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Conserved domains on  [gi|131888529|ref|NP_062312|]
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gamma-aminobutyric acid type B receptor subunit 1 precursor [Mus musculus]

Protein Classification

PBP1_GABAb_receptor and 7tmC_GABA-B-R1 domain-containing protein (domain architecture ID 11984914)

protein containing domains CCP, PBP1_GABAb_receptor, 7tmC_GABA-B-R1, and Ax_dynein_light

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
7tmC_GABA-B-R1 cd15291
gamma-aminobutyric acid type B receptor subunit 1, member of the class C family of ...
589-861 2.23e-166

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: 491.08  E-value: 2.23e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 589 KLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWL 668
Cdd:cd15291    1 KLFISMCLLASLGIFAAVFLLIFNIYNRHRRYIQLSQPHCNNVMLVGCILCLASVFLLGLDGRHVSRSHFPLVCQARLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 669 LGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEPK-E 747
Cdd:cd15291   81 LCLGFTLAYGSMFTKVWRVHRLTTKKKEKKETRKTLEPWKLYAVVGILLVVDVIILAIWQIVDPLHRTIEEFPLEEPKdT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 748 DIDVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSS 827
Cdd:cd15291  161 DEDVKILPQLEHCSSKKQNTWLGIVYGYKGLLLLFGLFLAYETRNVKVEKINDSRFVGMSIYNVVVLCLITAPVTMIISS 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 131888529 828 QQDAAFAFASLAIVFSSYITLVVLFVPKMRRLIT 861
Cdd:cd15291  241 QQDASFAFVSLAILFSSYITLVLIFVPKIRELIR 274
PBP1_GABAb_receptor cd06366
Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
170-562 5.29e-141

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). 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: 107361  Cd Length: 350  Bit Score: 428.60  E-value: 5.29e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 170 YIGALFPMSGgWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06366    1 RIGAIFDLSG-SWIGKAALPAIEMALEDVNADNSILPGYRLVLHVRDSKCDPVQAASAALDLLENKPVVAIIGPQCSSVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERV 329
Cdd:cd06366   80 EFVAEVANEWNVPVLSFAATSPSLSSRLQYPYFFRTTPSDSSQNPAIAALLKKFGWRRVATIYEDDDYGSGGLPDLVDAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 330 KEAGIEITFRQSFFS-----DPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWfktyD 404
Cdd:cd06366  160 QEAGIEISYRAAFPPsanddDITDALKKLKEKDSRVIVVHFSPDLARRVFCEAYKLGMMGKGYVWILTDWLSSNW----W 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 405 PSINCTVEEMTEAVEGHITTEIVMLNpantrsiSNMTSQEFVEKLTKRLKR-HPEETGGFQEAPLAYDAIWAlalalnkt 483
Cdd:cd06366  236 SSSDCTDEEMLEAMQGVIGVRSYVPN-------SSMTLQEFTSRWRKRFGNeNPELTEPSIYALYAYDAVWA-------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 484 sggggrsgvrledfnynnqtitdqiyramnSSSFEGVSGHVVFDaSGSRMAWTLIEQLQ--GGSYKKIGYYDStKDDLSW 561
Cdd:cd06366  301 ------------------------------STNFNGLSGPVQFD-GGRRLASPAFEIINiiGKGYRKIGFWSS-ESGLSV 348

                 .
gi 131888529 562 S 562
Cdd:cd06366  349 F 349
Sushi pfam00084
Sushi repeat (SCR repeat);
106-156 8.48e-08

Sushi repeat (SCR repeat);


:

Pssm-ID: 306569  Cd Length: 56  Bit Score: 51.74  E-value: 8.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 131888529  106 LENGKVflTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQ-GQWSTPKPHC 156
Cdd:pfam00084   7 LPNGSV--SATKNEYNYGAKVEYECDPGYRLVGNPVITCQEdGTWSPPFPEC 56
Ax_dynein_light super family cl23860
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
881-926 1.65e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


The actual alignment was detected with superfamily member pfam10211:

Pssm-ID: 313442  Cd Length: 187  Bit Score: 40.61  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 131888529  881 NNEEEKSRL------LEKENRELEKIIAEKEERVSELRHQLQSRQQIRSRRH 926
Cdd:pfam10211 116 QAEQGKSELekkiadLEEEKEELEKQVAELKAKCEAIEKREEERRQAEEKKH 167
 
Name Accession Description Interval E-value
7tmC_GABA-B-R1 cd15291
gamma-aminobutyric acid type B receptor subunit 1, member of the class C family of ...
589-861 2.23e-166

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: 491.08  E-value: 2.23e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 589 KLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWL 668
Cdd:cd15291    1 KLFISMCLLASLGIFAAVFLLIFNIYNRHRRYIQLSQPHCNNVMLVGCILCLASVFLLGLDGRHVSRSHFPLVCQARLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 669 LGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEPK-E 747
Cdd:cd15291   81 LCLGFTLAYGSMFTKVWRVHRLTTKKKEKKETRKTLEPWKLYAVVGILLVVDVIILAIWQIVDPLHRTIEEFPLEEPKdT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 748 DIDVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSS 827
Cdd:cd15291  161 DEDVKILPQLEHCSSKKQNTWLGIVYGYKGLLLLFGLFLAYETRNVKVEKINDSRFVGMSIYNVVVLCLITAPVTMIISS 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 131888529 828 QQDAAFAFASLAIVFSSYITLVVLFVPKMRRLIT 861
Cdd:cd15291  241 QQDASFAFVSLAILFSSYITLVLIFVPKIRELIR 274
PBP1_GABAb_receptor cd06366
Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
170-562 5.29e-141

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). 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: 107361  Cd Length: 350  Bit Score: 428.60  E-value: 5.29e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 170 YIGALFPMSGgWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06366    1 RIGAIFDLSG-SWIGKAALPAIEMALEDVNADNSILPGYRLVLHVRDSKCDPVQAASAALDLLENKPVVAIIGPQCSSVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERV 329
Cdd:cd06366   80 EFVAEVANEWNVPVLSFAATSPSLSSRLQYPYFFRTTPSDSSQNPAIAALLKKFGWRRVATIYEDDDYGSGGLPDLVDAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 330 KEAGIEITFRQSFFS-----DPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWfktyD 404
Cdd:cd06366  160 QEAGIEISYRAAFPPsanddDITDALKKLKEKDSRVIVVHFSPDLARRVFCEAYKLGMMGKGYVWILTDWLSSNW----W 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 405 PSINCTVEEMTEAVEGHITTEIVMLNpantrsiSNMTSQEFVEKLTKRLKR-HPEETGGFQEAPLAYDAIWAlalalnkt 483
Cdd:cd06366  236 SSSDCTDEEMLEAMQGVIGVRSYVPN-------SSMTLQEFTSRWRKRFGNeNPELTEPSIYALYAYDAVWA-------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 484 sggggrsgvrledfnynnqtitdqiyramnSSSFEGVSGHVVFDaSGSRMAWTLIEQLQ--GGSYKKIGYYDStKDDLSW 561
Cdd:cd06366  301 ------------------------------STNFNGLSGPVQFD-GGRRLASPAFEIINiiGKGYRKIGFWSS-ESGLSV 348

                 .
gi 131888529 562 S 562
Cdd:cd06366  349 F 349
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
186-545 4.23e-72

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: 307306  Cd Length: 316  Bit Score: 243.04  E-value: 4.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  186 ACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELlYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLS 265
Cdd:pfam01094   1 LVLLAMRLAVSDINADPGLLPGTKLEYIILDTCCDPSLALAAALDL-IKGKVVAIIGPSCSSVAIAVASLANLWKVPVIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  266 YGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSF--- 342
Cdd:pfam01094  80 YGSTSPALSDKNRYPTFLRTTPSDTSQAKAIADILKHFGWKRVALIYSDDDYGRSGLQALEDALRERGICVAYKAVIpps 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  343 -FSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWfligwyadnwfktydpsINCTVeemteavegh 421
Cdd:pfam01094 160 aDDEIVRKLLKEVKSKARVIVVCASSETARRLLKAARRLGMTGEGYVW-----------------ISPGF---------- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  422 itteivmlnpantrsisnmtsQEFVEKLTKRLKRHPEETGGFQEAP--LAYDAIWALALALNKTSGGGGRSGVRLEDFNY 499
Cdd:pfam01094 213 ---------------------SEFLLRWKSDRKELYENLGGLQVSYgaLAYDAVYLLAHALHNLLRDDGDPPGSNLSCDK 271
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 131888529  500 NNQtITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGS 545
Cdd:pfam01094 272 PWD-GGQLLLRYLKNVNFTGLTGNVQFDENGDRIPTYDILNLQGSG 316
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
169-554 2.84e-24

