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Conserved domains on  [gi|685806481|gb|AIP84816|]
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RNA fingerprint protein 35, partial [Eutropis quadricarinata]

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 ...
1-138 1.16e-62

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 cd15011:

Pssm-ID: 475119  Cd Length: 256  Bit Score: 195.75  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481   1 VVPVTIFMVKQWVDDTLPQTLCTTSALLYLFQGFSSNLMGSLVVSYNFYSLNKMGTSPgATKRPVSMIWAILTVWIVSLL 80
Cdd:cd15011   48 VVPVSIFMLMQWETDGLPQPLCTTSALLYLFQGLSSNLKASLIASYNFYTTKKLGWLQ-TTKRSVRVPWAVLTIWAASLL 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 685806481  81 ICVLPLCGWGTYTFTPWGCLTDCSSSYILFLFVIYSFCFGILVVLSVPLIYQLLCSDE 138
Cdd:cd15011  127 LSALPLCGWGSFVPTSWGCLVDCQSSYILFLFSLYSLCFCILVVLSVPLTYQLLCSDE 184
 
Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
1-138 1.16e-62

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. All GPCRs have 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.


Pssm-ID: 320139  Cd Length: 256  Bit Score: 195.75  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481   1 VVPVTIFMVKQWVDDTLPQTLCTTSALLYLFQGFSSNLMGSLVVSYNFYSLNKMGTSPgATKRPVSMIWAILTVWIVSLL 80
Cdd:cd15011   48 VVPVSIFMLMQWETDGLPQPLCTTSALLYLFQGLSSNLKASLIASYNFYTTKKLGWLQ-TTKRSVRVPWAVLTIWAASLL 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 685806481  81 ICVLPLCGWGTYTFTPWGCLTDCSSSYILFLFVIYSFCFGILVVLSVPLIYQLLCSDE 138
Cdd:cd15011  127 LSALPLCGWGSFVPTSWGCLVDCQSSYILFLFSLYSLCFCILVVLSVPLTYQLLCSDE 184
 
Name Accession Description Interval E-value
7tmA_GPR149 cd15011
G protein-coupled receptor 149, member of the class A family of seven-transmembrane G ...
1-138 1.16e-62

G protein-coupled receptor 149, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR149 is predominantly expressed in the ovary and is present at low levels in the brain and the digestive tract (stomach and small intestine). GPR149-null mice are viable and have normal maturation of the ovarian follicle, but show enhanced fertility and ovulation. Additionally, the null mice showed increased expression levels of growth differentiation factor 9 (Gdf9) in oocytes, and upregulated expression of cyclin D2, a downstream target of FSH (follicle-stimulating hormone) receptor signaling pathways that promotes granulosa cell proliferation. GPR149 is an orphan receptor with no known endogenous ligand as yet identified. Although categorized as a member of the class A GPCRs, GPR149 lacks the first two charged amino acids of the highly conserved Asp-Arg-Tyr (DRY) motif found in the third transmembrane helix (TM3) of class A receptors which is important for efficient G protein-coupled signal transduction. Moreover, the transmembrane domains and carboxyl terminus of GPR149 show low similarities to other GPCRs. All GPCRs have 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.


Pssm-ID: 320139  Cd Length: 256  Bit Score: 195.75  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481   1 VVPVTIFMVKQWVDDTLPQTLCTTSALLYLFQGFSSNLMGSLVVSYNFYSLNKMGTSPgATKRPVSMIWAILTVWIVSLL 80
Cdd:cd15011   48 VVPVSIFMLMQWETDGLPQPLCTTSALLYLFQGLSSNLKASLIASYNFYTTKKLGWLQ-TTKRSVRVPWAVLTIWAASLL 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 685806481  81 ICVLPLCGWGTYTFTPWGCLTDCSSSYILFLFVIYSFCFGILVVLSVPLIYQLLCSDE 138
Cdd:cd15011  127 LSALPLCGWGSFVPTSWGCLVDCQSSYILFLFSLYSLCFCILVVLSVPLTYQLLCSDE 184
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
1-162 6.91e-08

