Abstract:In order to analyze the conserved regions and the evolutionary relationship of fungal α-L-rhamnosidase in glucoside hydrolase family 78 (GH78), 87 sequences of GH78 fungal α-L-rhamnosidases were collected and compared by ClustalW2 software. In addition, the conserved amino acid sites and the common conserved regions of GH78 fungal α-L-rhamnosidases were obtained by Block Maker. Meanwhile, the signal peptide was predicted by SignalP 4.1 Server. Besides, the genetic distance and the phylogenetic tree of 87 sequences were constructed by MEGA6.0 software. Although the amino acid sequences of fungal α-L-rhamnosidases had various lengths, all contained three conserved regions, including AHGWSTGPTY, VTLDTGQNVAG and NELSIPTDGAKRD, as well as a number of conserved amino acid sites. Moreover, 29 sequences contained signal peptides. The genetic distance between the genera was from 0.7 to 48.5, and the genetic distance of interspecies was from 0.4 to 48.5. Interestingly, it was found that the phylogenetic tree of the phylogenetic system was not clustered by the source of the strain, but on whether the extracellular enzyme was clustered. In this study, the conserved region and evolutionary relationships of GH78 α-L-rhamnosidases were analyzed, which laid the foundation for engineering modification of α-L-rhamnosidase.
