3A7K,2JAF,1E12


Conserved Protein Domain Family
7tm_Halorhodopsin

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cd15243: 7tm_Halorhodopsin 
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light-driven inward chloride pump halorhodopsin, member of the seven-transmembrane GPCR superfamily
Halorhodopsin (HR) acts as a light-driven inward-directed chloride pump. When activated by yellow light, HR pumps chloride ions into the cell cytoplasm, generating a negative-inside membrane potential which drives proton uptake. The resulting electrochemical ion gradient provides an energy source to the cell and contributes to pH homeostasis. HR is found in phylogenetically ancient archaea, known as halobacteria which live in high salty environments. HR belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising light-driven retinal-binding outward pump bacteriorhodopsin (BR), light-gated cation channel channelrhodopsin (ChR), light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR), and other light-driven proton pumps such as blue-light absorbing and green-light absorbing proteorhodopsins, among others. They 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: 320371
View PSSM: cd15243
Aligned: 7 rows
Threshold Bit Score: 309.809
Threshold Setting Gi: 122920878
Created: 16-Feb-2014
Updated: 26-Jul-2017
Structure
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Program:
Drawing:
Aligned Rows:
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Conserved site includes 18 residues -Click on image for an interactive view with Cn3D
Feature 1:putative ligand binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
3A7K_A        32 PLLASSLYINIALAGLSILLFVFMTRGLDDpraKLIAVSTILVPVVSIASYTGLASGLTISVLEMPAGHFAEGssvmlgg 111
2JAF_A        27 ALLSSSLWVNVALAGIAILVFVYMGRTIRPgrpRLIWGATLMIPLVSISSYLGLLSGLTVGMIEMPAGHALAGemv---- 102
1E12_A         6 ALLSSSLWVNVALAGIAILVFVYMGRTIRPgrpRLIWGATLMIPLVSISSYLGLLSGLTVGMIEMPAGHALAGemv---- 81
gi 429137137  25 TLLALSFVVNIALAGLTILFIVALARGVTDpraKLIVISTMLISVVSISSYTGLASGLTLSFIEMPAGHSLAGeev---- 100
gi 461609     32 TLLASSLWINIALAGLSILLFVYMGRNVEDpraQLIFVATLMVPLVSISSYTGLVSGLTVSFLEMPAGHALAGqev---- 107
gi 2829811    27 FLLNSSLWVNIALAGVVILLFVAMGRELESsraKLIWVATMLVPLVSISSYAGLASGLTVGFLQMPPGHALAGqev---- 102
gi 50400166    9 AALASSIYVNIALAGLTIIVIAVMSRSIHDsraKLITMSTLMISVVSISSYMGLASGLTIDPLVMPEGHPLAGqev---- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                    #  #  ##  #                        #   #                #  ##  #    
3A7K_A       112 eevdgvvtmWGRYLTWALSTPMILLALGLLAGsnaTKLFTAITFDIAMCVTGLAAALTTsshlmRWFWYAISCACFIVVL 191
2JAF_A       103 ------rsqWGRYLTWALSTPMILLALGLLADvdlGSLFTVIAADIGMCVTGLAAAMTTsallfRWAFYAISCAFFVVVL 176
1E12_A        82 ------rsqWGRYLTWALSTPMILLALGLLADvdlGSLFTVIAADIGMCVTGLAAAMTTsallfRWAFYAISCAFFVVVL 155
gi 429137137 101 ------ltmWGRYLTWAFSTPFILIVLGMIAGsniTKIMTTVAMTIAMCVTGLAAALTTssllmRWWWFVLSSAFFLVII 174
gi 461609    108 ------ltpWGRYLTWALSTPMILIAVGLLAGsntTKLFTAVVADIGMCVTGLAAALTTssyllRWVWYAISCAFFVVVL 181
gi 2829811   103 ------lspWGRYLTWTFSTPMILLALGLLADtdmASLFTAITMDIGMCITGLAAALVTsshllRWVFYGISCAFFIAVL 176
gi 50400166   85 ------lslWGRYLTWAFSTPFILLALGLLARsttDKIFSAIVLDVFMCLTGLAAALTTsshamRWLWYALSTAFFVGVL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
Feature 1                                      #  ##  #                       #  ##           
3A7K_A       192 YILLVEWAQdakaAGTADIFSTLKLLTVVMWLGYPIVWALGVEGvav-lpVGYTSWAYSALDIVAKYIFAFLLLNYL 267
2JAF_A       177 SALVTDWAAsassAGTAEIFDTLRVLVVVLWLGYPIVWAVGVEGlalvqsVGATSWAYSVLDVFAKYVFAFILLRWV 253
1E12_A       156 SALVTDWAAsassAGTAEIFDTLRVLTVVLWLGYPIVWAVGVEGlalvqsVGATSWAYSVLDVFAKYVFAFILLRWV 232
gi 429137137 175 YVIMVDWTReadrTGTSDLFTTLKILTVVGWFGYPILWALGVEGfal-leVWMTSWGYSVLDIITKYIVTVLIVLYV 250
gi 461609    182 YILLAEWAEdaeiAGTADIFNTLKVLTVVLWLGYPIFWALGAEGlav-ldVAITSWAYSGMDIVAKYLFAFLLLRWV 257
gi 2829811   177 YVLLVEWPAdaeaAGTSEIFGTLKLLTVVLWLGYPILWALGSEGval-lsVGVTSWGYSGLDILAKYVFAFLLLRWV 252
gi 50400166  159 YYLLVEWPAeadeAGTADIFSTLQWMTIVLWIGYPVVWALGNEGlal-leVGATSWAYSGLDIFAKYAFTIILVLYV 234

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