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


Pssm-ID: 223755  Cd Length: 366  Bit Score: 106.37  E-value: 2.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 169 VYIGALFPMSGgwPGGQACQP---AVEMALEDVNSRRDILPdYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGC 245
Cdd:COG0683   11 IKIGVVLPLSG--PAAAYGQQiknGAELAVEEINAAGGILG-RKVELVVEDDASDPATAAAVARKLITQDGVDAVVGPTT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 246 SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLDD 324
Cdd:COG0683   88 SGVALAASPVAEEAGVPLISPSATAPQLTGRGLKPNVFRTGPTDNQQAAAAADyLVKKGGKKRVAIIGDDYAYGEGLADA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 325 LEERVKEAGIEITFRQSFFS---DPAVPVKNLKRQDARIIVGLFYETEArKVFCEVYKERLFGKKYVWFLIGWYADNWfk 401
Cdd:COG0683  168 FKAALKALGGEVVVEEVYAPgdtDFSALVAKIKAAGPDAVLVGGYGPDA-ALFLRQAREQGLKAKLIGGDGAGTAEFE-- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 402 tydpsinctvEEMTEAVEGHITTEIVMLNPANTRsisnmTSQEFVEKLTKRLKRhPEETGGFQEAplAYDAIWALALALN 481
Cdd:COG0683  245 ----------EIAGAGGAGAGLLATAYSTPDDSP-----ANKKFVEAYKAKYGD-PAAPSYFAAA--AYDAVKLLAKAIE 306
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 131888529 482 KTSGGGGRsgvrledfnynnqtitDQIYRAM-NSSSFEGVSGHVVFDASGSRM-AWTLIEQLQGGSYKKIGYYDS 554
Cdd:COG0683  307 KAGKSSDR----------------EAVAEALkGGKFFDTAGGPVTFDEKGDRGsKPVYVGQVQKGGDGKFVYAKP 365
7tm_3 pfam00003
7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane ...
784-856 2.19e-11

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: 306509  Cd Length: 110  Bit Score: 63.35  E-value: 2.19e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 131888529  784 IFLAYETKSVSTEkINDHRAVGMAIYNVAVLCLITAPVTMILSSQqDAAFAFASLAIVFSSYITLVVLFVPKM 856
Cdd:pfam00003  38 FFLAFKTRKLPSN-FNEAKYITFSMLNFLIVWVIFIPVYLSTKGS-KLQFAVEAFAILASSTGLLGCIFIPKC 108
Sushi pfam00084
Sushi repeat (SCR repeat);
106-156 8.48e-08

Sushi repeat (SCR repeat);


Pssm-ID: 306569  Cd Length: 56  Bit Score: 51.74  E-value: 8.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 131888529  106 LENGKVflTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQ-GQWSTPKPHC 156
Cdd:pfam00084   7 LPNGSV--SATKNEYNYGAKVEYECDPGYRLVGNPVITCQEdGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
105-157 9.30e-08

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056  Cd Length: 57  Bit Score: 51.31  E-value: 9.30e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 131888529 105 TLENGKVFLTGGDLPAldGARVDFRCDPDFHLVGSSRSIC-SQGQWSTPKPHCQ 157
Cdd:cd00033    6 VPENGTVTGSKGSYSY--GSTVTYSCNEGYTLVGSSTITCtENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
105-156 1.61e-07

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 50.60  E-value: 1.61e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 131888529   105 TLENGKVFLTGGDLPAldGARVDFRCDPDFHLVGSSRSIC-SQGQWSTPKPHC 156
Cdd:smart00032   6 DIENGTVTSSSGTYSY--GDTVTYSCDPGYTLIGSSTITClENGTWSPPPPTC 56
PHA02927 PHA02927
secreted complement-binding protein; Provisional
62-178 1.30e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943  Cd Length: 263  Bit Score: 50.81  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  62 IEYVCRGEREVVGPKVRKCLANGSWTDMDTPSR--CVRICSKSYLTLENGKvfLTGGDLPALDGARVDFRCDPDFHLVGS 139
Cdd:PHA02927 108 ITYSCNSGYQLIGESKSYCELGSTGSMVWNPEApiCESVKCQSPPSISNGR--HNGYEDFYTDGSVVTYSCNSGYSLIGN 185
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 131888529 140 SRSICSQGQWSTPkPHCQVNRTPHSERRAVYIGALFPMS 178
Cdd:PHA02927 186 SGVLCSGGEWSDP-PTCQIVKCPHPTISNGYLSSGFKRS 223
PRK15404 PRK15404
leucine ABC transporter subunit substrate-binding protein LivK; Provisional
171-338 8.90e-04

leucine ABC transporter subunit substrate-binding protein LivK; Provisional


Pssm-ID: 237959  Cd Length: 369  Bit Score: 42.32  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGgwPGGQ---ACQPAVEMALEDVNSRRDILPDyELKLIHHDSKCDPGQATKYLYELLyNDPIKIILMPGCSS 247
Cdd:PRK15404  28 IAIVGPMSG--PVAQygdMEFTGARQAIEDINAKGGIKGD-KLEGVEYDDACDPKQAVAVANKVV-NDGIKYVIGHLCSS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 248 vSTLvaEAARMWN---LIVLSYGSSSPALSNRqRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATI---QQTTE-VFT 319
Cdd:PRK15404 104 -STQ--PASDIYEdegILMITPAATAPELTAR-GYQLIFRTIGLDSDQGPTAAKyILEKVKPKRIAVLhdkQQYGEgLAR 179
                        170
                 ....*....|....*....
gi 131888529 320 STLDDLeervKEAGIEITF 338
Cdd:PRK15404 180 SVKDGL----KKAGANVVF 194
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
881-926 1.65e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 313442  Cd Length: 187  Bit Score: 40.61  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 131888529  881 NNEEEKSRL------LEKENRELEKIIAEKEERVSELRHQLQSRQQIRSRRH 926
Cdd:pfam10211 116 QAEQGKSELekkiadLEEEKEELEKQVAELKAKCEAIEKREEERRQAEEKKH 167
 
Name Accession Description Interval E-value
7tmC_GABA-B-R1 cd15291
gamma-aminobutyric acid type B receptor subunit 1, member of the class C family of ...
589-861 2.23e-166

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: 491.08  E-value: 2.23e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 589 KLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWL 668
Cdd:cd15291    1 KLFISMCLLASLGIFAAVFLLIFNIYNRHRRYIQLSQPHCNNVMLVGCILCLASVFLLGLDGRHVSRSHFPLVCQARLWL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 669 LGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEPK-E 747
Cdd:cd15291   81 LCLGFTLAYGSMFTKVWRVHRLTTKKKEKKETRKTLEPWKLYAVVGILLVVDVIILAIWQIVDPLHRTIEEFPLEEPKdT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 748 DIDVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSS 827
Cdd:cd15291  161 DEDVKILPQLEHCSSKKQNTWLGIVYGYKGLLLLFGLFLAYETRNVKVEKINDSRFVGMSIYNVVVLCLITAPVTMIISS 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 131888529 828 QQDAAFAFASLAIVFSSYITLVVLFVPKMRRLIT 861
Cdd:cd15291  241 QQDASFAFVSLAILFSSYITLVLIFVPKIRELIR 274
PBP1_GABAb_receptor cd06366
Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
170-562 5.29e-141

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). 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: 107361  Cd Length: 350  Bit Score: 428.60  E-value: 5.29e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 170 YIGALFPMSGgWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06366    1 RIGAIFDLSG-SWIGKAALPAIEMALEDVNADNSILPGYRLVLHVRDSKCDPVQAASAALDLLENKPVVAIIGPQCSSVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERV 329
Cdd:cd06366   80 EFVAEVANEWNVPVLSFAATSPSLSSRLQYPYFFRTTPSDSSQNPAIAALLKKFGWRRVATIYEDDDYGSGGLPDLVDAL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 330 KEAGIEITFRQSFFS-----DPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWfktyD 404
Cdd:cd06366  160 QEAGIEISYRAAFPPsanddDITDALKKLKEKDSRVIVVHFSPDLARRVFCEAYKLGMMGKGYVWILTDWLSSNW----W 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 405 PSINCTVEEMTEAVEGHITTEIVMLNpantrsiSNMTSQEFVEKLTKRLKR-HPEETGGFQEAPLAYDAIWAlalalnkt 483
Cdd:cd06366  236 SSSDCTDEEMLEAMQGVIGVRSYVPN-------SSMTLQEFTSRWRKRFGNeNPELTEPSIYALYAYDAVWA-------- 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 484 sggggrsgvrledfnynnqtitdqiyramnSSSFEGVSGHVVFDaSGSRMAWTLIEQLQ--GGSYKKIGYYDStKDDLSW 561
Cdd:cd06366  301 ------------------------------STNFNGLSGPVQFD-GGRRLASPAFEIINiiGKGYRKIGFWSS-ESGLSV 348

                 .
gi 131888529 562 S 562
Cdd:cd06366  349 F 349
7tmC_GABA-B-like cd15047
gamma-aminobutyric acid type B receptor and related proteins, member of the class C family of ...
590-861 2.63e-87

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: 282.91  E-value: 2.63e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 590 LFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGyhigRSQFPFVCQARLWLL 669
Cdd:cd15047    2 LFIVFTVLSGIGILLALVFLIFNIKFRKNRVIKMSSPLFNNLILLGCILCYISVILFGLDD----SKPSSFLCTARPWLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 670 GLGFSLGYGSMFTKIWWVHTVFTKKEEkkeWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEpkeDI 749
Cdd:cd15047   78 SIGFTLVFGALFAKTWRIYRIFTNKKL---KRIVIKDKQLLKIVGILLLIDIIILILWTIVDPLKPTRVLVLSEI---SD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 750 DVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQ 829
Cdd:cd15047  152 DVKYEYVVHCCSSSNGIIWLGILLAYKGLLLLFGCFLAWKTRNVDIEEFNESKYIGISIYNVLFLSVIGVPLSFVLTDSP 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 131888529 830 DAAFAFASLAIVFSSYITLVVLFVPKMRRLIT 861
Cdd:cd15047  232 DTSYLIISAAILFCTTATLCLLFVPKFWLLKR 263
PBP1_GPCR_family_C_like cd06350
Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
170-563 2.49e-75

