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Conserved domains on  [gi|1856631258|ref|NP_001371197|]
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metabotropic glutamate receptor 5 isoform b precursor [Homo sapiens]

Protein Classification

G-protein coupled receptor( domain architecture ID 11570937)

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 bind to and activate numerous downstream effector proteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
26-497 0e+00

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: 900.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   26 RVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVA 105
Cdd:cd06374      1 RLVARMPGDIIIGALFPVHHQPPLKKVFSRKCGEIREQYGIQRVEAMFRTLDKINKDPNLLPNITLGIEIRDSCWYSPVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  106 LEQSIEFIRDSLISSEEEEGLVRCVDG-SSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTL 184
Cdd:cd06374     81 LEQSIEFIRDSVASVEDEKDTQNTPDPtPLSPPENRKPIVGVIGPGSSSVTIQVQNLLQLFHIPQIGYSATSIDLSDKSL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  185 FKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKL 264
Cdd:cd06374    161 YKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEEGICIAHSDKIYSNAGEEEFDRLLRKL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  265 TSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKL 344
Cdd:cd06374    241 MNTPNKARVVVCFCEGETVRGLLKAMRRLNATGHFLLIGSDGWADRKDVVEGYEDEAAGGITIKIHSPEVESFDEYYFNL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  345 RPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYA- 423
Cdd:cd06374    321 KPETNSRNPWFREFWQHRFDCRLPGHPDENPYFKKCCTGEESLLGNYVQDSKLGFVINAIYAMAHALHRMQEDLCGGYSv 400
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1856631258  424 GLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDD 497
Cdd:cd06374    401 GLCPAMLPINGSLLLDYLLNVSFVGVSGDTIMFDENGDPPGRYDIMNFQKTGEGSYDYVQVGSWKNGSLKMDDE 474
7tmC_mGluR5 cd15450
metabotropic glutamate receptor 5 in group 1, member of the class C family of ...
578-827 7.76e-166

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: 490.65  E-value: 7.76e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15450      1 PEPIAAVVFACLGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 737
Cdd:cd15450     81 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  738 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 817
Cdd:cd15450    161 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 240
                          250
                   ....*....|
gi 1856631258  818 FVPKVYIILA 827
Cdd:cd15450    241 FVPKVYIILA 250
GluR_Homer-bdg pfam10606
Homer-binding domain of metabotropic glutamate receptor; This is the proline-rich region of ...
1130-1180 2.83e-22

Homer-binding domain of metabotropic glutamate receptor; This is the proline-rich region of metabotropic glutamate receptor proteins that binds Homer-related synaptic proteins. The Homer proteins form a physical tether linking mGluRs with the inositol trisphosphate receptors (IP3R) that appears to be due to the proline-rich "Homer ligand" (PPXXFr). Activation of PI turnover triggers intracellular calcium release. MGluR function is altered in the mouse model of human Fragile X syndrome mental retardation, a disorder caused by loss of function mutations in the Fragile X mental retardation gene Fmr1. Homer 3 (and to a lesser extent Homer 1b/c) has been shown to form a multimeric complex with mGlu1a and the IP3 receptor, indicating that Homers may play a role in the localization of receptors to their signalling partners.


:

Pssm-ID: 431390  Cd Length: 51  Bit Score: 90.99  E-value: 2.83e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1856631258 1130 ALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL 1180
Cdd:pfam10606    1 ALTPPSPFRDSVCSGSSSPGSPVSESMLCSPPSPTYTSLILRDYSQSSSTL 51
NCD3G pfam07562
Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several ...
508-558 2.15e-19

Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several highly-conserved Cys residues that are predicted to form disulphide bridges. It is predicted to lie outside the cell membrane, tethered to the pfam00003 in several receptor proteins.


:

Pssm-ID: 462210  Cd Length: 53  Bit Score: 82.69  E-value: 2.15e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1856631258  508 RSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYV-FDEYTCKACQLGSWP 558
Cdd:pfam07562    2 SSVCSESCPPGQRKSQQGGAPVCCWDCVPCPEGEISnTDSDTCKKCPEGQWP 53
 
Name Accession Description Interval E-value
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
26-497 0e+00

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: 900.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   26 RVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVA 105
Cdd:cd06374      1 RLVARMPGDIIIGALFPVHHQPPLKKVFSRKCGEIREQYGIQRVEAMFRTLDKINKDPNLLPNITLGIEIRDSCWYSPVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  106 LEQSIEFIRDSLISSEEEEGLVRCVDG-SSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTL 184
Cdd:cd06374     81 LEQSIEFIRDSVASVEDEKDTQNTPDPtPLSPPENRKPIVGVIGPGSSSVTIQVQNLLQLFHIPQIGYSATSIDLSDKSL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  185 FKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKL 264
Cdd:cd06374    161 YKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEEGICIAHSDKIYSNAGEEEFDRLLRKL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  265 TSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKL 344
Cdd:cd06374    241 MNTPNKARVVVCFCEGETVRGLLKAMRRLNATGHFLLIGSDGWADRKDVVEGYEDEAAGGITIKIHSPEVESFDEYYFNL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  345 RPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYA- 423
Cdd:cd06374    321 KPETNSRNPWFREFWQHRFDCRLPGHPDENPYFKKCCTGEESLLGNYVQDSKLGFVINAIYAMAHALHRMQEDLCGGYSv 400
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1856631258  424 GLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDD 497
Cdd:cd06374    401 GLCPAMLPINGSLLLDYLLNVSFVGVSGDTIMFDENGDPPGRYDIMNFQKTGEGSYDYVQVGSWKNGSLKMDDE 474
7tmC_mGluR5 cd15450
metabotropic glutamate receptor 5 in group 1, member of the class C family of ...
578-827 7.76e-166

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: 490.65  E-value: 7.76e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15450      1 PEPIAAVVFACLGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 737
Cdd:cd15450     81 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  738 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 817
Cdd:cd15450    161 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 240
                          250
                   ....*....|
gi 1856631258  818 FVPKVYIILA 827
Cdd:cd15450    241 FVPKVYIILA 250
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
67-472 4.90e-91

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: 296.60  E-value: 4.90e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   67 QRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIrdslisseeeeglvrcvdgssssfrsKKPIVGV 146
Cdd:pfam01094    1 LVLLAVRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLL--------------------------KGEVVAI 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  147 IGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGES 226
Cdd:pfam01094   55 IGPSCSSVASAVASLANEWKVPLISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGES 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  227 GMEAFKDMSAKEGICIAHSYKIYSNA-GEQSFDKLLKKLTShlpKARVVACFCEGMTVRGLLMAMRRLGLAGE-FLLLGS 304
Cdd:pfam01094  135 GLQALEDALRERGIRVAYKAVIPPAQdDDEIARKLLKEVKS---RARVIVVCCSSETARRLLKAARELGMMGEgYVWIAT 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  305 DGWADRYDVTDGYQREAVGGI-TIKLQSPDVKWFDDYYLKlrpetnhrnpwfqefwqhrfqcrlegfpqenskyNKTCNS 383
Cdd:pfam01094  212 DGLTTSLVILNPSTLEAAGGVlGFRLHPPDSPEFSEFFWE----------------------------------KLSDEK 257
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  384 SLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAglCDAMKPID-GRKLLESLMKTNFTGVSGDtILFDENGDS 462
Cdd:pfam01094  258 ELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRA--CGALGPWNgGQKLLRYLKNVNFTGLTGN-VQFDENGDR 334
                          410
                   ....*....|.
gi 1856631258  463 P-GRYEIMNFK 472
Cdd:pfam01094  335 InPDYDILNLN 345
7tm_3 pfam00003
7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane ...
573-821 2.05e-76

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: 252.58  E-value: 2.05e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  573 LRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIyCYLQRIGIG 652
Cdd:pfam00003    1 LDLSAPWGIVLEALAALGILLTLVLLVVFLLHRKTPIVKASNRSLSFLLLLGLLLLFLLAFLFIGKPTVT-CALRRFLFG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  653 LSPAMSYSALVTKTNRIARILAGSKKkictkkprFMSACAQLVIAFILICIQLgIIVALFIMEPPDIMHDYPSIREVYLI 732
Cdd:pfam00003   80 VGFTLCFSCLLAKTFRLVLIFRRRKP--------GPRGWQLLLLALGLLLVQV-IILTEWLIDPPFPEKDNLSEGKIILE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  733 C----NTTNLGVVtpLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYK------IITM 802
Cdd:pfam00003  151 CegstSIAFLDFV--LAYVGLLLLAGFLLAFKTRKLPDNFNEAKFITFSMLLSVLIWVAFIPMYLYGNKGkgtwdpVALA 228
                          250
                   ....*....|....*....
gi 1856631258  803 CFSVSLSATVALGCMFVPK 821
Cdd:pfam00003  229 IFAILASGWVLLGLYFIPK 247
GluR_Homer-bdg pfam10606
Homer-binding domain of metabotropic glutamate receptor; This is the proline-rich region of ...
1130-1180 2.83e-22

Homer-binding domain of metabotropic glutamate receptor; This is the proline-rich region of metabotropic glutamate receptor proteins that binds Homer-related synaptic proteins. The Homer proteins form a physical tether linking mGluRs with the inositol trisphosphate receptors (IP3R) that appears to be due to the proline-rich "Homer ligand" (PPXXFr). Activation of PI turnover triggers intracellular calcium release. MGluR function is altered in the mouse model of human Fragile X syndrome mental retardation, a disorder caused by loss of function mutations in the Fragile X mental retardation gene Fmr1. Homer 3 (and to a lesser extent Homer 1b/c) has been shown to form a multimeric complex with mGlu1a and the IP3 receptor, indicating that Homers may play a role in the localization of receptors to their signalling partners.


Pssm-ID: 431390  Cd Length: 51  Bit Score: 90.99  E-value: 2.83e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1856631258 1130 ALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL 1180
Cdd:pfam10606    1 ALTPPSPFRDSVCSGSSSPGSPVSESMLCSPPSPTYTSLILRDYSQSSSTL 51
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
143-311 5.39e-20

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: 92.30  E-value: 5.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:COG0683     72 VDAIVGPLSSGVALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDDY 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIAhsYKIYSNAGEQSFDKLLKKLTSHlpKARVVACFCEGMTVRGLLMAMRRLGLAGEFll 301
Cdd:COG0683    152 AYGQGLAAAFKAALKAAGGEVV--GEEYYPPGTTDFSAQLTKIKAA--GPDAVFLAGYGGDAALFIKQAREAGLKGPL-- 225
                          170
                   ....*....|
gi 1856631258  302 lgSDGWADRY 311
Cdd:COG0683    226 --NKAFVKAY 233
NCD3G pfam07562
Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several ...
508-558 2.15e-19

Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several highly-conserved Cys residues that are predicted to form disulphide bridges. It is predicted to lie outside the cell membrane, tethered to the pfam00003 in several receptor proteins.


Pssm-ID: 462210  Cd Length: 53  Bit Score: 82.69  E-value: 2.15e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1856631258  508 RSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYV-FDEYTCKACQLGSWP 558
Cdd:pfam07562    2 SSVCSESCPPGQRKSQQGGAPVCCWDCVPCPEGEISnTDSDTCKKCPEGQWP 53
 
Name Accession Description Interval E-value
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
26-497 0e+00

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: 900.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   26 RVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVA 105
Cdd:cd06374      1 RLVARMPGDIIIGALFPVHHQPPLKKVFSRKCGEIREQYGIQRVEAMFRTLDKINKDPNLLPNITLGIEIRDSCWYSPVA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  106 LEQSIEFIRDSLISSEEEEGLVRCVDG-SSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTL 184
Cdd:cd06374     81 LEQSIEFIRDSVASVEDEKDTQNTPDPtPLSPPENRKPIVGVIGPGSSSVTIQVQNLLQLFHIPQIGYSATSIDLSDKSL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  185 FKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKL 264
Cdd:cd06374    161 YKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEEGICIAHSDKIYSNAGEEEFDRLLRKL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  265 TSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKL 344
Cdd:cd06374    241 MNTPNKARVVVCFCEGETVRGLLKAMRRLNATGHFLLIGSDGWADRKDVVEGYEDEAAGGITIKIHSPEVESFDEYYFNL 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  345 RPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYA- 423
Cdd:cd06374    321 KPETNSRNPWFREFWQHRFDCRLPGHPDENPYFKKCCTGEESLLGNYVQDSKLGFVINAIYAMAHALHRMQEDLCGGYSv 400
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1856631258  424 GLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDD 497
Cdd:cd06374    401 GLCPAMLPINGSLLLDYLLNVSFVGVSGDTIMFDENGDPPGRYDIMNFQKTGEGSYDYVQVGSWKNGSLKMDDE 474
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
33-497 0e+00

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: 610.06  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   33 GDIIIGALFSVHHQPTVDkvheRKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEF 112
Cdd:cd06362      1 GDINLGGLFPVHERSSSG----ECCGEIREERGIQRLEAMLFAIDEINSRPDLLPNITLGFVILDDCSSDTTALEQALHF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  113 IRDSLISSEEEEGLVRCVDGSSS-SFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRV 191
Cdd:cd06362     77 IRDSLLSQESAGFCQCSDDPPNLdESFQFYDVVGVIGAESSSVSIQVANLLRLFKIPQISYASTSDELSDKERYPYFLRT 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  192 VPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHlPKA 271
Cdd:cd06362    157 VPSDSFQAKAIVDILLHFNWTYVSVVYSEGSYGEEGYKAFKKLARKAGICIAESERISQDSDEKDYDDVIQKLLQK-KNA 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  272 RVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNHR 351
Cdd:cd06362    236 RVVVLFADQEDIRGLLRAAKRLGASGRFIWLGSDGWGTNIDDLKGNEDVALGALTVQPYSEEVPRFDDYFKSLTPSNNTR 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  352 NPWFQEFWQHRFQCRlegFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLC-DAMK 430
Cdd:cd06362    316 NPWFREFWQELFQCS---FRPSRENSCNDDKLLINKSEGYKQESKVSFVIDAVYAFAHALHKMHKDLCPGDTGLCqDLMK 392
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1856631258  431 PIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDD 497
Cdd:cd06362    393 CIDGSELLEYLLNVSFTGEAGGEIRFDENGDGPGRYDIMNFQRNNDGSYEYVRVGVWDQYTQKLSLN 459
7tmC_mGluR5 cd15450
metabotropic glutamate receptor 5 in group 1, member of the class C family of ...
578-827 7.76e-166

