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Conserved domains on  [gi|1039731027|ref|XP_017169107|]
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uncharacterized protein LOC101055758 isoform X2 [Mus musculus]

Protein Classification

G-protein coupled receptor( domain architecture ID 11535993)

G-protein coupled receptor transmits physiological signals from the outside of the cell to the inside via G proteins 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
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
89-277 9.53e-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: 46.13  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027  89 LCWLVFGAQLSVGEGILLTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTMVILKNVGLFLIEGTSPTPASVFQs 167
Cdd:cd00637    70 LCKLLGFLQSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLiALIWLLSLLLALPPLLGWGVYDYGGYCCC- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 168 aPLCPVILNGMPARVIGMFSLAFL--LSVILVSYYLIY-------------QEGKRAGHFNKSNIKAQRTVLVHLLQISL 232
Cdd:cd00637   149 -CLCWPDLTLSKAYTIFLFVLLFLlpLLVIIVCYVRIFrklrrhrrrirssSSNSSRRRRRRRERKVTKTLLIVVVVFLL 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039731027 233 HVIPTLIIIGLGKRCGVFFFALNLALFGIFAFAQ---CFNPLVYGLHN 277
Cdd:cd00637   228 CWLPYFILLLLDVFGPDPSPLPRILYFLALLLAYlnsAINPIIYAFFN 275
 
Name Accession Description Interval E-value
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
89-277 9.53e-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: 46.13  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027  89 LCWLVFGAQLSVGEGILLTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTMVILKNVGLFLIEGTSPTPASVFQs 167
Cdd:cd00637    70 LCKLLGFLQSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLiALIWLLSLLLALPPLLGWGVYDYGGYCCC- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 168 aPLCPVILNGMPARVIGMFSLAFL--LSVILVSYYLIY-------------QEGKRAGHFNKSNIKAQRTVLVHLLQISL 232
Cdd:cd00637   149 -CLCWPDLTLSKAYTIFLFVLLFLlpLLVIIVCYVRIFrklrrhrrrirssSSNSSRRRRRRRERKVTKTLLIVVVVFLL 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039731027 233 HVIPTLIIIGLGKRCGVFFFALNLALFGIFAFAQ---CFNPLVYGLHN 277
Cdd:cd00637   228 CWLPYFILLLLDVFGPDPSPLPRILYFLALLLAYlnsAINPIIYAFFN 275
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
106-273 1.26e-05

7 transmembrane receptor (rhodopsin family); This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins.


Pssm-ID: 459624 [Multi-domain]  Cd Length: 256  Bit Score: 45.75  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 106 LTLTLMALNTYLAICYPLNSPSFVDSAK-YRILAGTWTMVILKNVGLFLIEGTSPTP-ASVFQSAPLCPVILNGMPARVI 183
Cdd:pfam00001  74 LLLTAISIDRYLAIVHPLRYKRRRTPRRaKVLILVIWVLALLLSLPPLLFGWTLTVPeGNVTVCFIDFPEDLSKPVSYTL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 184 GMFSLAFL--LSVILVSYYLIYQEGKRAGHFNKSN------IKAQRTVLVHLLQISLHVIPTLI--IIGLGKRCGVFFFA 253
Cdd:pfam00001 154 LISVLGFLlpLLVILVCYTLIIRTLRKSASKQKSSertqrrRKALKTLAVVVVVFILCWLPYHIvnLLDSLALDCELSRL 233
                         170       180
                  ....*....|....*....|...
gi 1039731027 254 LNLALFGIFAFA---QCFNPLVY 273
Cdd:pfam00001 234 LDKALSVTLWLAyvnSCLNPIIY 256
 
Name Accession Description Interval E-value
7tm_classA_rhodopsin-like cd00637
rhodopsin receptor-like class A family of the seven-transmembrane G protein-coupled receptor ...
89-277 9.53e-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: 46.13  E-value: 9.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027  89 LCWLVFGAQLSVGEGILLTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTMVILKNVGLFLIEGTSPTPASVFQs 167
Cdd:cd00637    70 LCKLLGFLQSVSLLASILTLTAISVDRYLAIVHPLRYRRRFTRRRAKLLiALIWLLSLLLALPPLLGWGVYDYGGYCCC- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 168 aPLCPVILNGMPARVIGMFSLAFL--LSVILVSYYLIY-------------QEGKRAGHFNKSNIKAQRTVLVHLLQISL 232
Cdd:cd00637   149 -CLCWPDLTLSKAYTIFLFVLLFLlpLLVIIVCYVRIFrklrrhrrrirssSSNSSRRRRRRRERKVTKTLLIVVVVFLL 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1039731027 233 HVIPTLIIIGLGKRCGVFFFALNLALFGIFAFAQ---CFNPLVYGLHN 277
Cdd:cd00637   228 CWLPYFILLLLDVFGPDPSPLPRILYFLALLLAYlnsAINPIIYAFFN 275
7tm_1 pfam00001
7 transmembrane receptor (rhodopsin family); This family contains, amongst other ...
106-273 1.26e-05

7 transmembrane receptor (rhodopsin family); This family contains, amongst other G-protein-coupled receptors (GCPRs), members of the opsin family, which have been considered to be typical members of the rhodopsin superfamily. They share several motifs, mainly the seven transmembrane helices, GCPRs of the rhodopsin superfamily. All opsins bind a chromophore, such as 11-cis-retinal. The function of most opsins other than the photoisomerases is split into two steps: light absorption and G-protein activation. Photoisomerases, on the other hand, are not coupled to G-proteins - they are thought to generate and supply the chromophore that is used by visual opsins.


