Elongation FactorFigure 2. Phylogeny of heterodimeric ATP sulfurylase subunits (CysDN). (a) Bayesian phylogeny of 416 amino acid residues of sulfate adenylyltransferase subunit 1 (CysN) and elongation factor 1 alpha (EF-1A) or elongation factor thermo unstable (EF-Tu) proteins. CysN, in green, formed a separate phylogenetic cluster from the homologous EF-1A and EF-Tu in blue. ANME proteins are bolded in red. The phylogenetic analysis distinguished CysN from their homologous elongation factor in ANME. (b) Bayesian phylogeny of 270 amino acid residues of sulfate adenylyltransferase subunit 2 (CysD) in green. They are found in ANME genomes next to CysN confirming that they are the heterodimeric ATP sulfurylase subunits. Asterisks (*) indicate proteins that have been studied biochemically or structurally (Andersen et al., 2000; Kobayashi et al., 2010; Liu et al., 1994; Mougous et al., 2006; Schmeing et al., 2009; Thirup et al., 2015; Vitagliano et al., 2001). Protein accession numbers from the NCBI database or gene IDs from the IMG database are shown in parentheses. Black dots on the branches represent Bayesian posterior probability values greater than 90%, and scale bar indicates the number of amino acid substitutions per site.