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Conserved domains on  [gi|71989223|ref|NP_001023783|]
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G-protein coupled receptors family 1 profile 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 ...
21-284 1.12e-61

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: 197.05  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223    21 TIGTFGVICNSSIVCIFLKEKSEKTAFNTICFFRATSNIIILTIaFLTNFLPKTLLGYSPYPDVIES-WLIHISHTLYLG 99
Cdd:pfam10328   2 LISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICLI-FLFYVVPMTLFQNSFLPEWLNShIIGLIAMGLYEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223   100 NEYQIVLIAINRFCAVFLPTKYATIFSLFNITIILVFIYIFRIAKKIYELLPEsakGCHALFSTNSLTWYFSTSPGCNST 179
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPE---GCHFYYNPETLTWSFEDTPCCDFI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223   180 ENALEMIKCT--FIMMAILNFITFLKILHSYKKSRKTETVvgARKRMCKNILCFLQTILQDSLYFIDMTFTFKLSSWSTN 257
Cdd:pfam10328 158 TWYLDFYKNLslVIITLFLNLLTAIKLRVSKKKSNTSSSE--SKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDN 235
                         250       260
                  ....*....|....*....|....*..
gi 71989223   258 RIWTYFSGTFVWECLHSFDGFIMIIFN 284
Cdd:pfam10328 236 RWFQFFFTTLSWVFVHALDGFIMLAFN 262
 
Name Accession Description Interval E-value
7TM_GPCR_Srx pfam10328
Serpentine type 7TM GPCR chemoreceptor Srx; Chemoreception is mediated in Caenorhabditis ...
21-284 1.12e-61

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: 197.05  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223    21 TIGTFGVICNSSIVCIFLKEKSEKTAFNTICFFRATSNIIILTIaFLTNFLPKTLLGYSPYPDVIES-WLIHISHTLYLG 99
Cdd:pfam10328   2 LISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICLI-FLFYVVPMTLFQNSFLPEWLNShIIGLIAMGLYEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223   100 NEYQIVLIAINRFCAVFLPTKYATIFSLFNITIILVFIYIFRIAKKIYELLPEsakGCHALFSTNSLTWYFSTSPGCNST 179
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPE---GCHFYYNPETLTWSFEDTPCCDFI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223   180 ENALEMIKCT--FIMMAILNFITFLKILHSYKKSRKTETVvgARKRMCKNILCFLQTILQDSLYFIDMTFTFKLSSWSTN 257
Cdd:pfam10328 158 TWYLDFYKNLslVIITLFLNLLTAIKLRVSKKKSNTSSSE--SKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDN 235
                         250       260
                  ....*....|....*....|....*..
gi 71989223   258 RIWTYFSGTFVWECLHSFDGFIMIIFN 284
Cdd:pfam10328 236 RWFQFFFTTLSWVFVHALDGFIMLAFN 262
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
16-140 1.61e-04

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: 42.66  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223  16 AFLMATIGTFGVICNSSIVCIFLKEKSEKTAFNTICFFRATSNIIILTIAFLTnFLPKTLLGYSPYPDVIESWLIHISHT 95
Cdd:cd00637   2 AVLYILIFVVGLVGNLLVILVILRNRRLRTVTNYFILNLAVADLLVGLLVIPF-SLVSLLLGRWWFGDALCKLLGFLQSV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71989223  96 LYLGNEYQIVLIAINRFCAVFLPTKYATIFSLFNITIILVFIYIF 140
Cdd:cd00637  81 SLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLIALIWLL 125
 
Name Accession Description Interval E-value
7TM_GPCR_Srx pfam10328
Serpentine type 7TM GPCR chemoreceptor Srx; Chemoreception is mediated in Caenorhabditis ...
21-284 1.12e-61

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: 197.05  E-value: 1.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223    21 TIGTFGVICNSSIVCIFLKEKSEKTAFNTICFFRATSNIIILTIaFLTNFLPKTLLGYSPYPDVIES-WLIHISHTLYLG 99
Cdd:pfam10328   2 LISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICLI-FLFYVVPMTLFQNSFLPEWLNShIIGLIAMGLYEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223   100 NEYQIVLIAINRFCAVFLPTKYATIFSLFNITIILVFIYIFRIAKKIYELLPEsakGCHALFSTNSLTWYFSTSPGCNST 179
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPE---GCHFYYNPETLTWSFEDTPCCDFI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223   180 ENALEMIKCT--FIMMAILNFITFLKILHSYKKSRKTETVvgARKRMCKNILCFLQTILQDSLYFIDMTFTFKLSSWSTN 257
Cdd:pfam10328 158 TWYLDFYKNLslVIITLFLNLLTAIKLRVSKKKSNTSSSE--SKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDN 235
                         250       260
                  ....*....|....*....|....*..
gi 71989223   258 RIWTYFSGTFVWECLHSFDGFIMIIFN 284
Cdd:pfam10328 236 RWFQFFFTTLSWVFVHALDGFIMLAFN 262
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
16-140 1.61e-04

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: 42.66  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223  16 AFLMATIGTFGVICNSSIVCIFLKEKSEKTAFNTICFFRATSNIIILTIAFLTnFLPKTLLGYSPYPDVIESWLIHISHT 95
Cdd:cd00637   2 AVLYILIFVVGLVGNLLVILVILRNRRLRTVTNYFILNLAVADLLVGLLVIPF-SLVSLLLGRWWFGDALCKLLGFLQSV 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 71989223  96 LYLGNEYQIVLIAINRFCAVFLPTKYATIFSLFNITIILVFIYIF 140
Cdd:cd00637  81 SLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLIALIWLL 125
7tmA_Opsins_type2_animals cd14969
type 2 opsins in animals, member of the class A family of seven-transmembrane G ...
14-216 2.26e-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: 39.11  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223  14 GVAFLMATIGTFGVICNSSIVCIFLKEKSEKTAFNTICFFRATSNIII----LTIAFLTNFLPKTLLGYSPYpdVIESWl 89
Cdd:cd14969   2 VLAVYLSLIGVLGVVLNGLVIIVFLKKKKLRTPLNLFLLNLALADLLMsvvgYPLSFYSNLSGRWSFGDPGC--VIYGF- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71989223  90 ihISHTLYLGNEYQIVLIAINRFCAVFLPTKYaTIFSLFNITIILVFIYIFRIAKKIYELLPESAKGCHALFSTNSLTWY 169
Cdd:cd14969  79 --AVTFLGLVSISTLAALAFERYLVIVRPLKA-FRLSKRRALILIAFIWLYGLFWALPPLFGWSSYVPEGGGTSCSVDWY 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 71989223 170 fSTSPGCNSTENALeMIKCTFIMMAILnFITFLKILHSYKKSRKTET 216
Cdd:cd14969 156 -SKDPNSLSYIVSL-FVFCFFLPLAII-IFCYYKIYRTLRKMSKRAA 199
 
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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