rhodopsin [Karlodinium veneficum]
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
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 ... |
19-237 | 5.60e-70 | ||||
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 cd15242: Pssm-ID: 475119 Cd Length: 229 Bit Score: 214.49 E-value: 5.60e-70
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| 7tm_Proteorhodopsin | cd15242 | green- and blue-light absorbing proteorhodopsins, member of the seven-transmembrane GPCR ... |
19-237 | 5.60e-70 | ||||
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: 214.49 E-value: 5.60e-70
|
||||||||
| COG5524 | COG5524 | Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms]; |
20-247 | 3.87e-44 | ||||
Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms]; Pssm-ID: 444275 Cd Length: 234 Bit Score: 148.54 E-value: 3.87e-44
|
||||||||
| Bac_rhodopsin | pfam01036 | Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ... |
19-239 | 2.21e-36 | ||||
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: 128.24 E-value: 2.21e-36
|
||||||||
| Bac_rhodopsin | smart01021 | Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ... |
24-247 | 8.57e-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: 92.73 E-value: 8.57e-23
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| 7tm_Proteorhodopsin | cd15242 | green- and blue-light absorbing proteorhodopsins, member of the seven-transmembrane GPCR ... |
19-237 | 5.60e-70 | ||||
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: 214.49 E-value: 5.60e-70
|
||||||||
| COG5524 | COG5524 | Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms]; |
20-247 | 3.87e-44 | ||||
Bacteriorhodopsin [Energy production and conversion, Signal transduction mechanisms]; Pssm-ID: 444275 Cd Length: 234 Bit Score: 148.54 E-value: 3.87e-44
|
||||||||
| Bac_rhodopsin | pfam01036 | Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ... |
19-239 | 2.21e-36 | ||||
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: 128.24 E-value: 2.21e-36
|
||||||||
| Bac_rhodopsin | smart01021 | Bacteriorhodopsin-like protein; The bacterial opsins are retinal-binding proteins that provide ... |
24-247 | 8.57e-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: 92.73 E-value: 8.57e-23
|
||||||||
| 7tm_Opsins_type1 | cd14965 | type 1 opsins, member of the seven-transmembrane GPCR superfamily; This group represents the ... |
21-237 | 4.25e-17 | ||||
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: 77.33 E-value: 4.25e-17
|
||||||||
| 7tm_SRI_SRII | cd15029 | light-sensor activating transmembrane transducer protein sensory rhodopsin I and II; member of ... |
20-237 | 1.48e-11 | ||||
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: 61.96 E-value: 1.48e-11
|
||||||||
| 7tm_bacteriorhodopsin | cd15244 | light-driven outward proton pump bacteriorhodopsin, member of the seven-transmembrane GPCR ... |
20-203 | 2.90e-08 | ||||
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: 52.77 E-value: 2.90e-08
|
||||||||
| 7tm_viral_rhod_II_OLPVRII-like | cd21087 | viral group II rhodopsins such as OLPVRII and similar proteins, members of the ... |
86-157 | 1.73e-03 | ||||
viral group II rhodopsins such as OLPVRII and similar proteins, members of the seven-transmembrane GPCR superfamily; The viral group II rhodopsins includes Organic Lake Phycodnavirus rhodopsin II (OLPVRII), a pentameric light-gated channel that is functionally analogous to well-studied pentameric ligand-gated ion channels playing crucial roles in many cellular processes. It is most likely specific for chloride. Members of this group are considered homologs of proteorhodopsins (PRs), which are blue-light absorbing and green-light absorbing proteins acting as light-driven proton pumps that play a major role in supplying light energy for phototropic marine microorganisms, by a mechanism similar to that of bacteriorhodopsin. Viral proteorhodopsins are predicted to function as sensory rhodopsins that could affect signaling, for example, phototaxis in the infected protists, perhaps stimulating relocation of the infected protists to areas that are rich in nutrients required for virus reproduction. PRs belong to the microbial rhodopsin family, also known as type 1 rhodopsins, which also comprise 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). 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: 410635 Cd Length: 210 Bit Score: 38.60 E-value: 1.73e-03
|
||||||||
| 7tm_ASR-like | cd15240 | Anabaena sensory rhodopsin and similar proteins, member of the seven-transmembrane GPCR ... |
25-229 | 2.41e-03 | ||||
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: 38.23 E-value: 2.41e-03
|
||||||||
| Blast search parameters | ||||
|
