Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction -- Shevtsov et al. 102 (49): 17600 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Shevtsov et al. 10.1073/pnas.0508728102.

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Fig. 6. Multiple sequence alignment of anti-TRAP protein (AT) with DnaJ segments containing cysteine-rich motifs. AT is represented by proteins from Bacillus subtilis and Bacillus licheniformis. DnaJ is represented by bacterial sequences (EcoDnaJ, Escherichia coli; BsubDnaJ, B. subtilis; BlichDnaJ, B. licheniformis; BhalDnaJ, Bacillus halodurans; MtuDnaJ, Mycobacterium tuberculosis), archaeal sequences (MthDnaJ, Methanosarcina thermophila; MethDnaJ, Methanothermobacter thermautotrophicus), and eukaryotic sequences (SavDnaJ, Streptomyces avermitilis; SceDnaJ(Ydj1), Saccharomyces cerevisiae; PfaDnaJ(Pfj1), Plasmodium falciparum; HsaDnaJ, Homo sapiens). The Cys and Gly residues of the C-X-X-C-X-G-X-G motif are highlighted by red and blue frames, respectively. Secondary structure of AT, determined in this study, is shown on the top of the figure (h, helix; e, strand).