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. 2015 Dec 13;5(2):212–223. doi: 10.1002/mbo3.321

Table 2.

Amino acid sequence alignment of the C‐helix in various microbial rhodopsins

Rhodopsin type Amino acid residue number in BR, PR, and NaR
BR 82 83 84 85 86 87 88 89 90 91 92 93 94 95 96
PR 94 95 96 97 98 99 100 101 102 103 104 105 106 107 108
NaR 109 110 111 112 113 114 115 116 117 118 119 120 121 122 123
BR R Y A D W L F T T P L L L L D
PR R Y I D W L L T V P L L I C E
NaRa R Y L N W L I D V P M L L F Q
ClRb R Y V N W M A T I P C L L L Q
XR R Y V D W L L T V P L L T V E
ActR R Y V D W L L T V P L L T V E
HR R Y L T W A F S T P F I L L A
SRI R Y V D W V V T T P L L V G F
SRII R Y I D W L V T T P L I V L Y
PRc R Y V D W V or I L T V P L M C V E
NaRc R Y L N W L I or T D V P M L L F Q
ClRc R Y V N W M A T I P C L L V Q

The bold indicates active site residues of microbial rhodopsins. This analysis was conducted as described by Inoue et al. (2013). PR, proteorhodopsin; BR, Bacteriorhodopsin; NaR, Sodium ion rhodopsin; ClR, chloride ion rhodopsin; XR, Xanthorhodopsin; ActR, Actinorhodopsin; SRI, sensory rhodopsin I; SRII, sensory rhodopsin II.

a

K. eikastus NBRC 100814T and N. dokdonensis DSW‐6T.

b

N. marinus S1‐08T.

c

Indicates the rhodopsins discovered during this study.