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: 490.65  E-value: 7.76e-166
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15450      1 PEPIAAVVFACLGLLATLFVTVIFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 737
Cdd:cd15450     81 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  738 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 817
Cdd:cd15450    161 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 240
                          250
                   ....*....|
gi 1856631258  818 FVPKVYIILA 827
Cdd:cd15450    241 FVPKVYIILA 250
7tmC_mGluR_group1 cd15285
metabotropic glutamate receptors in group 1, member of the class C family of ...
578-826 1.09e-156

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: 467.11  E-value: 1.09e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15285      1 TEAIVAMVFACVGILATLFVTVVFIRHNDTPVVKASTRELSYIILAGILLCYASTFALLAKPSTISCYLQRILPGLSFAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 737
Cdd:cd15285     81 IYAALVTKTNRIARILAGSKKKILTRKPRFMSASAQVVITGILISVEVAIIVVMLILEPPDATLDYPTPKRVRLICNTST 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  738 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 817
Cdd:cd15285    161 LGFVVPLGFDFLLILLCTLYAFKTRNLPENFNEAKFIGFTMYTTCVIWLAFLPIYFGSDNKEITLCFSVSLSATVALVFL 240

                   ....*....
gi 1856631258  818 FVPKVYIIL 826
Cdd:cd15285    241 FFPKVYIIL 249
PBP1_mGluR_groupIII cd06376
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
33-496 3.00e-155

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: 471.98  E-value: 3.00e-155
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   33 GDIIIGALFSVHHQptvdKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEF 112
Cdd:cd06376      5 GDITLGGLFPVHAR----GLAGVPCGEIKKEKGIHRLEAMLYALDQINSDPDLLPNVTLGARILDTCSRDTYALEQSLTF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  113 IRdSLISSEEEEglVRCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVV 192
Cdd:cd06376     81 VQ-ALIQKDTSD--VRCTNGDPPVFVKPEKVVGVIGASASSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  193 PSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEG-ICIAHSYKIYSNAGEQSFDKLLKKLtSHLPKA 271
Cdd:cd06376    158 PPDSFQAQAMVDIVKALGWNYVSTLASEGNYGEKGVESFVQISREAGgVCIAQSEKIPRERRTGDFDKIIKRL-LETPNA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  272 RVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNHR 351
Cdd:cd06376    237 RAVVIFADEDDIRRVLAAAKRANKTGHFLWVGSDSWGAKISPVLQQEDVAEGAITILPKRASIEGFDAYFTSRTLENNRR 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  352 NPWFQEFWQHRFQCRLEGFPQENSKYNKTCN--SSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAM 429
Cdd:cd06376    317 NVWFAEFWEENFNCKLTSSGSKKEDTLRKCTgqERIGRDSGYEQEGKVQFVVDAVYAMAHALHNMNKDLCPGYRGLCPEM 396
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1856631258  430 KPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNG-ELKMDD 496
Cdd:cd06376    397 EPAGGKKLLKYIRNVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNGSNYGYRLIGQWTDElQLNIED 464
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
31-490 2.20e-147

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: 451.20  E-value: 2.20e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   31 MPGDIIIGALFSVHHQPTvdkvHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSI 110
Cdd:cd06375      3 LEGDLVLGGLFPVHEKGE----GMEECGRINEDRGIQRLEAMLFAIDRINRDPHLLPGVRLGVHILDTCSRDTYALEQSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  111 EFIRDSLISSEEEEGLvrCVDGSSSSFRSKKP--IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYF 188
Cdd:cd06375     79 EFVRASLTKVDDSEYM--CPDDGSYAIQEDSPlpIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  189 MRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHl 268
Cdd:cd06375    157 ARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICIATAEKVGRSADRKSFDGVIRELLQK- 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  269 PKARVVACFCEGMTVRGLLMAMRRLGLAgeFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPET 348
Cdd:cd06375    236 PNARVVVLFTRSDDARELLAAAKRLNAS--FTWVASDGWGAQESIVKGSEDVAEGAITLELASHPIPDFDRYFQSLTPYN 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  349 NHRNPWFQEFWQHRFQCRLegfpQENSKYNKTCNSSLTL-KTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCD 427
Cdd:cd06375    314 NHRNPWFRDFWEQKFQCSL----QNKSQAASVSDKHLSIdSSNYEQESKIMFVVNAVYAMAHALHNMQRTLCPNTTRLCD 389
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  428 AMKPIDGRKLL-ESLMKTNFTGV-----SGDTILFDENGDSPGRYEIMNFKEM-GKDYFDYINVGSWDNG 490
Cdd:cd06375    390 AMRSLDGKKLYkDYLLNVSFTAPfppadAGSEVKFDAFGDGLGRYNIFNYQRAgGSYGYRYKGVGKWANS 459
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
36-329 1.21e-134

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: 411.70  E-value: 1.21e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   36 IIGALFSVHHQPTVdkvhERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRD 115
Cdd:cd04509      1 KVGVLFAVHGKGPS----GVPCGDIVAQYGIQRFEAMEQALDDINADPNLLPNNTLGIVIYDDCCDPKQALEQSNKFVND 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  116 SLISSEEEeglVRCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSD 195
Cdd:cd04509     77 LIQKDTSD---VRCTNGEPPVFVKPEGIKGVIGHLCSSVTIPVSNILELFGIPQITYAATAPELSDDRGYQLFLRVVPLD 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  196 AQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHLPkARVVA 275
Cdd:cd04509    154 SDQAPAMADIVKEKVWQYVSIVHDEGQYGEGGARAFQDGLKKGGLCIAFSDGITAGEKTKDFDRLVARLKKENN-IRFVV 232
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1856631258  276 CFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKL 329
Cdd:cd04509    233 YFGYHPEMGQILRAARRAGLVGKFQFMGSDGWANVSLSLNIAEESAEGLITIKP 286
7tmC_mGluR1 cd15449
metabotropic glutamate receptor 1 in group 1, member of the class C family of ...
578-827 2.10e-128

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: 392.84  E-value: 2.10e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15449      1 IESIIAVAFSCLGILVTMFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTN 737
Cdd:cd15449     81 CYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVVIASILISVQLTLVVTLIIMEPPMPILSYPSIKEVYLICNTSN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  738 LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCM 817
Cdd:cd15449    161 LGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCM 240
                          250
                   ....*....|
gi 1856631258  818 FVPKVYIILA 827
Cdd:cd15449    241 FTPKMYIIIA 250
7tmC_mGluRs_group2_3 cd15934
metabotropic glutamate receptors in group 2 and 3, member of the class C family of ...
581-826 8.26e-119

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: 367.71  E-value: 8.26e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15934      4 IVPVVFALLGILATLFVIVVFIRYNDTPVVKASGRELSYVLLTGILLCYLMTFVLLAKPSVITCALRRLGLGLGFSICYA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILAGSKKKicTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGV 740
Cdd:cd15934     84 ALLTKTNRISRIFNSGKRS--AKRPRFISPKSQLVICLGLISVQLIGVLVWLVVEPPGTRIDYPRRDQVVLKCKISDSSL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  741 VTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFG--SNYKI--ITMCFSVSLSATVALGC 816
Cdd:cd15934    162 LISLVYNMLLIILCTVYAFKTRKIPENFNEAKFIGFTMYTTCIIWLAFVPIYFGtsNDFKIqtTTLCVSISLSASVALGC 241
                          250
                   ....*....|
gi 1856631258  817 MFVPKVYIIL 826
Cdd:cd15934    242 LFAPKVYIIL 251
7tmC_mGluRs cd15045
metabotropic glutamate receptors, member of the class C family of seven-transmembrane G ...
578-826 1.52e-118

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: 366.96  E-value: 1.52e-118
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15045      1 PWAIGAMAFASLGILLTLFVLVVFVRYRDTPVVKASGRELSYVLLAGILLSYVMTFVLVAKPSTIVCGLQRFGLGLCFTV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKIctKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYP-SIREVYLICNTT 736
Cdd:cd15045     81 CYAAILTKTNRIARIFRLGKKSA--KRPRFISPRSQLVITGLLVSVQVLVLAVWLILSPPRATHHYPtRDKNVLVCSSAL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  737 NLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGS----NYKIITMCFSVSLSATV 812
Cdd:cd15045    159 DASYLIGLAYPILLIILCTVYAFKTRKIPEGFNEAKYIGFTMYTTCIIWLAFVPLYFTTasniEVRITTLSVSISLSATV 238
                          250
                   ....*....|....
gi 1856631258  813 ALGCMFVPKVYIIL 826
Cdd:cd15045    239 QLACLFAPKVYIIL 252
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
36-496 1.65e-113

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: 357.38  E-value: 1.65e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   36 IIGALFSVHHQPTVDKvherKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRD 115
Cdd:cd06350      1 IIGGLFPVHYRDDADF----CCCGILNPRGVQLVEAMIYAIEEINNDSSLLPNVTLGYDIRDTCSSSSVALESSLEFLLD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  116 SLISseeeeglvrCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSD 195
Cdd:cd06350     77 NGIK---------LLANSNGQNIGPPNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSDKIRYPYFLRTVPSD 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  196 AQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHlPKARVVA 275
Cdd:cd06350    148 TLQAKAIADLLKHFNWNYVSTVYSDDDYGRSGIEAFEREAKERGICIAQTIVIPENSTEDEIKRIIDKLKSS-PNAKVVV 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  276 CFCEGMTVRGLLMAMRRLGLAGeFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLklrpetnhrnpwf 355
Cdd:cd06350    227 LFLTESDARELLKEAKRRNLTG-FTWIGSDGWGDSLVILEGYEDVLGGAIGVVPRSKEIPGFDDYLK------------- 292
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  356 qefwqhrfqcrlegfpqenskynktcnssltlkthhvqdSKMGFVINAIYSmayglhnmqmslcpgyaglcdamkpidgr 435
Cdd:cd06350    293 ---------------------------------------SYAPYVIDAVYA----------------------------- 304
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1856631258  436 klleslmktnftgvsgdTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGE--LKMDD 496
Cdd:cd06350    305 -----------------TVKFDENGDGNGGYDIVNLQRTGTGNYEYVEVGTWDSNSggLSLNS 350
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
67-472 4.90e-91

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: 296.60  E-value: 4.90e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   67 QRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIrdslisseeeeglvrcvdgssssfrsKKPIVGV 146
Cdd:pfam01094    1 LVLLAVRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLL--------------------------KGEVVAI 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  147 IGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGES 226
Cdd:pfam01094   55 IGPSCSSVASAVASLANEWKVPLISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGES 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  227 GMEAFKDMSAKEGICIAHSYKIYSNA-GEQSFDKLLKKLTShlpKARVVACFCEGMTVRGLLMAMRRLGLAGE-FLLLGS 304
Cdd:pfam01094  135 GLQALEDALRERGIRVAYKAVIPPAQdDDEIARKLLKEVKS---RARVIVVCCSSETARRLLKAARELGMMGEgYVWIAT 211
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  305 DGWADRYDVTDGYQREAVGGI-TIKLQSPDVKWFDDYYLKlrpetnhrnpwfqefwqhrfqcrlegfpqenskyNKTCNS 383
Cdd:pfam01094  212 DGLTTSLVILNPSTLEAAGGVlGFRLHPPDSPEFSEFFWE----------------------------------KLSDEK 257
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  384 SLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAglCDAMKPID-GRKLLESLMKTNFTGVSGDtILFDENGDS 462
Cdd:pfam01094  258 ELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRA--CGALGPWNgGQKLLRYLKNVNFTGLTGN-VQFDENGDR 334
                          410
                   ....*....|.
gi 1856631258  463 P-GRYEIMNFK 472
Cdd:pfam01094  335 InPDYDILNLN 345
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
36-422 1.26e-87

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: 286.62  E-value: 1.26e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   36 IIGALFSVHHqptvdkvherkcgavREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRD 115
Cdd:cd06269      1 TIGALLPVHD---------------YLESGAKVLPAFELALSDVNSRPDLLPKTTLGLAIRDSECNPTQALLSACDLLAA 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  116 slisseeeeglvrcvdgssssfrskKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSD 195
Cdd:cd06269     66 -------------------------AKVVAILGPGCSASAAPVANLARHWDIPVLSYGATAPGLSDKSRYAYFLRTVPPD 120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  196 AQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAgEQSFDKLLKKLTSHLpkARVVA 275
Cdd:cd06269    121 SKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEELFQEKGGLITSRQSFDENK-DDDLTKLLRNLRDTE--ARVII 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  276 CFCEGMTVRGLLMAMRRLGLAG-EFLLLGSDGWADRYDVTDGYQREAVGG-ITIKLQSPDVKWFDDYYLKLRpetnhrnp 353
Cdd:cd06269    198 LLASPDTARSLMLEAKRLDMTSkDYVWFVIDGEASSSDEHGDEARQAAEGaITVTLIFPVVKEFLKFSMELK-------- 269
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1856631258  354 wfqefwqhrfQCRLEGFPQENSKYnktcnssltlkthhVQDSKMGFVINAIYSMAYG---LHNMQMSLCPGY 422
Cdd:cd06269    270 ----------LKSSKRKQGLNEEY--------------ELNNFAAFFYDAVLADRPGqfsIINLQYTEAGDY 317
7tm_classC_mGluR-like cd13953
metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled ...
581-826 7.56e-87

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: 281.43  E-value: 7.56e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd13953      4 IVLLVLAALGLLLTIFIWVVFIRYRNTPVVKASNRELSYLLLFGILLCFLLAFLFLLPPSDVLCGLRRFLFGLSFTLVFS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILagSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPD-IMHDYPSIREVYLICNTTNLG 739
Cdd:cd13953     84 TLLVKTNRIYRIF--KSGLRSSLRPKLLSNKSQLLLVLFLLLVQVAILIVWLILDPPKvEKVIDSDNKVVELCCSTGNIG 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  740 VVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGS--NYKIITMCFSVSLSATVALGCM 817
Cdd:cd13953    162 LILSLVYNILLLLICTYLAFKTRKLPDNFNEARYIGFSSLLSLVIWIAFIPTYFTTsgPYRDAILSFGLLLNATVLLLCL 241

                   ....*....
gi 1856631258  818 FVPKVYIIL 826
Cdd:cd13953    242 FLPKIYIIL 250
7tmC_mGluR2 cd15447
metabotropic glutamate receptor 2 in group 2, member of the class C family of ...
581-826 4.34e-85

