Prediction of an Unknown Protein’s Function Responsive to Salinity Stress in Durum Wheat

Document Type : Research Paper

Authors

1 PhD, Department of Plant Breeding, Islamic Azad University, Science and Research Branch, Tehran, Iran

2 Assistant Professor, Department of Computer Engineering, Islamic Azad University, Kermanshah Branch, Kermanshah, Iran

Abstract

Soil salinity is one of the most important factors in reducing the yield of durum wheat in Iran. high-throughput technologies advancement, while accelerating the production process of tolerant cultivars to ambience stresses, have made determining the function of newly discovered proteins a major challenge by generating large genomie informatics data. Therefore, the aim of this study was to predict the tertiary structure and function of unknown proteins responsive to salinity stress in durum wheat. The results of phyre software showed that the tertiary structure of the protein sequence has homology with A0A452XZB6 protein with 385 residues, 25 alpha helices and 23 beta sheets from the structural classification of Uniprot protein with E-value 1e-66 and 87 percent accuracy of assessment. The STRING site matched the protein function prediction with a localized Na+/H+ exchanger in the plasmamembrane. Prediction of transmembrane domains, identification of PTMs, and protein-specific motifs indicated that activation of this antiporter is probably accomplished by phosphorylation of serine threonine residues and plays an important role in salinity tolerance of durum wheat. This study provides a framework for future studies on the role of Na+/H+ plasma membrane exchangers and its relative contribution to the maintenance of cellular Na+ homeostasis in tolerance of durum wheat cultivars in saline soils.

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Volume 12, Issue 1
September 2021
Pages 59-66

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