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Conserved domains on  [gi|351063879|emb|CCD72121|]
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7TM GPCR serpentine receptor class x (Srx) domain-containing protein [Caenorhabditis elegans]

Protein Classification

serpentine type G-protein coupled receptor( domain architecture ID 10563435)

serpentine type G-protein coupled receptor, also known as seven TM receptor (Str), belongs to a family of seven-transmembrane (7TM) G protein-coupled receptors involved in chemoreception, a central sense of soil nematodes like Caenorhabditis elegans

CATH:  1.20.1070.10
Gene Ontology:  GO:0005886|GO:0004930
PubMed:  18050473|19458711

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7TM_GPCR_Srx pfam10328
Serpentine type 7TM GPCR chemoreceptor Srx; Chemoreception is mediated in Caenorhabditis ...
30-292 2.96e-57

Serpentine type 7TM GPCR chemoreceptor Srx; 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. Srx is part of the Srg superfamily of chemoreceptors. Chemoperception is one of the central senses of soil nematodes like C. elegans which are otherwise 'blind' and 'deaf'.


:

Pssm-ID: 431215  Cd Length: 262  Bit Score: 185.88  E-value: 2.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879   30 FTISLTGLIGNLSVFMFATTLKTLQNSFGRLSASQSFAEAVLCGVFLFFYCPMVLLDIPTFKRV--SAQVGLILLFCYDV 107
Cdd:pfam10328   1 FLISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICLIFLFYVVPMTLFQNSFLPEWlnSHIIGLIAMGLYEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  108 CIFSHLFIAFNRLCAISFPIEYNSFFNMRNTRILIALAYAIPCFTSIYMHLANNCNLPYVDFGWYFGVNTSADCDVIRFY 187
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPEGCHFYYNPETLTWSFEDTPCCDFITWY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  188 VDFCKDFGVVALIAIVDVGTIVMIKVTapgMKLLSANCAQSQKKRQREITFVKQALIQGAVFATELVFFFIISGMQSQPV 267
Cdd:pfam10328 161 LDFYKNLSLVIITLFLNLLTAIKLRVS---KKKSNTSSSESKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDNRW 237
                         250       260
                  ....*....|....*....|....*
gi 351063879  268 AIFLCTTVAWSLVHTIDPLVLILLN 292
Cdd:pfam10328 238 FQFFFTTLSWVFVHALDGFIMLAFN 262
 
Name Accession Description Interval E-value
7TM_GPCR_Srx pfam10328
Serpentine type 7TM GPCR chemoreceptor Srx; Chemoreception is mediated in Caenorhabditis ...
30-292 2.96e-57

Serpentine type 7TM GPCR chemoreceptor Srx; 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. Srx is part of the Srg superfamily of chemoreceptors. Chemoperception is one of the central senses of soil nematodes like C. elegans which are otherwise 'blind' and 'deaf'.


Pssm-ID: 431215  Cd Length: 262  Bit Score: 185.88  E-value: 2.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879   30 FTISLTGLIGNLSVFMFATTLKTLQNSFGRLSASQSFAEAVLCGVFLFFYCPMVLLDIPTFKRV--SAQVGLILLFCYDV 107
Cdd:pfam10328   1 FLISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICLIFLFYVVPMTLFQNSFLPEWlnSHIIGLIAMGLYEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  108 CIFSHLFIAFNRLCAISFPIEYNSFFNMRNTRILIALAYAIPCFTSIYMHLANNCNLPYVDFGWYFGVNTSADCDVIRFY 187
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPEGCHFYYNPETLTWSFEDTPCCDFITWY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  188 VDFCKDFGVVALIAIVDVGTIVMIKVTapgMKLLSANCAQSQKKRQREITFVKQALIQGAVFATELVFFFIISGMQSQPV 267
Cdd:pfam10328 161 LDFYKNLSLVIITLFLNLLTAIKLRVS---KKKSNTSSSESKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDNRW 237
                         250       260
                  ....*....|....*....|....*
gi 351063879  268 AIFLCTTVAWSLVHTIDPLVLILLN 292
Cdd:pfam10328 238 FQFFFTTLSWVFVHALDGFIMLAFN 262
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
26-211 5.36e-07