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: 276.81  E-value: 4.34e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15447      4 IGPVTISCLGILSTLFVVGVFVKNNETPVVKASGRELCYILLLGVLLCYLMTFIFIAKPSTAVCTLRRLGLGTSFAVCYS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILAGSKKKIctKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIRE--VYLICNTTNL 738
Cdd:cd15447     84 ALLTKTNRIARIFSGAKDGA--QRPRFISPASQVAICLALISCQLLVVLIWLLVEAPGTRKETAPERRyvVTLKCNSRDS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  739 GVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYF--GSNYKI--ITMCFSVSLSATVAL 814
Cdd:cd15447    162 SMLISLTYNVLLIILCTLYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYvtSSDYRVqtTTMCISVSLSGSVVL 241
                          250
                   ....*....|..
gi 1856631258  815 GCMFVPKVYIIL 826
Cdd:cd15447    242 GCLFAPKLHIIL 253
7tmC_mGluR_group3 cd15286
metabotropic glutamate receptors in group 3, member of the class C family of ...
578-833 1.53e-83

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: 273.22  E-value: 1.53e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15286      1 PWAAVPVALAVLGIIATLFVLVTFVRYNDTPIVRASGRELSYVLLTGIFLCYAITFLMVAEPGVGVCSLRRLFLGLGMSL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTkkPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDY-------PSIREVY 730
Cdd:cd15286     81 SYAALLTKTNRIYRIFEQGKKSVTP--PRFISPTSQLVITFSLISVQLLGVLAWFAVDPPHALIDYeegrtpdPEQARGV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  731 LICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGS-------NYKIITMC 803
Cdd:cd15286    159 LRCDMSDLSLICCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTCIVWLAFIPIFFGTaqsaeklYIQTATLT 238
                          250       260       270
                   ....*....|....*....|....*....|
gi 1856631258  804 FSVSLSATVALGCMFVPKVYIILAKPERNV 833
Cdd:cd15286    239 VSMSLSASVSLGMLYMPKVYVILFHPEQNV 268
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
36-500 1.39e-82

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: 277.99  E-value: 1.39e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   36 IIGALFSVHH------QPTVDKVHERKCgavrEQY---GIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVAL 106
Cdd:cd06364      1 IIGGLFPIHFrpvspdPDFTTEPHSPEC----EGFnfrGFRWAQTMIFAIEEINNSPDLLPNITLGYRIYDSCATISKAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  107 EQSIefirdSLISSEEEEGLV-RCvdgssssfRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLF 185
Cdd:cd06364     77 RAAL-----ALVNGQEETNLDeRC--------SGGPPVAAVIGESGSTLSIAVARTLGLFYIPQVSYFASCACLSDKKQF 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  186 KYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHS---YKIYSNAGEQSFDKLLK 262
Cdd:cd06364    144 PSFLRTIPSDYYQSRALAQLVKHFGWTWVGAIASDDDYGRNGIKAFLEEAEKLGICIAFSetiPRTYSQEKILRIVEVIK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  263 KLTshlpkARVVACFCEGMTVRGLLMAMRRLGLAGeFLLLGSDGWA--------DRYDVTDGyqreAVGgitIKLQSPDV 334
Cdd:cd06364    224 KST-----AKVIVVFSSEGDLEPLIKELVRQNITG-RQWIASEAWItssllatpEYFPVLGG----TIG---FAIRRGEI 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  335 KWFDDYYLKLRPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYN--KTCNSSLTLKTHH--VQD-SKMGF---VINAIYS 406
Cdd:cd06364    291 PGLKEFLLRVHPSKSPSNPFVKEFWEETFNCSLSSSSKSNSSSSsrPPCTGSENLENVQnpYTDvSQLRIsynVYKAVYA 370
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  407 MAYGLHNMQMslC-----PGYAGLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDY 481
Cdd:cd06364    371 IAHALHDLLQ--CepgkgPFSNGSCADIKKVEPWQLLYYLKHVNFTTKFGEEVYFDENGDPVASYDIINWQLSDDGTIQF 448
                          490       500
                   ....*....|....*....|....*
gi 1856631258  482 INVGSWD----NG-ELKMDDDEV-W 500
Cdd:cd06364    449 VTVGYYDasapSGeELVINESKIlW 473
7tmC_mGluR_group2 cd15284
metabotropic glutamate receptors in group 2, member of the class C family of ...
581-826 1.93e-82

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: 269.41  E-value: 1.93e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15284      4 IGPVTIACLGFLCTLFVIGVFIKHNNTPLVKASGRELCYILLFGVFLCYCMTFIFIAKPSPAICTLRRLGLGTSFAVCYS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILAGSKKKIctKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHD-YPSIRE-VYLICNTTNL 738
Cdd:cd15284     84 ALLTKTNRIARIFSGVKDGA--QRPRFISPSSQVFICLALISVQLLVVSVWLLVEAPGTRRYtLPEKREtVILKCNVRDS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  739 GVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYF--GSNYKI--ITMCFSVSLSATVAL 814
Cdd:cd15284    162 SMLISLTYDVVLVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYvtSSDYRVqtTTMCISVSLSGFVVL 241
                          250
                   ....*....|..
gi 1856631258  815 GCMFVPKVYIIL 826
Cdd:cd15284    242 GCLFAPKVHIIL 253
7tmC_mGluR4 cd15452
metabotropic glutamate receptor 4 in group 3, member of the class C family of ...
578-833 1.45e-79

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: 264.54  E-value: 1.45e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15452      1 PWAVVPLLLAVLGIIATLFVVVTFVRYNDTPIVKASGRELSYVLLTGIFLCYATTFLMIAEPDLGTCSLRRIFLGLGMSI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKIctKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDY-------PSIREVY 730
Cdd:cd15452     81 SYAALLTKTNRIYRIFEQGKRSV--SAPRFISPASQLVITFSLISLQLLGVCVWFLVDPSHSVVDYedqrtpdPQFARGV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  731 LICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSN-------YKIITMC 803
Cdd:cd15452    159 LKCDISDLSLICLLGYSMLLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIIWLAFIPIFFGTSqsaekmyIQTTTLT 238
                          250       260       270
                   ....*....|....*....|....*....|
gi 1856631258  804 FSVSLSATVALGCMFVPKVYIILAKPERNV 833
Cdd:cd15452    239 ISVSLSASVSLGMLYMPKVYVILFHPEQNV 268
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
36-357 8.90e-78

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 257.58  E-value: 8.90e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   36 IIGALFSVHHQptvdkvherkcgaVREQYGIQRVEAMLHTLERINsdptllpnitLGCEIRDSCWHSAVALEQSIEFIRD 115
Cdd:cd01391      1 IIGVVTSSLHQ-------------IREQFGIQRVEAIFHTADKLG----------ASVEIRDSCWHGSVALEQSIEFIRD 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  116 slisseeeeglvrcvdgssssfrskkPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSD 195
Cdd:cd01391     58 --------------------------NIAGVIGPGSSSVAIVIQNLAQLFDIPQLALDATSQDLSDKTLYKYFLSVVFSD 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  196 AQQARAMVDIVKRYNWTYVSAVHTE-GNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHlPKARVV 274
Cdd:cd01391    112 TLGARLGLDIVKRKNWTYVAAIHGEgLNSGELRMAGFKELAKQEGICIVASDKADWNAGEKGFDRALRKLREG-LKARVI 190
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  275 ACFCEgMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVtdGYQREAVGGITIKLQsPDVKWFDDYYLKLRPETN-HRNP 353
Cdd:cd01391    191 VCAND-MTARGVLSAMRRLGLVGDVSVIGSDGWADRDEV--GYEVEANGLTTIKQQ-KMGFGITAIKAMADGSQNmHEEV 266

                   ....
gi 1856631258  354 WFQE 357
Cdd:cd01391    267 WFDE 270
7tm_3 pfam00003
7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane ...
573-821 2.05e-76

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: 252.58  E-value: 2.05e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  573 LRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIyCYLQRIGIG 652
Cdd:pfam00003    1 LDLSAPWGIVLEALAALGILLTLVLLVVFLLHRKTPIVKASNRSLSFLLLLGLLLLFLLAFLFIGKPTVT-CALRRFLFG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  653 LSPAMSYSALVTKTNRIARILAGSKKkictkkprFMSACAQLVIAFILICIQLgIIVALFIMEPPDIMHDYPSIREVYLI 732
Cdd:pfam00003   80 VGFTLCFSCLLAKTFRLVLIFRRRKP--------GPRGWQLLLLALGLLLVQV-IILTEWLIDPPFPEKDNLSEGKIILE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  733 C----NTTNLGVVtpLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYK------IITM 802
Cdd:pfam00003  151 CegstSIAFLDFV--LAYVGLLLLAGFLLAFKTRKLPDNFNEAKFITFSMLLSVLIWVAFIPMYLYGNKGkgtwdpVALA 228
                          250
                   ....*....|....*....
gi 1856631258  803 CFSVSLSATVALGCMFVPK 821
Cdd:pfam00003  229 IFAILASGWVLLGLYFIPK 247
7tmC_mGluR3 cd15448
metabotropic glutamate receptor 3 in group 2, member of the class C family of ...
581-826 1.53e-75

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: 250.25  E-value: 1.53e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15448      4 IGPVTIACLGFICTCMVITVFIKHNNTPLVKASGRELCYILLFGVFLSYCMTFFFIAKPSPVICTLRRLGLGTSFAVCYS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILAGSKKKicTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDI-MHDYPSIRE-VYLICNTTNL 738
Cdd:cd15448     84 ALLTKTNCIARIFDGVKNG--AQRPKFISPSSQVFICLSLILVQIVVVSVWLILEAPGTrRYTLPEKREtVILKCNVKDS 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  739 GVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYF--GSNYKI--ITMCFSVSLSATVAL 814
Cdd:cd15448    162 SMLISLTYDVVLVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYvtSSDYRVqtTTMCISVSLSGFVVL 241
                          250
                   ....*....|..
gi 1856631258  815 GCMFVPKVYIIL 826
Cdd:cd15448    242 GCLFAPKVHIIL 253
7tmC_mGluR6 cd15453
metabotropic glutamate receptor 6 in group 3, member of the class C family of ...
578-834 9.17e-75

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: 248.79  E-value: 9.17e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15453      1 PWAAPPLLLAVLGILATTTVVITFVRFNNTPIVRASGRELSYVLLTGIFLIYAITFLMVAEPGAAVCAFRRLFLGLGTTL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKIctKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREV-------Y 730
Cdd:cd15453     81 SYSALLTKTNRIYRIFEQGKRSV--TPPPFISPTSQLVITFSLTSLQVVGVIAWLGAQPPHSVIDYEEQRTVdpeqargV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  731 LICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFG---SNYKI----ITMC 803
Cdd:cd15453    159 LKCDMSDLSLIGCLGYSLLLMVTCTVYAIKARGVPETFNEAKPIGFTMYTTCIIWLAFVPIFFGtaqSAEKIyiqtTTLT 238
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1856631258  804 FSVSLSATVALGCMFVPKVYIILAKPERNVR 834
Cdd:cd15453    239 VSLSLSASVSLGMLYVPKTYVILFHPEQNVQ 269
7tmC_mGluR8 cd15454
metabotropic glutamate receptor 8 in group 3, member of the class C family of ...
578-834 1.51e-73

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: 246.85  E-value: 1.51e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15454      1 PWAVVPVFVAILGIIATTFVIVTFVRYNDTPIVRASGRELSYVLLTGIFLCYAITFLMIATPDTGICSFRRVFLGLGMCF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTkkPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREV-------Y 730
Cdd:cd15454     81 SYAALLTKTNRIHRIFEQGKKSVTA--PKFISPASQLVITFSLISVQLLGVFVWFAVDPPHTIVDYGEQRTLdpekargV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  731 LICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSN-------YKIITMC 803
Cdd:cd15454    159 LKCDISDLSLICSLGYSILLMVTCTVYAIKTRGVPETFNEAKPIGFTMYTTCIIWLAFIPIFFGTAqsaermyIQTTTLT 238
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1856631258  804 FSVSLSATVALGCMFVPKVYIILAKPERNVR 834
Cdd:cd15454    239 ISMSLSASVSLGMLYMPKVYIIIFHPEQNVQ 269
7tmC_mGluR7 cd15451
metabotropic glutamate receptor 7 in group 3, member of the class C family of ...
578-834 1.08e-71

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: 241.47  E-value: 1.08e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15451      1 PWAVIPVFLAMLGIIATIFVMATFIRYNDTPIVRASGRELSYVLLTGIFLCYIITFLMIAKPDVAVCSFRRIFLGLGMCI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTkkPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDY-------PSIREVY 730
Cdd:cd15451     81 SYAALLTKTNRIYRIFEQGKKSVTA--PRLISPTSQLAITSSLISVQLLGVLIWFAVDPPNIIIDYdeqktmnPEQARGV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  731 LICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSN-------YKIITMC 803
Cdd:cd15451    159 LKCDITDLQIICSLGYSILLMVTCTVYAIKTRGVPENFNEAKPIGFTMYTTCIVWLAFIPIFFGTAqsaeklyIQTTTLT 238
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1856631258  804 FSVSLSATVALGCMFVPKVYIILAKPERNVR 834
Cdd:cd15451    239 ISMNLSASVALGMLYMPKVYIIIFHPELNVQ 269
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
36-497 4.05e-63

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: 222.52  E-value: 4.05e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   36 IIGALFSVHHQPTVDKV------HERKCGAVREQYgIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQS 109
Cdd:cd06365      1 IIGGVFPIHTFSEGKKKdfkeppSPLLCFRFSIKY-YQHLLAFLFAIEEINKNPDLLPNITLGFHIYDSCSSERLALESS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  110 iefirdSLISSEEEEGLV--RCVDGSsssfrskkPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKY 187
Cdd:cd06365     80 ------LSILSGNSEPIPnySCREQR--------KLVAFIGDLSSSTSVAMARILGLYKYPQISYGAFDPLLSDKVQFPS 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  188 FMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSH 267
Cdd:cd06365    146 FYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDDDYGEQFSQDLKKEMEKNGICVAFVEKIPTNSSLKRIIKYINQIIKS 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  268 LpkARVVACFCEGMTVRGLLMAMRRLGLAGEfLLLGSDGWadryDVTDGYQREAV----GGITIKLQSPDVKWFDDYYLK 343
Cdd:cd06365    226 S--ANVIIIYGDTDSLLELLFRLWEQLVTGK-VWITTSQW----DISTLPFEFYLnlfnGTLGFSQHSGEIPGFKEFLQS 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  344 LRPETNHRNPWFQEFWQHRFQCRlegFPQENSKYNKTC---NSSLTLKTHHVQDSKMGF---VINAIYSMAYGLHNMQMS 417
Cdd:cd06365    299 VHPSKYPEDIFLKTLWESYFNCK---WPDQNCKSLQNCcgnESLETLDVHSFDMTMSRLsynVYNAVYAVAHALHEMLLC 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  418 LCPGYAGLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWD-----NGEL 492
Cdd:cd06365    376 QPKTGPGNCSDRRNFQPWQLHHYLKKVQFTNPAGDEVNFDEKGDLPTKYDILNWQIFPNGTGTKVKVGTFDpsapsGQQL 455