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 recep; 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 devided 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: 153138  Cd Length: 348  Bit Score: 253.06  E-value: 2.49e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 170 YIGALFPMSGG--------WPGGQACQPAVEMALEDV---NSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYN---- 234
Cdd:cd06350    1 IIGGLFPLHSGsesvslkcGRFGKKGLQAAEAMLFAVeeiNNDPDLLPNITLGYHIYDSCCSPAVALRAALDLLLSgegt 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 235 ---------DPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGW 305
Cdd:cd06350   81 tppyscrkqPKVVAVIGPGSSSVSMAVAELLGLFKIPQISYGATSPLLSDKLQFPSFFRTVPSDTSQALAIVALLKHFGW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 306 KKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFF-----SDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKE 380
Cdd:cd06350  161 TWVGLVYSDDDYGRSGLSDLEEELEKNGICIAFVEAIPpssteEDIKRILKKLKSSTARVIVVFGDEDDALRLFCEAYKL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 381 RLfGKKYVWFLIGWYADnwfktydpsiNCTVEEMTEAVEGHITTEIVMlnpantrsISNMTSQEFVEKLTKrlkrhpeet 460
Cdd:cd06350  241 GM-TGKYWIISTDWDTS----------TCLLLFTLDAFQGVLGFSGHA--------PRSGEIPGFKDFLRK--------- 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 461 ggfqEAPLAYDAIWAlalalnktsggggrsgvrledfnynnqtitdqiyramnsssfegvsgHVVFDASGSRMAWTLIEQ 540
Cdd:cd06350  293 ----YAYNVYDAVYA-----------------------------------------------EVKFDENGDRLASYDIIN 321
                        410       420
                 ....*....|....*....|....*..
gi 131888529 541 LQ----GGSYKKIGYYDSTKDDLSWSK 563
Cdd:cd06350  322 WQifpgGGGFVKVGFWDPQGSGLSINE 348
7tmC_GABA-B-R2 cd15294
gamma-aminobutyric acid type B receptor subunit 2, member of the class C family of ...
590-861 6.07e-74

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: 246.57  E-value: 6.07e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 590 LFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWLL 669
Cdd:cd15294    2 LYSILSSLTIIGIILASAFLAFNIKFRNHRYIKMSSPYMNNLIILGCMLTYASVILLGLDGSLVSEKTFETLCTARTWIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 670 GLGFSLGYGSMFTKIWWVHTVFTKKEEKkewRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEPKEDI 749
Cdd:cd15294   82 CVGFTLAFGAMFSKTWRVHSIFTNVKLN---KKAIKDYKLFIIVGVLLLIDICILITWQIVDPFYRTVKELEPEPDPAGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 750 DVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQ 829
Cdd:cd15294  159 DILIRPELEYCESTHMTIFLGIIYAYKGLLMVFGCFLAWETRNVSIPALNDSKYIGMSVYNVVIMCVIGAAVSFILRDQP 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 131888529 830 DAAFAFASLAIVFSSYITLVVLFVPKMRRLIT 861
Cdd:cd15294  239 NVQFCIISLFIIFCTTITLCLVFVPKLIELRR 270
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
186-545 4.23e-72

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: 307306  Cd Length: 316  Bit Score: 243.04  E-value: 4.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  186 ACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELlYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLS 265
Cdd:pfam01094   1 LVLLAMRLAVSDINADPGLLPGTKLEYIILDTCCDPSLALAAALDL-IKGKVVAIIGPSCSSVAIAVASLANLWKVPVIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  266 YGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSF--- 342
Cdd:pfam01094  80 YGSTSPALSDKNRYPTFLRTTPSDTSQAKAIADILKHFGWKRVALIYSDDDYGRSGLQALEDALRERGICVAYKAVIpps 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  343 -FSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWfligwyadnwfktydpsINCTVeemteavegh 421
Cdd:pfam01094 160 aDDEIVRKLLKEVKSKARVIVVCASSETARRLLKAARRLGMTGEGYVW-----------------ISPGF---------- 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  422 itteivmlnpantrsisnmtsQEFVEKLTKRLKRHPEETGGFQEAP--LAYDAIWALALALNKTSGGGGRSGVRLEDFNY 499
Cdd:pfam01094 213 ---------------------SEFLLRWKSDRKELYENLGGLQVSYgaLAYDAVYLLAHALHNLLRDDGDPPGSNLSCDK 271
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 131888529  500 NNQtITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGS 545
Cdd:pfam01094 272 PWD-GGQLLLRYLKNVNFTGLTGNVQFDENGDRIPTYDILNLQGSG 316
PBP1_glutamate_receptors_like cd06269
Family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the ...
171-475 5.56e-55

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 recep; 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 I family. The family C GPCRs consist of metabotropic glutamate receptor (mGluR) receptors, a calcium-sensing receptor (CaSR), gamma-aminobutyric receptors (GABAb), 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: 153137  Cd Length: 298  Bit Score: 194.27  E-value: 5.56e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELL----YNDPIKIILMPGCS 246
Cdd:cd06269    2 IGGLFPLHSGGRFGEEGAFRAAAALFAVEEINNDLPNTTLGYEIYDSCCSPSDAFSAALDLCslleKSRGVVAVIGPSSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 247 SVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLE 326
Cdd:cd06269   82 SSAEAVASLLGALHIPQISYSATSPLLSDKEQFPSFLRTVPSDSSQAQAIVDLLKHFGWTWVGLVYSDDDYGRRLLELLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 327 ERVKEAGIEITFRQSFFSDPAVP---VKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYadnwfkty 403
Cdd:cd06269  162 EELEKNGICVAFVESIPDGSEDIrrlLKELKSSTARVIVVFSSEEDALRLLEEAVELGMMTGYHWIITDLWL-------- 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 131888529 404 dpsINCTVEEMTEAVEGHITteivmlnpantrsisnmtsqefvekltkrlkrhpeetgGFQEAPLAYDAIWA 475
Cdd:cd06269  234 ---TSCLDLELLEYFPGNLT--------------------------------------GFGEAALVYDAVYA 264
PBP1_ABC_transporter_GCPR_C_like cd04509
Family C of G-protein coupled receptors and their close homologs, the type I ...
170-475 4.02e-46

Family C of G-protein coupled receptors and their close homologs, the type I 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 I 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, phermone 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 - which is included in this CD - followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type II periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.


Pssm-ID: 107261  Cd Length: 299  Bit Score: 169.21  E-value: 4.02e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 170 YIGALFPMSGGWPG-GQACQPAVEMALEDVNSrRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSV 248
Cdd:cd04509    1 KIGVLFPLSGPYAEyGAFRLAGAQLAVEEINA-KGGIPGRKLELVIYDDQSDPARALAAARRLCQQEGVDALVGPVSSGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 249 STLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEER 328
Cdd:cd04509   80 ALAVAPVAEALKIPLISPGATAPGLTDKKGYPYLFRTGPSDEQQAEALADYIKEYNWKKVAILYDDDSYGRGLLEAFKAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 329 VKEAGIEITFRQSF---FSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLfGKKYVWFLI-GWYADNWFktyd 404
Cdd:cd04509  160 FKKKGGTVVGEEYYplgTTDFTSLLQKLKAAKPDVIVLCGSGEDAATILKQAAEAGL-TGGYPILGItLGLSDVLL---- 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 131888529 405 psinctvEEMTEAVEGHITTEIVMLNPANTRSisnmtsqeFVEKLTKRLKRHPEETGGFQEAPLAYDAIWA 475
Cdd:cd04509  235 -------EAGGEAAEGVLTGTPYFPGDPPPES--------FFFVRAAAREKKKYEDQPDYFAALAYDAVLL 290
PBP1_NPR_GC_like cd06352
Ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
183-553 5.36e-37

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 I periplasmic binding fold protein family.


Pssm-ID: 107347  Cd Length: 389  Bit Score: 145.15  E-value: 5.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 183 GGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLI 262
Cdd:cd06352   15 SLARVGPAIQLAVERVNADPNLLPGYDFTFVYLDTECSESVALLAAVDLYWEHNVDAFIGPGCPYACAPVARLAAHWNIP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 263 VLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQT-TEVFTSTLDDLEERVKEAGIEITFRQS 341
Cdd:cd06352   95 MISWGCVALSLSDKSEYPTLTRTLPPARKLGEAVLALLRWFNWHVAVVVYSDdSENCFFTLEALEAALREFNLTVSHVVF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 342 FFSDPAVP-----VKNLKRQdARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIG------WYADNWFKTYDPSINCT 410
Cdd:cd06352  175 MEDNSGAEdlleiLQDIKRR-SRIIIMCGSSEDVRELLLAAHDLGLTSGDYVFILIDlfnyslPYQNSYPWERGDGDDEK 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 411 VEEMTEAVeghittEIVMLNPANTRSIsnmtsQEFVEKLTKRLKR--HPEETGGFQEAPLA---YDAIWALALALNKTsg 485
Cdd:cd06352  254 AKEAYDAV------LTITLRPPDNPEY-----EEFSEEVKEAAKRppFNTDAEPEQVSPYAgylYDAVLLYAHALNET-- 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 131888529 486 gggrsgvRLEDFNYNNQTITDQIyraMNSSSFEGVSGHVVFDASGSRMA----WTLIEqlQGGSYKKIGYYD 553
Cdd:cd06352  321 -------LAEGGDYNGGLIITRR---MWNRTFSGITGPVTIDENGDREGdyslLDLDS--TGGQLEVVYLYD 380
PBP1_ABC_transporter_LIVBP_like cd06268
Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
171-477 8.38e-29

Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type I periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type I 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: 107263  Cd Length: 298  Bit Score: 119.06  E-value: 8.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKyLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06268    2 IGVLLPLSGPLaALGEPVRNGAELAVEEINAAGGIL-GRKIELVVEDTQGDPEAAAA-AARELVDDGVDAVIGPLSSGVA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRqRFPTFFRTHPSATLHNPTRVKLF-EKWGWKKIATIQQTTEVFTSTLDDLEER 328
Cdd:cd06268   80 LAAAPVAEEAGVPLISPGATSPALTGK-GNPYVFRTAPSDAQQAAALADYLaEKGKVKKVAIIYDDYAYGRGLAAAFREA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 329 VKEAGIEITFRQSF---FSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKkyvWFLIGWYADNWFKTYDP 405
Cdd:cd06268  159 LKKLGGEVVAEETYppgATDFSPLIAKLKAAGPDAVFLAGYGGDAALFLKQAREAGLKVP---IVGGDGAAAPALLELAG 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 131888529 406 sinctveemtEAVEGHITTEivmlnPANTRSISNMTSQEFVEKLTKRLKRHPEetggfQEAPLAYDAIWALA 477
Cdd:cd06268  236 ----------DAAEGVLGTT-----PYAPDDDDPAAAAFFQKAFKAKYGRPPD-----SYAAAAYDAVRLLA 287
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
169-554 2.84e-24

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


Pssm-ID: 223755  Cd Length: 366  Bit Score: 106.37  E-value: 2.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 169 VYIGALFPMSGgwPGGQACQP---AVEMALEDVNSRRDILPdYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGC 245
Cdd:COG0683   11 IKIGVVLPLSG--PAAAYGQQiknGAELAVEEINAAGGILG-RKVELVVEDDASDPATAAAVARKLITQDGVDAVVGPTT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 246 SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLDD 324
Cdd:COG0683   88 SGVALAASPVAEEAGVPLISPSATAPQLTGRGLKPNVFRTGPTDNQQAAAAADyLVKKGGKKRVAIIGDDYAYGEGLADA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 325 LEERVKEAGIEITFRQSFFS---DPAVPVKNLKRQDARIIVGLFYETEArKVFCEVYKERLFGKKYVWFLIGWYADNWfk 401
Cdd:COG0683  168 FKAALKALGGEVVVEEVYAPgdtDFSALVAKIKAAGPDAVLVGGYGPDA-ALFLRQAREQGLKAKLIGGDGAGTAEFE-- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 402 tydpsinctvEEMTEAVEGHITTEIVMLNPANTRsisnmTSQEFVEKLTKRLKRhPEETGGFQEAplAYDAIWALALALN 481
Cdd:COG0683  245 ----------EIAGAGGAGAGLLATAYSTPDDSP-----ANKKFVEAYKAKYGD-PAAPSYFAAA--AYDAVKLLAKAIE 306
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 131888529 482 KTSGGGGRsgvrledfnynnqtitDQIYRAM-NSSSFEGVSGHVVFDASGSRM-AWTLIEQLQGGSYKKIGYYDS 554
Cdd:COG0683  307 KAGKSSDR----------------EAVAEALkGGKFFDTAGGPVTFDEKGDRGsKPVYVGQVQKGGDGKFVYAKP 365
7tmC_GPR156 cd15292
orphan GPR156, member of the class C family of seven-transmembrane G protein-coupled receptors; ...
592-857 4.89e-24

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


Pssm-ID: 320419  Cd Length: 268  Bit Score: 104.05  E-value: 4.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 592 ISVSVLSSlGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGyhiGRSQFPFVCQARLWLLGL 671
Cdd:cd15292    5 VMWTLLSC-GILLALFFLAFTIRFRNNRIVKMSSPNLNVVTLLGSILTYTSGFLFGIQE---PGTSMETIFQVRIWLLCI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 672 GFSLGYGSMFTKIWWVHTVFTKKEEKKewRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLH--RTIETFAKEEPKeDI 749
Cdd:cd15292   81 GTSLVFGPILGKSWRLYRVFTQRVPDK--RVIIKDIQLLGLVAGLIFADVLLLLTWVLTDPVQcaRSLSAVIKAMEK-GI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 750 DVSIlPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQ 829
Cdd:cd15292  158 SYSV-SRMDFCASLYSDLWIILISGFKGSLLLYGTYLAGLTSNVSSPPVNQSLTIMVGVNLVTLTAGVVFPVTRFLHSWP 236
                        250       260
                 ....*....|....*....|....*...
gi 131888529 830 DAAFAFASLAIVFSSYITLVVLFVPKMR 857
Cdd:cd15292  237 NLVYGTTSGGIFVCTTTINCLIFIPQLK 264
7tm_classC_mGluR-like cd13953
metabotropic glutamate receptor-like class C family of seven-transmembrane G protein-coupled ...
592-860 1.38e-23

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  Cd Length: 251  Bit Score: 102.70  E-value: 1.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 592 ISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPlgldgyHIGRSQfPFVCQARLWLLGL 671
Cdd:cd13953    4 IVLLVLAALGLLLTIFIWVVFIRYRNTPVVKASNRELSYLLLFGILLCFLLAFL------FLLPPS-DVLCGLRRFLFGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 672 GFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHrtietfakeePKEDIDV 751
Cdd:cd13953   77 SFTLVFSTLLVKTNRIYRIFKSGLRSSLRPKLLSNKSQLLLVLFLLLVQVAILIVWLILDPPK----------VEKVIDS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 752 SILPQLEHCSSKkmNTWLGIFYGYKGLLLLLGIFLAYETKSVsTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDA 831
Cdd:cd13953  147 DNKVVELCCSTG--NIGLILSLVYNILLLLICTYLAFKTRKL-PDNFNEARYIGFSSLLSLVIWIAFIPTYFTTSGPYRD 223
                        250       260
                 ....*....|....*....|....*....
gi 131888529 832 afAFASLAIVFSSYITLVVLFVPKMRRLI 860
Cdd:cd13953  224 --AILSFGLLLNATVLLLCLFLPKIYIIL 250
Periplasmic_Binding_Protein_Type_1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
171-399 1.49e-23

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: 107248  Cd Length: 269  Bit Score: 102.66  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGWPGGQACQPAVEMALEDVNsrrdilpdYELKLIHHDSKCDPGQATKYLyELLYNDPIKIILMPGCSSVST 250
Cdd:cd01391    2 IGVLLPLSGSAPFGAQLLAGIELAAEEIG--------RGLEVILADSQSDPERALEAL-RDLIQQGVDGIIGPPSSSSAL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 251 LVAEAARMWNLIVLSYGSSSPALSnrqRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVF-TSTLDDLEERV 329
Cdd:cd01391   73 AVVELAAAAGIPVVSLDATAPDLT---GYPYVFRVGPDNEQAGEAAAEYLAEKGWKRVALIYGDDGAYgRERLEGFKAAL 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 131888529 330 KEAGIEI----TFRQSFFSDPAVPVKNLKR-QDARIIVGLFYETeARKVFCEVYKERLFGKKYVWFLI-GWYADNW 399
Cdd:cd01391  150 KKAGIEVvaieYGDLDTEKGFQALLQLLKAaPKPDAIFACNDEM-AAGALKAAREAGLTPGDISIIGFdGSPAALL 224
PBP1_NPR_like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
175-561 5.93e-21

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: 107368  Cd Length: 396  Bit Score: 96.16  E-value: 5.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 175 FPMSggWPggqACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKY----LYELLYNDPIKIILMPGCSSVST 250
Cdd:cd06373   13 YPWS--LP---RVGPAIDIAVERVNADPGLLPGHNITLVFEDSECKCGCSESEaplvAVDLYFQHKPDAFLGPGCEYAAA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 251 LVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATI----QQTTEVFTSTLDDLE 326
Cdd:cd06373   88 PVARFAAHWNVPVLTAGAPAAGFSDKSEYSTLTRTGPSYTKLGEFVLALHEHFNWSRAALLyhddKNDDRPCYFTLEGVY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 327 ERVKEAGIEITFRQSFFSDPAVPVKNLKR---QDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLI-----GWYADN 398
Cdd:cd06373  168 TVLKEENITVSDFPFDEDKELDDYKELLRdisKKGRVVIMCASPDTVREIMLAAHRLGLTSGEYVFFNIdlfgsSLYGGG 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 399 WFKTYDpsincTVEEMTEAVEGHITTEIVML----NPAntrsisnmtSQEFVEKLTKRLKR----HPEET------GGFq 464
Cdd:cd06373  248 PWWWER-----GDEDDEKAKEAYQALMTITLrepdNPE---------YKEFSLEVKERAKKkfntTSDDSlvnffaGAF- 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 465 eaplaYDAIWALALALNKTSGgggrsgvrlEDFNYNNQTitdQIYRAMNSSSFEGVSGHVVFDASGSR-MAWTLIE--QL 541
Cdd:cd06373  313 -----YDAVLLYALALNETLA---------EGGDPRDGT---NITRRMWNRTFEGITGNVSIDENGDReSDFSLWDmtDT 375
                        410       420
                 ....*....|....*....|
gi 131888529 542 QGGSYKKIGYYDSTKDDLSW 561
Cdd:cd06373  376 ETGTFEVVANYNGSNKTIEW 395
PBP1_ABC_ligand_binding_like_3 cd06336
Type I periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
170-482 6.64e-17