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: 50.36  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  26 TLAIFTISLTGLIGNLSVFMFATTLKTLQNSFGRLSASQSFAEAVLCGVFLFFYCPMVLLDIPTFKRVSAQV-GLILLFC 104
Cdd:cd00637    2 AVLYILIFVVGLVGNLLVILVILRNRRLRTVTNYFILNLAVADLLVGLLVIPFSLVSLLLGRWWFGDALCKLlGFLQSVS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879 105 YDVCIFSHLFIAFNRLCAISFPIEYNSFFNMRNTRILIALAYAIPCFtsiymhlannCNLPYVDFGWYFGVNTSADCDVI 184
Cdd:cd00637   82 LLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLIALIWLLSLL----------LALPPLLGWGVYDYGGYCCCCLC 151
                        170       180
                 ....*....|....*....|....*..
gi 351063879 185 RFYVDFCKDFGVVALIAIVDVGTIVMI 211
Cdd:cd00637  152 WPDLTLSKAYTIFLFVLLFLLPLLVII 178
 
Name Accession Description Interval E-value
7TM_GPCR_Srx pfam10328
Serpentine type 7TM GPCR chemoreceptor Srx; Chemoreception is mediated in Caenorhabditis ...
30-292 2.96e-57

Serpentine type 7TM GPCR chemoreceptor Srx; 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. Srx is part of the Srg superfamily of chemoreceptors. Chemoperception is one of the central senses of soil nematodes like C. elegans which are otherwise 'blind' and 'deaf'.


Pssm-ID: 431215  Cd Length: 262  Bit Score: 185.88  E-value: 2.96e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879   30 FTISLTGLIGNLSVFMFATTLKTLQNSFGRLSASQSFAEAVLCGVFLFFYCPMVLLDIPTFKRV--SAQVGLILLFCYDV 107
Cdd:pfam10328   1 FLISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICLIFLFYVVPMTLFQNSFLPEWlnSHIIGLIAMGLYEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  108 CIFSHLFIAFNRLCAISFPIEYNSFFNMRNTRILIALAYAIPCFTSIYMHLANNCNLPYVDFGWYFGVNTSADCDVIRFY 187
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPEGCHFYYNPETLTWSFEDTPCCDFITWY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  188 VDFCKDFGVVALIAIVDVGTIVMIKVTapgMKLLSANCAQSQKKRQREITFVKQALIQGAVFATELVFFFIISGMQSQPV 267
Cdd:pfam10328 161 LDFYKNLSLVIITLFLNLLTAIKLRVS---KKKSNTSSSESKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDNRW 237
                         250       260
                  ....*....|....*....|....*
gi 351063879  268 AIFLCTTVAWSLVHTIDPLVLILLN 292
Cdd:pfam10328 238 FQFFFTTLSWVFVHALDGFIMLAFN 262
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
26-211 5.36e-07

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: 50.36  E-value: 5.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  26 TLAIFTISLTGLIGNLSVFMFATTLKTLQNSFGRLSASQSFAEAVLCGVFLFFYCPMVLLDIPTFKRVSAQV-GLILLFC 104
Cdd:cd00637    2 AVLYILIFVVGLVGNLLVILVILRNRRLRTVTNYFILNLAVADLLVGLLVIPFSLVSLLLGRWWFGDALCKLlGFLQSVS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879 105 YDVCIFSHLFIAFNRLCAISFPIEYNSFFNMRNTRILIALAYAIPCFtsiymhlannCNLPYVDFGWYFGVNTSADCDVI 184
Cdd:cd00637   82 LLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLIALIWLLSLL----------LALPPLLGWGVYDYGGYCCCCLC 151
                        170       180
                 ....*....|....*....|....*..
gi 351063879 185 RFYVDFCKDFGVVALIAIVDVGTIVMI 211
Cdd:cd00637  152 WPDLTLSKAYTIFLFVLLFLLPLLVII 178
7tmA_GPR88-like cd15211
G protein-coupled receptor 88, member of the class A family of seven-transmembrane G ...
24-149 4.47e-04