                   ....*
gi 1856631258  493 KMDDD 497
Cdd:cd06365    456 IINDS 460
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
30-471 1.28e-54

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: 196.76  E-value: 1.28e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   30 HMPGDIIIGALFSVH-------HQPTvdKVHERKCGAVREqYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCwHS 102
Cdd:cd06363      2 RLPGDYLLGGLFPLHeltstlpHRPP--EPTDCSCDRFNL-HGYHLAQAMRFAVEEINNSSDLLPGVTLGYEIFDTC-SD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  103 AVALEQSIEFIrdSLISSEEEEGLVRCVDGSSSsfrskkpIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDK 182
Cdd:cd06363     78 AVNFRPTLSFL--SQNGSHDIEVQCNYTNYQPR-------VVAVIGPDSSELALTTAKLLGFFLMPQISYGASSEELSNK 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  183 TLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSN-AGEQSFDKLL 261
Cdd:cd06363    149 LLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAANTGICVAYQGLIPTDtDPKPKYQDIL 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  262 KKLTSHlpKARVVACFCEGMTVRGLLMAMRRLGLAGEfLLLGSDGWADRYDVT--DGYQR-EAVGGITIKLQSpdVKWFD 338
Cdd:cd06363    229 KKINQT--KVNVVVVFAPKQAAKAFFEEVIRQNLTGK-VWIASEAWSLNDTVTslPGIQSiGTVLGFAIQTGT--LPGFQ 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  339 DYylklrpetnhrnpwfqefwqhrfqcrlegfpQENSKYNktcnssltlkthhvqdskmgfVINAIYSMAYGLHNMqmsL 418
Cdd:cd06363    304 EF-------------------------------IYAFAFS---------------------VYAAVYAVAHALHNL---L 328
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1856631258  419 -CPgyAGLCDAMKPIDGRKLLESLMKTNFTgVSGDTILFDENGDSPGRYEIMNF 471
Cdd:cd06363    329 gCN--SGACPKGRVVYPWQLLEELKKVNFT-LLNQTIRFDENGDPNFGYDIVQW 379
7tmC_V2R_AA_sensing_receptor-like cd15044
vomeronasal type-2 pheromone receptors, amino acid-sensing receptors and closely related ...
581-826 1.18e-46

vomeronasal type-2 pheromone receptors, amino acid-sensing receptors and closely related proteins; member of the class C family of seven-transmembrane G protein-coupled receptors; This group is composed of vomeronasal type-2 pheromone receptors (V2Rs), a subgroup of broad-spectrum amino-acid sensing receptors including calcium-sensing receptor (CaSR) and GPRC6A, as well as their closely related proteins. 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 co-expressed 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 co-expressed 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. CaSR is a widely expressed GPCR that is involved in sensing small changes in extracellular levels of calcium ion to maintain a constant level of the extracellular calcium via modulating the synthesis and secretion of calcium regulating hormones, such as parathyroid hormone (PTH), in order to regulate Ca(2+)transport into or out of the extracellular fluid via kidney, intestine, and/or bone. For instance, when Ca2+ is high, CaSR downregulates PTH synthesis and secretion, leading to an increase in renal Ca2+ excretion, a decrease in intestinal Ca2+ absorption, and a reduction in release of skeletal Ca2+. GRPC6A (GPCR, class C, group 6, subtype A) is a widely expressed amino acid-sensing GPCR that is most closely related to CaSR. GPRC6A is most potently activated by the basic amino acids L-arginine, L-lysine, and L-ornithine and less potently by small aliphatic amino acids. Moreover, the receptor can be either activated or modulated by divalent cations such as Ca2+. GPRC6A is expressed in the testis, but not the ovary and specifically also binds to the osteoblast-derived hormone osteocalcin (OCN), which regulates testosterone production by the testis and male fertility independently of the hypothalamic-pituitary axis. Furthermore, GPRC6A knockout studies suggest that GRPC6A is involved in regulation of bone metabolism, male reproduction, energy homeostasis, glucose metabolism, and in activation of inflammation response, as well as prostate cancer growth and progression, among others.


Pssm-ID: 320172 [Multi-domain]  Cd Length: 251  Bit Score: 168.03  E-value: 1.18e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15044      4 ILLVILSILGIIFVLVVGGVFVRYRNTPIVKANNRELSYLILLSLFLCFSSSLFFIGEPQDWTCKLRQTMFGVSFTLCIS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILAGSKKKIctkkpRFMSACAQLVIAFILIC--IQLGIIVALFIMEPPDIMHDYPSI-REVYLICNT-T 736
Cdd:cd15044     84 CILTKTLKVLLAFSADKPLT-----QKFLMCLYLPILIVFTCtgIQVVICTVWLIFAPPTVEVNVSPLpRVIILECNEgS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  737 NLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGS--NYKIITMCFSVSLSATVAL 814
Cdd:cd15044    159 ILAFGTMLGYIAFLAFLCFLFAFKARKLPDNYNEAKFITFGMLVFFIVWISFVPAYLSTkgKFVVAVEIIAILASSYGLL 238
                          250
                   ....*....|..
gi 1856631258  815 GCMFVPKVYIIL 826
Cdd:cd15044    239 GCIFLPKCYVIL 250
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
36-488 3.16e-46

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: 171.79  E-value: 3.16e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   36 IIGALFSVHHQptVDKVHER-------KCGAVrEQYGIQRVEAMLHTLERINSDPtLLPNITLGCEIRDSCWHSAVALEQ 108
Cdd:cd06361      1 IIGGLFPIHEK--VLDLHDRptkpqifICTGF-DLRGFLQSLAMIHAIEMINNST-LLPGIKLGYEIYDTCSDVTKALQA 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  109 SIEFIR--DSLisseeeEGLVRCvdgSSSSFRskKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFK 186
Cdd:cd06361     77 TLRLLSkfNSS------NELLEC---DYTDYV--PPVKAVIGASYSEISIAVARLLNLQLIPQISYESSAPILSDKLRFP 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  187 YFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTS 266
Cdd:cd06361    146 SFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDDDYGRSALESFIIQAEAENVCIAFKEVLPAYLSDPTMNVRINDTIQ 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  267 HL---PKARVVACFCEGMTVRGLLMAMRRLGLAGefLLLGSDGWADRYDVTDGYQREAVGGIT-IKLQSPDVKWFDDyYL 342
Cdd:cd06361    226 TIqssSQVNVVVLFLKPSLVKKLFKEVIERNISK--IWIASDNWSTAREILKMPNINKVGKILgFTFKSGNISSFHN-YL 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  343 KlrpetnhrnpwfqefwqhrfqcrlegfpqenskynktcnsslTLKTHHVQdskmgfviNAIYSMAYGLHNMqmsLCPgy 422
Cdd:cd06361    303 K------------------------------------------NLLIYSIQ--------LAVTAIANALRKL---CCE-- 327
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1856631258  423 AGLCD--AMKPidgRKLLESLMKTNFTgVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYInVGSWD 488
Cdd:cd06361    328 RGCQDptAFQP---WELLKELKKVTFT-DDGETYHFDANGDLNTGYDLILWKEDNGHMTFTI-VAEYD 390
7tmC_V2R_pheromone cd15283
vomeronasal type-2 pheromone receptors, member of the class C family of seven-transmembrane G ...
581-826 3.22e-43

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: 158.21  E-value: 3.22e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15283      4 IALTVLSLLGSVLTAAVLVVFIKHRDTPIVKANNSELSYLLLLSLKLCFLCSLLFIGQPSTWTCMLRQTAFGISFVLCIS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTnrIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIRE-VYLICNT-TNL 738
Cdd:cd15283     84 CILAKT--IVVVAAFKATRPGSNIMKWFGPGQQRAIIFICTLVQVVICAIWLATSPPFPDKNMHSEHGkIILECNEgSVV 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  739 GVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGS--NYKIITMCFSVSLSATVALGC 816
Cdd:cd15283    162 AFYCVLGYIGLLALVSFLLAFLARKLPDNFNEAKFITFSMLVFCAVWVAFVPAYISSpgKYMVAVEIFAILASSAGLLGC 241
                          250
                   ....*....|
gi 1856631258  817 MFVPKVYIIL 826
Cdd:cd15283    242 IFAPKCYIIL 251
7tmC_V2R-like cd15280
vomeronasal type-2 receptor-like proteins, member of the class C family of seven-transmembrane ...
581-829 3.88e-40

vomeronasal type-2 receptor-like proteins, member of the class C family of seven-transmembrane G protein-coupled receptors; This group represents vomeronasal type-2 receptor-like proteins that are closely related to the V2R family of vomeronasal GPCRs. 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 co-expressed in the apical neurons of the VNO. Activation of V1R or V2R causes activation of phospholipase pathway, generating the secondary messengers diacylglycerol (DAG) and IP3. However, in contrast to V1Rs, V2Rs contain the long N-terminal extracellular domain, which is believed to bind pheromones. Human V2R1-like protein, also known as putative calcium-sensing receptor-like 1 (CASRL1), is not included here because it is a nonfunctional pseudogene.


Pssm-ID: 320407 [Multi-domain]  Cd Length: 253  Bit Score: 149.16  E-value: 3.88e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15280      4 ITLIALSIFGALVVLAVTVVYIMHRHTPLVKANDRELSFLIQMSLVITFLTSILFIGKPENWSCMARQITLALGFSLCLS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRI--ARILAGSKKKICTKKPRFmsacaQLVIAFILICIQLGIIVALFIMEPPDiMHDYPSIREVYLI--CNTT 736
Cdd:cd15280     84 SILGKTISLflRYRASKSETRLDSMHPIY-----QKIIVLICVLIEVGICTAYLILEPPR-MYKNTEVQNVKIIfeCNEG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  737 NLGVVTPL-GYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGS--NYKIITMCFSVSLSATVA 813
Cdd:cd15280    158 SIEFLCSIfGFDVFLALLCFLTAFVARKLPDNFNEGKFITFGMLVFFIVWISFVPAYLSTrgKFKVAVEIFAILASSFGL 237
                          250
                   ....*....|....*.
gi 1856631258  814 LGCMFVPKVYIILAKP 829
Cdd:cd15280    238 LGCIFVPKCYIILLKP 253
7tmC_CaSR cd15282
calcium-sensing receptor, member of the class C of seven-transmembrane G protein-coupled ...
578-826 9.94e-38

calcium-sensing receptor, member of the class C of seven-transmembrane G protein-coupled receptors; CaSR is a widely expressed GPCR that is involved in sensing small changes in extracellular levels of calcium ion to maintain a constant level of the extracellular calcium via modulating the synthesis and secretion of calcium regulating hormones, such as parathyroid hormone (PTH), in order to regulate Ca(2+)transport into or out of the extracellular fluid via kidney, intestine, and/or bone. For instance, when Ca2+ is high, CaSR downregulates PTH synthesis and secretion, leading to an increase in renal Ca2+ excretion, a decrease in intestinal Ca2+ absorption, and a reduction in release of skeletal Ca2+. CaSR is coupled to both G(q/11)-dependent activation of phospholipase and, subsequently, intracellular calcium mobilization and protein kinase C activation as well as G(i/o)-dependent inhibition of adenylate cyclase leading to inhibition of cAMP formation. CaSR is closely related to GRPC6A (GPCR, class C, group 6, subtype A), which is an amino acid-sensing GPCR that is most potently activated by the basic amino acids L-arginine, L-lysine, and L-ornithine. These receptors contain a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD), and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TASR1 receptors.


Pssm-ID: 320409 [Multi-domain]  Cd Length: 252  Bit Score: 142.40  E-value: 9.94e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15282      1 PFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLICCFSSSLIFIGEPQDWTCRLRQPAFGISFVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILagsKKKICTKKPR-FMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIRE-VYLICNT 735
Cdd:cd15282     81 CISCILVKTNRVLLVF---EAKIPTSLHRkWWGLNLQFLLVFLCTFVQIVICVIWLYTAPPSSYRNHELEDEiIFITCNE 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  736 TNLGVVTPL-GYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATV-- 812
Cdd:cd15282    158 GSLMALGFLiGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILASSfg 237
                          250
                   ....*....|....
gi 1856631258  813 ALGCMFVPKVYIIL 826
Cdd:cd15282    238 LLACIFFNKVYIIL 251
7tmC_GABA-B-like cd15047
gamma-aminobutyric acid type B receptor and related proteins, member of the class C family of ...
581-825 4.17e-35

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: 135.00  E-value: 4.17e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLI---AKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15047      4 IVFTVLSGIGILLALVFLIFNIKFRKNRVIKMSSPLFNNLILLGCILCYISVILFGlddSKPSSFLCTARPWLLSIGFTL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSKKKICTKKPRFMsacaqLVIAFILICIQLGIIVALFIMEPPDIMHDYPS--------IREV 729
Cdd:cd15047     84 VFGALFAKTWRIYRIFTNKKLKRIVIKDKQL-----LKIVGILLLIDIIILILWTIVDPLKPTRVLVLseisddvkYEYV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  730 YLICNTTN----LGVVtpLGYNGLLILSCTFYAFKTRNVP-ANFNEAKYIAFTMYTTCIIWLAFVPIYFGS----NYKII 800
Cdd:cd15047    159 VHCCSSSNgiiwLGIL--LAYKGLLLLFGCFLAWKTRNVDiEEFNESKYIGISIYNVLFLSVIGVPLSFVLtdspDTSYL 236
                          250       260
                   ....*....|....*....|....*
gi 1856631258  801 TMCFSVSLSATVALGCMFVPKVYII 825
Cdd:cd15047    237 IISAAILFCTTATLCLLFVPKFWLL 261
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
71-507 3.10e-33

