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Molecular signatures in protein sequences that are characteristic of cyanobacteria and plastid homologues, by R. S. Gupta, M. Pereira, C. Chandrasekera & V. Johari

International Journal of Systematic and Evolutionary Microbiology vol. 53, part 6, pp. 1833 – 1842

Supplementary Fig. A. Partial alignment of DNA helicase II (UvrD) sequences showing two additional signature sequences (boxed) that are characteristic of cyanobacteria. Dashes in the alignment indicate identity to the amino acid on the top line.

Supplementary Fig. B. Partial alignment of EF-Tu sequences showing a 5 aa conserved insert (boxed) that is characteristic of cyanobacteria and plastid homologues.

Supplementary Fig. C. Partial alignment of ribosomal S1 protein sequences showing two signatures (comprising of 2 aa and 7 aa deletions, underneath the boxed regions) that are characteristic of cyanobacteria. Most cyanobacteria have two different homologues of the S1 proteins, both of which lack these indels. The inserts are also not present in the plastid homologues.

Supplementary Fig. D. Partial alignment of inosine-5'-monophosphate dehydrogenease sequences showing two conserved signatures (a 1 aa deletion and a 6 aa insert) that are characteristic of cyanobacteria. The eukaryotic homologues are probably of either mitochondrial or nuclear–cytosolic origin.

Supplementary Fig. E. Partial alignment of sequences of the major sigma factor, ⁷⁰, showing a 1 aa deletion that is characteristic of cyanobacteria. Surprisingly, this insert is not found in the plastid homologues indicated.

Supplementary Fig. F. Partial alignment of the FtsH protein showing a 3 aa insert (boxed) that is characteristic of cyanobacteria. Cyanobacteria have two different FtsH homologues, of which only one contains this insert. The insert is also present in at least one of the plastid homologues.

[Single PDF of Supplementary Figs A–F] (153 KB)

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