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Conserved domains on  [gi|17561878|ref|NP_505938|]
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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 2.83e-67

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: 211.30  E-value: 2.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878    21 TIGMFGVFCNSVIIYIFLKEKSEKTAFNVICFFRAISNVIILTnVFLINFLPKTLLGFSPYPPVIES-WLINTSNTLYLG 99
Cdd:pfam10328   2 LISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICL-IFLFYVVPMTLFQNSFLPEWLNShIIGLIAMGLYEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878   100 NEYQIVLVAVNRFCALFFPTKYSKIFSVSHTTIILILIYFYRIAKKIYELLPEsakGCHALYSTEALAWYYSTAPECTWV 179
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPE---GCHFYYNPETLTWSFEDTPCCDFI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878   180 DNALEVIKYT--FMSMAFLNCITFLKILHFYRKSRktQEAVEVKKRWRKNIALFLQTILQDSLYFIDMTFTFELSSLSTN 257
Cdd:pfam10328 158 TWYLDFYKNLslVIITLFLNLLTAIKLRVSKKKSN--TSSSESKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDN 235

                         250       260
                  ....*....|....*....|....*..
gi 17561878   258 RVWTYFSGTFIWECLHSFDGFIMVLFN 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 2.83e-67

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: 211.30  E-value: 2.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878    21 TIGMFGVFCNSVIIYIFLKEKSEKTAFNVICFFRAISNVIILTnVFLINFLPKTLLGFSPYPPVIES-WLINTSNTLYLG 99
Cdd:pfam10328   2 LISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICL-IFLFYVVPMTLFQNSFLPEWLNShIIGLIAMGLYEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878   100 NEYQIVLVAVNRFCALFFPTKYSKIFSVSHTTIILILIYFYRIAKKIYELLPEsakGCHALYSTEALAWYYSTAPECTWV 179
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPE---GCHFYYNPETLTWSFEDTPCCDFI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878   180 DNALEVIKYT--FMSMAFLNCITFLKILHFYRKSRktQEAVEVKKRWRKNIALFLQTILQDSLYFIDMTFTFELSSLSTN 257
Cdd:pfam10328 158 TWYLDFYKNLslVIITLFLNLLTAIKLRVSKKKSN--TSSSESKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDN 235

                         250       260
                  ....*....|....*....|....*..
gi 17561878   258 RVWTYFSGTFIWECLHSFDGFIMVLFN 284
Cdd:pfam10328 236 RWFQFFFTTLSWVFVHALDGFIMLAFN 262
7tmA_Opsins_type2_animals cd14969
type 2 opsins in animals, member of the class A family of seven-transmembrane G ...
 14-140 4.11e-06

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: 47.59  E-value: 4.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878  14 VVAVLMGTIGMFGVFCNSVIIYIFLKEKSEKTAFNVICFFRAISNVIILTNVFLI----NFLPKTLLGFSPYppVIESWL 89
Cdd:cd14969   2 VLAVYLSLIGVLGVVLNGLVIIVFLKKKKLRTPLNLFLLNLALADLLMSVVGYPLsfysNLSGRWSFGDPGC--VIYGFA 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17561878  90 IntsNTLYLGNEYQIVLVAVNRFCALFFPTKYSKiFSVSHTTIILILIYFY 140
Cdd:cd14969  80 V---TFLGLVSISTLAALAFERYLVIVRPLKAFR-LSKRRALILIAFIWLY 126
 
Name Accession Description Interval E-value
7TM_GPCR_Srx pfam10328
Serpentine type 7TM GPCR chemoreceptor Srx; Chemoreception is mediated in Caenorhabditis ...
 21-284 2.83e-67

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: 211.30  E-value: 2.83e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878    21 TIGMFGVFCNSVIIYIFLKEKSEKTAFNVICFFRAISNVIILTnVFLINFLPKTLLGFSPYPPVIES-WLINTSNTLYLG 99
Cdd:pfam10328   2 LISLIGLVANLLVFIAFLKLPSLKNSFGILCLSQAIGNAIICL-IFLFYVVPMTLFQNSFLPEWLNShIIGLIAMGLYEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878   100 NEYQIVLVAVNRFCALFFPTKYSKIFSVSHTTIILILIYFYRIAKKIYELLPEsakGCHALYSTEALAWYYSTAPECTWV 179
Cdd:pfam10328  81 SPLSHLLIALNRFCAVFFPLKYEKIFSIKNTKIIIIFIWIVSIIFCTVFYEPE---GCHFYYNPETLTWSFEDTPCCDFI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878   180 DNALEVIKYT--FMSMAFLNCITFLKILHFYRKSRktQEAVEVKKRWRKNIALFLQTILQDSLYFIDMTFTFELSSLSTN 257
Cdd:pfam10328 158 TWYLDFYKNLslVIITLFLNLLTAIKLRVSKKKSN--TSSSESKRRRKREINFFKQTCFQDLLFLIDLVNYYIIAPLSDN 235

                         250       260
                  ....*....|....*....|....*..
gi 17561878   258 RVWTYFSGTFIWECLHSFDGFIMVLFN 284
Cdd:pfam10328 236 RWFQFFFTTLSWVFVHALDGFIMLAFN 262
7tmA_Opsins_type2_animals cd14969
type 2 opsins in animals, member of the class A family of seven-transmembrane G ...
 14-140 4.11e-06

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: 47.59  E-value: 4.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17561878  14 VVAVLMGTIGMFGVFCNSVIIYIFLKEKSEKTAFNVICFFRAISNVIILTNVFLI----NFLPKTLLGFSPYppVIESWL 89
Cdd:cd14969   2 VLAVYLSLIGVLGVVLNGLVIIVFLKKKKLRTPLNLFLLNLALADLLMSVVGYPLsfysNLSGRWSFGDPGC--VIYGFA 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 17561878  90 IntsNTLYLGNEYQIVLVAVNRFCALFFPTKYSKiFSVSHTTIILILIYFY 140
Cdd:cd14969  80 V---TFLGLVSISTLAALAFERYLVIVRPLKAFR-LSKRRALILIAFIWLY 126
7tmA_photoreceptors_insect cd15079
insect photoreceptors R1-R6 and similar proteins, member of the class A family of ...
 16-71 1.28e-03

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: 39.87  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 17561878  16 AVLMGTIGMFGVFCNSVIIYIFLKEKSEKTAFNVICFFRAISNVIILTN--VFLINFL 71
Cdd:cd15079   4 GFIYIFLGIVSLLGNGLVIYIFSTTKSLRTPSNMLVVNLAISDFLMMIKmpIFIYNSF 61
 
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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