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: 133.52  E-value: 3.10e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   71 AMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRdslisseeeeglvrcvdgssssfrSKKPIVGVIGPG 150
Cdd:cd06366     23 AAEMALEHINNRSDILPGYNLELIWNDTQCDPGLGLKALYDLLY------------------------TPPPKVMLLGPG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  151 SSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEA 230
Cdd:cd06366     79 CSSVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAED 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  231 FKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKK------LTSHLPKARVVacFCEgmtvrgllmaMRRLGLAGE---FLL 301
Cdd:cd06366    159 LEELLEEANITIVATESFSSEDPTDQLENLKEKdariiiGLFYEDAARKV--FCE----------AYKLGMYGPkyvWIL 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  302 LG--SDGWADRYDVTDG---YQ-REAVGG-ITIKLqspdVKWFDDYYLKLRPETNhrnpwfQEFWQhRFQCRLEGFPQEN 374
Cdd:cd06366    227 PGwyDDNWWDVPDNDVNctpEQmLEALEGhFSTEL----LPLNPDNTKTISGLTA------QEFLK-EYLERLSNSNYTG 295
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  375 SKYNktcnssltlkthhvqdskmGFVINAIYSMAYGLHNMQMSLCPGYAGLCDA--MKPIDGRKLLESLMKTNFTGVSGd 452
Cdd:cd06366    296 SPYA-------------------PFAYDAVWAIALALNKTIEKLAEYNKTLEDFtyNDKEMADLFLEAMNSTSFEGVSG- 355
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1856631258  453 TILFDENGDSPGRYEIMNFKEmGKdyfdYINVGSWDNgelkMDDDEVWSKKSNII 507
Cdd:cd06366    356 PVSFDSKGDRLGTVDIEQLQG-GS----YVKVGLYDP----NADSLLLLNESSIV 401
7tmC_GPRC6A cd15281
class C of seven-transmembrane G protein-coupled receptors, subtype 6A; GRPC6A (GPCR, class C, ...
581-826 3.49e-28

class C of seven-transmembrane G protein-coupled receptors, subtype 6A; GRPC6A (GPCR, class C, group 6, subtype A) is a widely expressed amino acid-sensing GPCR that is most closely related to CaSR. GPRC6A is most potently activated by the basic amino acids L-arginine, L-lysine, and L-ornithine and less potently by small aliphatic amino acids. Moreover, the receptor can be either activated or modulated by divalent cations such as Ca2+ and Mg2+. GPRC6A is expressed in the testis, but not the ovary and specifically also binds to the osteoblast-derived hormone osteocalcin (OCN), which regulates testosterone production by the testis and male fertility independently of the hypothalamic-pituitary axis. Furthermore, GPRC6A knockout studies suggest that GRPC6A is involved in regulation of bone metabolism, male reproduction, energy homeostasis, glucose metabolism, and in activation of inflammation response, as well as prostate cancer growth and progression, among others. GPRC6A has been suggested to couple to the Gq subtype of G proteins, leading to IP3 production and intracellular calcium mobilization. GPRC6A contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD), and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320408  Cd Length: 249  Bit Score: 114.49  E-value: 3.49e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15281      4 IVLLILSALGVLLIFFISALFTKNLNTPVVKAGGGPLCYVILLSHFGSFISTVFFIGEPSDLTCKTRQTLFGISFTLCVS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIarILAGS----KKKI--CTKKPrfmsacaqLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICN 734
Cdd:cd15281     84 CILVKSLKI--LLAFSfdpkLQELlkCLYKP--------IMIVFICTGIQVIICTVWLVFYKPFVDKNFSLPESIILECN 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  735 T-TNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIY---FGSNYKIITMCFsVSLSA 810
Cdd:cd15281    154 EgSYVAFGLMLGYIALLAFICFIFAFKGRKLPENYNEAKFITFGMLIYFIAWITFIPIYattFGKYVPAVEMIV-ILISN 232
                          250
                   ....*....|....*.
gi 1856631258  811 TVALGCMFVPKVYIIL 826
Cdd:cd15281    233 YGILSCTFLPKCYIIL 248
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
76-484 5.85e-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: 117.46  E-value: 5.85e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   76 LERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRdslisseeeeglvrcvdgssssfrsKKPIVGVIGPGSSSVA 155
Cdd:cd06352     28 IERINSEGLLLPGFNFEFTYRDSCCDESEAVGAAADLIY-------------------------KRNVDVFIGPACSAAA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  156 IQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAV-HTEGNYGESGMEAFKDM 234
Cdd:cd06352     83 DAVGRLATYWNIPIITWGAVSASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIySDDDSKCFSIANDLEDA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  235 SAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHlpkARVVACFCEGMTVRGLLMAMRRLGLA-GEFLLLGSD-------- 305
Cdd:cd06352    163 LNQEDNLTISYYEFVEVNSDSDYSSILQEAKKR---ARIIVLCFDSETVRQFMLAAHDLGMTnGEYVFIFIElfkdgfgg 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  306 GWADRYDVTDGYQREAVGG----ITIKLQSPD---VKWF-DDYYLKLRpetnhRNPWFqefwqhrfqCRLEGFpQENSKY 377
Cdd:cd06352    240 NSTDGWERNDGRDEDAKQAyeslLVISLSRPSnpeYDNFsKEVKARAK-----EPPFY---------CYDASE-EEVSPY 304
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  378 nktcnsSLTLktHhvqdskmgfviNAIYsmAYGlHNMQMSLCPGYAglcdamkPIDGRKLLESLMKTNFTGVSGDTIlFD 457
Cdd:cd06352    305 ------AAAL--Y-----------DAVY--LYA-LALNETLAEGGN-------YRNGTAIAQRMWNRTFQGITGPVT-ID 354
                          410       420
                   ....*....|....*....|....*..
gi 1856631258  458 ENGDspgRYEIMNFKEMGKDYFDYINV 484
Cdd:cd06352    355 SNGD---RDPDYALLDLDPSTGKFVVV 378
7tmC_TAS1R1 cd15289
type 1 taste receptor subtype 1, member of the class C of seven-transmembrane G ...
578-826 2.99e-24

type 1 taste receptor subtype 1, member of the class C of seven-transmembrane G protein-coupled receptors; This group represents TAS1R1, which is a member of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320416  Cd Length: 253  Bit Score: 103.27  E-value: 2.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15289      1 PVSWALLTALTLLLLLLAGTALLFALNLTTPVVKSAGGRTCFLMLGSLAAASCSLYCHFGEPTWLACLLKQPLFSLSFTV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILagskkKICTKKPRFMSACAQL--VIAFILIC--IQLGIIVALFIMEPPDIMHDYPSIRE-VYLI 732
Cdd:cd15289     81 CLSCIAVRSFQIVCIF-----KLASKLPRFYETWAKNhgPELFILISsaVQLLISLLWLVLNPPVPTKDYDRYPDlIVLE 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  733 C-NTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSAT 811
Cdd:cd15289    156 CsQTLSVGSFLELLYNCLLSISCFVFSYMGKDLPANYNEAKCITFSLLIYFISWISFFTTYSIYRGKYLMAINVLAILSS 235
                          250
                   ....*....|....*..
gi 1856631258  812 VA--LGCMFVPKVYIIL 826
Cdd:cd15289    236 LLgiFGGYFLPKVYIIL 252
7tmC_TAS1R cd15046
type 1 taste receptors, member of the class C of seven-transmembrane G protein-coupled ...
578-826 5.74e-24

type 1 taste receptors, member of the class C of seven-transmembrane G protein-coupled receptors; This subfamily represents the type I taste receptors (TAS1Rs) that belongs to the class C family of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320174 [Multi-domain]  Cd Length: 253  Bit Score: 102.60  E-value: 5.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAM 657
Cdd:cd15046      1 APTVAVLLLAALGLLSTLAILVIFWRNFNTPVVRSAGGPMCFLMLTLLLVAYMSVPVYFGPPKVSTCLLRQALFPLCFTV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILagskkKICTKKPR----FMSACAQLVIAFILICIQLGIIVALFIMEPP----DIMHDYPSIreV 729
Cdd:cd15046     81 CLACIAVRSFQIVCIF-----KMASRFPRaysyWVKYHGPYVSIAFITVLKMVIVVIGMLATPPspttDTDPDPKIT--I 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  730 YLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITmcfSVSLS 809
Cdd:cd15046    154 VSCNPNYRNSSLFNTSLDLLLSVVCFSFSYMGKDLPTNYNEAKFITFSLTFYFTSWISFCTFMLAYSGVLVT---IVDLL 230
                          250       260
                   ....*....|....*....|..
gi 1856631258  810 ATVA-----LGCMFVPKVYIIL 826
Cdd:cd15046    231 ATLLsllafSLGYFLPKCYIIL 252
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
71-491 6.00e-24

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: 105.79  E-value: 6.00e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   71 AMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIrdslisseeeeglvrcvdgssssfrsKKPIVGVIGPG 150
Cdd:cd06370     25 AITLAVDDVNNDPNLLPGHTLSFVWNDTRCDELLSIRAMTELW--------------------------KRGVSAFIGPG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  151 SS------SVAIqvqnllqlFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYG 224
Cdd:cd06370     79 CTcatearLAAA--------FNLPMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKW 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  225 ESGMEAFKDMSAKEGICIAH-----SYKIYSNAGEQSFDKLLKKLtshLPKARVVACFCEGMTVRGLLMAMRRLGL--AG 297
Cdd:cd06370    151 SKIADTIKELLELNNIEINHeeyfpDPYPYTTSHGNPFDKIVEET---KEKTRIYVFLGDYSLLREFMYYAEDLGLldNG 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  298 EFLLLGSDgwADRYDV-TDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNhRNPWFQEFWQhRFQCRLEGFPQeNSK 376
Cdd:cd06370    228 DYVVIGVE--LDQYDVdDPAKYPNFLSGDYTKNDTKEALEAFRSVLIVTPSPP-TNPEYEKFTK-KVKEYNKLPPF-NFP 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  377 YNKTCNSSLTLKTH--HVQDSKMgfvinaIYSMAygLHNMQMSlcpGYaglcdamKPIDGRKLLESLMKTNFTGVSGDTI 454
Cdd:cd06370    303 NPEGIEKTKEVPIYaaYLYDAVM------LYARA--LNETLAE---GG-------DPRDGTAIISKIRNRTYESIQGFDV 364
                          410       420       430
                   ....*....|....*....|....*....|....*..
gi 1856631258  455 LFDENGDSPGRYEIMNFKEMGKDyfdyiNVGSWDNGE 491
Cdd:cd06370    365 YIDENGDAEGNYTLLALKPNKGT-----NDGSYGLHP 396
7tm_GPCRs cd14964
seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary ...
583-821 3.01e-23

seven-transmembrane G protein-coupled receptor superfamily; This hierarchical evolutionary model represents the seven-transmembrane (7TM) receptors, often referred to as G protein-coupled receptors (GPCRs), which transmit physiological signals from the outside of the cell to the inside via G proteins. GPCRs constitute the largest known superfamily of transmembrane receptors across the three kingdoms of life that respond to a wide variety of extracellular stimuli including peptides, lipids, neurotransmitters, amino acids, hormones, and sensory stimuli such as light, smell and taste. All GPCRs share a common structural architecture comprising of seven-transmembrane (TM) alpha-helices interconnected by three extracellular and three intracellular loops. A general feature of GPCR signaling is agonist-induced conformational changes in the receptors, leading to activation of the heterotrimeric G proteins, which consist of the guanine nucleotide-binding G-alpha subunit and the dimeric G-beta-gamma subunits. The activated G proteins then bind to and activate numerous downstream effector proteins, which generate second messengers that mediate a broad range of cellular and physiological processes. However, some 7TM receptors, such as the type 1 microbial rhodopsins, do not activate G proteins. Based on sequence similarity, GPCRs can be divided into six major classes: class A (the rhodopsin-like family), class B (the Methuselah-like, adhesion and secretin-like receptor family), class C (the metabotropic glutamate receptor family), class D (the fungal mating pheromone receptors), class E (the cAMP receptor family), and class F (the frizzled/smoothened receptor family). Nearly 800 human GPCR genes have been identified and are involved essentially in all major physiological processes. Approximately 40% of clinically marketed drugs mediate their effects through modulation of GPCR function for the treatment of a variety of human diseases including bacterial infections.


Pssm-ID: 410628 [Multi-domain]  Cd Length: 267  Bit Score: 100.58  E-value: 3.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  583 AVVFACLGLLATLFVTVVFIIYRDTPvvkSSSRELCYIILAGICLGYLCTFCLIAKPKQIY--------CYLQRIGIGLS 654
Cdd:cd14964      5 LSLLTCLGLLGNLLVLLSLVRLRKRP---RSTRLLLASLAACDLLASLVVLVLFFLLGLTEassrpqalCYLIYLLWYGA 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  655 PAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSacaqLVIAFILICIqlGIIVALFIMEPPDIMHDYPSIREVYLICN 734
Cdd:cd14964     82 NLASIWTTLVLTYHRYFALCGPLKYTRLSSPGKTR----VIILGCWGVS--LLLSIPPLVGKGAIPRYNTLTGSCYLICT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  735 TTNLGVVTPLGYNGLLILSCTFYAFK----------------TRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYF----- 793
Cdd:cd14964    156 TIYLTWGFLLVSFLLPLVAFLVIFSRivlrlrrrvrairsaaSLNTDKNLKATKSLLILVITFLLCWLPFSIVFIlhalv 235
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1856631258  794 ----GSNYKIITMCFSVSLSATVALGCMFVPK 821
Cdd:cd14964    236 aagqGLNLLSILANLLAVLASTLNPFIYCLGN 267
GluR_Homer-bdg pfam10606
Homer-binding domain of metabotropic glutamate receptor; This is the proline-rich region of ...
1130-1180 2.83e-22

Homer-binding domain of metabotropic glutamate receptor; This is the proline-rich region of metabotropic glutamate receptor proteins that binds Homer-related synaptic proteins. The Homer proteins form a physical tether linking mGluRs with the inositol trisphosphate receptors (IP3R) that appears to be due to the proline-rich "Homer ligand" (PPXXFr). Activation of PI turnover triggers intracellular calcium release. MGluR function is altered in the mouse model of human Fragile X syndrome mental retardation, a disorder caused by loss of function mutations in the Fragile X mental retardation gene Fmr1. Homer 3 (and to a lesser extent Homer 1b/c) has been shown to form a multimeric complex with mGlu1a and the IP3 receptor, indicating that Homers may play a role in the localization of receptors to their signalling partners.


