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Conserved domains on  [gi|1864383739|pdb|7C7Q|B]
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Chain B, Gamma-aminobutyric acid type B receptor subunit 2

Protein Classification

class C G-protein coupled receptor; G-protein-coupled receptor( domain architecture ID 11570841)

class C 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 binds to and activates numerous downstream effector proteins; class C GPCRs include metabotropic glutamate receptors (mGluRs) and gamma-aminobutyric acid type B (GABA-B) receptors| G-protein-coupled receptor (GPCR) containing an extracellular PBP1 (type 1 periplasmic-binding protein) ligand-binding domain, belongs to the class C GPCRs, which are mainly composed of metabotropic glutamate receptors (mGluRs), gamma-aminobutyric acid type B (GABA-B) receptors, Ca(2+)-sensing receptors (CaSR), taste receptors (T1R), and pheromone receptors (V2R)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
47-449 0e+00

ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


:

Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 528.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLTkEVAKGSIGRGVLPAVELAIEQIRNES-LLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCP 125
Cdd:cd06366   2 IGGLFPLS-GSKGWWGGAGILPAAEMALEHINNRSdILPGYNLELIWNDTQCDPGLGLKALYDLLYTPPPKVMLLGPGCS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      126 SVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLT 205
Cdd:cd06366  81 SVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      206 GVLYGEDIEISDTESFSN-DPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEqvhT 284
Cdd:cd06366 161 ELLEEANITIVATESFSSeDPTDQLENLKEKDARIIIGLFYEDAARKVFCEAYKLGMYGPKYVWILPGWYDDNWWD---V 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      285 EANSSRCLRKNLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQYEREYNNKR--SGVGPSKFHGYAYDGIWVIAKTLQRAM 362
Cdd:cd06366 238 PDNDVNCTPEQMLEALEGHFSTELLPLNPDNTKTISGLTAQEFLKEYLERLsnSNYTGSPYAPFAYDAVWAIALALNKTI 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      363 ETLHAssRHQRIQDFNYTDHTLGRIILNAMNETNFFGVTGQVVFR-NGERMGTIKFTQFQDSREVKVGEYNAVADTL-EI 440
Cdd:cd06366 318 EKLAE--YNKTLEDFTYNDKEMADLFLEAMNSTSFEGVSGPVSFDsKGDRLGTVDIEQLQGGSYVKVGLYDPNADSLlLL 395

                ....*....
7C7Q_B      441 INDTIRFQG 449
Cdd:cd06366 396 NESSIVWPG 404
7tmC_GABA-B-R2 cd15294
gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of ...
469-738 4.29e-170

gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of seven-transmembrane G protein-coupled receptors; The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism.


:

Pssm-ID: 320421  Cd Length: 270  Bit Score: 490.02  E-value: 4.29e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      469 PLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWI 548
Cdd:cd15294   1 PLYSILSSLTIIGIILASAFLAFNIKFRNHRYIKMSSPYMNNLIILGCMLTYASVILLGLDGSLVSEKTFETLCTARTWI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      549 LTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEKYSMEPDPAGRDI 628
Cdd:cd15294  81 LCVGFTLAFGAMFSKTWRVHSIFTNVKLNKKAIKDYKLFIIVGVLLLIDICILITWQIVDPFYRTVKELEPEPDPAGDDI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      629 SIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNV 708
Cdd:cd15294 161 LIRPELEYCESTHMTIFLGIIYAYKGLLMVFGCFLAWETRNVSIPALNDSKYIGMSVYNVVIMCVIGAAVSFILRDQPNV 240
                       250       260       270
                ....*....|....*....|....*....|
7C7Q_B      709 QFCIVALVIIFCSTITLCLVFVPKLITLRT 738
Cdd:cd15294 241 QFCIISLFIIFCTTITLCLVFVPKLIELRR 270
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
47-449 0e+00

ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 528.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLTkEVAKGSIGRGVLPAVELAIEQIRNES-LLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCP 125
Cdd:cd06366   2 IGGLFPLS-GSKGWWGGAGILPAAEMALEHINNRSdILPGYNLELIWNDTQCDPGLGLKALYDLLYTPPPKVMLLGPGCS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      126 SVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLT 205
Cdd:cd06366  81 SVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      206 GVLYGEDIEISDTESFSN-DPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEqvhT 284
Cdd:cd06366 161 ELLEEANITIVATESFSSeDPTDQLENLKEKDARIIIGLFYEDAARKVFCEAYKLGMYGPKYVWILPGWYDDNWWD---V 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      285 EANSSRCLRKNLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQYEREYNNKR--SGVGPSKFHGYAYDGIWVIAKTLQRAM 362
Cdd:cd06366 238 PDNDVNCTPEQMLEALEGHFSTELLPLNPDNTKTISGLTAQEFLKEYLERLsnSNYTGSPYAPFAYDAVWAIALALNKTI 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      363 ETLHAssRHQRIQDFNYTDHTLGRIILNAMNETNFFGVTGQVVFR-NGERMGTIKFTQFQDSREVKVGEYNAVADTL-EI 440
Cdd:cd06366 318 EKLAE--YNKTLEDFTYNDKEMADLFLEAMNSTSFEGVSGPVSFDsKGDRLGTVDIEQLQGGSYVKVGLYDPNADSLlLL 395

                ....*....
7C7Q_B      441 INDTIRFQG 449
Cdd:cd06366 396 NESSIVWPG 404
7tmC_GABA-B-R2 cd15294
gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of ...
469-738 4.29e-170

gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of seven-transmembrane G protein-coupled receptors; The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism.


Pssm-ID: 320421  Cd Length: 270  Bit Score: 490.02  E-value: 4.29e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      469 PLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWI 548
Cdd:cd15294   1 PLYSILSSLTIIGIILASAFLAFNIKFRNHRYIKMSSPYMNNLIILGCMLTYASVILLGLDGSLVSEKTFETLCTARTWI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      549 LTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEKYSMEPDPAGRDI 628
Cdd:cd15294  81 LCVGFTLAFGAMFSKTWRVHSIFTNVKLNKKAIKDYKLFIIVGVLLLIDICILITWQIVDPFYRTVKELEPEPDPAGDDI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      629 SIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNV 708
Cdd:cd15294 161 LIRPELEYCESTHMTIFLGIIYAYKGLLMVFGCFLAWETRNVSIPALNDSKYIGMSVYNVVIMCVIGAAVSFILRDQPNV 240
                       250       260       270
                ....*....|....*....|....*....|
7C7Q_B      709 QFCIVALVIIFCSTITLCLVFVPKLITLRT 738
Cdd:cd15294 241 QFCIISLFIIFCTTITLCLVFVPKLIELRR 270
7tm_3 pfam00003
7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane ...
465-732 2.28e-68

7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane regions that forms the C-terminus of some subclass 3 G-coupled-protein receptors. It is often associated with a downstream cysteine-rich linker domain, NCD3G pfam07562, which is the human sweet-taste receptor, and the N-terminal domain, ANF_receptor pfam01094. The seven TM regions assemble in such a way as to produce a docking pocket into which such molecules as cyclamate and lactisole have been found to bind and consequently confer the taste of sweetness.


Pssm-ID: 459626 [Multi-domain]  Cd Length: 247  Bit Score: 225.62  E-value: 2.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        465 KISLPLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFvsektfetLCTV 544
Cdd:pfam00003   2 DLSAPWGIVLEALAALGILLTLVLLVVFLLHRKTPIVKASNRSLSFLLLLGLLLLFLLAFLFIGKPTV--------TCAL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        545 RTWILTVGYTTAFGAMFAKTWRVHAIFKNvkmKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVekysmepdpa 624
Cdd:pfam00003  74 RRFLFGVGFTLCFSCLLAKTFRLVLIFRR---RKPGPRGWQLLLLALGLLLVQVIILTEWLIDPPFPEKD---------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        625 grDISIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRD 704
Cdd:pfam00003 141 --NLSEGKIILECEGSTSIAFLDFVLAYVGLLLLAGFLLAFKTRKLP-DNFNEAKFITFSMLLSVLIWVAFIPMYLYGNK 217
                         250       260       270
                  ....*....|....*....|....*....|
7C7Q_B        705 QPNVQF--CIVALVIIFCSTITLCLVFVPK 732
Cdd:pfam00003 218 GKGTWDpvALAIFAILASGWVLLGLYFIPK 247
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
66-412 6.97e-51

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 181.43  E-value: 6.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B         66 VLPAVELAIEQI-RNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNhlMVFGGVCPSVTSIIAESLQGWNLVQLS 144
Cdd:pfam01094   2 VLLAVRLAVEDInADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKGEVV--AIIGPSCSSVASAVASLANEWKVPLIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        145 FAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFS-- 222
Cdd:pfam01094  80 YGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPpa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        223 ---NDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYepswweqvhteANSSRCLRKNLLAA 299
Cdd:pfam01094 160 qddDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGL-----------TTSLVILNPSTLEA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        300 MEGYIGVDFEPLSSKQIKTISGKTPQqyEREYNNKRSGVGPSKFHGYAYDGIWVIAKTLQRAMETLHASSRHQRIQDFNY 379
Cdd:pfam01094 229 AGGVLGFRLHPPDSPEFSEFFWEKLS--DEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRACGALGPWNG 306
                         330       340       350
                  ....*....|....*....|....*....|....
7C7Q_B        380 tdhtlGRIILNAMNETNFFGVTGQVVF-RNGERM 412
Cdd:pfam01094 307 -----GQKLLRYLKNVNFTGLTGNVQFdENGDRI 335
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
47-430 1.32e-22

ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 99.24  E-value: 1.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLTKEVAkgSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKyGPNHLMVFGGVCPS 126
Cdd:COG0683   6 IGVLLPLTGPYA--ALGQPIKNGAELAVEEINAAGGVLGRKIELVVEDDASDPDTAVAAARKLID-QDKVDAIVGPLSSG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      127 VTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILK-LLKHYQWKRVGTLTQDvqrfsevrNDlt 205
Cdd:COG0683  83 VALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDD--------YA-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      206 gvlYGEDIEisdtESFSNdpctSVKKLKGN---DVRIILGQFDQNmaakvfccAYEENMYGSKYQWIIPGWYEPSwweqv 282
Cdd:COG0683 153 ---YGQGLA----AAFKA----ALKAAGGEvvgEEYYPPGTTDFS--------AQLTKIKAAGPDAVFLAGYGGD----- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      283 hteanssrclrknllaamegyiGVDFeplsSKQIKTISGKTP--QQYEREYnNKRSGVGPSKFHGYAYDGIWVIAKTLQR 360
Cdd:COG0683 209 ----------------------AALF----IKQAREAGLKGPlnKAFVKAY-KAKYGREPSSYAAAGYDAALLLAEAIEK 261
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7C7Q_B      361 AMETLHASsrhqriqdfnytdhtlgriILNAMNETNFFGVTGQVVFR-NGERMGTIKFTQFQ-DSREVKVGE 430
Cdd:COG0683 262 AGSTDREA-------------------VRDALEGLKFDGVTGPITFDpDGQGVQPVYIVQVKaDGKFVVVET 314
PRK15404 PRK15404
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
70-237 7.91e-05

high-affinity branched-chain amino acid ABC transporter substrate-binding protein;


Pssm-ID: 237959 [Multi-domain]  Cd Length: 369  Bit Score: 45.78  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        70 VELAIEQIRNESLLRPYFLDLRLYDTECDNAKGL----KAFYDAIKYgpnhlmVFGGVCPSVTSIIAESLQGWNLVQLSF 145
Cdd:PRK15404  49 ARQAIEDINAKGGIKGDKLEGVEYDDACDPKQAVavanKVVNDGIKY------VIGHLCSSSTQPASDIYEDEGILMITP 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       146 AATTPVLADKKkYPYFFRTVPSDNAVNPAILK-LLKHYQWKRVGTLtQDVQRFSE-----VRNDL----TGVLYGEDIEI 215
Cdd:PRK15404 123 AATAPELTARG-YQLIFRTIGLDSDQGPTAAKyILEKVKPKRIAVL-HDKQQYGEglarsVKDGLkkagANVVFFEGITA 200
                        170       180
                 ....*....|....*....|..
7C7Q_B       216 SDTEsFSndpcTSVKKLKGNDV 237
Cdd:PRK15404 201 GDKD-FS----ALIAKLKKENV 217
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
47-449 0e+00

ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 528.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLTkEVAKGSIGRGVLPAVELAIEQIRNES-LLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCP 125
Cdd:cd06366   2 IGGLFPLS-GSKGWWGGAGILPAAEMALEHINNRSdILPGYNLELIWNDTQCDPGLGLKALYDLLYTPPPKVMLLGPGCS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      126 SVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLT 205
Cdd:cd06366  81 SVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      206 GVLYGEDIEISDTESFSN-DPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEqvhT 284
Cdd:cd06366 161 ELLEEANITIVATESFSSeDPTDQLENLKEKDARIIIGLFYEDAARKVFCEAYKLGMYGPKYVWILPGWYDDNWWD---V 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      285 EANSSRCLRKNLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQYEREYNNKR--SGVGPSKFHGYAYDGIWVIAKTLQRAM 362
Cdd:cd06366 238 PDNDVNCTPEQMLEALEGHFSTELLPLNPDNTKTISGLTAQEFLKEYLERLsnSNYTGSPYAPFAYDAVWAIALALNKTI 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      363 ETLHAssRHQRIQDFNYTDHTLGRIILNAMNETNFFGVTGQVVFR-NGERMGTIKFTQFQDSREVKVGEYNAVADTL-EI 440
Cdd:cd06366 318 EKLAE--YNKTLEDFTYNDKEMADLFLEAMNSTSFEGVSGPVSFDsKGDRLGTVDIEQLQGGSYVKVGLYDPNADSLlLL 395

                ....*....
7C7Q_B      441 INDTIRFQG 449
Cdd:cd06366 396 NESSIVWPG 404
7tmC_GABA-B-R2 cd15294
gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of ...
469-738 4.29e-170

gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of seven-transmembrane G protein-coupled receptors; The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism.