G protein-coupled receptor 88, member of the class A family of seven-transmembrane G protein-coupled receptors; GPR88, an orphan G protein-coupled receptor, is predominantly and almost exclusively expressed within medium spiny neurons (MSNs) of the brain's striatum in both human and rodents; thus it is also called Striatum-specific GPCR (STRG). The striatum is known to involve in motor coordination, reward-based decision making, and response learning. GPR88 is shown to co-localize with both dopamine D1 and D2 receptors and displays the highest sequence similarity to receptors for biogenic amines such as dopamine and serotonin. GPR88 knockout mice showed abnormal behaviors observed in schizophrenia, such as disrupted sensorimotor gating, increased stereotypic behavior and locomotor activity in response to treatment with dopaminergic compounds such as apomorphine and amphetamine, respectively, suggesting a role for GPR88 in dopaminergic signaling. Furthermore, the transcriptional profiling studies showed that GPR88 expression is altered in a number of psychiatric disorders such as depression, drug addiction, bipolar and schizophrenia, providing further evidence that GPR88 plays an important role in CNS signaling pathways related to psychiatric disorder. 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: 320339 [Multi-domain]  Cd Length: 283  Bit Score: 41.37  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 351063879  24 FVTLAIFTISLTGLIGNLSVFMFATTLKTLQNSFGRLSASQSFAEAVLCGvflfFYCP--MVLLDIPTFKRVSAQV--GL 99
Cdd:cd15211    1 SLSTVYSFLAVSGTLANVLVIYLVVSFKKLQTTSNAFIVNGCVADLLVCA----FWMPqeAVLGSTGTLLVLGYRLfrEG 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 351063879 100 ILLFCYDVCIFSHLFIAFNRLCAIS-FPIEYNSFFNMRNTRILIALAYAIP 149
Cdd:cd15211   77 LLFLGLTVSLLSHSLIALNRYVLITkLPAVYQALYQKRNTEWMIALSWALA 127
7tmA_TAAR5-like cd15317
trace amine-associated receptor 5 and similar receptors, member of the class A family of ...
98-154 4.35e-03

trace amine-associated receptor 5 and similar receptors, member of the class A family of seven-transmembrane G protein-coupled receptors; Included in this group are mammalian TAAR5, TAAR6, TAAR8, TAAR9, and similar proteins. They are among the 15 identified trace amine-associated receptors (TAARs), a distinct subfamily within the class A G protein-coupled receptors. Trace amines are endogenous amines of unknown function that have strong structural and metabolic similarity to classical monoamine neurotransmitters (serotonin, noradrenaline, adrenaline, dopamine, and histamine), which play critical roles in human and animal physiological activities such as cognition, consciousness, mood, motivation, perception, and autonomic responses. However, trace amines are found in the mammalian brain at very low concentrations compared to classical monoamines. Trace amines, including p-tyramine, beta-phenylethylamine, and tryptamine, are also thought to act as chemical messengers to exert their biological effects in vertebrates. 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: 320440 [Multi-domain]  Cd Length: 290  Bit Score: 38.20  E-value: 4.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 351063879  98 GLILLFCYdVCIFSHLFIAFNRLCAISFPIEYNSFFNMRNTRILIALAYAIPCFTSI 154
Cdd:cd15317   78 GLDLLLCT-TSIFHLCFIAIDRYYAVCDPLRYPSKITVQVAWRFIAIGWLVPGIYTF 133
 
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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