Primary sequence of a putative non-ATPase subunit of the 26S proteasome from Entamoeba histolytica is similar to the human and yeast S2 subunit.
The cDNA coding for a non-ATPase S2 subunit of the 26S proteasome from Entamoeba histolytica was cloned from a cDNA library (EhS2). The open reading frame has 2529 bp and the deduced amino acid sequence encodes a protein with a calculated molecular mass of 92,000 Da. EhS2 has 29-35% identity with the three other known S2 subunit sequences of yeasts and humans.
Hellberg
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A
Bernhard Nocht Institute for Tropical Medicine, Hamburg, Gerrmany.
Sommer
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Bruchhaus
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I
D000595:Amino Acid Sequence; D000818:Animals; D015152:Blotting, Northern; D015139:Blotting, Southern; D018076:DNA, Complementary; D016054:DNA, Protozoan; D004748:Entamoeba histolytica / Q000201:enzymology* / Q000235:genetics; D006801:Humans; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000235:genetics; D046988:Proteasome Endopeptidase Complex; D017386:Sequence Homology, Amino Acid; D015003:Yeasts / Q000201:enzymology / Q000235:genetics
D018076:DNA, Complementary; D016054:DNA, Protozoan; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease