Figure S1.
Multiple sequence alignment of vertebrate TTLL5 CID and RPGR BD. (A) TTLL5 CID. (B) RPGR miniBD. Secondary structure elements indicated above the sequence and based on our X-ray crystal structure of the complex; gaps of disordered, unmodeled residues are indicated by a dotted line. Hydrophobic residues at the CID–BD interface indicated with blue boxes. Residues mutated for ITC experiments indicated with black arrows above the sequence. Refer to the image caption for details. Panel A shows a multiple sequence alignment that compares a conserved protein region across several vertebrate species with annotated secondary structure elements and highlighted conserved residues. Panel B shows a sequence alignment representing a short conserved peptide region from different species, with residues highlighted to indicate conserved and functionally important positions.

Multiple sequence alignment of vertebrate TTLL5 CID and RPGR BD. (A) TTLL5 CID. (B) RPGR miniBD. Secondary structure elements indicated above the sequence and based on our X-ray crystal structure of the complex; gaps of disordered, unmodeled residues are indicated by a dotted line. Hydrophobic residues at the CID–BD interface indicated with blue boxes. Residues mutated for ITC experiments indicated with black arrows above the sequence.

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