Conservation of TLNRD1 and its alignment with talin R7R8 domains. (A) Amino acid sequence alignment of human TLNRD1 (UniProt accession no. Q9H1K6) and talin1 residues 1357–1653 encompassing R7R8 (UniProt accession no. Q9Y490). Domain boundaries are highlighted with orange corresponding to the four-helix domain and blue corresponding to the five-helix domain. (B) Tree diagram representing TLNRD1 presence and absence over evolution. TLNRD1 first appears in choanoflagellates and sponges and is conserved throughout vertebrate evolution. TLNRD1 has been lost from nematodes, arthropods, and Cnidaria. (C) TLNRD1-FL sequence conservation mapped onto the full-length TLNRD1 structure using ConSurf (Ashkenazy et al., 2016). Structure colored according to extent of conservation with blue indicating variability and purple indicating highly conserved residues. Residues important for dimerization (Q213, R246, F250, A260, and E267) are highlighted.
Figure S1.

Conservation of TLNRD1 and its alignment with talin R7R8 domains. (A) Amino acid sequence alignment of human TLNRD1 (UniProt accession no. Q9H1K6) and talin1 residues 1357–1653 encompassing R7R8 (UniProt accession no. Q9Y490). Domain boundaries are highlighted with orange corresponding to the four-helix domain and blue corresponding to the five-helix domain. (B) Tree diagram representing TLNRD1 presence and absence over evolution. TLNRD1 first appears in choanoflagellates and sponges and is conserved throughout vertebrate evolution. TLNRD1 has been lost from nematodes, arthropods, and Cnidaria. (C) TLNRD1-FL sequence conservation mapped onto the full-length TLNRD1 structure using ConSurf (Ashkenazy et al., 2016). Structure colored according to extent of conservation with blue indicating variability and purple indicating highly conserved residues. Residues important for dimerization (Q213, R246, F250, A260, and E267) are highlighted.

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