Pssm-ID: 320421  Cd Length: 270  Bit Score: 490.02  E-value: 4.29e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      469 PLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWI 548
Cdd:cd15294   1 PLYSILSSLTIIGIILASAFLAFNIKFRNHRYIKMSSPYMNNLIILGCMLTYASVILLGLDGSLVSEKTFETLCTARTWI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      549 LTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEKYSMEPDPAGRDI 628
Cdd:cd15294  81 LCVGFTLAFGAMFSKTWRVHSIFTNVKLNKKAIKDYKLFIIVGVLLLIDICILITWQIVDPFYRTVKELEPEPDPAGDDI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      629 SIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNV 708
Cdd:cd15294 161 LIRPELEYCESTHMTIFLGIIYAYKGLLMVFGCFLAWETRNVSIPALNDSKYIGMSVYNVVIMCVIGAAVSFILRDQPNV 240
                       250       260       270
                ....*....|....*....|....*....|
7C7Q_B      709 QFCIVALVIIFCSTITLCLVFVPKLITLRT 738
Cdd:cd15294 241 QFCIISLFIIFCTTITLCLVFVPKLIELRR 270
7tmC_GABA-B-like cd15047
gamma-aminobutyric acid type B receptor and related proteins, member of the class C family of ...
469-738 6.69e-116

gamma-aminobutyric acid type B receptor and related proteins, member of the class C family of seven-transmembrane G protein-coupled receptors; The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism. Also included in this group are orphan receptors, GPR156 and GPR158, which are closely related to the GABA-B receptor family.


Pssm-ID: 320175  Cd Length: 263  Bit Score: 350.71  E-value: 6.69e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      469 PLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSfvseKTFETLCTVRTWI 548
Cdd:cd15047   1 PLFIVFTVLSGIGILLALVFLIFNIKFRKNRVIKMSSPLFNNLILLGCILCYISVILFGLDDS----KPSSFLCTARPWL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      549 LTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEKYSMEPDPagrDI 628
Cdd:cd15047  77 LSIGFTLVFGALFAKTWRIYRIFTNKKLKRIVIKDKQLLKIVGILLLIDIIILILWTIVDPLKPTRVLVLSEISD---DV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      629 SIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNV 708
Cdd:cd15047 154 KYEYVVHCCSSSNGIIWLGILLAYKGLLLLFGCFLAWKTRNVDIEEFNESKYIGISIYNVLFLSVIGVPLSFVLTDSPDT 233
                       250       260       270
                ....*....|....*....|....*....|
7C7Q_B      709 QFCIVALVIIFCSTITLCLVFVPKLITLRT 738
Cdd:cd15047 234 SYLIISAAILFCTTATLCLLFVPKFWLLKR 263
7tmC_GABA-B-R1 cd15291
gamma-aminobutyric acid type B receptor subunit 1, member of the class C family of ...
469-738 2.86e-100

gamma-aminobutyric acid type B receptor subunit 1, member of the class C family of seven-transmembrane G protein-coupled receptors; The type B receptor for gamma-aminobutyric acid, GABA-B, is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism.


Pssm-ID: 320418  Cd Length: 274  Bit Score: 310.42  E-value: 2.86e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      469 PLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSEKTFETLCTVRTWI 548
Cdd:cd15291   1 KLFISMCLLASLGIFAAVFLLIFNIYNRHRRYIQLSQPHCNNVMLVGCILCLASVFLLGLDGRHVSRSHFPLVCQARLWL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      549 LTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIK---DQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEKYSME-PDPA 624
Cdd:cd15291  81 LCLGFTLAYGSMFTKVWRVHRLTTKKKEKKETRKtlePWKLYAVVGILLVVDVIILAIWQIVDPLHRTIEEFPLEePKDT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      625 GRDISIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRD 704
Cdd:cd15291 161 DEDVKILPQLEHCSSKKQNTWLGIVYGYKGLLLLFGLFLAYETRNVKVEKINDSRFVGMSIYNVVVLCLITAPVTMIISS 240
                       250       260       270
                ....*....|....*....|....*....|....
7C7Q_B      705 QPNVQFCIVALVIIFCSTITLCLVFVPKLITLRT 738
Cdd:cd15291 241 QQDASFAFVSLAILFSSYITLVLIFVPKIRELIR 274
7tm_3 pfam00003
7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane ...
465-732 2.28e-68

7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane regions that forms the C-terminus of some subclass 3 G-coupled-protein receptors. It is often associated with a downstream cysteine-rich linker domain, NCD3G pfam07562, which is the human sweet-taste receptor, and the N-terminal domain, ANF_receptor pfam01094. The seven TM regions assemble in such a way as to produce a docking pocket into which such molecules as cyclamate and lactisole have been found to bind and consequently confer the taste of sweetness.


Pssm-ID: 459626 [Multi-domain]  Cd Length: 247  Bit Score: 225.62  E-value: 2.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        465 KISLPLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFvsektfetLCTV 544
Cdd:pfam00003   2 DLSAPWGIVLEALAALGILLTLVLLVVFLLHRKTPIVKASNRSLSFLLLLGLLLLFLLAFLFIGKPTV--------TCAL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        545 RTWILTVGYTTAFGAMFAKTWRVHAIFKNvkmKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVekysmepdpa 624
Cdd:pfam00003  74 RRFLFGVGFTLCFSCLLAKTFRLVLIFRR---RKPGPRGWQLLLLALGLLLVQVIILTEWLIDPPFPEKD---------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        625 grDISIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRD 704
Cdd:pfam00003 141 --NLSEGKIILECEGSTSIAFLDFVLAYVGLLLLAGFLLAFKTRKLP-DNFNEAKFITFSMLLSVLIWVAFIPMYLYGNK 217
                         250       260       270
                  ....*....|....*....|....*....|
7C7Q_B        705 QPNVQF--CIVALVIIFCSTITLCLVFVPK 732
Cdd:pfam00003 218 GKGTWDpvALAIFAILASGWVLLGLYFIPK 247
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
66-412 6.97e-51

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 181.43  E-value: 6.97e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B         66 VLPAVELAIEQI-RNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNhlMVFGGVCPSVTSIIAESLQGWNLVQLS 144
Cdd:pfam01094   2 VLLAVRLAVEDInADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKGEVV--AIIGPSCSSVASAVASLANEWKVPLIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        145 FAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFS-- 222
Cdd:pfam01094  80 YGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPpa 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        223 ---NDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYepswweqvhteANSSRCLRKNLLAA 299
Cdd:pfam01094 160 qddDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGL-----------TTSLVILNPSTLEA 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        300 MEGYIGVDFEPLSSKQIKTISGKTPQqyEREYNNKRSGVGPSKFHGYAYDGIWVIAKTLQRAMETLHASSRHQRIQDFNY 379
Cdd:pfam01094 229 AGGVLGFRLHPPDSPEFSEFFWEKLS--DEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRACGALGPWNG 306
                         330       340       350
                  ....*....|....*....|....*....|....
7C7Q_B        380 tdhtlGRIILNAMNETNFFGVTGQVVF-RNGERM 412
Cdd:pfam01094 307 -----GQKLLRYLKNVNFTGLTGNVQFdENGDRI 335
7tmC_GPR156 cd15292
orphan GPR156, member of the class C family of seven-transmembrane G protein-coupled receptors; ...
470-733 7.17e-44

orphan GPR156, member of the class C family of seven-transmembrane G protein-coupled receptors; This subgroup represents orphan GPR156 that is closely related to the type B receptor for gamma-aminobutyric acid (GABA-B), which is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism.


Pssm-ID: 320419  Cd Length: 268  Bit Score: 159.52  E-value: 7.17e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      470 LYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSektFETLCTVRTWIL 549
Cdd:cd15292   2 LLGVMWTLLSCGILLALFFLAFTIRFRNNRIVKMSSPNLNVVTLLGSILTYTSGFLFGIQEPGTS---METIFQVRIWLL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      550 TVGYTTAFGAMFAKTWRVHAIF-KNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLR-RTVEKYSMEPDPAGRD 627
Cdd:cd15292  79 CIGTSLVFGPILGKSWRLYRVFtQRVPDKRVIIKDIQLLGLVAGLIFADVLLLLTWVLTDPVQcARSLSAVIKAMEKGIS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      628 ISIRPLlEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVSIPALNDSKYIGMSVYNVgimcIIGAAVSFLT----R 703
Cdd:cd15292 159 YSVSRM-DFCASLYSDLWIILISGFKGSLLLYGTYLAGLTSNVSSPPVNQSLTIMVGVNLV----TLTAGVVFPVtrflH 233
                       250       260       270
                ....*....|....*....|....*....|
7C7Q_B      704 DQPNVQFCIVALVIIFCSTITLCLVFVPKL 733
Cdd:cd15292 234 SWPNLVYGTTSGGIFVCTTTINCLIFIPQL 263
7tm_classC_mGluR-like cd13953
metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled ...
473-733 2.59e-39

metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled receptors superfamily; The class C GPCRs consist of glutamate receptors (mGluR1-8), the extracellular calcium-sensing receptors (caSR), the gamma-amino-butyric acid type B receptors (GABA-B), the vomeronasal type-2 pheromone receptors (V2R), the type 1 taste receptors (TAS1R), and the promiscuous L-alpha-amino acid receptor (GPRC6A), as well as several orphan receptors. Structurally, these receptors are typically composed of a large extracellular domain containing a Venus flytrap module which possesses the orthosteric agonist-binding site, a cysteine-rich domain (CRD) with the exception of GABA-B receptors, and the seven-transmembrane domains responsible for G protein activation. Moreover, the Venus flytrap module shows high structural homology with bacterial periplasmic amino acid-binding proteins, which serve as primary receptors in transport of a variety of soluble substrates such as amino acids and polysaccharides, among many others. The class C GPCRs exist as either homo- or heterodimers, which are essential for their function. The GABA-B1 and GABA-B2 receptors form a heterodimer via interactions between the N-terminal Venus flytrap modules and the C-terminal coiled-coiled domains. On the other hand, heterodimeric CaSRs and Tas1Rs and homodimeric mGluRs utilize Venus flytrap interactions and intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD), which can also acts as a molecular link to mediate the signal between the Venus flytrap and the 7TMs. Furthermore, members of the class C GPCRs bind a variety of endogenous ligands, ranging from amino acids, ions, to pheromones and sugar molecules, and play important roles in many physiological processes such as synaptic transmission, calcium homeostasis, and the sensation of sweet and umami tastes.


Pssm-ID: 320091 [Multi-domain]  Cd Length: 251  Bit Score: 145.84  E-value: 2.59e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      473 ILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSfvsektfETLCTVRTWILTVG 552
Cdd:cd13953   5 VLLVLAALGLLLTIFIWVVFIRYRNTPVVKASNRELSYLLLFGILLCFLLAFLFLLPPS-------DVLCGLRRFLFGLS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      553 YTTAFGAMFAKTWRVHAIFKNVKM---KKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRrtVEKYSMEPDpagrdis 629
Cdd:cd13953  78 FTLVFSTLLVKTNRIYRIFKSGLRsslRPKLLSNKSQLLLVLFLLLVQVAILIVWLILDPPK--VEKVIDSDN------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      630 irPLLEHCENTHmTIWLGIVYAYKGLLMLFGCFLAWETRNvsIPAL-NDSKYIGMSVYNVGIMCIIGAAVSFLTRdqPNV 708
Cdd:cd13953 149 --KVVELCCSTG-NIGLILSLVYNILLLLICTYLAFKTRK--LPDNfNEARYIGFSSLLSLVIWIAFIPTYFTTS--GPY 221
                       250       260
                ....*....|....*....|....*
7C7Q_B      709 QFCIVALVIIFCSTITLCLVFVPKL 733
Cdd:cd13953 222 RDAILSFGLLLNATVLLLCLFLPKI 246
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
66-357 8.28e-36

ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as natriuretic peptide receptors (NPRs), and N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of ionotropic glutamate rece; This CD represents the ligand-binding domain of the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic glutamate receptors, all of which are structurally similar and related to the periplasmic-binding fold type 1 family. The family C GPCRs consists of metabotropic glutamate receptor (mGluR), a calcium-sensing receptor (CaSR), gamma-aminobutyric acid receptor (GABAbR), the promiscuous L-alpha-amino acid receptor GPR6A, families of taste and pheromone receptors, and orphan receptors. Truncated splicing variants of the orphan receptors are not included in this CD. The family C GPCRs are activated by endogenous agonists such as amino acids, ions, and sugar based molecules. Their amino terminal ligand-binding region is homologous to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). The ionotropic glutamate receptors (iGluRs) have an integral ion channel and are subdivided into three major groups based on their pharmacology and structural similarities: NMDA receptors, AMPA receptors, and kainate receptors. The family of membrane bound guanylyl cyclases is further divided into three subfamilies: the ANP receptor (GC-A)/C-type natriuretic peptide receptor (GC-B), the heat-stable enterotoxin receptor (GC-C)/sensory organ specific membrane GCs such as retinal receptors (GC-E, GC-F), and olfactory receptors (GC-D and GC-G).