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: 51.66  E-value: 6.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481   1 VVPVTIFMVKQWVDDTLPQTLCTTSALLYLFQGFSSnLMGSLVVSYNFYSLNKMGTSPGATKRPVSMIWAILTVWIVSLL 80
Cdd:cd14964   50 VVLVLFFLLGLTEASSRPQALCYLIYLLWYGANLAS-IWTTLVLTYHRYFALCGPLKYTRLSSPGKTRVIILGCWGVSLL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  81 ICVLPLCGWgtytfTPWGCLTDCSSSYILFLFVIYSFCFGILVVLSVPLIYQLLCSDEQQHLYDDYHQIARGYFSPGSPP 160
Cdd:cd14964  129 LSIPPLVGK-----GAIPRYNTLTGSCYLICTTIYLTWGFLLVSFLLPLVAFLVIFSRIVLRLRRRVRAIRSAASLNTDK 203

                 ..
gi 685806481 161 VG 162
Cdd:cd14964  204 NL 205
7tmA_Melanopsin-like cd15083
vertebrate melanopsins and related opsins, member of the class A family of seven-transmembrane ...
56-127 1.33e-05

vertebrate melanopsins and related opsins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represent the Gq-coupled rhodopsin subfamily consists of melanopsins, insect photoreceptors R1-R6, invertebrate Gq opsins as well as their closely related opsins. Melanopsins (also called Opsin-4) are the primary photoreceptor molecules for non-visual functions such as the photo-entrainment of the circadian rhythm and pupillary constriction in mammals. Mammalian melanopsins are expressed only in the inner retina, whereas non-mammalian vertebrate melanopsins are localized in various extra-retinal tissues such as iris, brain, pineal gland, and skin. The outer photoreceptors (R1-R6) are the insect Drosophila equivalent to the vertebrate rods and are responsible for image formation and motion detection. The invertebrate G(q) opsins includes the arthropod and mollusk visual opsins as well as invertebrate melanopsins, which are also found in vertebrates. Arthropods possess color vision by the use of multiple opsins sensitive to different light wavelengths. Members of this subfamily belong to the class A of the G protein-coupled receptors and have seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320211 [Multi-domain]  Cd Length: 291  Bit Score: 45.02  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  56 TSPGATKRPVS---MIWAILTVWIVSLLICVLPLCGWGTYtfTPWGCLTDCSSSYILF-----LFVIYSFCFGILVVLSV 127
Cdd:cd15083  103 TRPMKASVRIShrrALIVIAVVWLYSLLWVLPPLFGWSRY--VLEGLLTSCSFDYLSRddanrSYVICLLIFGFVLPLLI 180
7tmA_Opsin_Gq_invertebrates cd15337
invertebrate Gq opsins, member of the class A family of seven-transmembrane G protein-coupled ...
42-124 1.59e-04

invertebrate Gq opsins, member of the class A family of seven-transmembrane G protein-coupled receptors; The invertebrate Gq-coupled opsin subfamily includes the arthropod and mollusc visual opsins. Like the vertebrate visual opsins, arthropods possess color vision by the use of multiple opsins sensitive to different light wavelengths. The invertebrate Gq opsins are closely related to the vertebrate melanopsins, the primary photoreceptor molecules for non-visual responses to light, and the R1-R6 photoreceptors, which are the fly equivalent to the vertebrate rods. The Gq opsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320459 [Multi-domain]  Cd Length: 292  Bit Score: 41.54  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  42 LVVSYNFYSLNKMgtspgaTKRPVSMIwaILTVWIVSLLICVLPLCGWGTYtfTPWGCLTDCS----------SSYILFL 111
Cdd:cd15337  101 LVIAKPLEAMKKM------TFKRAFIM--IIIIWLWSLLWSIPPFFGWGRY--VPEGFQTSCTfdylsrdlnnRLFILGL 170
                         90
                 ....*....|...
gi 685806481 112 FvIYSFCFGILVV 124
Cdd:cd15337  171 F-IFGFLCPLLII 182
7tmA_Retinal_GPR cd15072
retinal G protein coupled receptor, member of the class A family of seven-transmembrane G ...
65-139 4.67e-04

retinal G protein coupled receptor, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represents the retinal G-protein coupled receptor (RGR) found exclusively in retinal pigment epithelium (RPE) and Muller cells. RGR is a member of the class A rhodopsin-like receptor family. As with other opsins, RGR binds all-trans retinal and contains a conserved lysine reside on the seventh helix. RGR functions as a photoisomerase to catalyze the conversion of all-trans-retinal to 11-cis-retinal. Two mutations in RGR gene are found in patients with retinitis pigmentosa, indicating that RGR is essential to the visual process.


