3AM6


Conserved Protein Domain Family
7tm_ARII-like

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cd15238: 7tm_ARII-like 
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Acetabularia rhodopsin II and similar proteins, member of the seven-transmembrane GPCR superfamily
This subgroup includes the eukaryotic light-driven proton-pumping Acetabularia rhodopsin II from the giant unicellular marine alga Acetabularis acetabulum, as well as its closely related proteins. They belong to the microbial rhodopsin family, also known as type I rhodopsins, comprising the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-gated cation channel channelrhodopsin (ChR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), and the other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. Microbial rhodopsins have been found in various single-celled microorganisms from all three domains of life, including halophile archaea, gamma-proteobacteria, cyanobacteria, fungi, and green algae. While microbial (type 1) and animal (type 2) rhodopsins have no sequence similarity with each other, they share a common architecture consisting of seven-transmembrane alpha-helices (TM) connected by extracellular loops and intracellular loops. Both types of rhodopsins consist of opsin and a covalently attached retinal (the aldehyde of vitamin A), a photoreactive chromophore, via a protonated Schiff base linkage to an amino group of lysine in the middle of the seventh transmembrane helix (TM7). Upon the absorption of light, microbial rhodopsins undergo light-induced photoisomerization of all-trans retinal into the 13-cis isomer, whereas the photoisomerization of 11-cis retinal to all-trans isomer occurs in the animal rhodopsins. While animal visual rhodopsins are activated by light to catalyze GDP/GTP exchange in the alpha subunit of the retinal G protein transducin (Gt), microbial rhodopsins do not activate G proteins, but instead can function as light-dependent ion pumps, cation channels, and sensors.
Statistics
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PSSM-Id: 320366
View PSSM: cd15238
Aligned: 3 rows
Threshold Bit Score: 296.399
Threshold Setting Gi: 339717433
Created: 16-Feb-2014
Updated: 26-Jul-2017
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 16 residues -Click on image for an interactive view with Cn3D
Feature 1:ligand binding site [chemical binding site]
Evidence:
  • Structure:3AM6: Acetabularia acetabulum proton pumping rhodopsin Ar2 binds retinal, contacts at 4A.
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
3AM6_A         7 ETGMIAQWIVFAIMAAAAIAFGVAVHFRPSelKSAYYINIAICTIAATAYYAMAVnyqdltm-----ngerqvvYARYID 81
gi 385283154   8 EGGLVMYWVTFGLMAFSALAFAVMTFTRPLnkRSHGYITLAIVTIAAIAYYAMAAsggkalvsn-pdgnlrdiyYARYID 86
gi 333031605  10 TLGTDAQWVVFAVMALAAIVFSIAVQFRPLplRLTYYVNIAICTIAATAYYAMAVnggdnkptagtgaderqviYARYID 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        #  ##                           #   #               #  ##  #                    
3AM6_A        82 WVLTTPLLLLDLIVMTKmggVMISWVIGADIFMIVFGILGAfedehkfKWVYFIAGCVMQAVLTYGMYNATWKddlkkSP 161
gi 385283154  87 WFFTTPLLLLDIILLTGipiGVTLWIVLADVAMIMLGLFGAlst-nsyRWGYYGVSCAFFFVVLWGLFFPGAKgararGG 165
gi 333031605  90 WVFTTPLLLLDLVLLTNmpaTMIAWIMGADIAMIAFGIIGAftv-gsyKWFYFVVGCIMLAVLAWGMINPIFKeelqkHK 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
Feature 1                        #  ##  #                     #  ##           
3AM6_A       162 EYHSSYVSLLVFLSILWVFYPVVWAFGsgsgvlsvDNEAILMGILDVLAKPLFGMGCLIAH 222
gi 385283154 166 QVPGLYFGLAGYLALLWFGYPIVWGLAegsdyisvTAEAASYAGLDIAAKVVFGWAVMLSH 226
gi 333031605 169 EYTGAYTTLLIYLIVLWVIYPIVWGLGagghiigvDVEIIAMGILDLLAKPLYAIGVLITV 229

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