Pssm-ID: 380493 [Multi-domain]  Cd Length: 332  Bit Score: 138.32  E-value: 8.28e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       66 VLPAVELAIEQIR-NESLLRPYFLDLRLYDTECDNAKGLKAFYDAIkYGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLS 144
Cdd:cd06269  18 VLPAFELALSDVNsRPDLLPKTTLGLAIRDSECNPTQALLSACDLL-AAAKVVAILGPGCSASAAPVANLARHWDIPVLS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      145 FAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEISDTESFS-- 222
Cdd:cd06269  97 YGATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEELFQEKGGLITSRQSFDen 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      223 --NDPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEQVHTeanssrclrknLLAAM 300
Cdd:cd06269 177 kdDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFVIDGEASSSDEHGDE-----------ARQAA 245
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
7C7Q_B      301 EGYIGVDFEPLSSKQIKTISGKTPQQYEREYNNKRSGVGPSKFHGYAYDGIWVIAKT 357
Cdd:cd06269 246 EGAITVTLIFPVVKEFLKFSMELKLKSSKRKQGLNEEYELNNFAAFFYDAVLADRPG 302
7tmC_GPR158-like cd15293
orphan GPR158 and similar proteins, member of the class C family of seven-transmembrane G ...
469-733 2.43e-33

orphan GPR158 and similar proteins, member of the class C family of seven-transmembrane G protein-coupled receptors; This group includes orphan receptors GPR158, GPR158-like (also called GPR179) and similar proteins. These orphan receptors are closely related to the type B receptor for gamma-aminobutyric acid (GABA-B), which is activated by its endogenous ligand GABA, the principal inhibitory neurotransmitter. The functional GABA-B receptor is an obligatory heterodimer composed of two related subunits, GABA-B1, which is primarily involved in GABA ligand binding, and GABA-B2, which is responsible for both G-protein coupling and trafficking of the heterodimer to the plasma membrane. Activation of GABA-B couples to G(i/o)-type G proteins, which in turn modulate three major downstream effectors: adenylate cyclase, voltage-sensitive Ca2+ channels, and inwardly-rectifying K+ channels. Consequently, GABA-B receptor produces slow and sustained inhibitory responses by decreased neurotransmitter release via inhibition of Ca2+ channels and by postsynaptic hyperpolarization via the activation of K+ channels through the G-protein beta-gamma dimer. The GABA-B is expressed in both pre- and postsynaptic sites of glutamatergic and GABAergic neurons in the brain where it regulates synaptic activity. Thus, the GABA-B receptor agonist, baclofen, is used to treat muscle tightness and cramping caused by spasticity in multiple sclerosis patients. Moreover, GABA-B antagonists improves cognitive performance in mammals, while GABA-B agonists suppress cognitive behavior. In most of the class C family members, the extracellular Venus-flytrap domain in the N-terminus is connected to the seven-transmembrane (7TM) via a cysteine-rich domain (CRD). However, in the GABA-B receptor, the CRD is absent in both subunits and the Venus-flytrap ligand-binding domain is directly connected to the 7TM via a 10-15 amino acids linker, suggesting that GABA-B receptor may utilize a different activation mechanism.


Pssm-ID: 320420  Cd Length: 252  Bit Score: 128.87  E-value: 2.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      469 PLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSfvsektfETLCTVRTWI 548
Cdd:cd15293   1 VLRIAVLAVQAICILLCLVLALVVFRFRKVKVIKAASPILLELILFGALLLYFPVFILYFEPS-------VFRCILRPWF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      549 LTVGYTTAFGAMFAKTWRVHAIFKNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDplrrtvekysmePDPAGRDI 628
Cdd:cd15293  74 RHLGFAIVYGALILKTYRILVVFRSRSARRVHLTDRDLLKRLGLIVLVVLGYLAAWTAVN------------PPNVEVGL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      629 SIRPLLEHCENTHMTIWLGIVYAYKGLLMLFGCFLAWETRNVsiP-ALNDSKYIGMSVYNVGIMCIIGAAVSFLT--RDQ 705
Cdd:cd15293 142 TLTSSGLKFNVCSLDWWDYVMAIAELLFLLWGVYLCYAVRKA--PsAFNESRYISLAIYNELLLSVIFNIIRFFLlpSLH 219
                       250       260
                ....*....|....*....|....*...
7C7Q_B      706 PNVQFCIVALVIIFCSTITLCLVFVPKL 733
Cdd:cd15293 220 PDLLFLLFFLHTQLTVTVTLLLIFGPKF 247
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
47-434 9.96e-28

ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of membrane guanylyl-cyclase receptors. Membrane guanylyl cyclases (GC) have a single membrane-spanning region and are activated by endogenous and exogenous peptides. This family can be divided into three major subfamilies: the natriuretic peptide receptors (NPRs), sensory organ-specific membrane GCs, and the enterotoxin/guanylin receptors. The binding of peptide ligands to the receptor results in the activation of the cytosolic catalytic domain. Three types of NPRs have been cloned from mammalian tissues: NPR-A/GC-A, NPR-B/ GC-B, and NPR-C. In addition, two of the GCs, GC-D and GC-G, appear to be pseudogenes in humans. Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are produced in the heart, and both bind to the NPR-A. NPR-C, also termed the clearance receptor, binds each of the natriuretic peptides and can alter circulating levels of these peptides. The ligand binding domain of the NPRs exhibits strong structural similarity to the type 1 periplasmic binding fold protein family.


Pssm-ID: 380575 [Multi-domain]  Cd Length: 391  Bit Score: 115.92  E-value: 9.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLTkEVAKGSIGRGVLPAVELAIEQIRNE-SLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYgpNHLMVF-GGVC 124
Cdd:cd06352   2 VGVLAPSN-SQSLPVGYARSAPAIDIAIERINSEgLLLPGFNFEFTYRDSCCDESEAVGAAADLIYK--RNVDVFiGPAC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      125 PS---VTSIIAESlqgWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD-VQRFSEV 200
Cdd:cd06352  79 SAaadAVGRLATY---WNIPIITWGAVSASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDdDSKCFSI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      201 RNDL-TGVLYGEDIEISDTESFSNDPCTSVKKL--KGNDV-RIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEP 276
Cdd:cd06352 156 ANDLeDALNQEDNLTISYYEFVEVNSDSDYSSIlqEAKKRaRIIVLCFDSETVRQFMLAAHDLGMTNGEYVFIFIELFKD 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      277 SWWEQVHTEANSSRCLRKNLLAAMEGYIGVDFEPLSSKQIKTISGKTPQQYEREYNN--KRSGVGPSKFHGYAYDGIWVI 354
Cdd:cd06352 236 GFGGNSTDGWERNDGRDEDAKQAYESLLVISLSRPSNPEYDNFSKEVKARAKEPPFYcyDASEEEVSPYAAALYDAVYLY 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      355 AKTLQRAMEtlhassrhqriQDFNYTDHTLgriILNAMNETNFFGVTGQVVF-RNGERMGTIKFTQFQDS--REVKVGEY 431
Cdd:cd06352 316 ALALNETLA-----------EGGNYRNGTA---IAQRMWNRTFQGITGPVTIdSNGDRDPDYALLDLDPStgKFVVVLTY 381

                ...
7C7Q_B      432 NAV 434
Cdd:cd06352 382 DGT 384
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
50-409 1.34e-27

Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model.


Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 115.81  E-value: 1.34e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       50 LMPLTKEVAKGSIGRGVLPAVELAIEQIRNESLLRP-YFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLMVFGGVCpSVT 128
Cdd:cd06370   6 LTPYSGAGSYDRQGRVISGAITLAVDDVNNDPNLLPgHTLSFVWNDTRCDELLSIRAMTELWKRGVSAFIGPGCTC-ATE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      129 SIIAESlqgWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVL 208
Cdd:cd06370  85 ARLAAA---FNLPMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKWSKIADTIKELL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      209 YGEDIEISDTESF-SNDPCTS---------VKKLKgNDVRI--ILGQFdqNMAAKVFCCAYEENMYGSK-YQWII--PGW 273
Cdd:cd06370 162 ELNNIEINHEEYFpDPYPYTTshgnpfdkiVEETK-EKTRIyvFLGDY--SLLREFMYYAEDLGLLDNGdYVVIGveLDQ 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      274 YEPSWWEQ--VHTEANSSRCLRKNLLAAMEGYIGVDFEPLSS-------KQIKTISGKTPQQYEREYNNKRSGVgPSKFH 344
Cdd:cd06370 239 YDVDDPAKypNFLSGDYTKNDTKEALEAFRSVLIVTPSPPTNpeyekftKKVKEYNKLPPFNFPNPEGIEKTKE-VPIYA 317
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
7C7Q_B      345 GYAYDGIWVIAKTLQramETLhasSRHQRIQDfnytdhtlGRIILNAMNETNFFGVTGQVVF--RNG 409
Cdd:cd06370 318 AYLYDAVMLYARALN---ETL---AEGGDPRD--------GTAIISKIRNRTYESIQGFDVYidENG 370
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
62-410 5.75e-25

periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close homologs in other plants; This group includes the ligand-binding domain of Arabidopsis thaliana glutamate receptors, which have sequence similarity with animal ionotropic glutamate receptor and its close homologs in other plants. The ligand-binding domain of GABAb receptors are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380645 [Multi-domain]  Cd Length: 373  Bit Score: 107.70  E-value: 5.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       62 IGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKygpNHLMV--FGGVCPSVTSIIAESlqGwN 139
Cdd:cd19990  12 VGKEAKVAIEMAVSDFNSDSSSYGTKLVLHVRDSKGDPLQAASAALDLIK---NKKVEaiIGPQTSEEASFVAEL--G-N 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      140 LVQ---LSFAATTPVLAdKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEIS 216
Cdd:cd19990  86 KAQvpiISFSATSPTLS-SLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEVGSRIE 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      217 DTESFS-NDPCTSVK----KLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIpgwyepswweqvhTEANSS-- 289
Cdd:cd19990 165 YRVALPpSSPEDSIEeeliKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIV-------------TDGITNll 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      290 RCLRKNLLAAMEGYIGV--DFEPlsSKQIKTISGKTPQQYEREYNNKRSgVGPSKFHGYAYDGIWVIAktlqRAMETLha 367
Cdd:cd19990 232 DSLDSSTISSMQGVIGIktYIPE--SSEFQDFKARFRKKFRSEYPEEEN-AEPNIYALRAYDAIWALA----HAVEKL-- 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
7C7Q_B      368 SSRHQRIQDFNYtdhtlGRIILNAMNETNFFGVTGQVVFRNGE 410
Cdd:cd19990 303 NSSGGNISVSDS-----GKKLLEEILSTKFKGLSGEVQFVDGQ 340
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
47-430 1.32e-22

ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 99.24  E-value: 1.32e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLTKEVAkgSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKyGPNHLMVFGGVCPS 126
Cdd:COG0683   6 IGVLLPLTGPYA--ALGQPIKNGAELAVEEINAAGGVLGRKIELVVEDDASDPDTAVAAARKLID-QDKVDAIVGPLSSG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      127 VTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILK-LLKHYQWKRVGTLTQDvqrfsevrNDlt 205
Cdd:COG0683  83 VALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDD--------YA-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      206 gvlYGEDIEisdtESFSNdpctSVKKLKGN---DVRIILGQFDQNmaakvfccAYEENMYGSKYQWIIPGWYEPSwweqv 282
Cdd:COG0683 153 ---YGQGLA----AAFKA----ALKAAGGEvvgEEYYPPGTTDFS--------AQLTKIKAAGPDAVFLAGYGGD----- 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      283 hteanssrclrknllaamegyiGVDFeplsSKQIKTISGKTP--QQYEREYnNKRSGVGPSKFHGYAYDGIWVIAKTLQR 360
Cdd:COG0683 209 ----------------------AALF----IKQAREAGLKGPlnKAFVKAY-KAKYGREPSSYAAAGYDAALLLAEAIEK 261
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7C7Q_B      361 AMETLHASsrhqriqdfnytdhtlgriILNAMNETNFFGVTGQVVFR-NGERMGTIKFTQFQ-DSREVKVGE 430
Cdd:COG0683 262 AGSTDREA-------------------VRDALEGLKFDGVTGPITFDpDGQGVQPVYIVQVKaDGKFVVVET 314
7tmC_mGluRs cd15045
metabotropic glutamate receptors, member of the class C family of seven-transmembrane G ...
471-733 2.35e-19

metabotropic glutamate receptors, member of the class C family of seven-transmembrane G protein-coupled receptors; The metabotropic glutamate receptors (mGluRs) are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group I mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to (Gi/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320173 [Multi-domain]  Cd Length: 253  Bit Score: 88.46  E-value: 2.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      471 YSILS-ALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLfgldgsFVSEKTfETLCTVRTWIL 549
Cdd:cd15045   2 WAIGAmAFASLGILLTLFVLVVFVRYRDTPVVKASGRELSYVLLAGILLSYVMTFV------LVAKPS-TIVCGLQRFGL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      550 TVGYTTAFGAMFAKTWRVHAIF---KNVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPlRRTVEKYSmepdpaGR 626
Cdd:cd15045  75 GLCFTVCYAAILTKTNRIARIFrlgKKSAKRPRFISPRSQLVITGLLVSVQVLVLAVWLILSP-PRATHHYP------TR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      627 DISIRpLLEHCENTHMTIWLgivyAYKGLLMLFGCFLAWETRNvsIP-ALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQ 705
Cdd:cd15045 148 DKNVL-VCSSALDASYLIGL----AYPILLIILCTVYAFKTRK--IPeGFNEAKYIGFTMYTTCIIWLAFVPLYFTTASN 220
                       250       260
                ....*....|....*....|....*...
7C7Q_B      706 PNVQFCIVALVIIFCSTITLCLVFVPKL 733
Cdd:cd15045 221 IEVRITTLSVSISLSATVQLACLFAPKV 248
PBP1_ABC_ligand_binding-like cd06346
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
50-355 1.81e-16

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380569 [Multi-domain]  Cd Length: 314  Bit Score: 81.07  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       50 LMPLTKevAKGSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAF---YDAIKYgpnhLMVFGGVCPS 126
Cdd:cd06346   5 LLPLTG--PLASLGPPMLAAAELAVEEINAAGGVLGKKVELVVEDSQTDPTAAVDAArklVDVEGV----PAIVGAASSG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      127 VTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDvqrfsevrNDltg 206
Cdd:cd06346  79 VTLAVASVAVPNGVVQISPSSTSPALTTLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVN--------ND--- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      207 vlYGEDIEISDTESFsndpctsvKKLKG---NDVRIILGQFD-----QNMAAK----VFCCAYEENmyGSKY--QWIIPG 272
Cdd:cd06346 148 --YGQGLADAFKKAF--------EALGGtvtASVPYEPGQTSyraelAQAAAGgpdaLVLIGYPED--GATIlrEALELG 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      273 WYEPSWweqVHTEAN-SSRCLRKNLLAAMEGYIGVdfEPLSSkqiktiSGKTPQQYEREYnNKRSGVGPSKFHGYAYDGI 351
Cdd:cd06346 216 LDFTPW---IGTDGLkSDDLVEAAGAEALEGMLGT--APGSP------GSPAYEAFAAAY-KAEYGDDPGPFAANAYDAV 283

                ....
7C7Q_B      352 WVIA 355
Cdd:cd06346 284 MLLA 287
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
47-193 9.68e-16

ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate; categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (m; Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate and are categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). The metabotropic glutamate receptors (mGluR) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. The mGluRs are coupled to G proteins and are thus distinct from the iGluRs which internally contain ligand-gated ion channels. The mGluR structure is divided into three regions: the extracellular region, the seven-spanning transmembrane region and the cytoplasmic region. The extracellular region is further divided into the ligand-binding domain (LBD) and the cysteine-rich domain. The LBD has sequence similarity to the LIVBP, which is a bacterial periplasmic protein (PBP), as well as to the extracellular region of both iGluR and the gamma-aminobutyric acid (GABA)b receptor. iGluRs are divided into three main subtypes based on pharmacological profile: NMDA, AMPA, and kainate receptors. All family C GPCRs have a large extracellular N terminus that contain a domain with homology to bacterial periplasmic amino acid-binding proteins.


