Bioinformatics analysis of small G protein CaROP in pepper
[Objective]To clarify the biological function,physicochemical properties,protein structure and phylogenetic relationship of small G protein CaROP in pepper.[Methods]In this study,the physico-chemical properties of nine CaROP proteins were analyzed by using bioinformatics software such as ProtParam,ProtScale,SignalP5.0,TMHMM,NetPhos3.1 and NetCGlyc1.0;The structures of 9 CaROP proteins were pre-dicted and analyzed by using SOPMA,SWISS-MODEL and other bioinformatics software;The phylogenetic relationship of 9 CaROP proteins was analyzed by using bioinformatics software MEGA11.[Results]The re-sults of protein physicochemical properties analysis showed that the total average hydrophilicity of 9 CaROP proteins was less than 0,which were all hydrophilic proteins,and 6 of them were stable hydrophilic proteins;None of the 9 CaROP proteins had signal peptide,namely,they were non secretory proteins;Nine CaROP pro-teins had no transmembrane domain,namely,none of them were membrane proteins;All 9 CaROP proteins had phosphorylation sites and none had glycosylation sites.The results of protein structure prediction and analysis showed that the main secondary structural elements of 9 CaROP proteins were irregular curls and α-Spiral,followed by β-Fold,finally β-Corner.Phylogenetic analysis showed that nine CaROP proteins were clus-tered into four branches,of which each of branch I and branch III contained one CaROP protein,branch II con-tained two CaROP proteins,and the other five CaROP proteins were clustered in branch IV.[Conclusion]Nine CaROP proteins have the Rhoa domain and are all non-secretory hydrophilicproteins.The nine CaROP proteins were clustered into four branches in thephylogenetic tree,and the prediction results of their tertiary structure modeling were also ideal.The structure of the nine CaROP proteins was relatively stable.
peppersmall G protein ROPphysical and chemical properties of proteinprotein struc-turephylogenetic relationship
万方数据
维普
