Brr6 structure, mutations, and homology domains. (A) A cartoon of the Brr6 protein. The brr6.ds1 and brr6.ts8 mutations are indicated in red and orange, respectively. The domains predicted to span membranes are shown with blue hatching and the highly conserved cysteines are indicated by “C.” (B) Multiple sequence alignment of the conserved domains of Brr6-related proteins from the following organisms: Spom, Schizosaccharomyces pombe; Sjap, Schizosaccharomyces japonicus; Afum, Aspergillus fumigatus; Scer, Saccharomyces cerevisiae; Fneo, Filobasidiella neoformans var. neoformans; Pmar, Perkinsus marinus; Ddis, Dictyostelium discoideum; Pfal, Plasmodium falciparum; and Cpar, Cryptosporidium parvum. Amino acid sequences were aligned with the ClustalW program. Identical residues are indicated by black shading, conserved residues by gray. The single, large letters below the alignment highlight some key conserved amino acids, whereas the blocks of stripped blue shading above the alignments correspond to the hydrophobic stretches indicated in A.