Research article
Widespread presence of "bacterial-like" PPP phosphatases in eukaryotes
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Corresponding authors: Alexandra V Andreeva aandreeva@brookes.ac.uk - Mikhail A Kutuzov m.kutuzov@usa.net
- † Equal contributors
1 Research School of Biological and Molecular Sciences, Oxford Brookes University, Headington, Oxford OX3 OBP, UK
2 Present address: University of Illinois, College of Medicine, Department of Pharmacology, 835 S. Wolcott Ave, Chicago, IL 60612, USA
BMC Evolutionary Biology 2004, 4:47 doi:10.1186/1471-2148-4-47
Published: 19 November 2004Additional files
Additional File 1:
Neighbor-Net analysis of the conserved N-terminal subdomains (starting 5 amino acid residues before conserved GDXHG and ending 25 residues after GNH(E/D) of 104 bacterial, archaeal and eukaryotic PPP phosphatases. This version of Figure 4 is the original SplitsTree file that can be viewed using SplitsTree, freely available for download (see Methods). Bootstrap values (out of 100 resamplings) are shown and can be highlighted by selecting corresponding alternative splits. The file also contains the alignment used for the analysis (Input).
Format: NEX Size: 2.2MB Download file
Additional File 2:
Distinct conserved motifs in the C-termini of bacterial and "bacterial-like" PPP phosphatases from eukaryotes as opposed to archaeal and eukaryotic PPP phosphatases. This is an expanded version of Figure 5.
Format: DOC Size: 31KB Download file
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