Pssm-ID: 380573  Cd Length: 350  Bit Score: 79.26  E-value: 9.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLT------KEVAKGSIGRGVL--PAVELAIEQIRNESLLRPYF-LDLRLYDTECDNAKGLKAFYDAIK------ 111
Cdd:cd06350   2 IGGLFPVHyrddadFCCCGILNPRGVQlvEAMIYAIEEINNDSSLLPNVtLGYDIRDTCSSSSVALESSLEFLLdngikl 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      112 ---------YGPNHLMVFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHY 182
Cdd:cd06350  82 lansngqniGPPNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAKAIADLLKHF 161
                       170
                ....*....|.
7C7Q_B      183 QWKRVGTLTQD 193
Cdd:cd06350 162 NWNYVSTVYSD 172
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
66-411 3.52e-15

Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of natriuretic peptide receptor (NPR) family which consists of three different subtypes: type A natriuretic peptide receptor (NPR-A, or GC-A), type B natriuretic peptide receptors (NPR-B, or GC-B), and type C natriuretic peptide receptor (NPR-C). There are three types of natriuretic peptide (NP) ligands specific to the receptors: atrial NP (ANP), brain or B-type NP (BNP), and C-type NP (CNP). The NP family is thought to have arisen through gene duplication during evolution and plays an essential role in cardiovascular and body fluid homeostasis. ANP and BNP bind mainly to NPR-A, while CNP binds specifically to NPR-B. Both NPR-A and NPR-B have guanylyl cyclase catalytic activity and produces intracellular secondary messenger cGMP in response to peptide-ligand binding. Consequently, the NPR-A activation results in vasodilation and inhibition of vascular smooth muscle cell proliferation. NPR-C acts as the receptor for all the three members of NP family, and functions as a clearance receptor. Unlike NPR-A and -B, NPR-C lacks an intracellular guanylyl cyclase domain and is thought to exert biological actions by sequestration of released natriuretic peptides and/or inhibition of adenylyl cyclase.


Pssm-ID: 380596 [Multi-domain]  Cd Length: 394  Bit Score: 78.08  E-value: 3.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       66 VLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNHLmVFGGVCPSVTSIIAESLQGWNLVQLSF 145
Cdd:cd06373  19 VLPAIELALRRVERRGFLPGWRFQVHYRDTKCSDTLAPLAAVDLYCAKKVDV-FLGPVCEYALAPVARYAGHWNVPVLTA 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      146 AATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFS-EVRND---LTGVLYGEDIE-ISDTES 220
Cdd:cd06373  98 GGLAAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVALLYHDNLRRKaGNSNCyftLEGIFNALTGErDSIHKS 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      221 FSNDpcTSVKklkgNDVRIILgQFDQNMAAKVFCC------------AYEENMYGSKYQWI---IPGWYE---PSWWEQV 282
Cdd:cd06373 178 FDEF--DETK----DDFEILL-KRVSNSARIVILCaspdtvreimlaAHELGMINGEYVFFnidLFSSSSkgaRPWYREN 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      283 HTEANSSRclrknllaAMEGYigvdfEPLsskqiKTISGKTP--QQYER-----------EYNNKRSGVGP-SKFHGYAY 348
Cdd:cd06373 251 DTDERNEK--------ARKAY-----RAL-----LTVTLRRPdsPEYRNfseevkerakeKYNYFTYGDEEvNSFVGAFH 312
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
7C7Q_B      349 DGIWVIAKTLQramETLHassrhqriQDFNYTDhtlGRIILNAMNETNFFGVTGQVVF-RNGER 411
Cdd:cd06373 313 DAVLLYALALN---ETLA--------EGGSPRN---GTEITERMWNRTFEGITGNVSIdANGDR 362
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
119-440 3.62e-15

ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of the metabotropic glutamate receptors (mGluR), which are members of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses. mGluRs bind to glutamate and function as an excitatory neurotransmitter; they are involved in learning, memory, anxiety, and the perception of pain. Eight subtypes of mGluRs have been cloned so far, and are classified into three groups according to their sequence similarities, transduction mechanisms, and pharmacological profiles. Group I is composed of mGlu1R and mGlu5R that both stimulate PLC hydrolysis. Group II includes mGlu2R and mGlu3R, which inhibit adenylyl cyclase, as do mGlu4R, mGlu6R, mGlu7R, and mGlu8R, which form group III.


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 78.87  E-value: 3.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      119 VFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSD-NAVNpAILKLLKHYQWKRVGTLtqdvqrF 197
Cdd:cd06362 111 VIGAESSSVSIQVANLLRLFKIPQISYASTSDELSDKERYPYFLRTVPSDsFQAK-AIVDILLHFNWTYVSVV------Y 183
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      198 SEVRndltgvlYGE-------------DIEISDTESFSNDPCTS-----VKKL-KGNDVRIILGQFDQNMAAKVFcCAYE 258
Cdd:cd06362 184 SEGS-------YGEegykafkklarkaGICIAESERISQDSDEKdyddvIQKLlQKKNARVVVLFADQEDIRGLL-RAAK 255
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      259 ENMYGSKYQWIIPGwyepSWWEQVHteanssrcLRKNLLAAMEGYIGVDF--EPLSS----------------------- 313
Cdd:cd06362 256 RLGASGRFIWLGSD----GWGTNID--------DLKGNEDVALGALTVQPysEEVPRfddyfksltpsnntrnpwfrefw 323
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      314 ----KQIKTISGKTPQQYEREYNNKRSGVGPSKFHGYAYDGIWVIAKtlqrAMETLHASSRHQRIQDFNYTDHTL-GRII 388
Cdd:cd06362 324 qelfQCSFRPSRENSCNDDKLLINKSEGYKQESKVSFVIDAVYAFAH----ALHKMHKDLCPGDTGLCQDLMKCIdGSEL 399
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
7C7Q_B      389 LNAMNETNFFGVTGQVV--FRNGERMG--TIKFTQFQDSRE---VKVGEYNAVADTLEI 440
Cdd:cd06362 400 LEYLLNVSFTGEAGGEIrfDENGDGPGryDIMNFQRNNDGSyeyVRVGVWDQYTQKLSL 458
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
47-360 1.33e-14

periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.


Pssm-ID: 380492 [Multi-domain]  Cd Length: 298  Bit Score: 75.06  E-value: 1.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       47 IMGLMPLTKEVAkgSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKyGPNHLMVFGGVCPS 126
Cdd:cd06268   2 IGVVVPLTGPYA--DYGEEILRGVALAVEEINAAGGINGRKLELVIADDQGDPETAVAVARKLVD-DDKVLAVVGHYSSS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      127 VTSIIAESLQGWNLVQLSFAATTPVLaDKKKYPYFFRTVPSDNAVNPAILK-LLKHYQWKRVGTLTQDVQRFSEVRNDLT 205
Cdd:cd06268  79 VTLAAAPIYQEAGIPLISPGSTAPEL-TEGGGPYVFRTVPSDAMQAAALADyLAKKLKGKKVAILYDDYDYGKSLADAFK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      206 GVLYGEDIEISDTESFSN---DPCTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEenmYGSKYQWI-IPGWYEPSWweq 281
Cdd:cd06268 158 KALKALGGEIVAEEDFPLgttDFSAQLTKIKAAGPDVLFLAGYGADAANALKQARE---LGLKLPILgGDGLYSPEL--- 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7C7Q_B      282 vhteanssrclRKNLLAAMEGYIGVDfePLSSKQIKTISGKTPQQYEREYNNKrsgvgPSKFHGYAYDGIWVIAKTLQR 360
Cdd:cd06268 232 -----------LKLGGEAAEGVVVAV--PWHPDSPDPPKQAFVKAYKKKYGGP-----PSWRAATAYDATQALAGDRVQ 292
PBP1_ABC_ligand_binding-like cd19984
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-355 9.41e-14

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380639 [Multi-domain]  Cd Length: 296  Bit Score: 72.64  E-value: 9.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       52 PLTKEVAkgSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFY-----DAIKYgpnhlmVFGGVCPS 126
Cdd:cd19984   7 PLTGDAA--SYGEDMKNGIELAVEEINAAGGINGKKIELIYEDSKCDPKKAVSAANklinvDKVKA------IIGGVCSS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      127 VTSIIAESLQGWNLVQLSFAATTPVLadKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD-------VQRFSE 199
Cdd:cd19984  79 ETLAIAPIAEQNKVVLISPGASSPEI--TKAGDYIFRNYPSDAYQGKVLAEFAYNKLYKKVAILYENndygvglKDVFKK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      200 VRNDLTGvlygediEISDTESF---SNDPCTSVKKLKGNDVRIIL--GQFDQnmAAKVFCCAYEENMygsKYQWI-IPGW 273
Cdd:cd19984 157 EFEELGG-------KIVASESFeqgETDFRTQLTKIKAANPDAIFlpGYPKE--GGLILKQAKELGI---KAPILgSDGF 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      274 YEPSwweqvhteanssrcLRKNLLAAMEG--YIGVDFEPLSSKQIKtisgktpqQYEREYnNKRSGVGPSKFHGYAYDGI 351
Cdd:cd19984 225 EDPE--------------LLEIAGEAAEGviFTYPAFDDSSEKKQK--------FFFYRY-KEKYGKEPDIYAALAYDAV 281

                ....
7C7Q_B      352 WVIA 355
Cdd:cd19984 282 MILA 285
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
67-273 3.65e-13

Family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems; This CD includes members of the family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. The family C GPCR includes glutamate/glycine-gated ion channels such as the NMDA receptor, G-protein-coupled receptors, metabotropic glutamate, GABA-B, calcium sensing, pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. The glutamate receptors that form cation-selective ion channels, iGluR, can be classified into three different subgroups according to their binding-affinity for the agonists NMDA (N-methyl-D-asparate), AMPA (alpha-amino-3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid), and kainate. L-glutamate is a major neurotransmitter in the brain of vertebrates and acts through either mGluRs or iGluRs. mGluRs subunits possess seven transmembrane segments and a large N-terminal extracellular domain. ABC-type leucine-isoleucine-valine binding protein (LIVBP) is a bacterial periplasmic binding protein that has homology with the amino-terminal domain of the glutamate-receptor ion channels (iGluRs). The extracellular regions of iGluRs are made of two PBP-like domains in tandem, a LIVBP-like domain that constitutes the N terminus (included in this model) followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type 2 periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are also included in this family.


Pssm-ID: 380490  Cd Length: 306  Bit Score: 71.18  E-value: 3.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       67 LPAVELAIEQIRNESLLRPYF-LDLRLYDTECDN----AKGLKAFYDAI------KYGPNHLM-----------VFGGVC 124
Cdd:cd04509  30 FEAMEQALDDINADPNLLPNNtLGIVIYDDCCDPkqalEQSNKFVNDLIqkdtsdVRCTNGEPpvfvkpegikgVIGHLC 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      125 PSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQrfsevrndl 204
Cdd:cd04509 110 SSVTIPVSNILELFGIPQITYAATAPELSDDRGYQLFLRVVPLDSDQAPAMADIVKEKVWQYVSIVHDEGQ--------- 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      205 tgvlYGEdieiSDTESFSN------------DPCTSVKKLKGNDvRIILGQFDQNMAAKVFCCAYEENMYG--------- 263
Cdd:cd04509 181 ----YGE----GGARAFQDglkkgglciafsDGITAGEKTKDFD-RLVARLKKENNIRFVVYFGYHPEMGQilraarrag 251
                       250
                ....*....|...
7C7Q_B      264 --SKYQWIIP-GW 273
Cdd:cd04509 252 lvGKFQFMGSdGW 264
PBP1_ABC_ligand_binding-like cd06336
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
63-361 5.72e-13

type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.


Pssm-ID: 380559 [Multi-domain]  Cd Length: 345  Bit Score: 70.73  E-value: 5.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       63 GRGVLPAVELAIEQIRNESLL----RPYFLDLRLYDTECDNAKGLKAF-----YDAIKYgpnhlmVFGGVCPSVTSIIAE 133
Cdd:cd06336  16 GLPMLRGLELAADEINAAGGIkvggKKYKVEVVSYDDKYTPAEAVAAArrlvsQDGVKF------IFGPGGSAIAAAVQP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      134 SLQGWNLVQLSFAATTPVLadKKKYPYFFRTVPSDNAVNPAILKLLKHYQW-KRVGTLTQDVQRFSEVRNDLTGVLYGED 212
Cdd:cd06336  90 VTERNKVLLLTAAFSDPIL--GPDNPLLFRIPPTPYEYAPPFIKWLKKNGPiKTVALIAPNDATGKDWAAAFVAAWKAAG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      213 IEISDTESFSND------PCTSVKKLKgNDVrIILGQFDQNMAAKVFCCAYEEnmyGSKYQWIIPGWyepswweqvhteA 286
Cdd:cd06336 168 GEVVAEEFYDRGttdfypVLTKILALK-PDA-LDLGGSSPGPAGLIIKQAREL---GFKGPFVSEGG------------A 230
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7C7Q_B      287 NSSRCLRKNLLAAMEGYIGVDFEPLSSKQiktisGKTPQQYEREYnNKRSGVGPSKFHGYAYDGIWVIAKTLQRA 361
Cdd:cd06336 231 KADEILKEVGGEAAEGFIGVLPADDDPIA-----SPGAKAFVERY-KKKYGEPPNSESALFYDAAYILVKAMEKA 299
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
73-193 5.88e-13

ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the CaSR calcium-sensing receptor, which is a member of the family C receptors within the G-protein coupled receptor superfamily. CaSR provides feedback control of extracellular calcium homeostasis by responding sensitively to acute fluctuations in extracellular ionized Ca2+ concentration. This ligand-binding domain has homology to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). CaSR is widely expressed in mammalian tissues and is active in tissues that are not directly involved in extracellular calcium homeostasis. Moreover, CaSR responds to aromatic, aliphatic, and polar amino acids, but not to positively charged or branched chain amino acids, which suggests that changes in plasma amino acid levels are likely to modulate whole body calcium metabolism. Additionally, the family C GPCRs includes at least two receptors with broad-spectrum amino acid-sensing properties: GPRC6A which recognizes basic and various aliphatic amino acids, its gold-fish homolog the 5.24 chemoreceptor, and a specific taste receptor (T1R) which responds to aliphatic, polar, charged, and branched amino acids, but not to aromatic amino acids.


