Summary: Copies of a multi-gene family, named (protease 1, encoding a subtilisin-like serine protease were cloned from the opportunistic fungal pathogen Comparison of the nucleotide sequence of a genomic clone and a cDNA clone of from f. sp. revealed the presence of seven short introns. Several different domains were predicted from the deduced amino acid sequence: an N-terminal hydrophobic signal sequence, a pro-domain, a subtilisin-like catalytic domain, a P-domain (essential for proteolytic activity), a proline-rich domain, a serine/threonine-rich domain and a C-terminal hydrophobic domain. The catalytic domain showed high homology to other eukaryotic subtilisin-like serine proteases and possessed the three essential residues of the catalytic active site. Karyotypic analysis showed that was a multi-gene family, copies of which were present on all but one of the f. sp. chromosomes. The different copies of the genes showed nucleotide sequence heterogeneity, the highest level of divergence being in the proline-rich domain, which varied in both length and composition. Some copies of were contiguous with genes encoding the major surface glycoprotein.


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