Pssm-ID: 320200 [Multi-domain]  Cd Length: 260  Bit Score: 40.04  E-value: 4.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  65 VSMIWAILTVWIVSLLICVLPLCGWGTYTFTPWG--CLTDCSS---SYILFLFVIYSFCFGILVVL---SVPLIYQLLCS 136
Cdd:cd15072  110 STAISLVLFVWLFSAFWAAMPLLGWGEYDYEPLGtcCTLDYSKgdrNYVSYLFTMAFFNFILPLFIlltSYSSIEQKLKK 189

                 ...
gi 685806481 137 DEQ 139
Cdd:cd15072  190 EGH 192
7tmA_Prostanoid_R cd14981
G protein-coupled receptors for prostanoids, member of the class A family of ...
17-127 6.37e-04

G protein-coupled receptors for prostanoids, member of the class A family of seven-transmembrane G protein-coupled receptors; Prostanoids are the cyclooxygenase (COX) metabolites of arachidonic acid, which include the prostaglandins (PGD2, PGE2, PGF2alpha), prostacyclin (PGI2), and thromboxane A2 (TxA2). These five major bioactive prostanoids acts as mediators or modulators in a wide range of physiological and pathophysiological processes within the kidney and play important roles in inflammation, platelet aggregation, and vasoconstriction/relaxation, among many others. They act locally by preferentially interacting with G protein-coupled receptors designated DP, EP. FP, IP, and TP, respectively. The phylogenetic tree suggests that the prostanoid receptors can be grouped into two major branches: G(s)-coupled (DP1, EP2, EP4, and IP) and G(i)- (EP3) or G(q)-coupled (EP1, FP, and TP), forming three clusters.


Pssm-ID: 320112 [Multi-domain]  Cd Length: 288  Bit Score: 39.92  E-value: 6.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  17 LPQTLCTTSALLYLFQGFSSNLMGS-------LVVSYNFYsLNKMGTSPGAtkrpvsmiWAILT-VWIVSLLICVLPLCG 88
Cdd:cd14981   71 GGQPLCDYFGFMMSFFGLSSLLIVCamaverfLAITHPFF-YNSHVKKRRA--------RLMLGaVWAFALLIASLPLLG 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 685806481  89 WGTYT-FTP--WgCLTDCSSSYilFLFVIYSFCFGILVVLSV 127
Cdd:cd14981  142 LGSYVlQYPgtW-CFLDFYSKN--TGDAAYAYLYSILGLLIL 180
7tmA_photoreceptors_insect cd15079
insect photoreceptors R1-R6 and similar proteins, member of the class A family of ...
71-119 7.87e-04

insect photoreceptors R1-R6 and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes the insect photoreceptors and their closely related proteins. The Drosophila eye is composed of about 800 unit eyes called ommatidia, each of which contains eight photoreceptor cells (R1-R8). The six outer photoreceptors (R1-R6) function like the vertebrate rods and are responsible for motion detection in dim light and image formation. The R1-R6 photoreceptors express a blue-absorbing pigment, Rhodopsin 1(Rh1). The inner photoreceptors (R7 and R8) are considered the equivalent of the color-sensitive vertebrate cone cells, which express a range of different pigments. The R7 photoreceptors express one of two different UV absorbing pigments, either Rh3 or Rh4. Likewise, the R8 photoreceptors express either the blue absorbing pigment Rh5 or green absorbing pigment Rh6. These photoreceptors belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320207 [Multi-domain]  Cd Length: 292  Bit Score: 39.48  E-value: 7.87e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 685806481  71 ILTVWIVSLLICVLPLC-GWGTYtfTPWGCLTDCSSSYI-------LFLFVIYSFCF 119
Cdd:cd15079  119 ILFIWLYALPWALLPLLfGWGRY--VPEGFLTSCSFDYLtrdwntrSFVATIFVFAY 173
7tmA_Opsins_type2_animals cd14969
type 2 opsins in animals, member of the class A family of seven-transmembrane G ...
70-121 2.87e-03