Pssm-ID: 431390  Cd Length: 51  Bit Score: 90.99  E-value: 2.83e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1856631258 1130 ALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL 1180
Cdd:pfam10606    1 ALTPPSPFRDSVCSGSSSPGSPVSESMLCSPPSPTYTSLILRDYSQSSSTL 51
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
143-311 5.39e-20

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: 92.30  E-value: 5.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:COG0683     72 VDAIVGPLSSGVALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDDY 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIAhsYKIYSNAGEQSFDKLLKKLTSHlpKARVVACFCEGMTVRGLLMAMRRLGLAGEFll 301
Cdd:COG0683    152 AYGQGLAAAFKAALKAAGGEVV--GEEYYPPGTTDFSAQLTKIKAA--GPDAVFLAGYGGDAALFIKQAREAGLKGPL-- 225
                          170
                   ....*....|
gi 1856631258  302 lgSDGWADRY 311
Cdd:COG0683    226 --NKAFVKAY 233
7tmC_TAS1R3 cd15290
type 1 taste receptor subtype 3, member of the class C of seven-transmembrane G ...
578-826 1.96e-19

type 1 taste receptor subtype 3, member of the class C of seven-transmembrane G protein-coupled receptors; This group represents TAS1R3, which is a member of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320417 [Multi-domain]  Cd Length: 253  Bit Score: 89.35  E-value: 1.96e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  578 PEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCyiILAGICLGYLC-TFCL-IAKPKQIYCYLQRIGIGLSP 655
Cdd:cd15290      1 PESLGLLLLGVLLLVLQCSVGVLFLKHRGTPLVQASGGPLS--IFALLSLMGAClSLLLfLGQPSDVVCRLQQPLNALFL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  656 AMSYSALVTKTNRIARI----LAGSKKKICTKKPRfmsacAQLViafILIC--IQLGiIVALFIMEPPDIMHDYPSIR-- 727
Cdd:cd15290     79 TVCLSTILSISLQIFLVtefpKCAASHLHWLRGPG-----SWLV---VLICclVQAG-LCGWYVQDGPSLSEYDAKMTlf 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  728 -EVYLICNTTN-LGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYK---IITM 802
Cdd:cd15290    150 vEVFLRCPVEPwLGFGLMHGFNGALALISFMCTFMAQKPLKQYNLARDITFSTLIYCVTWVIFIPIYAGLQVKlrsIAQV 229
                          250       260
                   ....*....|....*....|....
gi 1856631258  803 CFSVsLSATVALGCMFVPKVYIIL 826
Cdd:cd15290    230 GFIL-LSNLGLLAAYYLPKCYLLL 252
NCD3G pfam07562
Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several ...
508-558 2.15e-19

Nine Cysteines Domain of family 3 GPCR; This conserved sequence contains several highly-conserved Cys residues that are predicted to form disulphide bridges. It is predicted to lie outside the cell membrane, tethered to the pfam00003 in several receptor proteins.


Pssm-ID: 462210  Cd Length: 53  Bit Score: 82.69  E-value: 2.15e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1856631258  508 RSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYV-FDEYTCKACQLGSWP 558
Cdd:pfam07562    2 SSVCSESCPPGQRKSQQGGAPVCCWDCVPCPEGEISnTDSDTCKKCPEGQWP 53
PBP1_ABC_ligand_binding-like cd06346
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-343 5.35e-18

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: 86.46  E-value: 5.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGN 222
Cdd:cd06346     68 VPAIVGAASSGVTLAVASVAVPNGVVQISPSSTSPALTTLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVNND 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  223 YGESGMEAFKDMSAKEGICIAHSykIYSNAGEQSFDKLLKKLTSHLPKARVVACFCEgmTVRGLLMAMRRLGLAGeFLLL 302
Cdd:cd06346    148 YGQGLADAFKKAFEALGGTVTAS--VPYEPGQTSYRAELAQAAAGGPDALVLIGYPE--DGATILREALELGLDF-TPWI 222
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1856631258  303 GSDGWA--DRYDVTDGYQREAVGGITIK-LQSPDVKWFDDYYLK 343
Cdd:cd06346    223 GTDGLKsdDLVEAAGAEALEGMLGTAPGsPGSPAYEAFAAAYKA 266
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
143-344 1.38e-17

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: 84.69  E-value: 1.38e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKtLFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd06268     68 VLAVVGHYSSSVTLAAAPIYQEAGIPLISPGSTAPELTEG-GGPYVFRTVPSDAMQAAALADyLAKKLKGKKVAILYDDY 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIahsykiysnAGEQSFDKLLKKLTSHLPKAR-----VVACFCEGMTVRGLLMAMRRLGLa 296
Cdd:cd06268    147 DYGKSLADAFKKALKALGGEI---------VAEEDFPLGTTDFSAQLTKIKaagpdVLFLAGYGADAANALKQARELGL- 216
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1856631258  297 gEFLLLGSDGWAdrYDVTDGYQREAVGGITI------KLQSPDVKWFDDYYLKL 344
Cdd:cd06268    217 -KLPILGGDGLY--SPELLKLGGEAAEGVVVavpwhpDSPDPPKQAFVKAYKKK 267
7tmC_TAS1R2 cd15288
type 1 taste receptor subtype 2, member of the class C of seven-transmembrane G ...
581-826 1.05e-16

type 1 taste receptor subtype 2, member of the class C of seven-transmembrane G protein-coupled receptors; This group represents TAS1R2, which is a member of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320415  Cd Length: 254  Bit Score: 81.37  E-value: 1.05e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15288      4 IVVALLAALGFLSTLAILVIFGRHFQTPVVRSAGGRMCFLMLAPLLVAYVNVPVYVGIPTVFTCLCRQTLFPLCFTVCIS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILagskkKICTKKPR----FMSACAQLVIAFILICIQLGIIVALFIMEPPDIM----HDYPSIreVYLI 732
Cdd:cd15288     84 CIAVRSFQIVCIF-----KMARRLPRaysyWVKYNGPYVFVALITLLKVVIVVINVLAHPTAPTtradPDDPQV--MILQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  733 CN-TTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTM---YTTCIIWLAFVPIYFGSNYKIITMCFSVSL 808
Cdd:cd15288    157 CNpNYRLALLFNTSLDLLLSVLGFCFAYMGKELPTNYNEAKFITLCMtfyFASSVFLCTFMSVYEGVLVTIFDALVTVIN 236
                          250
                   ....*....|....*...
gi 1856631258  809 SATVALGcMFVPKVYIIL 826
Cdd:cd15288    237 LLGISLG-YFGPKCYMIL 253
7tmC_GPR158-like cd15293
orphan GPR158 and similar proteins, member of the class C family of seven-transmembrane G ...
581-826 1.16e-16

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: 81.11  E-value: 1.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQR----IGIglspA 656
Cdd:cd15293      4 IAVLAVQAICILLCLVLALVVFRFRKVKVIKAASPILLELILFGALLLYFPVFILYFEPSVFRCILRPwfrhLGF----A 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  657 MSYSALVTKTNRIARILaGSKKkicTKKPRfMSACAQLVIAFILICIQLGIIVALFIMEPP--DIMHDYPSIREVYLICN 734
Cdd:cd15293     80 IVYGALILKTYRILVVF-RSRS---ARRVH-LTDRDLLKRLGLIVLVVLGYLAAWTAVNPPnvEVGLTLTSSGLKFNVCS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  735 TTNLGVVTPLGYngLLILSCT-FYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYF------GSNYKIITMCFSVS 807
Cdd:cd15293    155 LDWWDYVMAIAE--LLFLLWGvYLCYAVRKAPSAFNESRYISLAIYNELLLSVIFNIIRFfllpslHPDLLFLLFFLHTQ 232
                          250
                   ....*....|....*....
gi 1856631258  808 LSATVALGCMFVPKVYIIL 826
Cdd:cd15293    233 LTVTVTLLLIFGPKFYLVL 251
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
140-490 1.66e-16

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: 82.66  E-value: 1.66e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  140 KKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHT 219
Cdd:cd19990     62 NKKVEAIIGPQTSEEASFVAELGNKAQVPIISFSATSPTLSSLR-WPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYE 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  220 EGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHlpKARV-VACFCEGMTVRGLLMAmRRLGL-AG 297
Cdd:cd19990    141 DDDYGSGIIPYLSDALQEVGSRIEYRVALPPSSPEDSIEEELIKLKSM--QSRVfVVHMSSLLASRLFQEA-KKLGMmEK 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  298 EFLLLGSDGWADRYDVTDGYQREAVGG-ITIKLQSPDVKWFDDYYLKlrpetnhrnpwfqefWQHRFqcrlegfpqeNSK 376
Cdd:cd19990    218 GYVWIVTDGITNLLDSLDSSTISSMQGvIGIKTYIPESSEFQDFKAR---------------FRKKF----------RSE 272
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  377 YNKTCNSSLTLkthhvqdskmgFVINA---IYSMAYGLHNMQMSlCPGYAglcdamKPIDGRKLLESLMKTNFTGVSGDt 453
Cdd:cd19990    273 YPEEENAEPNI-----------YALRAydaIWALAHAVEKLNSS-GGNIS------VSDSGKKLLEEILSTKFKGLSGE- 333
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1856631258  454 ILFDENGDSPG-RYEIMNFKEMGkdyfdYINVGSWDNG 490
Cdd:cd19990    334 VQFVDGQLAPPpAFEIVNVIGKG-----YRELGFWSPG 366
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
143-461 1.79e-16

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: 82.19  E-value: 1.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd06342     67 VVAVIGHYNSGAAIAAAPIYAEAGIPMISPSATNPKLTEQG-YKNFFRVVGTDDQQGPAAADyAAKTLKAKRVAVIHDGT 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIAHSYKIysNAGEQSFDKLLKKLTSHlpKARVVacFCEGMTVRGLLMA--MRRLGLAGef 299
Cdd:cd06342    146 AYGKGLADAFKKALKALGGTVVGREGI--TPGTTDFSALLTKIKAA--NPDAV--YFGGYYPEAGLLLrqLREAGLKA-- 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  300 LLLGSDGWADRYDVTDGyqREAVGGITIKLQSPDVKwfddyylklrpetnhRNPWFQEFwqhrfqcrlegfpqeNSKYNK 379
Cdd:cd06342    218 PFMGGDGIVSPDFIKAA--GDAAEGVYATTPGAPPE---------------KLPAAKAF---------------LKAYKA 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  380 TcnssltlkthhvqdskmGFVINAIYSMayglhnmqmslcPGYAG---LCDAMK---PIDGRKLLESLMKTNFTGVSGdT 453
Cdd:cd06342    266 K-----------------FGEPPGAYAA------------YAYDAaqvLLAAIEkagSTDRAAVAAALRATDFDGVTG-T 315

                   ....*...
gi 1856631258  454 ILFDENGD 461
Cdd:cd06342    316 ISFDAKGD 323
7tmC_TAS1R2a-like cd15287
type 1 taste receptor subtype 2a and similar proteins, member of the class C of ...
581-826 4.48e-15

type 1 taste receptor subtype 2a and similar proteins, member of the class C of seven-transmembrane G protein-coupled receptors; This group includes TAS1R2a and its similar proteins found in fish. They are members of the type I taste receptor (TAS1R) family that belongs to the class C of G protein-coupled receptors. The functional TAS1Rs are obligatory heterodimers built from three known members, TAS1R1-3. TAS1R1 combines with TAS1R3 to form an umami taste receptor, which is responsible for the perception of savory taste, such as the food additive mono-sodium glutamate (MSG); whereas the combination of TAS1R2-TAS1R3 forms a sweet-taste receptor for sugars and D-amino acids. On the other hand, the type II taste receptors (TAS2Rs), which belong to the class A family of GPCRs, recognize bitter tasting compounds. In the case of sweet, for example, the TAS1R2-TAS1R3 heterodimer activates phospholipase C (PLC) via alpha-gustducin, a heterodimeric G protein that is involved in perception of sweet and bitter tastes. This activation leads to generation of inositol (1, 4, 5)-trisphosphate (IP3) and diacylglycerol (DAG), and consequently increases intracellular Ca2+ mobilization and activates a cation channel, TRPM5. In contrast to the TAS1R2-TAS1R3 heterodimer, TAS1R3 alone could activate adenylate cyclase leading to cAMP formation in the absence of alpha-gustducin. Each TAS1R contains a large extracellular Venus flytrap-like domain in the N-terminus, cysteine-rich domain (CRD) and seven-transmembrane (7TM) domain, which are characteristics of the class C GPCRs. The Venus flytrap-like domain shares strong sequence homology to bacterial periplasmic binding proteins and possess the orthosteric amino acid and calcium binding sites for members of the class C, including CaSR, GABA-B1, GPRC6A, mGlu, and TAS1R receptors.


Pssm-ID: 320414  Cd Length: 252  Bit Score: 76.26  E-value: 4.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYS 660
Cdd:cd15287      4 ILIMVGACVLVGLTLAVSVLFAINYNTPVVRSAGGPMCFLILGCLSLCSVSVFFYFGKPTVASCILRYFPFLLFYTVCLA 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  661 ALVTKTNRIARILagskkKICTKKPRFMSACAQ-----LVIAFILIcIQLGIIVALFIMEPPDIMHD---YPsiREVYLI 732
Cdd:cd15287     84 CFVVRSFQIVCIF-----KIAAKFPKLHSWWVKyhgqwLLIAVAFV-IQALLLITGFSFSPPKPYNDtswYP--DKIILS 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  733 CN----TTNLGVVTPLGYNGLlilsCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIY--FGSNYKIITMCFSV 806
Cdd:cd15287    156 CDinlkATSMSLVLLLSLCCL----CFIFSYMGKDLPKNYNEAKAITFCLLLLILTWIIFATEYmlYRGKYIQLLNALAV 231
                          250       260
                   ....*....|....*....|
gi 1856631258  807 SLSATVALGCMFVPKVYIIL 826
Cdd:cd15287    232 LSSLYSFLLWYFLPKCYIII 251
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-461 7.34e-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: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 74.12  E-value: 7.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlfKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd06347     68 VVAIIGPVTSSIALAAAPIAQKAKIPMITPSATNPLVTKGG--DYIFRACFTDPFQGAALAKfAYEELGAKKAAVLYDVS 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 N-YGESGMEAFKDMSAKEGICIAhsYKIYSNAGEQSFDKLLKKLTSHlpKARVVacFCEGMTVR-GLLM-AMRRLGLAGE 298
Cdd:cd06347    146 SdYSKGLAKAFKEAFEKLGGEIV--AEETYTSGDTDFSAQLTKIKAA--NPDVI--FLPGYYEEaALIIkQARELGITAP 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  299 FllLGSDGWadrydvtDGYQREAVGGitiklqspdvKWFDDYYLklrpeTNH-----RNPWFQEFWQhRFQcrlegfpqe 373
Cdd:cd06347    220 I--LGGDGW-------DSPELLELGG----------DAVEGVYF-----TTHfspddPSPEVQEFVK-AYK--------- 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  374 nSKYNKTcnssltlkthhvqdskmgfvINAIYSMAYGLHNMqmslcpgyagLCDAMK---PIDGRKLLESLMKT-NFTGV 449
Cdd:cd06347    266 -AKYGEP--------------------PNAFAALGYDAVML----------LADAIKragSTDPEAIRDALAKTkDFEGV 314
                          330
                   ....*....|..
gi 1856631258  450 SGdTILFDENGD 461
Cdd:cd06347    315 TG-TITFDPNGN 325
PBP1_ABC_HAAT-like cd06344
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-307 1.92e-12