Pssm-ID: 380587 [Multi-domain]  Cd Length: 473  Bit Score: 71.90  E-value: 5.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       73 AIEQI-RNESLLRPYFLDLRLYDTeCDN-AKGLKAfydAIKY--GPNHLMvFGGVC---PSVTSIIAESLQGWNLV---- 141
Cdd:cd06364  45 AIEEInNSPDLLPNITLGYRIYDS-CATiSKALRA---ALALvnGQEETN-LDERCsggPPVAAVIGESGSTLSIAvart 119
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
7C7Q_B      142 -------QLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD 193
Cdd:cd06364 120 lglfyipQVSYFASCACLSDKKQFPSFLRTIPSDYYQSRALAQLVKHFGWTWVGAIASD 178
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
69-200 1.02e-12

Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptor, the GABAb receptor, the calcium-sensing receptor (CaSR), the T1R taste receptor, and a small group of uncharacterized orphan receptors.


Pssm-ID: 380588 [Multi-domain]  Cd Length: 464  Bit Score: 71.14  E-value: 1.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       69 AVELAIEQI-RNESLLRPYFLDLRLYDTECDNAKGLKAF-------------YDAIKYGpNHLMVFGGVCPSVTSIIAES 134
Cdd:cd06365  41 AFLFAIEEInKNPDLLPNITLGFHIYDSCSSERLALESSlsilsgnsepipnYSCREQR-KLVAFIGDLSSSTSVAMARI 119
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
7C7Q_B      135 LQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD---VQRFSEV 200
Cdd:cd06365 120 LGLYKYPQISYGAFDPLLSDKVQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDddyGEQFSQD 188
7tmC_mGluR_group3 cd15286
metabotropic glutamate receptors in group 3, member of the class C family of ...
476-747 1.63e-12

metabotropic glutamate receptors in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors; The metabotropic glutamate receptors (mGluRs) in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320413  Cd Length: 271  Bit Score: 68.68  E-value: 1.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      476 ALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsfVSEKTFeTLCTVRTWILTVGYTT 555
Cdd:cd15286   8 ALAVLGIIATLFVLVTFVRYNDTPIVRASGRELSYVLLTGIFLCYAITFLM------VAEPGV-GVCSLRRLFLGLGMSL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      556 AFGAMFAKTWRVHAIFKNVKMK---KKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVEkYSME--PDPAgrdiSI 630
Cdd:cd15286  81 SYAALLTKTNRIYRIFEQGKKSvtpPRFISPTSQLVITFSLISVQLLGVLAWFAVDPPHALID-YEEGrtPDPE----QA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      631 RPLLEhCENTHMTIWLGIVYAYkgLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVgimCII---------GAAVSfl 701
Cdd:cd15286 156 RGVLR-CDMSDLSLICCLGYSL--LLMVTCTVYAIKARGVP-ETFNEAKPIGFTMYTT---CIVwlafipiffGTAQS-- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
7C7Q_B      702 tRDQPNVQFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNR 747
Cdd:cd15286 227 -AEKLYIQTATLTVSMSLSASVSLGMLYMPKVYVILFHPEQNVQKR 271
PBP1_GC_G-like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
69-413 1.97e-12

Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding domain of membrane guanylyl cyclase G (GC-G) which is a sperm surface receptor and might function, similar to its sea urchin counterpart, in the early signaling event that regulates the Ca2+ influx/efflux and subsequent motility response in sperm. GC-G appears to be a pseudogene in human. Furthermore, in contrast to the other orphan receptor GCs, GC-G has a broad tissue distribution in rat, including lung, intestine, kidney, and skeletal muscle.


Pssm-ID: 380595 [Multi-domain]  Cd Length: 390  Bit Score: 69.83  E-value: 1.97e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       69 AVELAIEQIRNE-SLLRPYFLDLRLYDTECDNAKGLKAFYDAIkYGPNHLMVFGGVCP---SVTSIIAESlqgWNLVQLS 144
Cdd:cd06372  22 AIQLAVDKVNSEpSLLGNYSLDFVYTDCGCNAKESLGAFIDQV-QKENISALFGPACPeaaEVTGLLASE---WNIPMFG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      145 FAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTL--TQDVQRFSEVrNDLTGVLYGE---DIEISDTE 219
Cdd:cd06372  98 FVGQSPKLDDRDVYDTYVKLVPPLQRIGEVLVKTLQFFGWTHVAMFggSSATSTWDKV-DELWKSVENQlkfNFNVTAKV 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      220 SF-SNDPCTSVKKLK--GNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIPGWYEPSWWEQVHTEANSSRCLR--- 293
Cdd:cd06372 177 KYdTSNPDLLQENLRyiSSVARVIVLICSSEDARSILLEAEKLGLMDGEYVFFLLQQFEDSFWKEVLNDEKNQVFLKaye 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      294 KNLLAAMEGYIGVDFEPLsSKQIKTISGKTPqqyerEYNNKRSGVGPSKFHGYAYDGIWVIAKTLQramETLHASSrhqr 373
Cdd:cd06372 257 MVFLIAQSSYGTYGYSDF-RKQVHQKLRRAP-----FYSSISSEDQVSPYSAYLHDAVLLYAMGLK---EMLKDGK---- 323
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
7C7Q_B      374 iqdfnytDHTLGRIILNAM---NETNFFGVTGQVVF-RNGERMG 413
Cdd:cd06372 324 -------DPRDGRALLQTLrgyNQTTFYGITGLVYLdVQGERHM 360
7tmC_mGluR4 cd15452
metabotropic glutamate receptor 4 in group 3, member of the class C family of ...
477-748 2.78e-12

metabotropic glutamate receptor 4 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors; The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320568 [Multi-domain]  Cd Length: 327  Bit Score: 68.47  E-value: 2.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      477 LTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsfVSEKTFETlCTVRTWILTVGYTTA 556
Cdd:cd15452   9 LAVLGIIATLFVVVTFVRYNDTPIVKASGRELSYVLLTGIFLCYATTFLM------IAEPDLGT-CSLRRIFLGLGMSIS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      557 FGAMFAKTWRVHAIFKNVKMK---KKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTVE-KYSMEPDPAgrdiSIRP 632
Cdd:cd15452  82 YAALLTKTNRIYRIFEQGKRSvsaPRFISPASQLVITFSLISLQLLGVCVWFLVDPSHSVVDyEDQRTPDPQ----FARG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      633 LLEhCENTHMTiwLGIVYAYKGLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTR---DQPNVQ 709
Cdd:cd15452 158 VLK-CDISDLS--LICLLGYSMLLMVTCTVYAIKTRGVP-ETFNEAKPIGFTMYTTCIIWLAFIPIFFGTSqsaEKMYIQ 233
                       250       260       270
                ....*....|....*....|....*....|....*....
7C7Q_B      710 FCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRR 748
Cdd:cd15452 234 TTTLTISVSLSASVSLGMLYMPKVYVILFHPEQNVPKRK 272
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
52-190 2.94e-12

type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine); This subgroup includes the type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems that are involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine). This subgroup also includes a leucine-specific binding protein (or LivK), which is very similar in sequence and structure to leucine-isoleucine-valine binding protein (LIVBP). ABC-type active transport systems are transmembrane proteins that function in the transport of diverse sets of substrates across extra- and intracellular membranes, including carbohydrates, amino acids, inorganic ions, dipeptides and oligopeptides, metabolic products, lipids and sterols, and heme, to name a few.


Pssm-ID: 380565 [Multi-domain]  Cd Length: 334  Bit Score: 68.71  E-value: 2.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       52 PLTKEVAkgSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECD------NAKGLKAfyDAIkygpnhLMVFGGVCP 125
Cdd:cd06342   7 PLTGPNA--ALGQDIRNGAELAVDEINAKGGGLGFKIELVAQDDACDpaqavaAAQKLVA--DGV------VAVIGHYNS 76
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7C7Q_B      126 SVTSIIAESLQGWNLVQLSFAATTPVLAdKKKYPYFFRTVPSDNAVNPAILK-LLKHYQWKRVGTL 190
Cdd:cd06342  77 GAAIAAAPIYAEAGIPMISPSATNPKLT-EQGYKNFFRVVGTDDQQGPAAADyAAKTLKAKRVAVI 141
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
61-203 1.24e-11

ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste receptor. The T1R is a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptors, GABAb receptors, the calcium-sensing receptor (CaSR), the V2R pheromone receptors, and a small group of uncharacterized orphan receptors.


Pssm-ID: 380586 [Multi-domain]  Cd Length: 418  Bit Score: 67.33  E-value: 1.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       61 SIGRGVLPAVELAIEQIRNESLLRP-YFLDLRLYDTeC---------------DNAKGLKAFYDAIKYGPNHLMVFGGVC 124
Cdd:cd06363  39 LHGYHLAQAMRFAVEEINNSSDLLPgVTLGYEIFDT-CsdavnfrptlsflsqNGSHDIEVQCNYTNYQPRVVAVIGPDS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      125 PSVTSIIAeSLQGWNLV-QLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTL-------TQDVQR 196
Cdd:cd06363 118 SELALTTA-KLLGFFLMpQISYGASSEELSNKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLgsddeygQDGLQL 196

                ....*..
7C7Q_B      197 FSEVRND 203
Cdd:cd06363 197 FSEKAAN 203
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
73-193 1.91e-11

ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor; This family includes the ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor, and its fish homolog, the 5.24 chemoreceptor. GPRC6A is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses.


Pssm-ID: 380584 [Multi-domain]  Cd Length: 401  Bit Score: 66.63  E-value: 1.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       73 AIEQIRNESLLRPYFLDLRLYDTECDNAKGLKA---------------FYDAIKYGPNHLMVFGGVCPSVTSIIAESLQG 137
Cdd:cd06361  44 AIEMINNSTLLPGIKLGYEIYDTCSDVTKALQAtlrllskfnssnellECDYTDYVPPVKAVIGASYSEISIAVARLLNL 123
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
7C7Q_B      138 WNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD 193
Cdd:cd06361 124 QLIPQISYESSAPILSDKLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTD 179
7tmC_mGluR8 cd15454
metabotropic glutamate receptor 8 in group 3, member of the class C family of ...
477-751 2.02e-11

metabotropic glutamate receptor 8 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors; The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320570 [Multi-domain]  Cd Length: 311  Bit Score: 65.81  E-value: 2.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      477 LTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsFVSEKTFetLCTVRTWILTVGYTTA 556
Cdd:cd15454   9 VAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYAITFLM-----IATPDTG--ICSFRRVFLGLGMCFS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      557 FGAMFAKTWRVHAIFKNVK---MKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPlRRTVEKYSME--PDPagrdISIR 631
Cdd:cd15454  82 YAALLTKTNRIHRIFEQGKksvTAPKFISPASQLVITFSLISVQLLGVFVWFAVDP-PHTIVDYGEQrtLDP----EKAR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      632 PLLEhCENTHMTIWLGIVYAYkgLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPN---V 708
Cdd:cd15454 157 GVLK-CDISDLSLICSLGYSI--LLMVTCTVYAIKTRGVP-ETFNEAKPIGFTMYTTCIIWLAFIPIFFGTAQSAErmyI 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
7C7Q_B      709 QFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRRFQF 751
Cdd:cd15454 233 QTTTLTISMSLSASVSLGMLYMPKVYIIIFHPEQNVQKRKRSF 275
7tmC_mGluR_group1 cd15285
metabotropic glutamate receptors in group 1, member of the class C family of ...
476-733 2.90e-11

metabotropic glutamate receptors in group 1, member of the class C family of seven-transmembrane G protein-coupled receptors; Group 1 mGluRs includes mGluR1 and mGluR5, as well as their closely related invertebrate receptors. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320412  Cd Length: 250  Bit Score: 64.58  E-value: 2.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      476 ALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFGLDGSFVSektfetlCTVRTWILTVGYTT 555
Cdd:cd15285   8 VFACVGILATLFVTVVFIRHNDTPVVKASTRELSYIILAGILLCYASTFALLAKPSTIS-------CYLQRILPGLSFAM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      556 AFGAMFAKTWRVHAIFknvKMKKKIIKDQKLLVIVGGMLLIDLCILICWQAVdplRRTVEKYSMEPDPAGRDISIRPLLE 635
Cdd:cd15285  81 IYAALVTKTNRIARIL---AGSKKKILTRKPRFMSASAQVVITGILISVEVA---IIVVMLILEPPDATLDYPTPKRVRL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      636 HCENThmTIWLGIVYAYKGLLMLFGCFLAWETRNVsiPA-LNDSKYIGMSVYNVgimCIIGAAvsFLTrdqpnVQFCIVA 714
Cdd:cd15285 155 ICNTS--TLGFVVPLGFDFLLILLCTLYAFKTRNL--PEnFNEAKFIGFTMYTT---CVIWLA--FLP-----IYFGSDN 220
                       250       260
                ....*....|....*....|....*
7C7Q_B      715 LVIIFC------STITLCLVFVPKL 733
Cdd:cd15285 221 KEITLCfsvslsATVALVFLFFPKV 245
7tmC_mGluR2 cd15447
metabotropic glutamate receptor 2 in group 2, member of the class C family of ...
466-733 5.78e-11

