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Conserved domains on  [gi|392926155|ref|NP_001257033|]
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G-protein coupled receptors family 1 profile domain-containing protein [Caenorhabditis elegans]

Protein Classification

G-protein coupled receptor( domain architecture ID 11606548)

G-protein coupled receptor (GPCR) transmits physiological signals from the outside of the cell to the inside by binding to an extracellular agonist, which induces conformational changes that lead to the activation of heterotrimeric G proteins, which then bind to and activate numerous downstream effector proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmA_FMRFamide_R-like cd14978
FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of ...
35-348 9.05e-42

FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes Drosophila melanogaster G-protein coupled FMRFamide (Phe-Met-Arg-Phe-NH2) receptor DrmFMRFa-R and related invertebrate receptors, as well as the vertebrate proteins GPR139 and GPR142. DrmFMRFa-R binds with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. FMRFamide is a neuropeptide from the family of FMRFamide-related peptides (FaRPs), which all containing a C-terminal RFamide (Arg-Phe-NH2) motif and have diverse functions in the central and peripheral nervous systems. FMRFamide is an important neuropeptide in many types of invertebrates such as insects, nematodes, molluscs, and worms. In invertebrates, the FMRFamide-related peptides are involved in the regulation of heart rate, blood pressure, gut motility, feeding behavior, and reproduction. On the other hand, in vertebrates such as mice, they play a role in the modulation of morphine-induced antinociception. Orphan receptors GPR139 and GPR142 are very closely related G protein-coupled receptors, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and mediates enhancement of glucose-stimulated insulin secretion, whereas GPR139 is mostly expressed in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139.


:

Pssm-ID: 410630 [Multi-domain]  Cd Length: 299  Bit Score: 148.55  E-value: 9.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  35 IHIPLSISICIFGAASNVFNIIVLTRKRMRTPINILLTGLSIAQWLLATNYFLYLLLEYYRYQCVqLLWSEAFTRYRFFN 114
Cdd:cd14978    2 LYGYVLPVICIFGIIGNILNLVVLTRKSMRSSTNVYLAALAVSDILVLLSALPLFLLPYIADYSS-SFLSYFYAYFLPYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 115 VNLNTVFHTIAFTTTIVVAVFRYCALKFPIQAnRFIYKCQPAIAANVIIWIIIPIISLPLFFISEVKIVARDHVaydlqC 194
Cdd:cd14978   81 YPLANTFQTASVWLTVALTVERYIAVCHPLKA-RTWCTPRRARRVILIIIIFSLLLNLPRFFEYEVVECENCNN-----N 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 195 EMEGPLYDLSYQESPLLVSAVFWAFGIVFKLLPSLILSILLIALIRSLKSVERRRKNwkrtqganiCTNSERKAKRKLTT 274
Cdd:cd14978  155 SYYYVIPTLLRQNETYLLKYYFWLYAIFVVLLPFILLLILNILLIRALRKSKKRRRL---------LRRRRRLLSRSQRR 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926155 275 RPRTTRMLVIILLLCVMVELPMGILNLCVAIYGEEFGNRYYDPVGNLMEMLTLLYSSVSFVLYCTMSNEYLSTF 348
Cdd:cd14978  226 ERRTTIMLIAVVIVFLICNLPAGILNILEAIFGESFLSPIYQLLGDISNLLVVLNSAVNFIIYCLFSSKFRRTF 299
 
Name Accession Description Interval E-value
7tmA_FMRFamide_R-like cd14978
FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of ...
35-348 9.05e-42

FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes Drosophila melanogaster G-protein coupled FMRFamide (Phe-Met-Arg-Phe-NH2) receptor DrmFMRFa-R and related invertebrate receptors, as well as the vertebrate proteins GPR139 and GPR142. DrmFMRFa-R binds with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. FMRFamide is a neuropeptide from the family of FMRFamide-related peptides (FaRPs), which all containing a C-terminal RFamide (Arg-Phe-NH2) motif and have diverse functions in the central and peripheral nervous systems. FMRFamide is an important neuropeptide in many types of invertebrates such as insects, nematodes, molluscs, and worms. In invertebrates, the FMRFamide-related peptides are involved in the regulation of heart rate, blood pressure, gut motility, feeding behavior, and reproduction. On the other hand, in vertebrates such as mice, they play a role in the modulation of morphine-induced antinociception. Orphan receptors GPR139 and GPR142 are very closely related G protein-coupled receptors, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and mediates enhancement of glucose-stimulated insulin secretion, whereas GPR139 is mostly expressed in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139.