type 2 opsins in animals, member of the class A family of seven-transmembrane G protein-coupled receptors; This rhodopsin family represents the type 2 opsins found in vertebrates and invertebrates except sponge. Type 2 opsins primarily function as G protein coupled receptors and are responsible for vision as well as for circadian rhythm and pigment regulation. On the contrary, type 1 opsins such as bacteriorhodopsin and proteorhodopsin are found in both prokaryotic and eukaryotic microbes, functioning as light-gated ion channels, proton pumps, sensory receptors and in other unknown functions. Although these two opsin types share seven-transmembrane domain topology and a conserved lysine reside in the seventh helix, type 1 opsins do not activate G-proteins and are not evolutionarily related to type 2. Type 2 opsins can be classified into six distinct subfamilies including the vertebrate opsins/encephalopsins, the G(o) opsins, the G(s) opsins, the invertebrate G(q) opsins, the photoisomerases, and the neuropsins.


Pssm-ID: 381741 [Multi-domain]  Cd Length: 284  Bit Score: 37.96  E-value: 2.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 685806481  70 AILTVWIVSLLICVLPLCGWGTYTFTPWGclTDCS----------SSYILFLFViysFCFGI 121
Cdd:cd14969  119 LIAFIWLYGLFWALPPLFGWSSYVPEGGG--TSCSvdwyskdpnsLSYIVSLFV---FCFFL 175
7tmA_Opsin5_neuropsin cd15074
neuropsin (Opsin-5), member of the class A family of seven-transmembrane G protein-coupled ...
62-127 2.92e-03

neuropsin (Opsin-5), member of the class A family of seven-transmembrane G protein-coupled receptors; Neuropsin, also known as Opsin-5, is a photoreceptor protein expressed in the retina, brain, testes, and spinal cord. Neuropsin belongs to the type 2 opsin family of the class A G-protein coupled receptors. Mammalian neuropsin activates Gi protein-mediated photo-transduction pathway in a UV-dependent manner, whereas, in non-mammalian vertebrates, neuropsin is involved in regulating the photoperiodic control of seasonal reproduction in birds such as quail. As with other opsins, it may also act as a retinal photoisomerase.


Pssm-ID: 320202 [Multi-domain]  Cd Length: 284  Bit Score: 37.64  E-value: 2.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685806481  62 KRPVSMIwAILTVWIVSLLICVLPLCGWGTYTFTPWGclTDCS------------SSYILFLFViysFCFGILVVLSV 127
Cdd:cd15074  112 SRRHVCI-VIVAIWLYALFWAVAPLVGWGSYGPEPFG--TSCSidwtgasasvggMSYIISIFI---FCYLLPVLIIV 183
7tmA_EDG-like cd14972
endothelial differentiation gene family, member of the class A family of seven-transmembrane G ...
70-136 5.18e-03

endothelial differentiation gene family, member of the class A family of seven-transmembrane G protein-coupled receptors; This group represents the endothelial differentiation gene (Edg) family of G-protein coupled receptors, melanocortin/ACTH receptors, and cannabinoid receptors as well as their closely related receptors. The Edg GPCRs bind blood borne lysophospholipids including sphingosine-1-phosphate (S1P) and lysophosphatidic acid (LPA), which are involved in the regulation of cell proliferation, survival, migration, invasion, endothelial cell shape change and cytoskeletal remodeling. The Edg receptors are classified into two subfamilies: the lysophosphatidic acid subfamily that includes LPA1 (Edg2), LPA2 (Edg4), and LPA3 (Edg7); and the S1P subfamily that includes S1P1 (Edg1), S1P2 (Edg5), S1P3 (Edg3), S1P4 (Edg6), and S1P5 (Edg8). Melanocortin receptors bind a group of pituitary peptide hormones known as melanocortins, which include adrenocorticotropic hormone (ACTH) and the different isoforms of melanocyte-stimulating hormones. Two types of cannabinoid receptors, CB1 and CB2, are activated by naturally occurring endocannabinoids, cannabis plant-derived cannabinoids such as tetrahydrocannabinol, or synthetic cannabinoids. The CB receptors are involved in the various physiological processes such as appetite, mood, memory, and pain sensation. CB1 receptor is expressed predominantly in central and peripheral neurons, while CB2 receptor is found mainly in the immune system.