metabotropic glutamate receptor 2 in group 2, member of the class C family of seven-transmembrane G protein-coupled receptors; The metabotropic glutamate receptors (mGluRs) in group 2 include mGluR 2 and 3. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320563  Cd Length: 254  Bit Score: 63.79  E-value: 5.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      466 ISLPLYSILSALTILGMIMasaflffniKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsfvSEKTFETLCTVR 545
Cdd:cd15447   7 VTISCLGILSTLFVVGVFV---------KNNETPVVKASGRELCYILLLGVLLCYLMTFIF-------IAKPSTAVCTLR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      546 TWILTVGYTTAFGAMFAKTWRVHAIFKNVK---MKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPlrrtvEKYSMEPD 622
Cdd:cd15447  71 RLGLGTSFAVCYSALLTKTNRIARIFSGAKdgaQRPRFISPASQVAICLALISCQLLVVLIWLLVEA-----PGTRKETA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      623 PAGRDISIrpLLEHCENTHMTIWLgivyAYKGLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLT 702
Cdd:cd15447 146 PERRYVVT--LKCNSRDSSMLISL----TYNVLLIILCTLYAFKTRKCP-ENFNEAKFIGFTMYTTCIIWLAFLPIFYVT 218
                       250       260       270
                ....*....|....*....|....*....|.
7C7Q_B      703 RDQPNVQFCIVALVIIFCSTITLCLVFVPKL 733
Cdd:cd15447 219 SSDYRVQTTTMCISVSLSGSVVLGCLFAPKL 249
7tmC_mGluR6 cd15453
metabotropic glutamate receptor 6 in group 3, member of the class C family of ...
477-748 6.86e-11

metabotropic glutamate receptor 6 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors; The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320569 [Multi-domain]  Cd Length: 273  Bit Score: 63.51  E-value: 6.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      477 LTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsfVSEKTFeTLCTVRTWILTVGYTTA 556
Cdd:cd15453   9 LAVLGILATTTVVITFVRFNNTPIVRASGRELSYVLLTGIFLIYAITFLM------VAEPGA-AVCAFRRLFLGLGTTLS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      557 FGAMFAKTWRVHAIFKNVKMK---KKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTV---EKYSMEPDPAgrdisi 630
Cdd:cd15453  82 YSALLTKTNRIYRIFEQGKRSvtpPPFISPTSQLVITFSLTSLQVVGVIAWLGAQPPHSVIdyeEQRTVDPEQA------ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      631 RPLLEhCENTHMTIwLGIVyAYKGLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPN--- 707
Cdd:cd15453 156 RGVLK-CDMSDLSL-IGCL-GYSLLLMVTCTVYAIKARGVP-ETFNEAKPIGFTMYTTCIIWLAFVPIFFGTAQSAEkiy 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
7C7Q_B      708 VQFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRR 748
Cdd:cd15453 232 IQTTTLTVSLSLSASVSLGMLYVPKTYVILFHPEQNVQKRK 272
7tmC_mGluRs_group2_3 cd15934
metabotropic glutamate receptors in group 2 and 3, member of the class C family of ...
476-733 2.92e-10

metabotropic glutamate receptors in group 2 and 3, member of the class C family of seven-transmembrane G protein-coupled receptors; The metabotropic glutamate receptors (mGluRs) are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. The mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group I mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to (Gi/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320600  Cd Length: 252  Bit Score: 61.47  E-value: 2.92e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      476 ALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsfVSEKTFETlCTVRTWILTVGYTT 555
Cdd:cd15934   8 VFALLGILATLFVIVVFIRYNDTPVVKASGRELSYVLLTGILLCYLMTFVL------LAKPSVIT-CALRRLGLGLGFSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      556 AFGAMFAKTWRVHAIFKNVK--MKK-KIIKDQKLLVIVGGMLLIDLCILICWQAVDPlRRTVEKYsmePDpagRDISIrp 632
Cdd:cd15934  81 CYAALLTKTNRISRIFNSGKrsAKRpRFISPKSQLVICLGLISVQLIGVLVWLVVEP-PGTRIDY---PR---RDQVV-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      633 LLEHCENTHMTIWLgivyAYKGLLMLFGCFLAWETRNvsIPA-LNDSKYIGMSVYNVgimCIIGAA---VSFLTRDQPNV 708
Cdd:cd15934 152 LKCKISDSSLLISL----VYNMLLIILCTVYAFKTRK--IPEnFNEAKFIGFTMYTT---CIIWLAfvpIYFGTSNDFKI 222
                       250       260
                ....*....|....*....|....*
7C7Q_B      709 QFCIVALVIIFCSTITLCLVFVPKL 733
Cdd:cd15934 223 QTTTLCVSISLSASVALGCLFAPKV 247
PBP1_ABC_ligand_binding-like cd06345
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
63-422 1.15e-09

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380568 [Multi-domain]  Cd Length: 356  Bit Score: 60.74  E-value: 1.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       63 GRGVLPAVELAIEQIrNES---LLRPyfLDLRLYDTECDNAKGLKAFYDAIkYGPNHLMVFGGVCPSVTSIIAESLQGWN 139
Cdd:cd06345  13 GEAMERGAELAVEEI-NAAggiLGRK--VELVVADTQGKPEDGVAAAERLI-TEDKVDAIVGGFRSEVVLAAMEVAAEYK 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      140 LVQLSFAATTPVLADK-----KKYPYFFRTVPSDNAVNPAILKLLKHYQ-----WKRVGTLTQDVQRFSEVRNDLTGVLY 209
Cdd:cd06345  89 VPFIVTGAASPAITKKvkkdyEKYKYVFRVGPNNSYLGATVAEFLKDLLveklgFKKVAILAEDAAWGRGIAEALKKLLP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      210 GEDIEISDTESFSNDpcTSvkklkgnDVRIILGQFDQNMAAKVFCCAYEENmyGSKY--QW-----------IIPGWYEP 276
Cdd:cd06345 169 EAGLEVVGVERFPTG--TT-------DFTPILSKIKASGADVIVTIFSGPG--GILLvkQWaelgvpaplvgINVPAQDP 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      277 SWWEQVHTEAnssrclrknllaamEGYIGVDFEPLSSKqiktISGKTPQQYEReYnNKRSGVGPSKFHGYAYDGIWVIAK 356
Cdd:cd06345 238 EFWENTGGAG--------------EYEITLAFAAPKAK----VTPKTKPFVDA-Y-KKKYGEAPNYTAYTAYDAIYILAE 297
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7C7Q_B      357 TLQRAmetlhassrhqriqdfNYTDhtlGRIILNAMNETNFFGVTGQVVFRNGERMG----------TIKFTQFQD 422
Cdd:cd06345 298 AIERA----------------GSTD---PDALVKALEKTDYEGVRGRIKFDKKDEYPhdvkygpgyvTGLIFQWQD 354
Peripla_BP_6 pfam13458
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ...
60-361 3.86e-09

Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.


Pssm-ID: 433225 [Multi-domain]  Cd Length: 342  Bit Score: 59.21  E-value: 3.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B         60 GSIGRGVLPAVELAIEQIrNES---LLRPyfLDLRLYDTECDNAKGLKAFYDAIKYGpNHLMVFGGVCPSVTSIIAESLQ 136
Cdd:pfam13458  15 ASSGKSSRAGARAAIEEI-NAAggvNGRK--IELVVADDQGDPDVAAAAARRLVDQD-GVDAIVGGVSSAVALAVAEVLA 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        137 GWNLVQLSFAATTPvladKKKYPYFFRTVPSDNA-VNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEI 215
Cdd:pfam13458  91 KKGVPVIGPAALTG----EKCSPYVFSLGPTYSAqATALGRYLAKELGGKKVALIGADYAFGRALAAAAKAAAKAAGGEV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        216 SDTESFS---NDPCTSVKKLKGNDVRIILGQFDQNMAAKvFCCAYEE-NMYGSKYQWIIPGWYEPSwweqvhteanssrc 291
Cdd:pfam13458 167 VGEVRYPlgtTDFSSQVLQIKASGADAVLLANAGADTVN-LLKQAREaGLDAKGIKLVGLGGDEPD-------------- 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7C7Q_B        292 LRKNLLAAMEG-YIGVDFEPlsskqikTISGKTPQQYEREYNNKRSGVGPSKFHGYAYDGIWVIAKTLQRA 361
Cdd:pfam13458 232 LKALGGDAAEGvYATVPFFP-------DLDNPATRAFVAAFAAKYGEAPPTQFAAGGYIAADLLLAALEAA 295
7tmC_mGluR7 cd15451
metabotropic glutamate receptor 7 in group 3, member of the class C family of ...
477-751 4.17e-09

metabotropic glutamate receptor 7 in group 3, member of the class C family of seven-transmembrane G protein-coupled receptors; The receptors in group 3 include mGluRs 4, 6, 7, and 8. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320567  Cd Length: 307  Bit Score: 58.88  E-value: 4.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      477 LTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLfgldgsfVSEKTFETLCTVRTWILTVGYTTA 556
Cdd:cd15451   9 LAMLGIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFL-------MIAKPDVAVCSFRRIFLGLGMCIS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      557 FGAMFAKTWRVHAIFKNVKMK---KKIIKDQKLLVIVGGMLLIDLCILICWQAVDPLRRTV---EKYSMEPDPAgrdisi 630
Cdd:cd15451  82 YAALLTKTNRIYRIFEQGKKSvtaPRLISPTSQLAITSSLISVQLLGVLIWFAVDPPNIIIdydEQKTMNPEQA------ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      631 RPLLEhCENTHMTIWLGIVYAYkgLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPN--- 707
Cdd:cd15451 156 RGVLK-CDITDLQIICSLGYSI--LLMVTCTVYAIKTRGVP-ENFNEAKPIGFTMYTTCIVWLAFIPIFFGTAQSAEkly 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
7C7Q_B      708 VQFCIVALVIIFCSTITLCLVFVPKLITLRTNPDAATQNRRFQF 751
Cdd:cd15451 232 IQTTTLTISMNLSASVALGMLYMPKVYIIIFHPELNVQKRKRSF 275
7tmC_mGluR3 cd15448
metabotropic glutamate receptor 3 in group 2, member of the class C family of ...
480-733 4.46e-09

metabotropic glutamate receptor 3 in group 2, member of the class C family of seven-transmembrane G protein-coupled receptors; The metabotropic glutamate receptors (mGluRs) in group 2 include mGluR 2 and 3. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320564  Cd Length: 254  Bit Score: 58.04  E-value: 4.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      480 LGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsfvSEKTFETLCTVRTWILTVGYTTAFGA 559
Cdd:cd15448  12 LGFICTCMVITVFIKHNNTPLVKASGRELCYILLFGVFLSYCMTFFF-------IAKPSPVICTLRRLGLGTSFAVCYSA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      560 MFAKTWRVHAIFKNVK---MKKKIIKDQKLLVIVGGMLLIDLCILICWQAVD-PLRRtveKYSMepdPAGRDISIrpLLE 635
Cdd:cd15448  85 LLTKTNCIARIFDGVKngaQRPKFISPSSQVFICLSLILVQIVVVSVWLILEaPGTR---RYTL---PEKRETVI--LKC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      636 HCENTHMTIWLgivyAYKGLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNVQFCIVAL 715
Cdd:cd15448 157 NVKDSSMLISL----TYDVVLVILCTVYAFKTRKCP-ENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCI 231
                       250
                ....*....|....*...
7C7Q_B      716 VIIFCSTITLCLVFVPKL 733
Cdd:cd15448 232 SVSLSGFVVLGCLFAPKV 249
7tmC_mGluR_group2 cd15284
metabotropic glutamate receptors in group 2, member of the class C family of ...
477-733 8.15e-09

metabotropic glutamate receptors in group 2, member of the class C family of seven-transmembrane G protein-coupled receptors; The metabotropic glutamate receptors (mGluRs) in group 2 include mGluR 2 and 3. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320411  Cd Length: 254  Bit Score: 57.17  E-value: 8.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      477 LTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLFgldgsfvSEKTFETLCTVRTWILTVGYTTA 556
Cdd:cd15284   9 IACLGFLCTLFVIGVFIKHNNTPLVKASGRELCYILLFGVFLCYCMTFIF-------IAKPSPAICTLRRLGLGTSFAVC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      557 FGAMFAKTWRVHAIFKNVK---MKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDP--LRRtvekysmEPDPAGRDISIr 631
Cdd:cd15284  82 YSALLTKTNRIARIFSGVKdgaQRPRFISPSSQVFICLALISVQLLVVSVWLLVEApgTRR-------YTLPEKRETVI- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      632 pLLEHCENTHMTIWLgivyAYKGLLMLFGCFLAWETRNVSiPALNDSKYIGMSVYNVGIMCIIGAAVSFLTRDQPNVQFC 711
Cdd:cd15284 154 -LKCNVRDSSMLISL----TYDVVLVILCTVYAFKTRKCP-ENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTT 227
                       250       260
                ....*....|....*....|..
7C7Q_B      712 IVALVIIFCSTITLCLVFVPKL 733
Cdd:cd15284 228 TMCISVSLSGFVVLGCLFAPKV 249
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
152-443 2.70e-08

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR1, an essential channel-forming subunit of the NMDA receptor. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer ccomposed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. When co-expressed with NR1, the NR3 subunits form receptors that are activated by glycine alone and therefore can be classified as excitatory glycine receptors. NR1/NR3 receptors are calcium-impermeable and unaffected by ligands acting at the NR2 glutamate-binding site


Pssm-ID: 380602  Cd Length: 364  Bit Score: 56.58  E-value: 2.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      152 LADKKKYPYFFRTVP--SDNAvnPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDIEI-------SDTESFS 222
Cdd:cd06379 104 FSDKNIHVSFLRTVPpySHQA--DVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETLAETKDIKIekviefePGEKNFT 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      223 NDpctsVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIpgwyepswweqvhteanSSRCLRKNLLAamEG 302
Cdd:cd06379 182 SL----LEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIV-----------------TEQALAASNVP--DG 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      303 YIGVdfeplsskqiKTISGKTPQQYEReynnkrsgvgpskfhgyayDGIWVIAK---TLQRAMETLHASSRHQRIQDFNY 379
Cdd:cd06379 239 VLGL----------QLIHGKNESAHIR-------------------DSVSVVAQairELFRSSENITDPPVDCRDDTNIW 289
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7C7Q_B      380 TDhtlGRIILNAMNETNF-FGVTGQVVF-RNGERMGT---IKFTQFQDSReVKVGEYNAVADT---LEIIND 443
Cdd:cd06379 290 KS---GQKFFRVLKSVKLsDGRTGRVEFnDKGDRIGAeydIINVQNPRKL-VQVGIYVGSQRPtksLLSLND 357
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
119-190 5.20e-08

ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain of the group II metabotropic glutamate receptor, a family that contains mGlu2R and mGlu3R, all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes


Pssm-ID: 380598 [Multi-domain]  Cd Length: 462  Bit Score: 55.98  E-value: 5.20e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7C7Q_B      119 VFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTL 190
Cdd:cd06375 114 VIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTV 185
PBP1_ABC_RPA1789-like cd06333
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ...
61-382 5.37e-08

type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, RPA1791-1793), involved in active transport of lignin-derived aromatic substrates, and its close homologs; This group includes RPA1789 (CouP) from Rhodopseudomonas palustris and its close homologs in other bacteria. RPA1789 (CouP) is the periplasmic binding-protein component of an ABC system (CouPSTU; RPA1789, RPA1791-1793) that is involved in the active transport of lignin-derived aromatic substrates. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).


