Evolutionary classification,structure and physicochemical properties of apple small G protein MdoROP
[Objective]To obtain six MdoROP proteins and analyze their motif composition,phylogenetic relationship,protein structure and physicochemical properties.[Method]Apple leaves were taken for ex vivo sterilization,and various bioinformatics software such as SMARTS and MEGA 11 were used to predict and analyze them.[Result]The MdoROP proteins can be cate-gorized into the same class and all have no specific motifs based on differences in the composition of the protein motifs.It is shown that the above 6 motifs are the conserved motifs of 6 MdoROP proteins.The length of MdoROP protein was between 197-211 aa;The fat index is between 87.24-92.56;The molecular weight of protein is 21 463.75-23 587.2 Da;The hydro-philicity of 6 MdoROP proteins was between-0.125--0.077 and all were negative,and all 6 MdoROP proteins were alka-line hydrophilic proteins,all of which were localized to cell membrane,cytoplasm and nucleus and did not have signal peptides and transmembrane domains.The secondary structural elements of MdoROP protein are mainly irregular coil and α helix.[Con-clusion]The six MdoROP proteins belong to the small G protein ROP family of apples,which are phosphorylated proteins and basic hydrophilic proteins,neither of which are secreted proteins or membrane proteins.Irregular coils and α helixes were the main secondary structures of the six MdoROP proteins,and the prediction results of the tertiary structure of ROP genes were consistent with the secondary structure.In summary,the results of this study will lay a strong foundation and provide theoretical support for the subsequent in-depth study of the biological function of MdoROP protein.It contributes to the subsequent in-depth study of the biological functions of apple MdoROP proteins.
applesmall G protein MdoROPphylogenetic relationshipphysicochemical propertiesprotein structure
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