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


Pssm-ID: 107331  Cd Length: 347  Bit Score: 83.13  E-value: 6.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 170 YIGALFPMSGG---WpgGQACQPAVEMALEDVNSRRDILPD---YELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMP 243
Cdd:cd06336    1 KIGFSGPLSGPaaaW--GLPGLRGVQLAAEEINAAGGIKVGgkkYKVEIVSYDDKYDPAEAAANARRLVQQDGVKFILGP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 244 GCSSVSTL--VAEAARMwnlIVLSYGSSSPALSNRQrFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTST 321
Cdd:cd06336   79 IGGGITAAqqITERNKV---LLLTAYSSDLSIDTAG-NPLTFRVPPIYNVYGVPFLAYAKKPGGKKVALLGPNDAYGQPW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 322 LDDLEERVKEAGIEITFRQSF------FSDPAVPVKNLKrQDArIIVGLFYETEARKVFcevyKE-RLFGKKYVWflIGW 394
Cdd:cd06336  155 VAAYKAAWEAAGGKVVSEEPYdpgttdFSPIVTKLLAEK-PDV-IFLGGPSPAPAALVI----KQaRELGFKGGF--LSC 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 395 YADNwfktYDPSInctVEEMTEAVEGHITTEIVMLNPANTrsiSNMTsQEFVEKLTkrlKRHPEETGgfQEAPLAYDAIW 474
Cdd:cd06336  227 TGDK----YDELL---VATGADFMEGVYFQFPDVDDPALA---FPRA-KAFVEEYK---KRYGEPPN--SEAAVSYDAVY 290

                 ....*...
gi 131888529 475 ALALALNK 482
Cdd:cd06336  291 ILKAAMEA 298
PBP1_ABC_LIVBP_like cd06342
Type I periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
171-534 7.82e-17

Type I 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 includes the type I 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: 107337  Cd Length: 334  Bit Score: 82.59  E-value: 7.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGWPG-GQACQPAVEMALEDVNSRRDILPdYELKLIHHDSKCDPGQAT----KylyelLYNDPIKIILMPGC 245
Cdd:cd06342    2 IGVAGPLTGPNAAlGKDIKNGAQLAVEDINAKGGGKG-VKLELVVEDDQADPKQAVavaqK-----LVDDGVVGVVGHLN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 246 SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQrFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLDD 324
Cdd:cd06342   76 SGVTIPASPIYADAGIVMISPAATNPKLTERG-YKNVFRVVARDDQQGPAAAKyAVETLKAKKVAIIDDKTAYGQGLADE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 325 LEERVKEAGIEITFRQSF------FSdpAVpVKNLKRQDARIIvglF---YETEARKVFCEVYKERLFGKkyvwfLIGwy 395
Cdd:cd06342  155 FKKALKAAGGKVVAREGTtdgatdFS--AI-LTKIKAANPDAV---FfggYYPEAGPLVRQMRQLGLKAP-----FMG-- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 396 ADNwfkTYDPSInctVEEMTEAVEGHITTE---IVMLNPANtrsisnmtsQEFVEKLTkrlKRHPEETGGFqeAPLAYDA 472
Cdd:cd06342  222 GDG---LCDPEF---IKIAGDAAEGTYATFpggPLEKMPAG---------KAFVARYK---AKFGDPPGAY--APYAYDA 281
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 131888529 473 IWALALALNKTsggggrsgvrledfnynnQTITDQIYR-AMNSSSFEGVSGHVVFDASGSRMA 534
Cdd:cd06342  282 ANVLAEAIKKA------------------GSTDPAKVAdALRKVDFDGVTGKISFDAKGDLKG 326
PBP1_NPR_B cd06384
Ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B ...
189-562 1.98e-16

Ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B natriuretic peptide receptor (NPR-B). NPR-B is one of three known single membrane-spanning natriuretic peptide receptors that have been identified. Natriuretic peptides are family of structurally related but genetically distinct hormones/paracrine factors 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. Like NPR-A (or GC-A), NPR-B (or GC-B) is a transmembrane guanylyl cyclase, an enzyme that catalyzes the synthesis of cGMP. NPR-B is the predominant natriuretic peptide receptor in the brain. The rank of order activation of NPR-B by natriuretic peptides is CNP>>ANP>BNP. Homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux.


Pssm-ID: 107379  Cd Length: 399  Bit Score: 82.54  E-value: 1.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 189 PAVEMALEDVNSRRDILPDYELKLIHHDSKcDPGQATKYLYEL------LYNDPiKIILMPGCSSVSTLVAEAARMWNLI 262
Cdd:cd06384   22 PAIRMAVERIQNKGKLLRGYTITLLNKSSE-LNGGCSESLAPLhavdlkLYSDP-DVFFGPGCVYPTASVARFATHWRLP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 263 VLSYGSSSPALSNRQ-RFPTFFRTHPSATLHNPTRVKLFEKWGWkkiatiqqTTEVFTSTLD-DLEER----VKEaGIEI 336
Cdd:cd06384  100 LITAGAPAFGFSNKTdEYRTTVRTGPSTTKLGEFVNHLHEHFNW--------TSRAALLYLDlKTDDRphyfISE-GVFL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 337 TFRQSFFSDPAVPVKNLKRQDARIIVGlFYETEARKVF-C-----------EVYKERLFGKKYVWFLIGWYADNWF--KT 402
Cdd:cd06384  171 ALQEENANVSAHPYHIEKNSDIIEIIQ-FIKQNGRIVYiCgpletfleimlQAQREGLTPGDYVFFYLDVFGESLRvkSP 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 403 YDPSINCTVEEMTEAVEGHITTEIVMLNPANtrsisNMTSQEFVEKLTKRLKrhpEETGGFQEAPLA-------YDAIWA 475
Cdd:cd06384  250 RESYKQMNHSSWTVLKEAFKSVFVITYREPE-----NPEYKEFQRELHARAK---EDFGVELEPSLMnfiagcfYDGVML 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 476 LALALNKTsggggrsgvrLEDFNYNNQTITdqIYRAMNSSSFEGVSGHVVFDASGSR----MAWTLIEQlQGGSYKKIGY 551
Cdd:cd06384  322 YAMALNET----------LAEGGSQKDGLN--ITRKMQDRRFWGVTGLVSIDKNNDRdidfDLWAMTDH-ETGKYEVVAH 388
                        410
                 ....*....|.
gi 131888529 552 YDSTKDDLSWS 562
Cdd:cd06384  389 YNGITKQIVWS 399
PBP1_Speract_GC_like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
190-350 2.15e-16

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: 107365  Cd Length: 404  Bit Score: 82.38  E-value: 2.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 190 AVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLyNDPIKIILMPGCS-SVSTLVAEAarmWNLIVLSYGS 268
Cdd:cd06370   24 ALTLAVEDVNADPNLLPGYKLQFEWVDTHGDEVLSIRAVSDWW-KRGVVAFIGPECTcTTEARLAAA---WNLPMISYKC 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 269 SSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITfRQSFFSDPAV 348
Cdd:cd06370  100 DEEPVSDKSKYPTFARTVPPSIQVVKSVIALLKHFNWNKFSVVYENDSKYSSVFETLKEEAELRNITIS-HVEYYADFYP 178

                 ..
gi 131888529 349 PV 350
Cdd:cd06370  179 PD 180
Peripla_BP_6 pfam13458
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ...
169-533 2.27e-15

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


Pssm-ID: 316020  Cd Length: 342  Bit Score: 78.48  E-value: 2.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  169 VYIGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSS 247
Cdd:pfam13458   2 IKIGVLTPLSGPYaSSGKSSRAGARAAAEEINAAGGIN-GRKIELVVADDQGDPDVAAAAARRLVDQDGVDALVGGLSSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  248 VSTLVAEAARMWNLIVLsygsSSPALSNRQRFPTFFRTHPSA-TLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLE 326
Cdd:pfam13458  81 VALAVAPVLAKKGVPVI----GPAALTGEPCSPNVFSLGPTYsAQATALGQYLAKELGGKKVALITADYAFGRALAAAAK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  327 ERVKEAGIEITfrQSFF-----SDPAVPVKNLKRQDARIIVGLFYETEArKVFCEVYKERLFGKKYVWFLIGWYADNWFK 401
Cdd:pfam13458 157 AALKAAGGEVV--GEVRyplgtTDFSSQVLQIKASGADAVLLANAGADA-VAFIKQAREAGLDAKGIPLVGLGGDEPDLK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  402 TYDPsinctveemtEAVEGHITTEIVMLNPANTRsisnmtSQEFVEKLTkrlKRHPEETGGfQEAPLAYDAIWALALALN 481
Cdd:pfam13458 234 ALGG----------DAAEGVYSTTPFFPDLDNPA------NRAFVAAYA---AKYGEAPPT-QFAAGGYIAADLLLAALK 293
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 131888529  482 KTsggggrsgvrledfnynnQTIT-DQIYRAMNSSSFEGVSGHVVFDASGSRM 533
Cdd:pfam13458 294 AA------------------GSDTrEAVIAALRALPYDGLFGPVGFRAEDHQA 328
PBP1_mGluR cd06362
Ligand binding domain of the metabotropic glutamate receptors (mGluR); Ligand binding domain ...
169-560 2.50e-15

