author(s)
Manchi Rajesh, Biju Sam Kamalam, Alexander Ciji, Md. Shabaz Akhtar, Debajit Sarma, Narrotam Prasad Sahu and Atul Kumar Singh

abstract
In this manuscript, we report the cloning and in silico characterization of elongation factor 1A in a coldwater Trans-Himalayan cyprinid, Schizothorax richardsonii. The sequenced elongation factor 1A (SrEF1A) consisted of 1290 bp long partial ORF, which included a start codon (ATG) and 430 deduced amino acids. The SrEF1A sequence showed high homology (≥90%) with other teleosts and higher vertebrates. Phylogenetic analysis, multiple sequence alignment and prediction of conserved residues indicated a close evolutionary relationship among the cyprinids and conservation of SrEF1A protein across the vertebrate class. The deduced SrEF1A protein did not contain any signal peptide, but had two potential N-glycosylation motifs at 284^th and 314^th amino acid residue. Presence of many serine, threonine and tyrosine phosphorylation sites was also predicted, suggesting a potential post-translational regulation of the SrEF1A protein. In silico predictions of sub-cellular localization, function and protein-protein network illustrate the role of SrEF1A in the protein synthesis machinery of the cell. Finally, a reliable tertiary structure of SrEF1A protein was predicted with ten helixes and nineteen beta sheets. Ligand (GDP) binding sites in the tertiary structure were predicted at 15-22, 154, 156, 157 and 194-196 amino acid residues.