Sequence homology between EF-1 alpha, the alpha-chain of elongation factor 1 from Artemia salina and elongation factor EF-Tu from Escherichia coli.
In the course of a structural analysis of the alpha-chain of elongation factor 1 from Artemia salina cysts, we present four amino acid sequences comprising together half of the polypeptide chain. A comparison of these sequences with the primary structure of elongation factor EF-Tu from Escherichia coli reveals a clear correspondence between the eukaryotic and prokaryotic protein throughout their polypeptide chains. The results support a basic conservation of the structure of the aminoacyl-tRNA carrying enzyme in evolution. The occurrence, in the eukaryotic factor, of several epsilon-trimethyllysine residues, is remarkable.
D000595:Amino Acid Sequence; D000818:Animals; D001156:Artemia / Q000032:analysis*; D005075:Biological Evolution; D004926:Escherichia coli / Q000032:analysis*; D020648:Peptide Elongation Factor 1; D010444:Peptide Elongation Factor Tu; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D014357:Trypsin
D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D010446:Peptide Fragments; D014357:Trypsin; D010444:Peptide Elongation Factor Tu