(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Platyhelminthes: NE > Trematoda: NE > Digenea: NE > Opisthorchiida: NE > Opisthorchiata: NE > Opisthorchiidae: NE > Clonorchis: NE > Clonorchis sinensis: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA DPEILENATQIIRNYGFHVEEHYVKTADGYILCLIRMRNPNIELNKKVVF LQHGLLDSAHTWINNLRNQSLAFILADAGFDVWLGNSRGSTYSRKHEKYD THHIEFWEFSWDQMAQFDLPASLYHVLQVSGSNTVGYVGHSQGAQIALAQ FNRDPELQSHISLFVALAPVAYLGNIASPIRYIAPFARTVERVWDLFGHG EFLSSTRLLHFLAYFLCGRGHIPFVCTNVVYLLAGYDARNTNLTRLPVYI AHTPAGTSAKNMVHYCQGISTDQFQAFDYGKVKNLEIYGQKTPPKYDLSK FTVPTAVFSGGNDWLAVEKDVDRLIDQIKPAVISHINFPEYNHLDFVWGM DAAIVLYPEVLRLLNQY
Reference
Title: Cloning, characterization, and expression of a novel secretory lipase-like gene from Clonorchis sinensis Hu F, Chen W, Li L, Lu Y, Song W, Kuang Y, Zhang F Ref: Parasitol Res, 105:1661, 2009 : PubMed
A secretory lipase-like gene was isolated from total cDNA of adult Clonorchis sinensis. The gene has an open reading frame of 1,218 bp long and encodes for a protein of 406 amino acids including a putative signal peptide of 20 amino acids. The deduced amino acid sequence including signal peptide has 42-45% identity with lipase of other species and two typical enzymic active sites that contain consensus sequence (Gly-X-Ser-X-Gly) of lipase. The cDNA encoding this protein was subcloned into pET-28a (+) expression vector and expressed in Escherichia coli. The expressed fusion protein has a molecular mass of about 45 kDa. Prediction of signal peptide and Western blot analysis indicated that the secretory lipase-like protein is an excretory-secretory product of C. sinensis. Immunostaining revealed that the secretory lipase-like protein was localized in the tegument of the adult worm and metacercaria. These results provide basis for further studies on the nutrition taking and invasion of C. sinensis mediated by the secretory lipase-like protein.
