Extended Data Fig. 9: Domain analysis and homology-based structure prediction of a bacterial TIR–STING protein.
From: Cyclic GMP–AMP signalling protects bacteria against viral infection
a, Schematics of HHpred29 homology-based search results of the Prevotella corporis TIR–STING protein (Supplementary Table 1). b, Phyre235 secondary structure prediction of the TIR domain in the P. corporis TIR–STING protein, compared to the solved crystal structure of the human TIR domain protein MyD88 (PDB accession 2Z5V_A). c, Phyre235 secondary structure prediction of the STING domain in the P. corporis TIR–STING protein, compared to the solved crystal structure of the human STING protein (PDB accession 5BQX_A). Black, identical residues; grey, similar residues. Secondary structure prediction for the bacterial protein appears above the alignment; secondary structure of solved human domain appears below the alignment. d, Structural alignment of human TIR domain protein MYD88 and the modelled bacterial TIR domain. e, Structural alignment of human STING domain and the modelled bacterial STING domain. In d, e, blue and red represent the structure of the human protein and the model of the bacterial domain structure, respectively.