Pssm-ID: 380556 [Multi-domain]  Cd Length: 342  Bit Score: 55.63  E-value: 5.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       61 SIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAF--------YDAIkygpnhlmvfggVCPSVTSI-- 130
Cdd:cd06333  14 SLGIPERNAVELLVEQINAAGGINGRKLELIVYDDESDPTKAVTNArklieedkVDAI------------IGPSTTGEsl 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      131 ----IAESLQgwnLVQLSFAATTPVLADKKKYpyFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTG 206
Cdd:cd06333  82 avapIAEEAK---VPLISLAGAAAIVEPVRKW--VFKTPQSDSLVAEAILDYMKKKGIKKVALLGDSDAYGQSGRAALKK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      207 VLYGEDIEISDTESFS-NDpcTSVK----KLKGNDVR-IILGQFDQnMAAKVFccayeENMYGSKYQWIIpgwyepswwe 280
Cdd:cd06333 157 LAPEYGIEIVADERFArTD--TDMTaqltKIRAAKPDaVLVWASGP-PAALVA-----KNLRQLGYKGPI---------- 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      281 qVHTEANSSRCLRKNLLAAMEGYIGV-------DFEPLSSKQIKTIsgktpQQYEREYnNKRSGVGPSKFHGYAYDGIWV 353
Cdd:cd06333 219 -YQSHGAANQDFIKLAGKAAEGVILPagkllvaDQLPDSDPQKKVL-----LEFVKAY-EAKYGEGPSTFAGHAYDALLL 291
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
7C7Q_B      354 IAKTLQR-----------AMETLHASSRHQRIQDFNYTDH 382
Cdd:cd06333 292 LVEAIEPaggtdraalrdALENTKGLVGVTGVYNFSPTDH 331
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
50-361 5.41e-08

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 55.31  E-value: 5.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       50 LMPLTKEVAkgSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGpNHLMVFGGVCPSVTS 129
Cdd:cd19980   5 IAPLSGPVA--ALGQQVLNGAKLAVEEINAKGGVLGRKLELVVEDDKCPPAEGVAAAKKLITDD-KVPAIIGAWCSSVTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      130 IIAESLQGWNLVQLSFAATTPVLAdKKKYPYFFRTVPSD----NAVNPAILKLLKhyqWKRVGTLTQD-------VQRFS 198
Cdd:cd19980  82 AVMPVAERAKVPLVVEISSAPKIT-EGGNPYVFRLNPTNsmlaKAFAKYLADKGK---PKKVAFLAENddygrgaAEAFK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      199 EVRNDLTGVLYGEDIEISDTESFSndpcTSVKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMygsKYQWIIPGwyepSW 278
Cdd:cd19980 158 KALKAKGVKVVATEYFDQGQTDFT----TQLTKLKAANPDAIFVVAETEDGALILKQARELGL---KQQLVGTG----GT 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      279 WEQVHTEANSSrclrknllaAMEGYIGVD-FEPlsskqikTISGKTPQQyEREYNNKRSGVGPSKFHGYAYDGIWVIAKT 357
Cdd:cd19980 227 TSPDLIKLAGD---------AAEGVYGASiYAP-------TADNPANKA-FVAAYKKKYGEPPDKFAALGYDAVMVIAEA 289

                ....
7C7Q_B      358 LQRA 361
Cdd:cd19980 290 IKKA 293
PBP1_As_SBP-like cd06330
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
48-193 1.33e-07

periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea that is predicted to be involved in the efflux of toxic compounds. Members of this subgroup include proteins from Herminiimonas arsenicoxydans, which is resistant to arsenic (As) and various heavy metals such as cadmium and zinc. Moreover, they show significant sequence similarity to the cluster of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa.


Pssm-ID: 380553 [Multi-domain]  Cd Length: 342  Bit Score: 54.10  E-value: 1.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       48 MGLM-PLTKEVAkgSIGRGVLPAVELAIEQIrNES---LLRPyfLDLRLYDTECDNAKGLKAFYDAI-KYGPNHLM--VF 120
Cdd:cd06330   2 IGVItPLSGAAA--VYGEPARNGAELAVEEI-NAAggiLGRK--IELVVRDDKGKPDEAVRAARELVlQEGVDFLIgtIS 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
7C7Q_B      121 GGVCPSVTSIIAESlqgwNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQ--WKRVGTLTQD 193
Cdd:cd06330  77 SGVALAVAPVAEEL----KVLFIATDAATDRLTEENFNPYVFRTSPNTYMDAVAAALYAAKKPpdVKRWAGIGPD 147
PBP1_mGluR_groupIII cd06376
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
119-190 1.43e-07

ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain of the group III metabotropic glutamate receptor, a family which contains mGlu4R, mGluR6R, mGluR7, and mGluR8; all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.


Pssm-ID: 380599 [Multi-domain]  Cd Length: 467  Bit Score: 54.81  E-value: 1.43e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7C7Q_B      119 VFGGVCPSVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTL 190
Cdd:cd06376 111 VIGASASSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTL 182
PBP1_sensory_GC_DEF-like cd06371
ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are ...
69-194 2.72e-07

ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues; This group includes the ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues. They share a similar topology with an N-terminal extracellular ligand-binding domain, a single transmembrane domain, and a C-terminal cytosolic region that contains kinase-like and catalytic domains. GC-D is specifically expressed in a subpopulation of olfactory sensory neurons. GC-E and GC-F are colocalized within the same photoreceptor cells of the retina and have important roles in phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. GC-D expressing neurons have been implicated in pheromone detection and GC-D is phylogenetically more similar to the Ca2+-regulated GC-E and GC-F than to receptor GC-A, -B and -C which are activated by peptide ligands. Moreover, these olfactory GCs and retinal GCs share characteristic sequence similarity in a regulatory domain that is involved in the binding of GCAPs, suggesting GC-D activity may be regulated by an unknown extracellular ligand and intracellular Ca2+. Rodent GC-D-expressing neurons have been implicated in pheromone detection and were recently shown to respond to atmospheric CO2 which is an olfactory stimulus for many invertebrates and regulates some insect innate behavior, such as the location of food and hosts.


Pssm-ID: 380594 [Multi-domain]  Cd Length: 379  Bit Score: 53.47  E-value: 2.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       69 AVELAIEQI-RNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKY-----GPnhlmVFGGVCPSvtsiiAESL-QGWNLV 141
Cdd:cd06371  22 AARLAVSRInKDPSLDLGYWFDYVILPEDCETSKALAAFSSAEGRasgfvGP----VNPGYCEA-----ASLLaQEWDKA 92
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
7C7Q_B      142 QLSFAATTPVLadkKKYPYFFRTVPSDNAVnpaILKLLKHYQWKRVGTLT--QDV 194
Cdd:cd06371  93 LFSWGCVNHEL---NSYPTFARTLPPPADV---LYTVLRYFRWAHVAVVSspQDL 141
7tmC_mGluR5 cd15450
metabotropic glutamate receptor 5 in group 1, member of the class C family of ...
480-733 3.30e-07

metabotropic glutamate receptor 5 in group 1, member of the class C family of seven-transmembrane G protein-coupled receptors; Group 1 mGluRs includes mGluR1 and mGluR5, as well as their closely related invertebrate receptors. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320566  Cd Length: 250  Bit Score: 52.29  E-value: 3.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      480 LGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLfgldgsfVSEKTFETLCTVRTWILTVGYTTAFGA 559
Cdd:cd15450  12 LGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFC-------LIAKPKQIYCYLQRIGIGLSPAMSYSA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      560 MFAKTWRVHAIfknVKMKKKIIKDQKLLVIVGGMLLIDLCILICWQavdpLRRTVEKYSMEPDPAGRDI-SIRPLLEHCE 638
Cdd:cd15450  85 LVTKTNRIARI---LAGSKKKICTKKPRFMSACAQLVIAFILICIQ----LGIIVALFIMEPPDIMHDYpSIREVYLICN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      639 NTHmtiwLGIV--YAYKGLLMLFGCFLAWETRNVsiPA-LNDSKYIGMSVYNVGIMCIIGAAVSFLTrdqpNVQFCIVAL 715
Cdd:cd15450 158 TTN----LGVVtpLGYNGLLILSCTFYAFKTRNV--PAnFNEAKYIAFTMYTTCIIWLAFVPIYFGS----NYKIITMCF 227
                       250
                ....*....|....*...
7C7Q_B      716 VIIFCSTITLCLVFVPKL 733
Cdd:cd15450 228 SVSLSATVALGCMFVPKV 245
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
126-238 3.54e-07

ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of the group I metabotropic glutamate receptor, a family containing mGlu1R and mGlu5R, all of which stimulate phospholipase C (PLC) hydrolysis. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.


Pssm-ID: 380597 [Multi-domain]  Cd Length: 474  Bit Score: 53.50  E-value: 3.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      126 SVTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD-------VQRFS 198
Cdd:cd06374 129 SVTIQVQNLLQLFHIPQIGYSATSIDLSDKSLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEgnygesgIEAFK 208
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
7C7Q_B      199 EVRNDltgvlygEDIEISDTESFSNDPCTS-----VKKLKGNDVR 238
Cdd:cd06374 209 ELAAE-------EGICIAHSDKIYSNAGEEefdrlLRKLMNTPNK 246
PBP1_ABC_ligand_binding-like cd06335
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
60-364 4.17e-07

type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.


Pssm-ID: 380558 [Multi-domain]  Cd Length: 348  Bit Score: 52.61  E-value: 4.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       60 GSIGRGVLPAVELAIEQIrNES---LLRPyfLDLRLYDTECDNAKGLKAFYDAI-KYGPnhLMVFGGVCPSVTSIIAESL 135
Cdd:cd06335  13 AELGESARRGVELAVEEI-NAAggiLGRK--IELVERDDEANPTKAVQNAQELIdKEKV--VAIIGPTNSGVALATIPIL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      136 QGWNLVQLSFAATTPVLADK--KKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTGVLYGEDI 213
Cdd:cd06335  88 QEAKIPLIIPVATGTAITKPpaKPRNYIFRVAASDTLQADFLVDYAVKKGFKKIAILHDTTGYGQGGLKDVEAALKKRGI 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      214 EISDTESFS---NDPCTSVKKLK--GNDVRIILGQFDqnMAAKVfcCAYEENMygskyqwiipGWYEP---SWweqvhte 285
Cdd:cd06335 168 TPVATESFKigdTDMTPQLLKAKdaGADVILVYGLGP--DLAQI--LKAMEKL----------GWKVPlvgSW------- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      286 ANSSRCLRKNLLAAMEGYIGV---DFEPLSSKQIKTIsgktpQQYEREYNNKRSGVGPSKFHGyaYDGIWVIAKTLQRAM 362
Cdd:cd06335 227 GLSMPNFIELAGPLAEGTIMTqtfIEDYLTPRAKKFI-----DAYKKKYGTDRIPSPVSAAQG--YDAVYLLAAAIKQAG 299

                ..
7C7Q_B      363 ET 364
Cdd:cd06335 300 ST 301
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-191 3.41e-06

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 49.85  E-value: 3.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       52 PLTKEVAkgSIGRGVLPAVELAIEQIrNESL-LRPYFLDLRLYDTECDNAKGLKAFYDAI-KYGPnhLMVFGGVCPSVTS 129
Cdd:cd06347   7 PLTGEAA--AYGQPALNGAELAVDEI-NAAGgILGKKIELIVYDNKSDPTEAANAAQKLIdEDKV--VAIIGPVTSSIAL 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
7C7Q_B      130 IIAESLQGWNLVQLSFAATTPVLADKKkyPYFFRTVPSDN-----AVNPAILKLlkhyQWKRVGTLT 191
Cdd:cd06347  82 AAAPIAQKAKIPMITPSATNPLVTKGG--DYIFRACFTDPfqgaaLAKFAYEEL----GAKKAAVLY 142
7tmC_mGluR1 cd15449
metabotropic glutamate receptor 1 in group 1, member of the class C family of ...
473-733 6.29e-05

metabotropic glutamate receptor 1 in group 1, member of the class C family of seven-transmembrane G protein-coupled receptors; Group 1 mGluRs includes mGluR1 and mGluR5, as well as their closely related invertebrate receptors. They are homodimeric class C G-protein coupled receptors which are activated by glutamate, the major excitatory neurotransmitter of the CNS. mGluRs are involved in regulating neuronal excitability and synaptic transmission via intracellular activation of second messenger signaling pathways. While the ionotropic glutamate receptor subtypes (AMPA, NMDA, and kainite) mediate fast excitatory postsynaptic transmission, mGluRs are known to mediate slower excitatory postsynaptic responses and to be involved in synaptic plasticity in the mammalian brain. In addition to seven-transmembrane helices, the class C GPCRs are characterized by a large N-terminal extracellular Venus flytrap-like domain, which is composed of two adjacent lobes separated by a cleft which binds an endogenous ligand. Moreover, they exist as either homo- or heterodimers, which are essential for their function. For instance, mGluRs form homodimers via interactions between the N-terminal Venus flytrap domains and the intermolecular disulphide bonds between cysteine residues located in the cysteine-rich domain (CRD). At least eight different subtypes of metabotropic receptors (mGluR1-8) have been identified and further classified into three groups based on their sequence homology, pharmacological properties, and signaling pathways. Group 1 (mGluR1 and mGluR5) receptors are predominantly located postsynaptically on neurons and are involved in long-term synaptic plasticity in the brain, including long-term potentiation (LTP) in the hippocampus and long-term depression (LTD) in the cerebellum. They are coupled to G(q/11) proteins, thereby activating phospholipase C to generate inositol-1,4,5-triphosphate (IP3) and diacyglycerol (DAG), which in turn lead to Ca2+ release and protein kinase C activation, respectively. Group 1 mGluR expression is shown to be strongly upregulated in animal models of epilepsy, brain injury, inflammatory, and neuropathic pain, as well as in patients with amyotrophic lateral sclerosis or multiple sclerosis. Group 2 (mGluR2 and mGluR3) and 3 (mGluR4, mGluR6, mGluR7, and mGluR8) receptors are predominantly localized presynaptically in the active region of neurotransmitter release. They are coupled to G(i/o) proteins, which leads to inhibition of adenylate cyclase activity and cAMP formation, and consequently to a decrease in protein kinase A (PKA) activity. Ultimately, activation of these receptors leads to inhibition of neurotransmitter release such as glutamate and GABA via inhibition of Ca2+ channels and activation of K+ channels. Furthermore, while activation of Group 1 mGluRs increases NMDA (N-methyl-D-aspartate) receptor activity and risk of neurotoxicity, Group 2 and 3 mGluRs decrease NMDA receptor activity and prevent neurotoxicity.


