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bacteriorhodopsin
The bacterial opsins are retinal-binding proteins that provide light- dependent ion transport and sensory functions to a family of halophilic bacteria [2,3]. They are integral membrane proteins believed to contain seven transmembrane (TM) domains, the last of which contains the attachment point for retinal (a conserved lysine). This family also includes distantly related proteins that do not contain the retinal binding lysine and so cannot function as opsins. Some fungal examples are: Swiss:O74870, Swiss:P25619, Swiss:P38079, Swiss:Q12117. [1]. 8676377. Electron-crystallographic refinement of the structure of bacteriorhodopsin. Grigorieff N, Ceska TA, Downing KH, Baldwin JM, Henderson R;. J Mol Biol 1996;259:393-421. [2]. 2468194. Two pumps, one principle: light-driven ion transport in halobacteria. Oesterhelt D, Tittor J;. Trends Biochem Sci. 1989;14:57-61. [3]. 2591367. Primary structure of sensory rhodopsin I, a prokaryotic photoreceptor. Blanck A, Oesterhelt D, Ferrando E, Schegk ES, Lottspeich F;. EMBO J. 1989;8:3963-3971. (from Pfam)
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