Pssm-ID: 410630 [Multi-domain]  Cd Length: 299  Bit Score: 148.55  E-value: 9.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  35 IHIPLSISICIFGAASNVFNIIVLTRKRMRTPINILLTGLSIAQWLLATNYFLYLLLEYYRYQCVqLLWSEAFTRYRFFN 114
Cdd:cd14978    2 LYGYVLPVICIFGIIGNILNLVVLTRKSMRSSTNVYLAALAVSDILVLLSALPLFLLPYIADYSS-SFLSYFYAYFLPYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 115 VNLNTVFHTIAFTTTIVVAVFRYCALKFPIQAnRFIYKCQPAIAANVIIWIIIPIISLPLFFISEVKIVARDHVaydlqC 194
Cdd:cd14978   81 YPLANTFQTASVWLTVALTVERYIAVCHPLKA-RTWCTPRRARRVILIIIIFSLLLNLPRFFEYEVVECENCNN-----N 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 195 EMEGPLYDLSYQESPLLVSAVFWAFGIVFKLLPSLILSILLIALIRSLKSVERRRKNwkrtqganiCTNSERKAKRKLTT 274
Cdd:cd14978  155 SYYYVIPTLLRQNETYLLKYYFWLYAIFVVLLPFILLLILNILLIRALRKSKKRRRL---------LRRRRRLLSRSQRR 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926155 275 RPRTTRMLVIILLLCVMVELPMGILNLCVAIYGEEFGNRYYDPVGNLMEMLTLLYSSVSFVLYCTMSNEYLSTF 348
Cdd:cd14978  226 ERRTTIMLIAVVIVFLICNLPAGILNILEAIFGESFLSPIYQLLGDISNLLVVLNSAVNFIIYCLFSSKFRRTF 299
7TM_GPCR_Srw pfam10324
Serpentine type 7TM GPCR chemoreceptor Srw; Chemoreception is mediated in Caenorhabditis ...
43-353 4.86e-06

Serpentine type 7TM GPCR chemoreceptor Srw; Chemoreception is mediated in Caenorhabditis elegans by members of the seven-transmembrane G-protein-coupled receptor class (7TM GPCRs) of proteins which are of the serpentine type. Srw is a solo family amongst the superfamilies of chemoreceptors. Chemoperception is one of the central senses of soil nematodes like C. elegans which are otherwise 'blind' and 'deaf'. The genes encoding Srw do not appear to be under as strong an adaptive evolutionary pressure as those of Srz.


Pssm-ID: 402097  Cd Length: 318  Bit Score: 47.97  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155   43 ICIFGAASNVFNIIVLTRKRMRT-PINILLTGLSIAQWLLAT----NYFLYLLLEYYRYQCVQLLWSEAFTRYRFFNVnL 117
Cdd:pfam10324   6 LSFIGFIINIFHLIILTRKSMRTsSINIIMIGIAICDIITMLltiyNFIPEFIISYENSECIPPDSYLKVLLDWILES-L 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  118 NTVFHTIAFTTTIVVAVFRYCALKFPIqaNRFIYKC-QPAIAANVIIWIIIPIISLPLFFISEVKIVARDHVAY-DLQCE 195
Cdd:pfam10324  85 QDYSRRCSTWLGVFMALIRTLVVKNPM--SNKIQKLsKPKFGLIIIIIVFILSLPISIFYYFRYEIVEVGGIWKpPPNCA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  196 MEGPLYdlSYQESPLLVSAVFWAF------------GIVFKLLPSLILSILLIALIRSLKSVERRRKNwkrtqganicTN 263
Cdd:pfam10324 163 GFPPNY--TETRYVLVVSELFTANdglllkifllidGIFSKIIPCILLPILTILLIIELRKAKKSRKN----------LS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  264 SERKAKRKLTTRprttrmLVIILLLCVMV-ELPMGILNLCVAIYGEEFGNRY-YDPVGNLMEMLTLLYSSVSFVLYCTMS 341
Cdd:pfam10324 231 SSSKNKSDRTTK------LVIFMTISFFIaEFPLGISYIIQFFFTDNPGIRRiLTYLSVIFSLLFTINSISHCFICFLMS 304
                         330
                  ....*....|..
gi 392926155  342 NEYLSTFRALFF 353
Cdd:pfam10324 305 SQYRKTAKKLFG 316
 
