A. Keith Dunker(email@example.com)
Ethan C. Garner(firstname.lastname@example.org)
Celeste J. Brown(email@example.com)
School of Molecular Biosciences, Washington State University, Pullman,
WA 99164-4660, USA
School of Electrical Engineering and Computer Sciences,
Washington State University, Pullman, WA 99164-2752, USA
Intrinsic protein disorder refers to segments or to whole proteins that fail to fold completely on their own. Here we predicted disorder on protein sequences from 34 genomes, including 22 bacteria, 7 archaea, and 5 eucaryotes. Predicted disordered segments ≥ 50, ≥ 40, and ≥ 30 in length were determined as well as proteins estimated to be wholly disordered. The five eucaryotes were separated from bacteria and archaea by having the highest percentages of sequences predicted to have disordered segments ≥ 50 in length: from 25% for Plasmodium to 41% for Drosophila. Estimates of wholly disordered proteins in the bacteria ranged from 1% to 8%, averaging to 3 ± 2%, estimates in various archaea ranged from 2 to 11%, plus an apparently anomalous 18%, averaging to 7 ± 5% that drops to 5 ± 3% if the high value is discarded. Estimates in the 5 eucarya ranged from 3 to 17%. The putative wholly disordered proteins were often ribosomal proteins, but in addition about equal numbers were of known and unknown function. Overall, intrinsic disorder appears to be a common, with eucaryotes perhaps having a higher percentage of native disorder than archaea or bacteria.