Abstract
Calmodulin is one of the calcium-binding proteins and is distributed widely in eukaryotes. The amino acid sequences were studied of calmodulin taken from bovine brain, scallop ( Patinopecten), sea anemone ( Metridium senile) and tetrahymena ( Tetrahymena pyriformis). One notable feature of the primary structure of calmodulin is its internal homology. It can be subdivided into four domains with similar amino acid sequences. This homology implies that the primary structure of calmodulin has been elongated twice by intragenic duplication. Using this intragenic duplication model, the amino acid sequences of calmodulin from those four species were analyzed in detail. This kind of approach has proved very useful for investigation of the origin and evolution of this protein.
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