Name Accession Description Interval E-value
7tmA_FMRFamide_R-like cd14978
FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of ...
35-348 9.05e-42

FMRFamide (Phe-Met-Arg-Phe) receptors and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes Drosophila melanogaster G-protein coupled FMRFamide (Phe-Met-Arg-Phe-NH2) receptor DrmFMRFa-R and related invertebrate receptors, as well as the vertebrate proteins GPR139 and GPR142. DrmFMRFa-R binds with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. FMRFamide is a neuropeptide from the family of FMRFamide-related peptides (FaRPs), which all containing a C-terminal RFamide (Arg-Phe-NH2) motif and have diverse functions in the central and peripheral nervous systems. FMRFamide is an important neuropeptide in many types of invertebrates such as insects, nematodes, molluscs, and worms. In invertebrates, the FMRFamide-related peptides are involved in the regulation of heart rate, blood pressure, gut motility, feeding behavior, and reproduction. On the other hand, in vertebrates such as mice, they play a role in the modulation of morphine-induced antinociception. Orphan receptors GPR139 and GPR142 are very closely related G protein-coupled receptors, but they have different expression patterns in the brain and in other tissues. These receptors couple to inhibitory G proteins and activate phospholipase C. Studies suggested that dimer formation may be required for their proper function. GPR142 is predominantly expressed in pancreatic beta-cells and mediates enhancement of glucose-stimulated insulin secretion, whereas GPR139 is mostly expressed in the brain and is suggested to play a role in the control of locomotor activity. Tryptophan and phenylalanine have been identified as putative endogenous ligands of GPR139.


Pssm-ID: 410630 [Multi-domain]  Cd Length: 299  Bit Score: 148.55  E-value: 9.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  35 IHIPLSISICIFGAASNVFNIIVLTRKRMRTPINILLTGLSIAQWLLATNYFLYLLLEYYRYQCVqLLWSEAFTRYRFFN 114
Cdd:cd14978    2 LYGYVLPVICIFGIIGNILNLVVLTRKSMRSSTNVYLAALAVSDILVLLSALPLFLLPYIADYSS-SFLSYFYAYFLPYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 115 VNLNTVFHTIAFTTTIVVAVFRYCALKFPIQAnRFIYKCQPAIAANVIIWIIIPIISLPLFFISEVKIVARDHVaydlqC 194
Cdd:cd14978   81 YPLANTFQTASVWLTVALTVERYIAVCHPLKA-RTWCTPRRARRVILIIIIFSLLLNLPRFFEYEVVECENCNN-----N 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 195 EMEGPLYDLSYQESPLLVSAVFWAFGIVFKLLPSLILSILLIALIRSLKSVERRRKNwkrtqganiCTNSERKAKRKLTT 274
Cdd:cd14978  155 SYYYVIPTLLRQNETYLLKYYFWLYAIFVVLLPFILLLILNILLIRALRKSKKRRRL---------LRRRRRLLSRSQRR 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392926155 275 RPRTTRMLVIILLLCVMVELPMGILNLCVAIYGEEFGNRYYDPVGNLMEMLTLLYSSVSFVLYCTMSNEYLSTF 348
Cdd:cd14978  226 ERRTTIMLIAVVIVFLICNLPAGILNILEAIFGESFLSPIYQLLGDISNLLVVLNSAVNFIIYCLFSSKFRRTF 299
7TM_GPCR_Srw pfam10324
Serpentine type 7TM GPCR chemoreceptor Srw; Chemoreception is mediated in Caenorhabditis ...
43-353 4.86e-06

Serpentine type 7TM GPCR chemoreceptor Srw; Chemoreception is mediated in Caenorhabditis elegans by members of the seven-transmembrane G-protein-coupled receptor class (7TM GPCRs) of proteins which are of the serpentine type. Srw is a solo family amongst the superfamilies of chemoreceptors. Chemoperception is one of the central senses of soil nematodes like C. elegans which are otherwise 'blind' and 'deaf'. The genes encoding Srw do not appear to be under as strong an adaptive evolutionary pressure as those of Srz.