Pssm-ID: 320565  Cd Length: 250  Bit Score: 45.39  E-value: 6.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      473 ILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFlfgldgSFVSEKTFeTLCTVRTWILTVG 552
Cdd:cd15449   5 IAVAFSCLGILVTMFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPF------TLIAKPTT-TSCYLQRLLVGLS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      553 YTTAFGAMFAKTWRVHAIFKNvkMKKKIIKDQKLLVIVGGMLLIdLCILICWQavdpLRRTVEKYSMEP-DPAGRDISIR 631
Cdd:cd15449  78 SAMCYSALVTKTNRIARILAG--SKKKICTRKPRFMSAWAQVVI-ASILISVQ----LTLVVTLIIMEPpMPILSYPSIK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      632 PLLEHCENTHMTIWLGIvyAYKGLLMLFGCFLAWETRNVsiPA-LNDSKYIGMSVYNVGIMCIIGAAVSFLTrdqpNVQF 710
Cdd:cd15449 151 EVYLICNTSNLGVVAPL--GYNGLLIMSCTYYAFKTRNV--PAnFNEAKYIAFTMYTTCIIWLAFVPIYFGS----NYKI 222
                       250       260
                ....*....|....*....|...
7C7Q_B      711 CIVALVIIFCSTITLCLVFVPKL 733
Cdd:cd15449 223 ITTCFAVSLSVTVALGCMFTPKM 245
PRK15404 PRK15404
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
70-237 7.91e-05

high-affinity branched-chain amino acid ABC transporter substrate-binding protein;


Pssm-ID: 237959 [Multi-domain]  Cd Length: 369  Bit Score: 45.78  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B        70 VELAIEQIRNESLLRPYFLDLRLYDTECDNAKGL----KAFYDAIKYgpnhlmVFGGVCPSVTSIIAESLQGWNLVQLSF 145
Cdd:PRK15404  49 ARQAIEDINAKGGIKGDKLEGVEYDDACDPKQAVavanKVVNDGIKY------VIGHLCSSSTQPASDIYEDEGILMITP 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       146 AATTPVLADKKkYPYFFRTVPSDNAVNPAILK-LLKHYQWKRVGTLtQDVQRFSE-----VRNDL----TGVLYGEDIEI 215
Cdd:PRK15404 123 AATAPELTARG-YQLIFRTIGLDSDQGPTAAKyILEKVKPKRIAVL-HDKQQYGEglarsVKDGLkkagANVVFFEGITA 200
                        170       180
                 ....*....|....*....|..
7C7Q_B       216 SDTEsFSndpcTSVKKLKGNDV 237
Cdd:PRK15404 201 GDKD-FS----ALIAKLKKENV 217
PBP1_ABC_HAAT-like cd06344
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
63-410 8.44e-05

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of hydrophobic amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380567 [Multi-domain]  Cd Length: 332  Bit Score: 45.29  E-value: 8.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       63 GRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYdAIKYGPNHLMVFG----GVCPSvTSIIAESlqgW 138
Cdd:cd06344  14 GDLFLEGVELAVEEINAAGGVLGRKIRLVEYDDEASVDKGLAIAQ-RFADNPDVVAVIGhrssYVAIP-ASIIYER---A 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      139 NLVQLSFAATTPVLADKKkYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDvqrfsevrNDltgvlYGED------ 212
Cdd:cd06344  89 GLLMLSPGATAPKLTQHG-FKYIFRNIPSDEDIARQLARYAARQGYKRIVIYYDD--------DS-----YGKGlanafe 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      213 -------IEISDTESFSNDpctsvkklkGNDVRIILG---QFDQNMAakVFCCAYEEnmygSKYQWI---------IP-- 271
Cdd:cd06344 155 eearelgITIVDRRSYSSD---------EEDFRRLLSkwkALDFFDA--IFLAGSMP----EGAEFIkqarelgikVPii 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      272 ---GWYEPSWWEqvhtEANSsrclrknllAAMEGYIGVDFEPlsskqiktiSGKTP--QQYEREYnNKRSGVGPSKFHGY 346
Cdd:cd06344 220 ggdGLDSPELIE----IAGK---------AAEGVVVATVFDP---------DDPRPevRAFVEAF-RKKYGREPDVWAAQ 276
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
7C7Q_B      347 AYDGIWVIAktlqRAMETLHASSRhqriqdfnytdhtlgRIILNAMNET-NFFGVTGQVVF-RNGE 410
Cdd:cd06344 277 GYDAVKLLA----EAIEKAGSTVP---------------AKIASALRFLeNWEGVTGTYSFdANGD 323
PBP1_SBP-like cd19989
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
50-193 1.17e-04

periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.


Pssm-ID: 380644 [Multi-domain]  Cd Length: 299  Bit Score: 44.96  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       50 LMPLTKEVAkgSIGRGVLPAVELAIEQIrNES---LLRPYflDLRLYDTECDNAKGLKAFYDAIKyGPNHLMVFGGVCPS 126
Cdd:cd19989   5 LTPLSGPYA--ALGEEARRGAQLAVEEI-NAAggiLGRPV--ELVVEDTEGKPATAVQKARKLVE-QDGVDFLTGAVSSA 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
7C7Q_B      127 VTSIIAESLQGWNLVQLSFAATTPVLADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD 193
Cdd:cd19989  79 VALAVAPKAAELKVPYLVTVAADDELTGENCNRYTFRVNTSDRMIARALAPWLAENGGKKWYIVYAD 145
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
61-193 1.72e-04

ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C natriuretic peptide receptor (NPR-C). NPR-C is found in atrial, mesentery, placenta, lung, kidney, venous tissue, aortic smooth muscle, and aortic endothelial cells. The affinity of NPR-C for natriuretic peptides is ANP>CNP>BNP. The extracellular domain of NPR-C is about 30% identical to NPR-A and NPR-B. However, unlike the cyclase-linked receptors, it contains only 37 intracellular amino acids and no guanylyl cyclase activity. Major function of NPR-C is to clear natriuretic peptides from the circulation or extracellular surroundings through constitutive receptor-mediated internalization and degradation.


Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 44.85  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       61 SIGRgVLPAVELAIEQIRNESLLRP-YFLDLRLYDTECDNaKGLKAFYD---AIKYGPNhlMVFGGVCPSVTSIIAESLQ 136
Cdd:cd06386  18 SLTR-VRPAIEYALRSVEGNGLLPPgTRFNVAYEDSDCGN-RALFSLVDrvaQKRAKPD--LILGPVCEYAAAPVARLAS 93
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
7C7Q_B      137 GWNLVQLSFAATTPVLADKKK-YPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQD 193
Cdd:cd06386  94 HWNLPMLSAGALAAGFSHKDSeYSHLTRVAPAYAKMGEMFLALFRHHHWSRAFLVYSD 151
PBP1_SBP-like cd06329
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ...
60-167 2.17e-04

periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.


Pssm-ID: 380552 [Multi-domain]  Cd Length: 343  Bit Score: 44.19  E-value: 2.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       60 GSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIKYGPNhlMVFGGVCPSVTSIIAESLQGWN 139
Cdd:cd06329  13 ASVGEIYLKGLQFAIEEINAGGGLLGRKIELVPFDNKGSPQEALIQLKKAIDQGIR--FVLQGNSSAVAGALIDAIEKHN 90
                        90       100       110
                ....*....|....*....|....*....|....*
7C7Q_B      140 L-------VQLSFAATTPVLADKKKYPYFFRTVPS 167
Cdd:cd06329  91 QrnpdkrvLFLNYGAEAPELTGAKCSFWHFRFDAN 125
7tmC_V2R_pheromone cd15283
vomeronasal type-2 pheromone receptors, member of the class C family of seven-transmembrane G ...
469-731 3.12e-04

vomeronasal type-2 pheromone receptors, member of the class C family of seven-transmembrane G protein-coupled receptors; This group represents vomeronasal type-2 pheromone receptors (V2Rs). Members of the V2R family of vomeronasal GPCRs are involved in detecting protein pheromones for social and sexual cues between the same species. V2Rs and G-alpha(o) protein are coexpressed in the basal layer of the vomeronasal organ (VNO), which is the sensory organ of the accessory olfactory system present in amphibians, reptiles, and non-primate mammals such as mice and rodents, but it is non-functional or absent in humans, apes, and monkeys. On the other hand, members of the V1R receptor family and G-alpha(i2) protein are coexpressed in the apical neurons of the VNO. Activation of V1R or V2R causes activation of phospholipase pathway, producing the second messengers diacylglycerol (DAG) and IP3. However, in contrast to V1Rs, V2Rs contain the long N-terminal extracellular domain, which is believed to bind pheromones.


Pssm-ID: 320410 [Multi-domain]  Cd Length: 252  Bit Score: 43.03  E-value: 3.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      469 PLYSILSALTILGMIMASAFLFFNIKNRNQKLIKMSSPYMNNLIILGGMLSYASIFLfgldgsFVSEKTFETlCTVRTWI 548
Cdd:cd15283   1 PLGIALTVLSLLGSVLTAAVLVVFIKHRDTPIVKANNSELSYLLLLSLKLCFLCSLL------FIGQPSTWT-CMLRQTA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      549 LTVGYTTAFGAMFAKTWRVHAIFKNVK---MKKKIIKDQKLLVIVGGMLLIDLCILICWQAVDPlrrtvekysmePDPAg 625
Cdd:cd15283  74 FGISFVLCISCILAKTIVVVAAFKATRpgsNIMKWFGPGQQRAIIFICTLVQVVICAIWLATSP-----------PFPD- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      626 rdisirpllehcENTHMTIWLGIVYAYKGLLMLFGCFLAwetrnvsipalndskYIGMsvynVGIMCIIgaaVSFLTRDQ 705
Cdd:cd15283 142 ------------KNMHSEHGKIILECNEGSVVAFYCVLG---------------YIGL----LALVSFL---LAFLARKL 187
                       250       260
                ....*....|....*....|....*....
7C7Q_B      706 P---NVQFCIVALVIIFCStitLCLVFVP 731
Cdd:cd15283 188 PdnfNEAKFITFSMLVFCA---VWVAFVP 213
PBP1_iGluR_NMDA cd06367
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic ...
140-271 5.28e-04

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptors. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. The function of the NMDA subtype receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer comprising two NR1 and two NR2 (A, B, C, and D) or NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 380590 [Multi-domain]  Cd Length: 357  Bit Score: 43.00  E-value: 5.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      140 LVQLSFAAT---TPVL----------ADKKKYPYFFRTVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRNDLTG 206
Cdd:cd06367  79 AQILDFIAAqtlTPVLglhgrssmimADKSEHSMFLQFGPPIEQQASVMLNIMEEYDWYIVSLVTTYFPGYQDFVNKLRS 158
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7C7Q_B      207 VLygEDIEISDTESFSNDPCTS---------VKKLKGNDVRIILGQFDQNMAAKVFCCAYEENMYGSKYQWIIP 271
Cdd:cd06367 159 TI--ENSGWELEEVLQLDMSLDdgdsklqaqLKKLQSPEARVILLYCTKEEATYVFEVAASVGLTGYGYTWLVG 230
PBP1_ABC_HAAT-like cd06348
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
50-222 2.66e-03

type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380571 [Multi-domain]  Cd Length: 342  Bit Score: 40.68  E-value: 2.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B       50 LMPLTKEVAkgSIGRGVLPAVELAIEQIRNESLLRPYFLDLRLYDTECDNAKGLKAFYDAIkYGPNHLMVFGgvcPSVTS 129
Cdd:cd06348   5 ALSLTGPGA--LYGQSQKNGAQLAVEEINAAGGVGGVKIELIVEDTAGDPEQAINAFQKLI-NQDKVLAILG---PTLSS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7C7Q_B      130 I------IAESLqgwNLVQLSFAATTPVLADKKkyPYFFR-TVPSDNAVNPAILKLLKHYQWKRVGTLTQDVQRFSEVRN 202
Cdd:cd06348  79 EafaadpIAQQA---KVPVVGISNTAPGITDIG--PYIFRnSLPEDKVIPPTVKAAKKKYGIKKVAVLYDQDDAFTVSGT 153
                       170       180
                ....*....|....*....|.
7C7Q_B      203 D-LTGVLYGEDIEISDTESFS 222
Cdd:cd06348 154 KvFPAALKKNGVEVLDTETFQ 174
 
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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