Cloning and sequence analysis of Astacin like metalloproteinase gene from Indian oyster, Magallana bilineata (R?ding, 1798)

Abstract

Astacins are a group of zinc-dependent metalloproteases with diverse roles in biological systems such as embryonic development, connective tissue remodelling, digestion, and processing of biologically active peptides. This paper describes the cloning of an Astacin like metalloproteinase (Mbi-ALMP) from the digestive tissues of Magallana bilineata. The Mbi-ALMP encodes a deduced 440 amino acid protein which includes an N-terminal signal peptide. The Mbi-ALMP possesses several of the characteristic features of the Astacin family like the pro-peptide domain, Astacin catalytic domain with Zinc binding motif, and met-turn, followed by a MAM (meprin, A5 protein, receptor protein-tyrosine phosphatase ?) carboxy-terminal domain. Amino acid sequence alignment and phylogenetic analysis of the protease domain indicate Mbi-ALMP to have a high degree of sequence homology to other Astacin like metalloproteases from different species.