Pssm-ID: 459624 [Multi-domain]  Cd Length: 256  Bit Score: 45.75  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 106 LTLTLMALNTYLAICYPLNSPSFVDSAK-YRILAGTWTMVILKNVGLFLIEGTSPTP-ASVFQSAPLCPVILNGMPARVI 183
Cdd:pfam00001  74 LLLTAISIDRYLAIVHPLRYKRRRTPRRaKVLILVIWVLALLLSLPPLLFGWTLTVPeGNVTVCFIDFPEDLSKPVSYTL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 184 GMFSLAFL--LSVILVSYYLIYQEGKRAGHFNKSN------IKAQRTVLVHLLQISLHVIPTLI--IIGLGKRCGVFFFA 253
Cdd:pfam00001 154 LISVLGFLlpLLVILVCYTLIIRTLRKSASKQKSSertqrrRKALKTLAVVVVVFILCWLPYHIvnLLDSLALDCELSRL 233
                         170       180
                  ....*....|....*....|...
gi 1039731027 254 LNLALFGIFAFA---QCFNPLVY 273
Cdd:pfam00001 234 LDKALSVTLWLAyvnSCLNPIIY 256
7tmA_AstC_insect cd15094
somatostatin-like receptor for allatostatin C, member of the class A family of ...
106-218 8.19e-04

somatostatin-like receptor for allatostatin C, member of the class A family of seven-transmembrane G protein-coupled receptors; G protein-coupled somatostatin receptors (SSTRs) are composed of five distinct subtypes (SSTR1-5) that display strong sequence similarity with opioid receptors. All five receptor subtypes bind the natural somatostatin (somatotropin release inhibiting factor), a polypeptide hormone that regulates a wide variety of physiological functions such as neurotransmission, cell proliferation, contractility of smooth muscle cells, and endocrine signaling as well as inhibition of the release of many secondary hormones. In Drosophila melanogaster and other insects, a 15-amino-acid peptide named allatostatin C(AstC) binds the somatostatin-like receptors. Two AstC receptors have been identified in Drosophila with strong sequence homology to human somatostatin and opioid receptors.


Pssm-ID: 320222 [Multi-domain]  Cd Length: 282  Bit Score: 40.15  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 106 LTLTLMALNTYLAICYPLNSPSFVDSAKYRIL-AGTWTMVILKNVGLFLIegTSPTPASVFQSaplCPVI------LNGM 178
Cdd:cd15094    88 FTLTVMSADRYLAVCHPIRSMRYRTPFIAKVVcATTWSISFLVMLPIILY--ASTVPDSGRYS---CTIVwpdssaVNGQ 162
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039731027 179 PARVIGMFSLAFL--LSVILVSYYLIYQEGKRAGHFNKSNIK 218
Cdd:cd15094   163 KAFTLYTFLLGFAipLLLISVFYTLVILRLRTVGPKNKSKEK 204
7tmA_GPRnna14-like cd15001
GPRnna14 and related proteins, member of the class A family of seven-transmembrane G ...
105-199 6.35e-03

GPRnna14 and related proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; This group includes the orphan G-protein coupled receptor GPRnna14 found in body louse (Pediculus humanus humanus) as well as its closely related proteins of unknown function. These receptors are members of the class A rhodopsin-like G-protein coupled receptors. As an obligatory parasite of humans, the body louse is an important vector for human diseases, including epidemic typhus, relapsing fever, and trench fever. GPRnna14 shares significant sequence similarity with the members of the neurotensin receptor family. 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: 320132 [Multi-domain]  Cd Length: 266  Bit Score: 37.64  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 105 LLTLTLMALNTYLAICYPLNSPSF--VDSAKyRILAGTWTMVILKNVGLFLIEGTSPTPASVFQSAPLCPVILNGM---P 179
Cdd:cd15001    87 VLTLTAISIERYYVILHPMKAKSFctIGRAR-KVALLIWILSAILASPVLFGQGLVRYESENGVTVYHCQKAWPSTlysR 165
                          90       100
                  ....*....|....*....|
gi 1039731027 180 ARVIGMFSLAFLLSVILVSY 199
Cdd:cd15001   166 LYVVYLAIVIFFIPLIVMTF 185
7tmA_amine_R-like cd14967
amine receptors and similar proteins, member of the class A family of seven-transmembrane G ...
106-279 7.07e-03

amine receptors and similar proteins, member of the class A family of seven-transmembrane G protein-coupled receptors; Amine receptors of the class A family of GPCRs include adrenoceptors, 5-HT (serotonin) receptors, muscarinic cholinergic receptors, dopamine receptors, histamine receptors, and trace amine receptors. The receptors of amine subfamily are major therapeutic targets for the treatment of neurological disorders and psychiatric diseases. 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: 320098 [Multi-domain]  Cd Length: 259  Bit Score: 37.16  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 106 LTLTLMALNTYLAICYPLNSPSFVDSAK-YRILAGTWTMVILknVGLFLIEGTSPTPaSVFQSAPLCPVILNgmPARVIG 184
Cdd:cd14967    88 LNLCAISLDRYLAITRPLRYRQLMTKKRaLIMIAAVWVYSLL--ISLPPLVGWRDET-QPSVVDCECEFTPN--KIYVLV 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039731027 185 MFSLAFLL--SVILVSYYLIYQEGKRaghfnksNIKAQRTVLVHLLQISLHVIPTLIIIGLGKRCGVFFF-ALNLALFGI 261
Cdd:cd14967   163 SSVISFFIplLIMIVLYARIFRVARR-------ELKAAKTLAIIVGAFLLCWLPFFIIYLVSAFCPPDCVpPILYAVFFW 235
                         170
                  ....*....|....*....
gi 1039731027 262 FAFAQ-CFNPLVYGLHNRD 279
Cdd:cd14967   236 LGYLNsALNPIIYALFNRD 254
 
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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