FB2026_02 , released June 18, 2026
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Citation
Swaffield, J.C., Purugganan, M.D. (1997). The evolution of the conserved ATPase domain (CAD): reconstructing the history of an ancient protein module.  J. Mol. Evol. 45(5): 549--563.
FlyBase ID
FBrf0099556
Publication Type
Research paper
Abstract
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.
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    J. Mol. Evol.
    Title
    Journal of Molecular Evolution
    Publication Year
    1971-
    ISBN/ISSN
    0022-2844
    Data From Reference
    Genes (3)