Additional file 19.

Amino acid sequence alignment of selected G-domains. Amino acid sequence alignment of the G-domains of Irga6, Irgb6 and Irgm3 form Mus musculus (MM), Ffh and FtsY from Thermus aquaticus (TA). The positions of G1, G3, G4 and G5 were fixed manually. Irga6 residues of the catalytic interface (Additional file 8 and 8) are highlighted in red. Residues buried in the interface of the Ffh-FtsY dimer (PDB 1RJ9) [20] were calculated with CNSsolve [59] module buried surface [60] with a probe radius of 1.4 Å and are highlighted in red. The tendency of the interface residues to align reflects the almost equal relative spatial orientation of the G-domains in the complexes and conserved structural features of G-domains. The G1, G3, G4 and G5-motifs are highlighted by a green box.

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Pawlowski et al. BMC Biology 2011 9:7   doi:10.1186/1741-7007-9-7