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Conserved domains on  [gi|154757830|emb|CAO82329|]
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bacteriorhodopsin, partial [Halorubrum sp. TP025]

Protein Classification

G protein-coupled receptor family protein( domain architecture ID 705710)

G protein-coupled receptor family protein is a seven-transmembrane G protein-coupled receptor (7TM-GPCR) family protein which typically transmits an extracellular signal into the cell by the conformational rearrangement of the 7TM helices and by the subsequent binding and activation of an intracellular heterotrimeric G protein; GPCR ligands include light-sensitive compounds, odors, pheromones, hormones, and neurotransmitters

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
7tm_GPCRs super family cl28897
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
 11-123 1.48e-45

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


The actual alignment was detected with superfamily member cd15244:

Pssm-ID: 475119  Cd Length: 221  Bit Score: 146.76  E-value: 1.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  11 KVDRVSIGTLVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVL 90
Cdd:cd15244   96 GADRNTIATLIGLDVIMIVTGLVAALTKVPAARIVWWAISTAAFLAVLYFLVVGLTAEASSRSPEVASTFNTLRNLTLVL 175

                         90       100       110
                 ....*....|....*....|....*....|...
gi 154757830  91 WTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:cd15244  176 WACYPIVWLIGTEGFGIVGLNIETLLFMVLDLT 208
 
Name Accession Description Interval E-value
7tm_bacteriorhodopsin cd15244
light-driven outward proton pump bacteriorhodopsin, member of the seven-transmembrane GPCR ...
 11-123 1.48e-45

light-driven outward proton pump bacteriorhodopsin, member of the seven-transmembrane GPCR superfamily; Bacteriorhodopsin (BR) serves as a light-driven retinal-binding outward proton pump, generating an outside positive membrane potential and thus creating an inwardly directed proton motive force (PMF) necessary for ATP synthesis. BR belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising light-driven inward chloride pump halorhodopsin (HR), 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.


Pssm-ID: 320372  Cd Length: 221  Bit Score: 146.76  E-value: 1.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  11 KVDRVSIGTLVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVL 90
Cdd:cd15244   96 GADRNTIATLIGLDVIMIVTGLVAALTKVPAARIVWWAISTAAFLAVLYFLVVGLTAEASSRSPEVASTFNTLRNLTLVL 175

                         90       100       110
                 ....*....|....*....|....*....|...
gi 154757830  91 WTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:cd15244  176 WACYPIVWLIGTEGFGIVGLNIETLLFMVLDLT 208
Bac_rhodopsin pfam01036
Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ...
 11-123 6.34e-29

Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide light- dependent ion transport and sensory functions to a family of halophilic bacteria. 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.


Pssm-ID: 460037  Cd Length: 224  Bit Score: 104.35  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830   11 KVDRVSIGTLVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVA-STFNTLTALVLV 89
Cdd:pfam01036  95 KADRRTIGWLITADILMIVTGYLGALTSTGLVRYLWFAIGTAFFLYVLYVLFKPFAEAAKTRPSGLArSLYTTLRNLFVV 174

                          90       100       110
                  ....*....|....*....|....*....|....
gi 154757830   90 LWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:pfam01036 175 SWLLYPIVWLLGPEGAGVLDVTVRTALYVVLDFV 208
COG5524 COG5524
Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms];
11-123 3.26e-25

Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms];


Pssm-ID: 444275  Cd Length: 234  Bit Score: 95.00  E-value: 3.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  11 KVDRVSIGTLVGVDALMIVTGLIGALShTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVL 90
Cdd:COG5524   91 GASRRLLVTLVGADVLMIVTGLAGALS-TGPARWLWGLLSTAAFLVILYLLLGPLRRSAARQGGEVRSLFGKLRNLLVVL 169

                         90       100       110
                 ....*....|....*....|....*....|...
gi 154757830  91 WTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:COG5524  170 WLIYPIVWLLGPEGLGLLDVTIETVGYTYLDLL 202
Bac_rhodopsin smart01021
Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ...
 12-122 1.91e-23

Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide light- dependent ion transport and sensory functions to a family of halophilic bacteria.. 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).


