Homology of functionally diverse proteins.
Disulphide-rich proteins of widely differing functions were aligned with the aid of their half-cystinyl residues. This led to the grouping of ribonuclease, phospholipase A, lysozyme, snake venom toxins, bee and scorpion venom peptides, and the plant proteins potatoe carboxypeptidase inhibitor, ragweed pollen allergen, mistletoe toxins and pineapple sulfhydryl protease inhibitor into one super-family of proteins. Very few deletions/insertions were needed to effect alignment and probabilities were calculated for random occurrence of the matches that were found.
D000485:Allergens / Q000032:analysis; D000595:Amino Acid Sequence; D001516:Bees; D003553:Cystine; D004220:Disulfides; D004791:Enzyme Inhibitors / Q000032:analysis; D007768:Lactalbumin / Q000032:analysis; D009113:Muramidase / Q000032:analysis; D010740:Phospholipases / Q000032:analysis; D011487:Protein Conformation; D011506:Proteins / Q000032:analysis*; D012260:Ribonucleases / Q000032:analysis; D012605:Scorpions; D012910:Snake Venoms / Q000032:analysis; D013223:Statistics as Topic; D014118:Toxins, Biological / Q000032:analysis; D014688:Venoms / Q000032:analysis
D000485:Allergens; D004220:Disulfides; D004791:Enzyme Inhibitors; D011506:Proteins; D012910:Snake Venoms; D014118:Toxins, Biological; D014688:Venoms; D003553:Cystine; D007768:Lactalbumin; D010740:Phospholipases; D012260:Ribonucleases; D009113:Muramidase