Abstract
We have cloned a gene, pepC, encoding a serine proteinase, PEPC, from Aspergillus niger by screening a phage λ genomic DNA library with a gene ( PRB1) from Saccharomyces cerevisiae which codes for proteinase YscB. The nucleotide (nt) sequence of pepC revealed that the gene is composed of two exons of 369 nt and 1230 nt separated by a single 70-nt intron. The deduced protein of 533 amino acids (aa) has a putative signal sequence for transport into the endoplasmic reticulum. Based on the extensive homology shown with serine proteinases (SerP) of the subtilisin family, which includes the active site triad, we hypothesise that the protein is made as a larger precursor which is matured by the cleavage of 130–140 aa from its N terminus and possibly by the removal of approx. 70 aa from its C terminus.
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