Pssm-ID: 214978  Cd Length: 233  Bit Score: 90.42  E-value: 1.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830    12 VDRVSIGTLVGVDALMIVTGLIGALSHTPlARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLW 91
Cdd:smart01021  97 VSRATIAFLIAADVVMIVTGLAAALTTST-YKWGWFTISTAAFLVLLYVLLVPLRRSAKARGSEVRRLFLTLRNLTVVLW 175

                           90       100       110
                   ....*....|....*....|....*....|.
gi 154757830    92 TAYPILWIIGtEGAGVVGLGIETLLFMVLDV 122
Cdd:smart01021 176 LLYPIVWGLG-EGGNLIQVDSEAIFYGILDV 205
 
Name Accession Description Interval E-value
7tm_bacteriorhodopsin cd15244
light-driven outward proton pump bacteriorhodopsin, member of the seven-transmembrane GPCR ...
 11-123 1.48e-45

light-driven outward proton pump bacteriorhodopsin, member of the seven-transmembrane GPCR superfamily; Bacteriorhodopsin (BR) serves as a light-driven retinal-binding outward proton pump, generating an outside positive membrane potential and thus creating an inwardly directed proton motive force (PMF) necessary for ATP synthesis. BR belongs to the microbial rhodopsin family, also known as type I rhodopsins, comprising light-driven inward chloride pump halorhodopsin (HR), 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.


Pssm-ID: 320372  Cd Length: 221  Bit Score: 146.76  E-value: 1.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  11 KVDRVSIGTLVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVL 90
Cdd:cd15244   96 GADRNTIATLIGLDVIMIVTGLVAALTKVPAARIVWWAISTAAFLAVLYFLVVGLTAEASSRSPEVASTFNTLRNLTLVL 175

                         90       100       110
                 ....*....|....*....|....*....|...
gi 154757830  91 WTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:cd15244  176 WACYPIVWLIGTEGFGIVGLNIETLLFMVLDLT 208
7tm_Opsins_type1 cd14965
type 1 opsins, member of the seven-transmembrane GPCR superfamily; This group represents the ...
 11-123 1.22e-30

type 1 opsins, member of the seven-transmembrane GPCR superfamily; This group represents the microbial rhodopsin family, also known as type 1 rhodopsins, which can function as light-dependent ion pumps, cation channels, and sensors. 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. Members of the type I rhodopsin family include: light-driven inward chloride pump halorhodopsin (HR); light-driven outward proton pump bacteriorhodopsin (BR); light-gated cation channel channelrhodopsin (ChR); light-sensor activating transmembrane transducer proteins, sensory rhodopsin I and II (SRI and II); 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. 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.


Pssm-ID: 410629  Cd Length: 214  Bit Score: 108.53  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  11 KVDRVSIGTLVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVL 90
Cdd:cd14965   90 GADRATILALIGADVIMIVTGLIGALSIVTTVKWLWFLIGLCAFIVVLYGLAKNYREAAKAKSPEVASLYTKLAWLTIVL 169

                         90       100       110
                 ....*....|....*....|....*....|...
gi 154757830  91 WTAYPILWIIGtEGAGVVGLGIETLLFMVLDVT 123
Cdd:cd14965  170 WIAYPIVWIFG-EGGAVLSVSFETLLYTILDLF 201
Bac_rhodopsin pfam01036
Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ...
 11-123 6.34e-29

Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide light- dependent ion transport and sensory functions to a family of halophilic bacteria. 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.


Pssm-ID: 460037  Cd Length: 224  Bit Score: 104.35  E-value: 6.34e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830   11 KVDRVSIGTLVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVA-STFNTLTALVLV 89
Cdd:pfam01036  95 KADRRTIGWLITADILMIVTGYLGALTSTGLVRYLWFAIGTAFFLYVLYVLFKPFAEAAKTRPSGLArSLYTTLRNLFVV 174

                          90       100       110
                  ....*....|....*....|....*....|....
gi 154757830   90 LWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:pfam01036 175 SWLLYPIVWLLGPEGAGVLDVTVRTALYVVLDFV 208
COG5524 COG5524
Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms];
11-123 3.26e-25

Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms];


Pssm-ID: 444275  Cd Length: 234  Bit Score: 95.00  E-value: 3.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  11 KVDRVSIGTLVGVDALMIVTGLIGALShTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVL 90
Cdd:COG5524   91 GASRRLLVTLVGADVLMIVTGLAGALS-TGPARWLWGLLSTAAFLVILYLLLGPLRRSAARQGGEVRSLFGKLRNLLVVL 169

                         90       100       110
                 ....*....|....*....|....*....|...
gi 154757830  91 WTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:COG5524  170 WLIYPIVWLLGPEGLGLLDVTIETVGYTYLDLL 202
Bac_rhodopsin smart01021
Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ...
 12-122 1.91e-23

Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide light- dependent ion transport and sensory functions to a family of halophilic bacteria.. 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).