Ligand binding domain of the 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: 107357  Cd Length: 452  Bit Score: 79.59  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 169 VYIGALFPMSGGWPGGQACQPAVE---------M--ALEDVNSRRDILPDYELKLIHHDSkC-----DPGQATKYLYELL 232
Cdd:cd06362    3 IILGGLFPVHSKGTGGEPCGEIKEqrgiqrleaMlfALDEINNDPTLLPGITLGAHILDT-CsrdtyALEQSLEFVRASL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 233 YND------------------PIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNP 294
Cdd:cd06362   82 TKIddcvycdggspppnnspkPVAGVIGASYSSVSIQVANLLRLFKIPQISYASTSPELSDKTRYDYFSRTVPPDSFQAQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 295 TRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGI-------------EITFRQSFFsdpavpvKNLKRQDARII 361
Cdd:cd06362  162 AMVDIVKAFNWTYVSTVASEGNYGEKGIEAFEKLAAERGIciagsekipssatEEEFDNIIR-------KLLSKPNARVV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 362 VgLFYETEARKVFCEVYKERLFGKKYVWflIGwyADNWFKTYDPsinctVEEMTEAVEGHITTEI------------VML 429
Cdd:cd06362  235 V-LFCREDDIRGLLAAAKRLNAEGHFQW--IA--SDGWGARNSV-----VEGLEDVAEGAITIELqsaevpgfdeyfLSL 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 430 NPANTRsiSNMTSQEFVE-----KLTKRLKRHPEETGG---------FQEAPLAY--DAIWALALALNKTSggggrsgvr 493
Cdd:cd06362  305 TPENNS--RNPWFREFWEqkfncKLTGNGSTKDNTCCTerilllsnyEQESKVQFviDAVYAMAHALHNMH--------- 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 494 lEDFNYNNQTITDQIYRA---------MNSSSFEGVSGHVVFDASGSRMAWTLIEQLQ----GGSYKKIGYYdstKDDLS 560
Cdd:cd06362  374 -RDLCPGTTGLCDAMKPIdgrkllfylRNVSFSGLAGGPVRFDANGDGPGRYDIFNYQrtngKYDYVKVGSW---KGELS 449
PBP1_ABC_ligand_binding_like_11 cd06346
Type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
171-337 2.72e-14

Type I 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 includes the type I 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: 107341  Cd Length: 312  Bit Score: 74.60  E-value: 2.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRrDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06346    2 IGILLPLTGDLaSYGPPMADAAELAVKEVNAA-GGVLGEPVTLVTADTQTDPAAGVAAATKLVNVDGVPGIVGAACSGVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVL-SYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATI-------QQTTEVFTST 321
Cdd:cd06346   81 IAALTSVAVPNGVVMiSPSSTSPTLTTLDDNGLFFRTAPSDALQGQALAQLAAERGYKSVATTyinndygVGLADAFTKA 160
                        170
                 ....*....|....*.
gi 131888529 322 lddleerVKEAGIEIT 337
Cdd:cd06346  161 -------FEALGGTVT 169
PBP1_NPR_A cd06385
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A ...
180-559 7.18e-14

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: 107380  Cd Length: 405  Bit Score: 74.76  E-value: 7.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 180 GWP-GGqacqPAVEMALEDVNSRRDILPDYELKLIHHDSK-----CDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVA 253
Cdd:cd06385   16 AWPrVG----PALERAIDRVNADPDLLPGLHLQYVLGSSEnkegvCSDSAAPLVAVDLKFTHNPWAFIGPGCDYTASPVA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 254 EAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKkiatiQQTTEVFTSTLDD--------- 324
Cdd:cd06385   92 RFTTHWDVPLVTAGAPALGFGVKDEYATITRTGPTHKKLGEFVLHIHQHFGWR-----SHAMLIYSDNKVDdrpcyfame 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 325 -LEERVKEAGIEItFRQSFFSDPAVPVKNLKR---QDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADN-- 398
Cdd:cd06385  167 gLYMELKKNNITV-VDLVFEEDDLINYTTLLQdikQKGRVIYVCCSPDIFRRLMLQFWREGLPSEDYVFFYIDLFGASlq 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 399 -------WFKtyDPSINCTVEEMTEAVEghITTeivmlnpanTRSISNMTSQEFVEKLTKRLKR---HPEE-------TG 461
Cdd:cd06385  246 gpdpkrpWYR--GDADDAAAREAFQSVK--ILT---------YKEPQNPEYKEFLSDLKTDAKEmfnFTVEdslmniiAG 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 462 GFqeaplaYDAIWALALALNKTSGgggrsgvrledfnyNNQTIT--DQIYRAMNSSSFEGVSGHVVFDASGSR----MAW 535
Cdd:cd06385  313 GF------YDGVMLYAHALNETMA--------------KGGTRPpgTAITQRMWNRTFYGVTGFVKIDDNGDRetdfALW 372
                        410       420
                 ....*....|....*....|....
gi 131888529 536 TLIEQlQGGSYKKIGYYDSTKDDL 559
Cdd:cd06385  373 DMTDT-ESGDFQVVSVYNGTQKQL 395
PBP1_ABC_ligand_binding_like_10 cd06345
Type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
171-539 2.38e-13

Type I 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 includes the type I 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: 107340  Cd Length: 344  Bit Score: 72.40  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06345    2 IGVLAPLSGGAsTTGEAMWNGAELAAEEINAAGGIL-GRKVELVFEDTEGSPEDAVRAFERLVSQDKVDAVVGGYSSEVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNR---QRFPTFFRTHPSATLH-----NPTRVKLFEKWGWKKIATIQQTTEvFTST 321
Cdd:cd06345   81 LALQDVAAENKVPFIVTGAASPEITTAddyETYKYVFRAGPTNSSYaqsvaDALKETLVDKHGFKTAAIVAEDAA-WGKG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 322 LDD-LEERVKEAGIEI----TFRQSfFSDPAVPVKNLKRQDARIIVGLFYETEArkvfcevykerlfgkkyVWFLIGWYA 396
Cdd:cd06345  160 IDAgIKALLPEAGLEVvsveRFSPD-TTDFTPILQQIKAADPDVIIAGFSGNVG-----------------VLFTQQWAE 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 397 DNW-FKTYDPSINCTVEEMTEAVEGhiTTEIVMLNPANTRSISNMTS--QEFVEKLTKRLKRHPEETGGfqeapLAYDAI 473
Cdd:cd06345  222 QKVpIPTIGISVEGNSPAFWKATNG--AGNYVITAESGAPGVEAITDktVPFTEAYEAKFGGPPNYMGA-----STYDSI 294
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 131888529 474 WALALALNKTSGgggrsgvrledfnynnqTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIE 539
Cdd:cd06345  295 YILAEAIERAGS-----------------TDGDALVEALEKTDFVGTAGRIQFYGDDSAFAHGLEY 343
7tmC_GPR158-like cd15293
orphan GPR158 and similar proteins, member of the class C family of seven-transmembrane G ...
592-859 3.22e-13

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: 70.71  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 592 ISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYhigrsqfPFVCQARLWLLGL 671
Cdd:cd15293    4 IAVLAVQAICILLCLVLALVVFRFRKVKVIKAASPILLELILFGALLLYFPVFILYFEPS-------VFRCILRPWFRHL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 672 GFSLGYGSMFTKIWWVHTVFTKKEEKkewRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIetfakeepKEDIDV 751
Cdd:cd15293   77 GFAIVYGALILKTYRILVVFRSRSAR---RVHLTDRDLLKRLGLIVLVVLGYLAAWTAVNPPNVEV--------GLTLTS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 752 SILpQLEHCSSkkmNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEkINDHRAVGMAIYNVAVLCLI--TAPVTMILSSQQ 829
Cdd:cd15293  146 SGL-KFNVCSL---DWWDYVMAIAELLFLLWGVYLCYAVRKAPSA-FNESRYISLAIYNELLLSVIfnIIRFFLLPSLHP 220
                        250       260       270
                 ....*....|....*....|....*....|
gi 131888529 830 DAAFAFASLAIVFSSYITLVVLFVPKMRRL 859
Cdd:cd15293  221 DLLFLLFFLHTQLTVTVTLLLIFGPKFYLV 250
PBP1_ABC_ligand_binding_like_6 cd06340
Type I periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
171-482 6.34e-13

Type I 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 includes the type I 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: 107335  Cd Length: 347  Bit Score: 71.15  E-value: 6.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGWPG-GQACQPAVEMALEDVNSRRDI--LPDYELKLIHHDSKCDPGQATKYLYELLYNDpiKIILMPGC-- 245
Cdd:cd06340    2 IGVLLPLSGGLAAiGQQCKAGAELAVEEINAAGGIksLGGAKLELVFGDSQGNPDIGATEAERLITEE--GVVALVGAyq 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 246 SSVSTLVAEAARMWNLIVLSYGSSSPALSnRQRFPTFFRTHPSATLHNPTRVK----LFEKWG--WKKIATIQQTTEVFT 319
Cdd:cd06340   80 SAVTLAASQVAERYGVPFVVDGAVSDSIT-ERGFKYTFRITPHDGMFTRDMFDflkdLNEKTGkpLKTVALVHEDTEFGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 320 STLDDLEERVKEAGIEITFRQSFfsDPAVP-----VKNLKRQDARIIVGLFYETEARKvFCEVYKERLFGKKYVWFLIGW 394
Cdd:cd06340  159 SVAEAIKKFAKERGFEIVEDISY--PANARdltseVLKLKAANPDAILPASYTNDAIL-LVRTMKEQRVEPKAVYSVGGG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 395 YADNWFktydpsinctVEEMTEAVEGHITTEiVMLNPANTRsisnmtsqefVEKLTKRLK-RHPEETGGfqEAPLAYDAI 473
Cdd:cd06340  236 AEDPSF----------VKALGKDAEGILTRN-EWSDPKDPM----------AKDLNKRFKaRFGVDLSG--NSARAYTAV 292