Pssm-ID: 341317 [Multi-domain]  Cd Length: 275  Bit Score: 36.89  E-value: 5.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  70 AILTVWIVSLLICVLPLCGWGTYTFTPWGCLTDC---SSSYILFLFVIYSFCFGILVVLSVPlIYQLLCS 136
Cdd:cd14972  117 LIALVWVWSVLLALLPVLGWNCVLCDQESCSPLGpglPKSYLVLILVFFFIALVIIVFLYVR-IFWCLWR 185
7tmA_TXA2_R cd15143
thromboxane A2 receptor, member of the class A family of seven-transmembrane G protein-coupled ...
21-126 5.58e-03

thromboxane A2 receptor, member of the class A family of seven-transmembrane G protein-coupled receptors; The thromboxane receptor, also known as the prostanoid TP receptor, is a class A G-protein coupled receptor whose endogenous ligand is thromboxane A2 (TXA2). TXA2 is the major product of cyclooxygenase metabolite of arachidonic acid that found predominantly in platelets and stimulates platelet aggregation, Ca2+ influx into platelets, and also causes vasoconstriction. TXA2 has been shown to be involved in immune regulation, angiogenesis and metastasis, among many others. Activation of TXA2 receptor is coupled to G(q) and G(13), resulting in the activations of phospholipase C and RhoGEF, respectively. TXA2 receptor is widely distributed in the body and is abundantly expressed in thymus and spleen.


Pssm-ID: 320271 [Multi-domain]  Cd Length: 296  Bit Score: 37.11  E-value: 5.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  21 LCTTSALLYLFQGFSSNLMGSLVVSYNFYSLNKMGTSPGAT--KRPVSMIwaiLTVWIVSLLICVLPLCGWGTYTFT--- 95
Cdd:cd15143   81 LCNFMGLSMVFYGLCPLLLGATMAVERFFGINRPFSRSTAMskRRAWYMV---GMVWAFAFLLGLLPILGLGRYTLQypg 157
                         90       100       110
                 ....*....|....*....|....*....|.
gi 685806481  96 PWGCLTDCSSSYILFLFVIYSFCFGILVVLS 126
Cdd:cd15143  158 SWCFLTLLFDSKDVAFGLLFSFLGILSVGLS 188
7tmA_Melanopsin cd15336
vertebrate melanopsins (Opsin-4), member of the class A family of seven-transmembrane G ...
60-135 8.15e-03

vertebrate melanopsins (Opsin-4), member of the class A family of seven-transmembrane G protein-coupled receptors; Melanopsin (also called Opsin-4) is the G protein-coupled photopigment that mediates non-visual responses to light. In mammals, these photoresponses include the photo-entrainment of circadian rhythm, pupillary constriction, and acute nocturnal melatonin suppression. Mammalian melanopsins are expressed only in the inner retina, whereas non-mammalian vertebrate melanopsins are localized in various extra-retinal tissues such as iris, brain, pineal gland, and skin. Melanopsins belong the class A of the G protein-coupled receptors and possess seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops.


Pssm-ID: 320458 [Multi-domain]  Cd Length: 290  Bit Score: 36.62  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685806481  60 ATKRPVSMIwaILTVWIVSLLICVLPLCGWGTYtfTPWGCLTDCSSSYILF-----LFVIYSFCFgilvVLSVPLIYQLL 134
Cdd:cd15336  112 VSKKRAMII--ILLVWLYSLAWSLPPLFGWSAY--VPEGLLTSCTWDYMTFtpsvrAYTMLLFCF----VFFIPLGIIIY 183

                 .
gi 685806481 135 C 135
Cdd:cd15336  184 C 184
 
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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