Evolution of substrate specificities in the P-type ATPase superfamily.
P-type ATPases make up a large superfamily of ATP-driven pumps involved in the transmembrane transport of charged substrates. We have performed an analysis of conserved core sequences in 159 P-type ATPases. The various ATPases group together in five major branches according to substrate specificity, and not according to the evolutionary relationship of the parental species, indicating that invention of new substrate specificities is accompanied by abrupt changes in the rate of sequence evolution. A hitherto-unrecognized family of P-type ATPases has been identified that is expected to be represented in all the major phyla of eukarya.
Axelsen
K B
KB
Department of Plant Physiology, Institute of Molecular Biology, Copenhagen University, Oster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark. axe.biobase.dk
Palmgren
M G
MG
D000251:Adenosine Triphosphatases / Q000145:classification* / Q000502:physiology*; D000595:Amino Acid Sequence; D000818:Animals; D001105:Archaea / Q000201:enzymology; D001419:Bacteria / Q000201:enzymology; D001665:Binding Sites; D017124:Conserved Sequence; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013379:Substrate Specificity
D000251:Adenosine Triphosphatases