                 ....*....
gi 131888529 474 WALALALNK 482
Cdd:cd06340  293 LVIADALER 301
PBP1_GC_G_like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
190-533 1.14e-12

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


Pssm-ID: 107367  Cd Length: 391  Bit Score: 70.66  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 190 AVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSS 269
Cdd:cd06372   22 ALQIAMDKVNSDPVYLGNYSMEFTYTNSTCSAKESLAGFIDQVQKEHISALFGPACPEAAEVTGLLASQWNIPMFGFVGQ 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 270 SPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEvfTSTLDDLEERVK--EAGIE----ITFRQSFF 343
Cdd:cd06372  102 TAKLDNRFLYDTYVKLVPPKQKIGEVLQKSLQHFGWKHIGLFGGSSR--DSSWDEVDELWKavENQLKfhfnITATVRYS 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 344 S-DPAVPVKNLKRQD--ARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKtydpsinctvEEMTEAVEG 420
Cdd:cd06372  180 SsNPDLLQEKLRYISsvARVIILICSSEDAKAILQAAEKLGLMKGKFVFFLLQQFEDNFWK----------EVLTDDQVQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 421 HITT--EIVMLnPANTRSISNMTSQEFVEKLTKRLKRHPEE---TGGFQEAPL-AY--DAIWALALALNKTSGGGgrsgv 492
Cdd:cd06372  250 HLPKvyESVFL-IAPSSYGGYSGGYEFRKQVYQKLKRPPFQsslSSEEQVSPYsAYlhDAVLLYALAVKEMLKAG----- 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 131888529 493 rlEDFnYNNQTITdQIYRAMNSSSFEGVSGHVVFDASGSRM 533
Cdd:cd06372  324 --KDF-RNGRQLV-STLRGANQVELQGITGLVLLDEQGKRQ 360
PBP1_iGluR_N_LIVBP_like cd06351
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
171-393 1.17e-12

N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the NMDA, AMPA, and kainate receptor subtypes of ionotropic glutamate receptors (iGluRs); N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the NMDA, AMPA, and kainate receptor subtypes of ionotropic glutamate receptors (iGluRs). While this N-terminal domain belongs to the periplasmic-binding fold type I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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. Glutamate mediates the majority of excitatory synaptic transmission in the central nervous system via two broad classes of ionotropic receptors characterized by their response to glutamate agonists: N-methyl-aspartate (NMDA) and non-NMDA receptors. NMDA receptors have intrinsically slow kinetics, are highly permeable to Ca2+, and are blocked by extracellular Mg2+ in a voltage-dependent manner. On the other hand, non-NMDA receptors have faster kinetics, are weakly permeable to Ca2+, and are not blocked by extracellular Mg2+. While non-NMDA receptors typically mediate excitatory synaptic responses at resting membrane potentials, NMDA receptors contribute to several forms of synaptic plasticity and are suggested to play an important role in the development of synaptic pathways.


Pssm-ID: 107346  Cd Length: 328  Bit Score: 69.84  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGgwpggQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKC-DPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06351    2 IGAIFDRDA-----RKEELAFRAAIDALNTENLNALPTKLSVEVVEVNTnDPFSLLRAVCDLLVSQGVAAIFGPTSSESA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPS-ATLHNPTrVKLFEKWGWKKIATIQQTTEVFtSTLDDLEER 328
Cdd:cd06351   77 SAVQSICDALEIPHISISGGSEGLSDKEESSTTLQLYPSlEDLADAL-LDLLEYYNWTKFAIIYDSDEGL-SRLQELLDE 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 131888529 329 VKEAGIEITFRQ-SFFSDPAVPVKNL--KRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIG 393
Cdd:cd06351  155 SGIKGIQVTVRRlDLDDDNYRQLLKElkRSESRRIILDCSSEEEAKEILEQAVELGMMGYGYHWILTN 222
PBP1_mGluR_groupI cd06374
Ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
236-553 6.03e-12

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: 107369  Cd Length: 472  Bit Score: 68.77  E-value: 6.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 236 PIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTT 315
Cdd:cd06374  117 PIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSIDLSDKTLFKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEG 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 316 EVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPV--KNLKRQDARI----IVGLFYETEARKVFCEVYKERLFGKKYVW 389
Cdd:cd06374  197 NYGESGMEAFKELAAHEGLCIAHSDKIYSNAGEQSfdRLLRKLRSRLpkarVVVCFCEGMTVRGLLMAMRRLGVGGEFQL 276
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 390 flIGwyADNWFKTYDpsincTVEEMTEAVEGHITTEI------------VMLNP-ANTRsisNMTSQEFVE-KLTKRLKR 455
Cdd:cd06374  277 --IG--SDGWADRDD-----VVEGYEEEAEGGITIKLqspevpsfddyyLKLRPeTNTR---NPWFREFWQhRFQCRLPG 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 456 HPEETGGF---------------QEAPLAY--DAIWALALALNKTSGGGGRSGVRL-EDFNYNNQTitdQIYRAMNSSSF 517
Cdd:cd06374  345 HPQENPNYikictgnesldeqyvQDSKMGFviNAIYAMAHGLHNMHQDLCPGHVGLcDAMKPIDGR---KLLEYLLKTSF 421
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 131888529 518 EGVSGH-VVFDASGSRMAWTLIEQLQggsYKKIGYYD 553
Cdd:cd06374  422 SGVSGEeVYFDENGDSPGRYDIMNLQ---YTEDLRFD 455
PBP1_NPR_C_like cd06386
Ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
189-552 7.05e-12

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


Pssm-ID: 107381  Cd Length: 387  Bit Score: 68.28  E-value: 7.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 189 PAVEMALEDVNSRRDILPDYELKLIHHDSKCdPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGS 268
Cdd:cd06386   21 PAIEYAQRRLEANRLLFPGFRFNVHYEDSDC-GNEALFSLVDRSCARKPDLILGPVCEYAAAPVARLASHWNIPMISAGA 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 269 SSPALSNRQR-FPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQttevftstlDDLEER---VKEAGIEITFRQSFFS 344
Cdd:cd06386  100 LAAGFSHKKSeYSHLTRVAPSYVKMGETFSALFERFHWRSALLVYE---------DDKQERncyFTLEGVHHVFQEEGYH 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 345 DPAVPVKNLKRQDARIIVGLFYETEARKVFC-----------EVYKERLFGKKYVWFLI-----GWYADNWFKTYDpsin 408
Cdd:cd06386  171 MSIYPFDETKDLDLDEIIRAIQASERVVIMCagadtirsimlAAHRRGLTSGDYIFFNIelfnsSSYGDGSWKRGD---- 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 409 ctvEEMTEAVEGHITTEIVMLnpanTRSIsnmtSQEFvEKLTKRLKRHPEETG-------------GFQEAPLAYdaiwa 475
Cdd:cd06386  247 ---KHDFEAKQAYSSLNTVTL----LRTV----KPEF-EKFSMEVKSSVEKAGdlndcdyvnmfveGFHDAILLY----- 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 476 lALALNKTSGgggrsgvrledfNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSR------MAWTlieQLQGGSYKKI 549
Cdd:cd06386  310 -ALALHEVLK------------NGYSKKDGTKITQRMWNRTFEGIAGQVSIDANGDRygdfsvIAMT---DVEAGTYEVV 373

                 ...
gi 131888529 550 GYY 552
Cdd:cd06386  374 GNY 376
PBP1_Taste_receptor cd06363
Ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
190-389 7.94e-12

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: 107358  Cd Length: 410  Bit Score: 68.09  E-value: 7.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 190 AVEMALEDVNSRRDILPDYEL--KLIHHdskCDPGQATKYLYELL---------YNDPI----KIILMPGC-SSVSTLVA 253
Cdd:cd06363   47 AMRFAVEEINNSTSLLPGVTLgyEIFDH---CSDSANFPPTLSLLsvngsriepQCNYTnyqpRVVAVIGPdSSTLALTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 254 EAARMWNLI-VLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEA 332
Cdd:cd06363  124 APLFSFFLIpQISYGASSEVLSNKELYPSFLRTVPSDKDQIEAMVQLLQEFGWNWVAFLGSDDEYGRDGLQLFSELIANT 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 131888529 333 GIEITFR----QSFFSDPAVP--VKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKkyVW 389
Cdd:cd06363  204 GICIAYQglipLDTDPETDYQqiLKQINQTKVNVIVVFASRQPAEAFFNSVIQQNLTGK--VW 264
7tm_3 pfam00003
7 transmembrane sweet-taste receptor of 3 GCPR; This is a domain of seven transmembrane ...
784-856 2.19e-11

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: 306509  Cd Length: 110  Bit Score: 63.35  E-value: 2.19e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 131888529  784 IFLAYETKSVSTEkINDHRAVGMAIYNVAVLCLITAPVTMILSSQqDAAFAFASLAIVFSSYITLVVLFVPKM 856
Cdd:pfam00003  38 FFLAFKTRKLPSN-FNEAKYITFSMLNFLIVWVIFIPVYLSTKGS-KLQFAVEAFAILASSTGLLGCIFIPKC 108
PBP1_ABC_ligand_binding_like_12 cd06347
Type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
171-530 2.04e-09