Pssm-ID: 214978  Cd Length: 233  Bit Score: 90.42  E-value: 1.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830    12 VDRVSIGTLVGVDALMIVTGLIGALSHTPlARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLW 91
Cdd:smart01021  97 VSRATIAFLIAADVVMIVTGLAAALTTST-YKWGWFTISTAAFLVLLYVLLVPLRRSAKARGSEVRRLFLTLRNLTVVLW 175

                           90       100       110
                   ....*....|....*....|....*....|.
gi 154757830    92 TAYPILWIIGtEGAGVVGLGIETLLFMVLDV 122
Cdd:smart01021 176 LLYPIVWGLG-EGGNLIQVDSEAIFYGILDV 205
7tm_Opsin-1_euk cd15028
proton pumping rhodopsins in fungi and algae, member of the seven-transmembrane GPCR ...
 16-122 6.77e-17

proton pumping rhodopsins in fungi and algae, member of the seven-transmembrane GPCR superfamily; This subgroup represents uncharacterized proton pumping rhodopsins found in fungi and algae. They belong to the microbial rhodopsin family, also known as type I rhodopsins, consisting of 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.


Pssm-ID: 320156  Cd Length: 231  Bit Score: 73.08  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  16 SIGTLVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYP 95
Cdd:cd15028  112 DILVAIVADVIMVLTGLFAAFGHSTGQKWGWFTISCIAFLTVVYHLGVNGRRAARARSSKTRRLFGAIAVYTLVLWTLYP 191

                         90       100
                 ....*....|....*....|....*..
gi 154757830  96 ILWIIGtEGAGVVGLGIETLLFMVLDV 122
Cdd:cd15028  192 IVWALG-DGARKISVDAEIIAYAVLDV 217
7tm_SRI_SRII cd15029
light-sensor activating transmembrane transducer protein sensory rhodopsin I and II; member of ...
 12-123 8.11e-17

light-sensor activating transmembrane transducer protein sensory rhodopsin I and II; member of the seven-transmembrane GPCR superfamily; This subgroup includes the light-sensor activating transmembrane transducer proteins, sensory rhodopsin I (SRI) and II (SRII, also called phoborhodopsin). SRI and SRII are responsible for positive (attractive) and negative (repellent) phototaxis in halobacteria, respectively, thereby controlling the cell's directional movement in response to changes in light intensity by swimming either towards or away from the light. Both sensory rhodopsins belong to the family of microbial rhodopsins, also known as type I rhodopsins, consisting of the light-driven inward chloride pump halorhodopsin (HR), the outward proton pump bacteriorhodopsin (BR), the light-gated cation channel channelrhodopsin (ChR), 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.


Pssm-ID: 320157  Cd Length: 214  Bit Score: 72.75  E-value: 8.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  12 VDRVSIGTLVGVDALMIVTGLIGALShTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLW 91
Cdd:cd15029   91 ASRRTIAGVVAADAVMIVFGFAAAVT-SGTLRWALFGVGAAAFLGLLYLLYGPFPRSAPADDPRVRSLFRLLRNHTVVLW 169

                         90       100       110
                 ....*....|....*....|....*....|..
gi 154757830  92 TAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:cd15029  170 LAYPVVWLLGPAGVGLLTAEGTALVIAYLDVV 201
7tm_ASR-like cd15240
Anabaena sensory rhodopsin and similar proteins, member of the seven-transmembrane GPCR ...
 17-123 8.19e-15

Anabaena sensory rhodopsin and similar proteins, member of the seven-transmembrane GPCR superfamily; This subgroup includes eubacterial sensory rhodopsin from the freshwater cyanobacterium Anabaena and its closely related proteins. Unlike other sensory rhodopsins (SRI and SRII), the Anabaena sensory rhodopsin (ASR) activates a soluble transducer protein (ASRT), which may leading to transcriptional control of several genes. Although ASRT was shown to interact with DNA in vitro, the exact mechanism of photosensory transduction is not clearly understood. Moreover, the regulation of CRP (cAMP receptor protein) expression by ASR has been reported demonstrating a direct interaction of the C-terminal region of ASR with DNA, suggesting that ASR itself may also work as a transcription factor. ASR belongs 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.


Pssm-ID: 320368  Cd Length: 221  Bit Score: 67.51  E-value: 8.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  17 IGTLVGVDALMIVT-GLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYP 95
Cdd:cd15240  101 VIGFLMSDQIMIVTaLLFGLSSERAWVKWTWYACSCGAFLGVLYGIWVPLREETRTERSDLANAYRKNVAFLTVVWIIYP 180

                         90       100
                 ....*....|....*....|....*...
gi 154757830  96 ILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:cd15240  181 IVLIVGPDGLGWISPTLDTALFAVLDFF 208
7tm_Halorhodopsin cd15243
light-driven inward chloride pump halorhodopsin, member of the seven-transmembrane GPCR ...
 12-122 1.65e-12

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.


