Skip to main content
Fig. 3 | BMC Genomics

Fig. 3

From: Genome-wide identification and characterization of superoxide dismutases in four oyster species reveals functional differentiation in response to biotic and abiotic stress

Fig. 3

Phylogenetic, Motif/domain, conserved ligands, and protein model analysis of SODs revealed the function diversity. cg: Crassostrea gigas, cv: Crassostrea virginica, CH: Crassostrea hongkongensis, Sgl: Saccostrea glomerata, H_sapiens: Homo sapiens, M_musculus: Mus musculus, D_rerio: Danio rerio, D_melanogaster: Drosophila melanogaster, and C_elegans: Caenorhabditis elegans. “I” to “VI” represented the six clades. Circles, triangles, and no mark near the tree represented the cytosolic, mitochondrial, and extracellular sub-cellular of SODs, respectively. The proteins in seven colors represented the protein models predicted by phyre2. In the Domain/motif part, colored cylinders (green and pink) represent the Cu/Zn-SOD and Mn-SOD domains. The rectangles numbered one to thirteen represent motifs. The Conserved Ligands part displayed the most important ligands for enzyme activity of SODs. The “i”,“ii”,“iii”, and “iv”in both second and third part were the numeric of multi-domain Cu/Zn-SOD (clade I). “a” to “g” in the third and fourth part represented the corresponding models of encoded proteins. In the protein model part, the models were predicted by SWISS-MODEL based on the model predicted in phyre2, so, the same color of the letters in the first, third, and fourth part were same. The orange sphere in “a” and “b” was the copper ion, the blue sphere in “b” and “c” was zinc ion, the purple sphere in “g” was manganese ion

Back to article page