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: 69.95  E-value: 1.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGN 222
Cdd:cd06344     66 VVAVIGHRSSYVAIPASIIYERAGLLMLSPGATAPKLTQHG-FKYIFRNIPSDEDIARQLARYAARQGYKRIVIYYDDDS 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  223 YGESGMEAFKDMSAKEGICIAHSYKIYSNagEQSFDKLLKKLTSHlpkarvvaCFCEGMTVRGLLMA-------MRRLGL 295
Cdd:cd06344    145 YGKGLANAFEEEARELGITIVDRRSYSSD--EEDFRRLLSKWKAL--------DFFDAIFLAGSMPEgaefikqARELGI 214
                          170
                   ....*....|..
gi 1856631258  296 agEFLLLGSDGW 307
Cdd:cd06344    215 --KVPIIGGDGL 224
7tmC_GABA-B-R1 cd15291
gamma-aminobutyric acid type B receptor subunit 1, member of the class C family of ...
581-822 3.43e-12

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: 68.13  E-value: 3.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  581 IAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQI-------YCYLQR--IGI 651
Cdd:cd15291      4 ISMCLLASLGIFAAVFLLIFNIYNRHRRYIQLSQPHCNNVMLVGCILCLASVFLLGLDGRHVsrshfplVCQARLwlLCL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  652 GLSpaMSYSALVTKTNRIARILAGSKKKICTKKPrfMSACAQLVIAFILICIQLGIIVALFIMEP------------PDI 719
Cdd:cd15291     84 GFT--LAYGSMFTKVWRVHRLTTKKKEKKETRKT--LEPWKLYAVVGILLVVDVIILAIWQIVDPlhrtieefpleePKD 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  720 MHDYPSIREVYLICNTTN----LGVVtpLGYNGLLILSCTFYAFKTRNVPANF-NEAKYIAFTMYTTCIIWLAFVPI--Y 792
Cdd:cd15291    160 TDEDVKILPQLEHCSSKKqntwLGIV--YGYKGLLLLFGLFLAYETRNVKVEKiNDSRFVGMSIYNVVVLCLITAPVtmI 237
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1856631258  793 FGS----NYKIITMcfSVSLSATVALGCMFVPKV 822
Cdd:cd15291    238 ISSqqdaSFAFVSL--AILFSSYITLVLIFVPKI 269
PBP1_ABC_ligand_binding-like cd06335
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
139-295 9.96e-12

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: 68.02  E-value: 9.96e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  139 SKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTL--FKYFMRVVPSDAQQARAMVDIVKRYNWTYVSA 216
Cdd:cd06335     64 DKEKVVAIIGPTNSGVALATIPILQEAKIPLIIPVATGTAITKPPAkpRNYIFRVAASDTLQADFLVDYAVKKGFKKIAI 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  217 VHTEGNYGESGMEAFKDMSAKEGICIAHSYKIysNAGEQSfdkllkkLTSHLPKAR-----VVACFCEGMTVRGLLMAMR 291
Cdd:cd06335    144 LHDTTGYGQGGLKDVEAALKKRGITPVATESF--KIGDTD-------MTPQLLKAKdagadVILVYGLGPDLAQILKAME 214

                   ....
gi 1856631258  292 RLGL 295
Cdd:cd06335    215 KLGW 218
PBP1_ABC_ligand_binding-like cd19984
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
135-309 3.07e-11

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: 65.70  E-value: 3.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  135 SSFRSKKPIVGV---IGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDktLFKYFMRVVPSDAQQARAMVDIVKRYNW 211
Cdd:cd19984     57 SAANKLINVDKVkaiIGGVCSSETLAIAPIAEQNKVVLISPGASSPEITK--AGDYIFRNYPSDAYQGKVLAEFAYNKLY 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  212 TYVSAVHTEGNYGESGMEAFKDMSAKEG--ICIAHSYKIysnaGEQSFDKLLKKLTSHLPKARVVAcfceGMTVRGLLMA 289
Cdd:cd19984    135 KKVAILYENNDYGVGLKDVFKKEFEELGgkIVASESFEQ----GETDFRTQLTKIKAANPDAIFLP----GYPKEGGLIL 206
                          170       180
                   ....*....|....*....|..
gi 1856631258  290 --MRRLGLAGEFllLGSDGWAD 309
Cdd:cd19984    207 kqAKELGIKAPI--LGSDGFED 226
PBP1_ABC_HAAT-like cd19986
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
139-341 7.71e-10

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: 380641 [Multi-domain]  Cd Length: 297  Bit Score: 61.49  E-value: 7.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  139 SKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIaYSATSMDLSDKTLfKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAV 217
Cdd:cd19986     64 SDDKVVAVIGPHYSTQVLAVSPLVKEAKIPVI-TGGTSPKLTEQGN-PYMFRIRPSDSVSAKALAKyAVEELGAKKIAIL 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  218 HTEGNYGESGMEAFKDMSAKEGIcIAHSYKIYsNAGEQSFdkllkklTSHLpkARVVACFCEGMTVRG-------LLMAM 290
Cdd:cd19986    142 YDNDDFGTGGADVVTAALKALGL-EPVAVESY-NTGDKDF-------TAQL--LKLKNSGADVIIAWGhdaeaalIARQI 210
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1856631258  291 RRLGLagEFLLLGSDGWADRYDV-TDGYQREAVGGITIKLQS---PDVKWFDDYY 341
Cdd:cd19986    211 RQLGL--DVPVIGSSSFATPTVLlLAGEALEGIYSVTDFVPSdpdPKVQAFVKKY 263
7tmC_GABA-B-R2 cd15294
gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of ...
586-822 9.65e-10

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: 60.90  E-value: 9.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  586 FACLGL-LATLFVTVVfIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCL-----IAKPK--QIYCYLQRIGIGLSPAM 657
Cdd:cd15294      9 LTIIGIiLASAFLAFN-IKFRNHRYIKMSSPYMNNLIILGCMLTYASVILLgldgsLVSEKtfETLCTARTWILCVGFTL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  658 SYSALVTKTNRIARILAGSK--KKICTKKPRFMsacaqlvIAFILICIQLGIIVALFIMEP-----------PDIMHDYP 724
Cdd:cd15294     88 AFGAMFSKTWRVHSIFTNVKlnKKAIKDYKLFI-------IVGVLLLIDICILITWQIVDPfyrtvkelepePDPAGDDI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  725 SIREVYLICNTTNLGVVTPL--GYNGLLILSCTFYAFKTRNV--PAnFNEAKYIAFTMYTTCIIWLAFVPIYF----GSN 796
Cdd:cd15294    161 LIRPELEYCESTHMTIFLGIiyAYKGLLMVFGCFLAWETRNVsiPA-LNDSKYIGMSVYNVVIMCVIGAAVSFilrdQPN 239
                          250       260
                   ....*....|....*....|....*.
gi 1856631258  797 YKIITMCFSVSLSATVALGCMFVPKV 822
Cdd:cd15294    240 VQFCIISLFIIFCTTITLCLVFVPKL 265
PBP1_ABC_RPA1789-like cd06333
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ...
143-297 1.28e-09

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: 61.41  E-value: 1.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKtlFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGN 222
Cdd:cd06333     68 VDAIIGPSTTGESLAVAPIAEEAKVPLISLAGAAAIVEPV--RKWVFKTPQSDSLVAEAILDYMKKKGIKKVALLGDSDA 145
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1856631258  223 YGESGMEAFKDMSAKEGICIA--HSYkiysNAGEQSFDKLLKKLTSHLPKARVVACFCEGMTVrgLLMAMRRLGLAG 297
Cdd:cd06333    146 YGQSGRAALKKLAPEYGIEIVadERF----ARTDTDMTAQLTKIRAAKPDAVLVWASGPPAAL--VAKNLRQLGYKG 216
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-304 1.48e-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: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 61.08  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSdKTLFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd19980     68 VPAIIGAWCSSVTLAVMPVAERAKVPLVVEISSAPKIT-EGGNPYVFRLNPTNSMLAKAFAKyLADKGKPKKVAFLAEND 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIAHSYkiYSNAGEQSFDKLLKKLTSHLPKARVVACFCEGMTvrGLLMAMRRLGLAGEFLL 301
Cdd:cd19980    147 DYGRGAAEAFKKALKAKGVKVVATE--YFDQGQTDFTTQLTKLKAANPDAIFVVAETEDGA--LILKQARELGLKQQLVG 222

                   ...
gi 1856631258  302 LGS 304
Cdd:cd19980    223 TGG 225
PBP1_ABC_HAAT-like cd19988
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-306 3.18e-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 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: 380643 [Multi-domain]  Cd Length: 302  Bit Score: 56.52  E-value: 3.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDkTLFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd19988     68 VWAIIGSINSSCTLAAIRVALKAGVPQINPGSSAPTITE-SGNPWVFRCTPDDRQQAYALVDyAFEKLKVTKIAVLYVND 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIAHSykIYSNAGEQSFDKLLKKLTSHLPKARVVAcfceGMTVRGLLMA--MRRLGLAGEf 299
Cdd:cd19988    147 DYGRGGIDAFKDAAKKYGIEVVVE--ESYNRGDKDFSPQLEKIKDSGAQAIVMW----GQYTEGALIAkqARELGLKQP- 219

                   ....*..
gi 1856631258  300 lLLGSDG 306
Cdd:cd19988    220 -LFGSDG 225
PBP1_ABC_HAAT-like cd19985
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
139-310 5.72e-08

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: 380640 [Multi-domain]  Cd Length: 321  Bit Score: 56.13  E-value: 5.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  139 SKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLsdkTLF-KYFMRVVPSDAQQARAM----VDIVKRYNwty 213
Cdd:cd19985     63 VSDKALAVIGHYYSSASIAAGKIYKKAGIPAITPSATADAV---TRDnPWYFRVIFNDSLQGRFLanyaKKVLKKDK--- 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  214 VSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGE--QSFDKLLKKLTSHLPKARVVacFCEGMTVRG--LLMA 289
Cdd:cd19985    137 VSIIYEEDSYGKSLASVFEATARALGLKVLKKWSFDTDSSQldQNLDQIVDELKKAPDEPGVI--FLATHADEGakLIKK 214
                          170       180
                   ....*....|....*....|.
gi 1856631258  290 MRRLGLagEFLLLGSDGWADR 310
Cdd:cd19985    215 LRDAGL--KAPIIGPDSLASE 233
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
164-500 6.73e-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: 56.19  E-value: 6.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  164 LFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIA 243
Cdd:cd06379     89 FYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETLAETKDIKIE 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  244 HSYKIysNAGEQSFDKLL---KKLTShlpkaRVVACFCEGMTVRGLLMAMRRLGLAGEflllgsdGWAdrYDVTD--GYQ 318
Cdd:cd06379    169 KVIEF--EPGEKNFTSLLeemKELQS-----RVILLYASEDDAEIIFRDAAMLNMTGA-------GYV--WIVTEqaLAA 232
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  319 REAVGGItiklqspdvkwfddyylklrpetnhrnpwfqefwqhrFQCRLEGFPQENSkynktcnssltlkthHVQDSkMG 398
Cdd:cd06379    233 SNVPDGV-------------------------------------LGLQLIHGKNESA---------------HIRDS-VS 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  399 FVINAIYSMAYglHNMQMSLCPGYaglCDAMKPI--DGRKLLESLMKTNFT-GVSGDtILFDENGDSPG-RYEIMNFKEM 474
Cdd:cd06379    260 VVAQAIRELFR--SSENITDPPVD---CRDDTNIwkSGQKFFRVLKSVKLSdGRTGR-VEFNDKGDRIGaEYDIINVQNP 333
                          330       340       350
                   ....*....|....*....|....*....|...
gi 1856631258  475 GKdyfdYINVGSWDNGE------LKMDDDE-VW 500
Cdd:cd06379    334 RK----LVQVGIYVGSQrptkslLSLNDRKiIW 362
PBP1_ABC_HAAT-like cd06349
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-304 1.06e-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 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: 380572 [Multi-domain]  Cd Length: 338  Bit Score: 52.19  E-value: 1.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSdkTLFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd06349     68 VVAVIGDFSSSCSMAAAPIYEEAGLVQISPTASHPDFT--KGGDYVFRNSPTQAVEAPFLADyAVKKLGAKKIAIIYLNT 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIahSYKIYSNAGEQSFDKLLKKLTShlPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLL 301
Cdd:cd06349    146 DWGVSAADAFKKAAKALGGEI--VATEAYLPGTKDFSAQITKIKN--ANPDAIYLAAYYNDAALIAKQARQLGWDVQIFG 221

                   ...
gi 1856631258  302 LGS 304
Cdd:cd06349    222 SSS 224
PBP1_NPR_A cd06385
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A ...
76-347 1.92e-06

Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A natriuretic peptide receptor (NPR-A). NPR-A is one of three known single membrane-spanning natriuretic peptide receptors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. NPR-A is highly expressed in kidney, adrenal, terminal ileum, adipose, aortic, and lung tissues. The rank order of NPR-A activation by natriuretic peptides is ANP>BNP>>CNP. Single allele-inactivating mutations in the promoter of human NPR-A are associated with hypertension and heart failure.