Pssm-ID: 320371  Cd Length: 226  Bit Score: 61.36  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  12 VDRVSIGTLVGVDALMIVTGLIGALSHTPLA-RYSWWLFSTICMIVVLYFLATSLRAAAKERGpeVASTFNTLTALVLVL 90
Cdd:cd15243  103 SNTTKLFTAIAADIGMCVTGLAAALTTSSHLmRWVWYAISCAFFVVVLYVLLVEWAADADAAG--TADIFSTLKVLTVVL 180

                         90       100       110
                 ....*....|....*....|....*....|..
gi 154757830  91 WTAYPILWIIGTEGAGVVGLGIETLLFMVLDV 122
Cdd:cd15243  181 WLGYPIVWALGVEGLALLSVGATSWAYSGLDI 212
7tm_YRO2_fungal-like cd15239
fungal YRO2 and related proteins, member of the seven-transmembrane GPCR superfamily; This ...
 26-122 3.11e-10

fungal YRO2 and related proteins, member of the seven-transmembrane GPCR superfamily; This subgroup includes the yeast YRO2 protein and it closely related proteins. Although the exact function of these proteins is unknown, they show strong sequence homology to the family of microbial rhodopsins, 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.


Pssm-ID: 320367  Cd Length: 227  Bit Score: 55.21  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  26 LMIVTGLIGALSHTplaRYSW--WLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYPILWIIgTE 103
Cdd:cd15239  119 VWVVSLLVGALVHS---TYKWgyFTFGCVALLYVAYSLLTRGRRSARRLGLDVRRFYLILAGWLMLIWLLYPIAWGL-SE 194

                         90
                 ....*....|....*....
gi 154757830 104 GAGVVGLGIETLLFMVLDV 122
Cdd:cd15239  195 GGNVIQPDSEAIFYGILDL 213
7tm_Proteorhodopsin cd15242
green- and blue-light absorbing proteorhodopsins, member of the seven-transmembrane GPCR ...
 20-109 9.19e-10

green- and blue-light absorbing proteorhodopsins, member of the seven-transmembrane GPCR superfamily; This subgroup represents blue-light absorbing and green-light absorbing proteorhodopsins (PRs), which act as a light-driven proton pump that plays a major role in supplying light energy for phototropic marine microorganisms, by a mechanism similar to that of bacteriorhodopsin. PRs are found in most marine bacteria in surface waters, as well as in archaea and eukaryotes. They belong to the microbial rhodopsin family, also known as type 1 rhodopsins, comprising the light-driven inward chloride pump halorhodopsin (HR), the light-gated cation channel channelrhodopsin (ChR), the light-sensor activating transmembrane transducer protein sensory rhodopsin II (SRII), the light-sensor activating soluble transducer protein Anabaena sensory rhodopsin (ASR), and the other light-driven proton pumps such as bacteriorhodopsin (BR). 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.


Pssm-ID: 320370  Cd Length: 229  Bit Score: 53.86  E-value: 9.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  20 LVGVDALMIVTGLIGALSHTPLARYSWWLFSTICMIVVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWTAYPILWI 99
Cdd:cd15242  112 LGGASALMIVLGYPGEIGADLGTRWLWGVLSMIPFLYIIYELFVGLAKAIARQPAAVRGAVNTLRWIVLVGWAIYPIGYM 191

                         90
                 ....*....|
gi 154757830 100 IGTEGAGVVG 109
Cdd:cd15242  192 AGYLGLTGGG 201
7tm_ARII-like cd15238
Acetabularia rhodopsin II and similar proteins, member of the seven-transmembrane GPCR ...
 15-122 5.75e-09

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.


Pssm-ID: 320366  Cd Length: 219  Bit Score: 51.80  E-value: 5.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  15 VSIGTLVGVDALMIVTGLIGALShtpLARYSWWLFSTICMI--VVLYFLATSLRAAAKERGPEVASTFNTLTALVLVLWT 92
Cdd:cd15238  100 GMILWIVGADIAMIMFGIFGAFS---TNSYKWGYFGVGCAMfaVLLWGMFNPGAKGALAKGGEYPGLYFGLLGYLALLWV 176

                         90       100       110
                 ....*....|....*....|....*....|
gi 154757830  93 AYPILWIIGtEGAGVVGLGIETLLFMVLDV 122
Cdd:cd15238  177 GYPIVWGLG-EGSDYISVDAEAISMGILDI 205
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
 11-123 6.77e-05

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 40.49  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154757830  11 KVDRVSIGTLVGVDALMIVTGLIGALS------------HTPLARYSWWLFSTICMIVVLYFLATSLRAAAKE------- 71
Cdd:cd14964  113 GKTRVIILGCWGVSLLLSIPPLVGKGAipryntltgscyLICTTIYLTWGFLLVSFLLPLVAFLVIFSRIVLRlrrrvra 192

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154757830  72 ----------RGPEVASTFNTLTALVLVLWTAYPILWIIGTEGAGVVGLGIETLLFMVLDVT 123
Cdd:cd14964  193 irsaaslntdKNLKATKSLLILVITFLLCWLPFSIVFILHALVAAGQGLNLLSILANLLAVL 254
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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