Pssm-ID: 402097  Cd Length: 318  Bit Score: 47.97  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155   43 ICIFGAASNVFNIIVLTRKRMRT-PINILLTGLSIAQWLLAT----NYFLYLLLEYYRYQCVQLLWSEAFTRYRFFNVnL 117
Cdd:pfam10324   6 LSFIGFIINIFHLIILTRKSMRTsSINIIMIGIAICDIITMLltiyNFIPEFIISYENSECIPPDSYLKVLLDWILES-L 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  118 NTVFHTIAFTTTIVVAVFRYCALKFPIqaNRFIYKC-QPAIAANVIIWIIIPIISLPLFFISEVKIVARDHVAY-DLQCE 195
Cdd:pfam10324  85 QDYSRRCSTWLGVFMALIRTLVVKNPM--SNKIQKLsKPKFGLIIIIIVFILSLPISIFYYFRYEIVEVGGIWKpPPNCA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  196 MEGPLYdlSYQESPLLVSAVFWAF------------GIVFKLLPSLILSILLIALIRSLKSVERRRKNwkrtqganicTN 263
Cdd:pfam10324 163 GFPPNY--TETRYVLVVSELFTANdglllkifllidGIFSKIIPCILLPILTILLIIELRKAKKSRKN----------LS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  264 SERKAKRKLTTRprttrmLVIILLLCVMV-ELPMGILNLCVAIYGEEFGNRY-YDPVGNLMEMLTLLYSSVSFVLYCTMS 341
Cdd:pfam10324 231 SSSKNKSDRTTK------LVIFMTISFFIaEFPLGISYIIQFFFTDNPGIRRiLTYLSVIFSLLFTINSISHCFICFLMS 304
                         330
                  ....*....|..
gi 392926155  342 NEYLSTFRALFF 353
Cdd:pfam10324 305 SQYRKTAKKLFG 316
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
39-341 6.11e-06

rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor superfamily; Class A rhodopsin-like receptors constitute about 90% of all GPCRs. The class A GPCRs include the light-sensitive rhodopsin as well as receptors for biogenic amines, lipids, nucleotides, odorants, peptide hormones, and a variety of other ligands. 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. Based on sequence similarity, GPCRs can be divided into six major classes: class A (rhodopsin-like family), class B (Methuselah-like, adhesion and secretin-like receptor family), class C (metabotropic glutamate receptor family), class D (fungal mating pheromone receptors), class E (cAMP receptor family), and class F (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: 410626 [Multi-domain]  Cd Length: 275  Bit Score: 47.28  E-value: 6.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  39 LSISICIFGAASNVFNIIVLTR-KRMRTPINILLTGLSIAQWLLATNYFLYLLLEYYRYqcvQLLWSEAFTRYRFFnvnL 117
Cdd:cd00637    4 LYILIFVVGLVGNLLVILVILRnRRLRTVTNYFILNLAVADLLVGLLVIPFSLVSLLLG---RWWFGDALCKLLGF---L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 118 NTVFHTIAFTTTIVVAVFRYCALKFPIQANRFIYKCQPAIAANVIIWIIIPIISLPLFFISEVKIVARDHVAYDLQCEME 197
Cdd:cd00637   78 QSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLIALIWLLSLLLALPPLLGWGVYDYGGYCCCCLCWPDLTL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 198 GPLYDLSYQ----ESPLLVsaVFWAFGIVFKLLpslilsillialirslksveRRRKNWKRTQGANICTNSERKAKRKlt 273
Cdd:cd00637  158 SKAYTIFLFvllfLLPLLV--IIVCYVRIFRKL--------------------RRHRRRIRSSSSNSSRRRRRRRERK-- 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392926155 274 trprTTRMLVIILLLCVMVELPMGILNLCVAIYGEEFgnRYYDPVGNLMEMLTLLYSSVSFVLYCTMS 341
Cdd:cd00637  214 ----VTKTLLIVVVVFLLCWLPYFILLLLDVFGPDPS--PLPRILYFLALLLAYLNSAINPIIYAFFN 275
7tmA_ETH-R cd14997
ecdysis-triggering hormone receptors, member of the class A family of seven-transmembrane G ...
43-348 1.48e-04

