Journal of Molecular Evolution

, Volume 45, Issue 5, pp 549–563

The Evolution of the Conserved ATPase Domain (CAD): Reconstructing the History of an Ancient Protein Module

  • Jonathan C.  Swaffield
  • Michael D.  Purugganan

DOI: 10.1007/PL00006259

Cite this article as:
Swaffield, J. & Purugganan, M. J Mol Evol (1997) 45: 549. doi:10.1007/PL00006259


The AAA proteins (ATPases Associated with a variety of cellular Activities) are found in eubacterial, archaebacterial, and eukaryotic species and participate in a large number of cellular processes, including protein degradation, vesicle fusion, cell cycle control, and cellular secretory processes. The AAA proteins are characterized by the presence of a 230 to 250-amino acid ATPase domain referred to as the Conserved ATPase Domain or CAD. Phylogenetic analysis of 133 CAD sequences from 38 species reveal that AAA CADs are organized into discrete groups that are related not only in structure but in cellular function. Evolutionary analyses also indicate that the CAD was present in the last common ancestor of eubacteria, archaebacteria, and eukaryotes. The eubacterial CADs are found in metalloproteases, while CAD-containing proteins in the archaebacterial and eukaryotic lineages appear to have diversified by a series of gene duplication events that lead to the establishment of different functional AAA proteins, including proteasomal regulatory, NSF/Sec, and Pas proteins. The phylogeny of the CADs provides the basis for establishing the patterns of evolutionary change that characterize the AAA proteins.

Key words: AAA proteins — ATPase — Proteasome — NSF — Sec — Pas — Metalloprotease 

Copyright information

© Springer-Verlag New York Inc. 1997

Authors and Affiliations

  • Jonathan C.  Swaffield
    • 1
  • Michael D.  Purugganan
    • 1
  1. 1.Department of Genetics, North Carolina State University, P.O. Box 7614, Raleigh, NC 27695-7614, USAUS

Personalised recommendations