Pssm-ID: 380608 [Multi-domain]  Cd Length: 408  Bit Score: 51.74  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   76 LERINSDPTLLPNitlgceirdscWHsavaleqsiefIRDSLISSEEEEGLvrCVDgssssfrSKKPIVGV--------- 146
Cdd:cd06385     28 LERVNARPDLLPG-----------WH-----------VRTVLGSSENKEGV--CSD-------STAPLVAVdlkfehhpa 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  147 --IGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYG 224
Cdd:cd06385     77 vfLGPGCVYTAAPVARFTAHWRVPLLTAGAPALGFGVKDEYALTTRTGPSHKKLGEFVARLHRRYGWERRALLVYADRKG 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  225 ES-----GMEA-FKDMSAKEGICIAHsyKIYSNAGEQSFDKLLKKLTShlpKARVVACFCEGMTVRGLLMAMRRLGLAGE 298
Cdd:cd06385    157 DDrpcffAVEGlYMQLRRRLNITVDD--LVFNEDEPLNYTELLRDIRQ---KGRVIYVCCSPDTFRKLMLQAWREGLCGE 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1856631258  299 ----FLL------LGSDGWAD------RYDVTDGYQREAVGGITI-KLQSPDVKWFDDYYLKLRPE 347
Cdd:cd06385    232 dyafFYIdifgasLQSGQFPDpqrpweRGDADDNSAREAFQAVKIiTYKEPDNPEYKEFLKQLKTE 297
7tmC_Boss cd15042
Bride of sevenless, member of the class C family of seven-transmembrane G protein-coupled ...
582-826 6.35e-06

Bride of sevenless, member of the class C family of seven-transmembrane G protein-coupled receptors; Bride of Sevenless (Boss) is a putative Drosophila melanogaster G protein-coupled receptor that functions as a glucose-responding receptor to regulate energy metabolism. Boss is expressed predominantly in the fly's fat body, a nutrient-sensing tissue functionally analogous to the mammalian liver and adipose tissues, and in photoreceptor cells. Boss, which is expressed on the surface of R8 photoreceptor cell, binds and activates the Sevenless receptor tyrosine kinase on the neighboring R7 precursor cell. Activation of Sevenless results in phosphorylation of the Sevenless, triggering a signaling transduction cascade through Ras pathway that ultimately leads to the differentiation of the R7 precursor into a fully functional R7 photoreceptor, the last of eight photoreceptors to differentiate in each ommatidium of the developing Drosophila eye. In the absence of either of Sevenless or Boss, the R7 precursor fails to differentiate as a photoreceptor and instead develops into a non-neuronal cone cell. Moreover, Boss mutants in Drosophila showed elevated food intake, but reduced stored triglyceride levels, suggesting that Boss may play a role in regulating energy homeostasis in nutrient sensing tissues. Furthermore, GPRC5B, a mammalian Boss homolog, activates obesity-associated inflammatory signaling in adipocytes, and that the GPRC5B knockout mice showed resistance to high-fat diet-induced obesity and insulin resistance.


Pssm-ID: 320170  Cd Length: 238  Bit Score: 48.95  E-value: 6.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  582 AAVVFACLGLLATLfVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCT---FCL--IAKPKQIYCYLQRIGIGLSPA 656
Cdd:cd15042      5 AFLTAAILGILFCC-AILVFIVVRVTTKDVLEGNPVLTILLLLALIFTFLSflpFSMedDYFGKNSLCAVRILLTTLAFG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  657 MSYSALVTKtnriARILAGSkkkicTKKPRFMSACA---QLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLic 733
Cdd:cd15042     84 FTFSLMLSR----ALFLALS-----TGEGGFLSHVNgylQSVMCLFSFGVQVAMSVQYFVLNHANSAVIYRGLWFIAL-- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  734 nttnlgvvtpLGYNG-LLILSCTFYAFKTRnVPANFNEAKYIAFTMYTTCIIWLAFVP--IYFGSNYKIITMCFSVSLSA 810
Cdd:cd15042    153 ----------LGYDIfLLIALFVLCPFIFR-SQRNYREGKYFFGASIGLLVIWVIWLPcfLLMGPEWRDAVISFGLVATA 221
                          250
                   ....*....|....*.
gi 1856631258  811 TVALGCMFVPKVYIIL 826
Cdd:cd15042    222 YAILVGILVPRTYLMT 237
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
63-299 9.78e-06

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: 49.19  E-value: 9.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   63 QYGIQRVEAMlhtlerinsdpTLLPNITLGCEIRDSCWHSAVALEQSIEFIrdslisseeeegLVRCVDGssssfrskkp 142
Cdd:cd06373     24 ELALRRVERR-----------GFLPGWRFQVHYRDTKCSDTLAPLAAVDLY------------CAKKVDV---------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 ivgVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGN 222
Cdd:cd06373     71 ---FLGPVCEYALAPVARYAGHWNVPVLTAGGLAAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVALLYHDNL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  223 YGESG-------MEAFKDMSAKEGICIAHSYKIYSNaGEQSFDKLLKKLTSHlpkARVVACFCEGMTVRGLLMAMRRLGL 295
Cdd:cd06373    148 RRKAGnsncyftLEGIFNALTGERDSIHKSFDEFDE-TKDDFEILLKRVSNS---ARIVILCASPDTVREIMLAAHELGM 223

                   ....*
gi 1856631258  296 A-GEF 299
Cdd:cd06373    224 InGEY 228
PBP1_ABC_ligand_binding-like cd06340
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
143-240 2.50e-05

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. 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, their ligand specificity has not been determined experimentally.


Pssm-ID: 380563 [Multi-domain]  Cd Length: 352  Bit Score: 47.94  E-value: 2.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlFKYFMRVVPSDAQQARAMVDIVKRYNWTY------VSA 216
Cdd:cd06340     71 VVAIIGAYSSSVTLAASQVAERYGVPFVTASAVADEITERG-FKYVFRTAPTASQFAEDAVDFLKELAKKKgkkikkVAI 149
                           90       100
                   ....*....|....*....|....
gi 1856631258  217 VHTEGNYGESGMEAFKDMSAKEGI 240
Cdd:cd06340    150 IYEDSAFGTSVAKGLKKAAKKAGL 173
PBP1_As_SBP-like cd06330
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
146-213 1.69e-04

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: 45.24  E-value: 1.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1856631258  146 VIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTY 213
Cdd:cd06330     71 LIGTISSGVALAVAPVAEELKVLFIATDAATDRLTEENFNPYVFRTSPNTYMDAVAAALYAAKKPPDV 138
PBP1_ABC_HAAT-like cd06348
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-307 2.26e-04

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: 44.92  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlfKYFMRVVPSDAQQARAMVDIV-KRYNWTYVSAVHTEG 221
Cdd:cd06348     68 VLAILGPTLSSEAFAADPIAQQAKVPVVGISNTAPGITDIG--PYIFRNSLPEDKVIPPTVKAAkKKYGIKKVAVLYDQD 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 N-YGESGMEAFKDMSAKEGICIAHSYKiySNAGEQSFDKLLKKLTSHLPKARVV-ACFCEGmtvrGLLM-AMRRLGLAGE 298
Cdd:cd06348    146 DaFTVSGTKVFPAALKKNGVEVLDTET--FQTGDTDFSAQLTKIKALNPDAIVIsALAQEG----ALIVkQARELGLKGP 219

                   ....*....
gi 1856631258  299 FllLGSDGW 307
Cdd:cd06348    220 I--VGGNGF 226
PBP1_ABC_ligand_binding-like cd19982
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
139-336 2.28e-04

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. 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, their ligand specificity has not been determined experimentally.


Pssm-ID: 380637 [Multi-domain]  Cd Length: 302  Bit Score: 44.58  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  139 SKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSmDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRY-NWTYVSAV 217
Cdd:cd19982     64 SQDKVPLIVGGYSSGITLPVAAVAERQKIPLLVPTAAD-DDITKPGYKYVFRLNPPASIYAKALFDFFKELvKPKTIAIL 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  218 HTEGNYGESGMEAFKDMSAKEGICI--AHSYKiysnAGEQSFDKLLKKLTSHLPKarvVACFCEGMTVRGLLM-AMRRLG 294
Cdd:cd19982    143 YENTAFGTSVAKAARRFAKKRGIEVvaDESYD----KGATDFKPLLNKVKAANPD---VVYMVSYLNDAILLMrQAKELG 215
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1856631258  295 LAGEfLLLGSDGWADRYDVTD--GYQREAVggITIKLQSPDVKW 336
Cdd:cd19982    216 LNPK-LFAGGGAGFTIPEFLKqaGPLAEYV--VTATLWSPDVKY 256
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
58-212 5.29e-04

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors, non-NMDA ionotropic receptors which respond to the neurotransmitter glutamate. 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. Kainate receptors have five subunits, GluR5, GluR6, GluR7, KA1 and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined.


Pssm-ID: 380605  Cd Length: 335  Bit Score: 43.75  E-value: 5.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258   58 GAVREQYGIQRVEAMLHTLERINSDPTLlPNITLgceirdscwhsavalEQSIEFI--RDSLISSEE-----EEGlvrcv 130
Cdd:cd06382      3 GGIFDEDDEDLEIAFKYAVDRINRERTL-PNTKL---------------VPDIERVprDDSFEASKKvcellEEG----- 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  131 dgssssfrskkpIVGVIGPGSSSVAIQVQNLLQLFNIPQIaysATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYN 210
Cdd:cd06382     62 ------------VAAIFGPSSPSSSDIVQSICDALEIPHI---ETRWDPKESNRDTFTINLYPDPDALSKAYADLVKSLN 126

                   ..
gi 1856631258  211 WT 212
Cdd:cd06382    127 WK 128
PBP1_YraM_LppC_lipoprotein-like cd06339
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup ...
146-264 5.43e-04

periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup includes periplasmic binding component of lipoprotein LppC, an immunodominant antigen, whose molecular function is not characterized. Members of this subgroup are predicted to be involved in transport of lipid compounds, and they are sequence similar to the family of ABC-type hydrophobic amino acid transporters (HAAT).


Pssm-ID: 380562 [Multi-domain]  Cd Length: 331  Bit Score: 43.41  E-value: 5.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  146 VIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMrvvpSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGE 225
Cdd:cd06339     63 IIGPLLKSSVAALAAAAQALGVPVLALNNDESATAGPGLFQFGL----SPEDEARQAARYAVQQGLRRFAVLAPDNAYGQ 138
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1856631258  226 SGMEAFKDMSAKEGICIAHSYKIysNAGEQSFDKLLKKL 264
Cdd:cd06339    139 RVANAFREAWQALGGTVVAVESY--DPDETDFSAAIRRL 175
PBP1_RPA0668_benzoate-like cd20014
type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the ...
146-334 1.26e-03

type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the active transport of lignin-derived benzoate derivative compounds, and its close homologs; This group includes RPA0668 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0668 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. 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: 380667 [Multi-domain]  Cd Length: 346  Bit Score: 42.61  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  146 VIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVkrYNWTYVSAVHTEGNY-- 223
Cdd:cd20014     69 LVGPVSSGVALAIRDVVEQAKVPLIVANAGANALTRAACSPYIFRTSFSNWQLGYALGKYA--AENVGKTVVTIASDYaa 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  224 GESGMEAFKDMSAKEGICIAhsYKIYSNAGE-QSFDKLLKKLTSHLPKArVVACFCEGMTVRgLLMAMRRLGLAGEFLLL 302
Cdd:cd20014    147 GREVVAGFKEGFEAAGGKVV--GEIWTPLGTtTDFSPYLTQIAASGPDA-VYAFFAGADAVR-FVKQYAEFGLKGKIPLY 222
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1856631258  303 GSdGWadrydVTDGY----QREAV-GGITIKLQSPDV 334
Cdd:cd20014    223 GP-GF-----LTDEDvlpaLGEAAeGIITVLHYAPTL 253
PBP1_SBP-like cd19989
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
146-239 1.47e-03

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: 41.88  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  146 VIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVD-IVKRY--NWTYVSAVHTegn 222
Cdd:cd19989     71 LTGAVSSAVALAVAPKAAELKVPYLVTVAADDELTGENCNRYTFRVNTSDRMIARALAPwLAENGgkKWYIVYADYA--- 147
                           90
                   ....*....|....*..
gi 1856631258  223 YGESGMEAFKDMSAKEG 239
Cdd:cd19989    148 WGQSSAEAFKEAIEELG 164
PBP1_ABC_HAAT-like cd19983
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
143-366 1.50e-03

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: 380638 [Multi-domain]  Cd Length: 303  Bit Score: 42.19  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlfKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd19983     67 VVAIIGHMTSAMTVAVLPVINEAKVLMISPTVSTPELSGKD--DYFFRVTPTTRESAQALARyAYNRGGLRRVAVIYDLS 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 N--YGESGMEAFKDMSAKEGICIAhSYKIYSNAGEQSFDKLLKKLTSHLPKARVVACfcegmtvRGLLMAM--RRLGLAG 297
Cdd:cd19983    145 NraYSESWLDNFRSEFEALGGRIV-AEIPFSSGADVDFSDLARRLLASKPDGLLLVA-------SAVDTAMlaQQIRKLG 216
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  298 -EFLLLGSDGWADRYDVTDGYQreAVGGITIkLQSpdvkwFDDyylklrpetNHRNPWFQEFwQHRFQCR 366
Cdd:cd19983    217 sKIPLFSSAWAATEELLELGGK--AVEGMLF-SQA-----YDR---------NSSNPRYLAF-KEAYEER 268
Peripla_BP_6 pfam13458
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ...
143-310 1.61e-03

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


Pssm-ID: 433225 [Multi-domain]  Cd Length: 342  Bit Score: 42.26  E-value: 1.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSAtsmdLSDKTLFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:pfam13458   70 VDAIVGGVSSAVALAVAEVLAKKGVPVIGPAA----LTGEKCSPYVFSLGPTYSAQATALGRyLAKELGGKKVALIGADY 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  222 NYGESGMEAFKDMSAKEGICIAHSykIYSNAGEQSFDKLLKKLTSHLPKArVVACFCEGMTVrGLLMAMRRLGLAGEFLL 301
Cdd:pfam13458  146 AFGRALAAAAKAAAKAAGGEVVGE--VRYPLGTTDFSSQVLQIKASGADA-VLLANAGADTV-NLLKQAREAGLDAKGIK 221

                   ....*....
gi 1856631258  302 LGSDGWADR 310
Cdd:pfam13458  222 LVGLGGDEP 230
PBP1_ABC_ligand_binding-like cd06343
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
143-240 5.96e-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, 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: 380566 [Multi-domain]  Cd Length: 355  Bit Score: 40.24  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1856631258  143 IVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTlFKYFMRVVPSDAQQARAMVD-IVKRYNWTYVSAVHTEG 221
Cdd:cd06343     75 VFAIVGGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPP-KPYTFGVQPSYEDEGRILADyIVETLPAAKVAVLYQND 153
                           90
                   ....*....|....*....
gi 1856631258  222 NYGESGMEAFKDMSAKEGI 240
Cdd:cd06343    154 DFGKDGLEGLKEALKAYGL 172
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
150-219 8.77e-03

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of NMDA receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR2 subunit of NMDA receptor family. 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 composed 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. 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: 380601  Cd Length: 356  Bit Score: 39.97  E-value: 8.77e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1856631258  150 GSSSVAiQVQNLLQLFN---IPQIAYSAtSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHT 219
Cdd:cd06378     72 DQEAVA-QILDFISLQTylpILGISGGS-ANVLLDKEEGSTFLQLGPSIEQQATVMLNILEEYDWHQFSVVTS 142
 
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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