ecdysis-triggering hormone receptors, member of the class A family of seven-transmembrane G protein-coupled receptors; This subgroup represents the ecdysis-triggering hormone receptors found in insects, which are members of the class A family of seven-transmembrane G-protein coupled receptors. Ecdysis-triggering hormones are vital regulatory signals that govern the stereotypic physiological sequence leading to cuticle shedding in insects. Thus, the ETH signaling system has been a target for the design of more sophisticated insect-selective pest control strategies. Two subtypes of ecdysis-triggering hormone receptor were identified in Drosophila melanogaster. Blood-borne ecdysis-triggering hormone (ETH) activates the behavioral sequence through direct actions on the central nervous system. In insects, ecdysis is thought to be controlled by the interaction between peptide hormones; in particular between ecdysis-triggering hormone (ETH) from the periphery and eclosion hormone (EH) and crustacean cardioactive peptide (CCAP) from the central nervous system. 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: 320128 [Multi-domain]  Cd Length: 294  Bit Score: 43.43  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  43 ICIFGAASNVF-NIIVLTRKRMRTPINILLTGLSIAQWLLatnyflyllleyyRYQCVQLLWSEAFTRY---------RF 112
Cdd:cd14997   10 IFVVGVLGNVLvGIVVWKNKDMRTPTNIFLVNLSVADLLV-------------LLVCMPVALVETWAREpwllgefmcKL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 113 FNVNLNTVFHTiAFTTTIVVAVFRYCALKFPIQANRFIYKCQPAIAAnVIIWIIIPIISLPLFFISEVKIVarDHVAYDL 192
Cdd:cd14997   77 VPFVELTVAHA-SVLTILAISFERYYAICHPLQAKYVCTKRRALVII-ALIWLLALLTSSPVLFITEFKEE--DFNDGTP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 193 --QCEMEgplydLSYQESPLLVSAVFWAFGIVfkllpslilsilLIALIRSLKSVERRRKNWKRtqgANICTNSERKAKR 270
Cdd:cd14997  153 vaVCRTP-----ADTFWKVAYILSTIVVFFVV------------PLAILSGLYSVICRRLVGHP---ALESRRADAANRH 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155 271 KLTTRPRTTRMLVIILLLCVMVELPMGILNLCVaIYG-----EEFGNRYYDPVGNLMEMLTLLYSSVSFVLYCTMSNEYL 345
Cdd:cd14997  213 TLRSRRQVVYMLITVVVLFFVCLLPFRVVTLWI-IFApdedlQALGLEGYLNLLVFCRVMVYLNSALNPILYNLMSTKFR 291

                 ...
gi 392926155 346 STF 348
Cdd:cd14997  292 SAF 294
7tmA_Opsins_type2_animals cd14969
type 2 opsins in animals, member of the class A family of seven-transmembrane G ...
43-149 7.67e-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: 7.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392926155  43 ICIFGAASNVFNIIVLTRKR-MRTPINILLTGLSIAQWLLATNYFLYLLLEyyryqCVQLLWSEAFTR---YRFFnvnlN 118
Cdd:cd14969   10 IGVLGVVLNGLVIIVFLKKKkLRTPLNLFLLNLALADLLMSVVGYPLSFYS-----NLSGRWSFGDPGcviYGFA----V 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 392926155 119 TVFHTIAFTTTIVVAVFRYCALKFPIQANRF 149
Cdd:cd14969   81 TFLGLVSISTLAALAFERYLVIVRPLKAFRL 111
 
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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