Type I 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 includes the type I 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: 107342  Cd Length: 334  Bit Score: 60.26  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGWP-GGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06347    2 IGVNLPLTGDVAaYGQSEKNGAKLAVKEINAAGGVL-GKKIELVVEDNKSDKEEAANAATRLIDQDKVVAIIGPVTSGAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRQRFptFFRthpsATLHNPTRVKL-----FEKWGWKKIATIQQTTEVFTSTLDD 324
Cdd:cd06347   81 LAAGPIAEDAKVPMITPSATNPKVTQGKDY--VFR----VCFIDPFQGTVmakfaTENLKAKKAAVLYDNSSDYSKGLAK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 325 -LEERVKEAGIEITFRQSF------FSdpaVPVKNLKRQDARIIVGLFYETEARKVfceVYKERLFGKKYVWFliGwyAD 397
Cdd:cd06347  155 aFKEAFKKLGGEIVAEETFnagdtdFS---AQLTKIKAKNPDVIFLPGYYTEVGLI---AKQARELGIKVPIL--G--GD 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 398 NWfktyDpsiNCTVEEM-TEAVEGHITTeivmlNPANTRSISNMtSQEFVEKLTKRLKRHPEetggfQEAPLAYDAIWAL 476
Cdd:cd06347  225 GW----D---SPKLEEAgGAAAEGVYFT-----THFSADDPTPK-AKKFVKAYKAKYGKEPD-----AFAALGYDAYYLL 286
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 131888529 477 ALALNKTsggggrsgvrledfnyNNQTITDQIYRAMNSSSFEGVSGHVVFDASG 530
Cdd:cd06347  287 ADAIERA----------------GSTDPEAIRDALAKTKDFDGVTGKITIDENG 324
PBP1_Arsenic_SBP_like cd06330
Periplasmic solute-binding domain of active transport proteins; Periplasmic solute-binding ...
171-530 2.10e-09

Periplasmic solute-binding domain of active transport proteins; Periplasmic solute-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 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: 107325  Cd Length: 346  Bit Score: 60.36  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSG-GWPGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06330    2 IGVITFLSGrAAIFGEPARNGAELAVEEINAAGGIG-GRKIELVVRDEAGKPDEAIREARELVENEGVDMLIGLISSGVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEK--WGWKKIATI-------QQTTEVFTS 320
Cdd:cd06330   81 LAVAPVAEELKVFFIATDPGTPRLTEEPDNPYVFRTRNSTIMDAVAGALYAAKldKKAKTWATInpdyaygQDAWADFKA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 321 TLddleervKEAGIEITFRQSFFSDPAVP-----VKNLKRQDARII---------VGLFYETEARKVFCevykerlfGKK 386
Cdd:cd06330  161 AL-------KRLRPDVEVVSEQWPKLGAPdygseITALLAAKPDAIfsslwggdlVTFVRQANARGLFD--------GTT 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 387 YVWFLIGWYADNWFKtydpsinctvEEMteaVEGHITT-----EIVMLNPANtrsisnmtsQEFVEKLTKRLKRHPeeTG 461
Cdd:cd06330  226 VVLTLTGAPELAPLG----------DEM---PEGVIIGgrgpyFIPPDTPEN---------KAFVDAYQEKYGDYP--TY 281
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 131888529 462 GFQEaplAYDAIWALALALNKTSGGggrsgvrledfnyNNQTITDQIYRAMNSSSFEGVSGHVVFDASG 530
Cdd:cd06330  282 GAYG---AYQAVMALAAAVEKAGAT-------------DGGAPPEQIAAALEGLSFETPGGPITMRAAD 334
PBP1_mGluR_groupIII cd06376
Ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
169-423 1.71e-08

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: 107371  Cd Length: 463  Bit Score: 57.97  E-value: 1.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 169 VYIGALFPMSGGWPGGQACQP-----------AVEMALEDVNSRRDILPD---------------YELK--------LIH 214
Cdd:cd06376    3 ITLGGLFPVHARGPAGVPCGDikkengihrleAMLYALDQINSDPDLLPNvtlgarildtcsrdtYALEqsltfvqaLIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 215 HDS---KCDPGQATkylyelLYNDPIKIILMPGC--SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSA 289
Cdd:cd06376   83 KDTsdvRCTNGEPP------VFVKPEKVVGVIGAsaSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 290 TLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAG---IEITFRQSFFSDPAVPVKNLKR----QDARIIV 362
Cdd:cd06376  157 SFQAQAMVDIVKALGWNYVSTLASEGNYGESGVEAFTQISREAGgvcIAQSIKIPREPRPGEFDKIIKRlletPNARAVI 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 131888529 363 GLFYETEARKVFCEVYKERLFGkKYVWflIGwyADNWFKTYDPSINctveeMTEAVEGHIT 423
Cdd:cd06376  237 IFANEDDIRRVLEAAKRANQVG-HFLW--VG--SDSWGAKISPILQ-----QEDVAEGAIT 287
7tmC_mGluRs cd15045
metabotropic glutamate receptors, member of the class C family of seven-transmembrane G ...
592-856 1.80e-08

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  Cd Length: 253  Bit Score: 56.10  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 592 ISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLgldgyhIGRSQfPFVCQARLWLLGL 671
Cdd:cd15045    4 IGAMAFASLGILLTLFVLVVFVRYRDTPVVKASGRELSYVLLAGILLSYVMTFVL------VAKPS-TIVCGLQRFGLGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 672 GFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETfakeePKEDIDV 751
Cdd:cd15045   77 CFTVCYAAILTKTNRIARIFRLGKKSAKRPRFISPRSQLVITGLLVSVQVLVLAVWLILSPPRATHHY-----PTRDKNV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 752 SIlpqlehCSSKKmNTWLGIFYGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDA 831
Cdd:cd15045  152 LV------CSSAL-DASYLIGLAYPILLIILCTVYAFKTRKIP-EGFNEAKYIGFTMYTTCIIWLAFVPLYFTTASNIEV 223
                        250       260
                 ....*....|....*....|....*
gi 131888529 832 AFAFASLAIVFSSYITLVVLFVPKM 856
Cdd:cd15045  224 RITTLSVSISLSATVQLACLFAPKV 248
PBP1_GPC6A_like cd06361
Ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
233-399 3.06e-08

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: 107356  Cd Length: 403  Bit Score: 56.80  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 233 YNDPIKIILMPGCSSVSTLVAeaaRMWNLIVL---SYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIA 309
Cdd:cd06361  100 YVPRIKAVIGAGYSEISMAVS---RMLNLQLIpqvSYASTAEILSDKIRFPSFLRTVPSDFYQTKAMAHLIKKSGWNWVG 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 310 TIQQTTEVFTSTLDDLEERVKEAGIEITFRQ---SFFSDPAVPVKN-------LKRQDARIIVGLFYETEARKVFcEVYK 379
Cdd:cd06361  177 IIITDDDYGRSALETFIIQAEANGVCIAFKEilpASLSDNTKLNRIirttekiIEENKVNVIVVFARQFHVFLLF-NKAI 255
                        170       180
                 ....*....|....*....|
gi 131888529 380 ERLFGKkyVWFLigwyADNW 399
Cdd:cd06361  256 ERNINK--VWIA----SDNW 269
PBP1_ABC_ligand_binding_like_5 cd06338
Type I periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
171-370 7.05e-08

Type I 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 includes the type I 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); however their ligand specificity has not been determined experimentally.


Pssm-ID: 107333  Cd Length: 345  Bit Score: 55.35  E-value: 7.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILPD---YELKLIHHDSKCDPGQATKyLYELLYN-DPIKIILMPGC 245
Cdd:cd06338    2 IGASLSLTGPLaGGGQLTQRGYELWVEDVNAAGGIKGGgkgYPVELIYYDDQSNPARAAR-AYERLITqDKVDFLLGPYS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 246 SSVSTLVAEAARMWNLIVLSYGSSSPALSnRQRFPTFFRTHP--SATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLD 323
Cdd:cd06338   81 SGLTLAAAPVAEKYGVPMVAGSGASDSIF-AQGFKYVFGTLPpaSQYAKSLLEMLVALDPRPKKVAILYADDPFSQDVAE 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 131888529 324 DLEERVKEAGIEITFRQSF---FSDPAVPVKNLKRQDARIIVGLFYETEA 370
Cdd:cd06338  160 GAREKAEAAGLEVVYDETYppgTADLSPLISKAKAAGPDAVVVAGHFPDA 209
Sushi pfam00084
Sushi repeat (SCR repeat);
106-156 8.48e-08

Sushi repeat (SCR repeat);


Pssm-ID: 306569  Cd Length: 56  Bit Score: 51.74  E-value: 8.48e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 131888529  106 LENGKVflTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQ-GQWSTPKPHC 156
Cdd:pfam00084   7 LPNGSV--SATKNEYNYGAKVEYECDPGYRLVGNPVITCQEdGTWSPPFPEC 56
CCP cd00033
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ...
105-157 9.30e-08

Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.


Pssm-ID: 153056  Cd Length: 57  Bit Score: 51.31  E-value: 9.30e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 131888529 105 TLENGKVFLTGGDLPAldGARVDFRCDPDFHLVGSSRSIC-SQGQWSTPKPHCQ 157
Cdd:cd00033    6 VPENGTVTGSKGSYSY--GSTVTYSCNEGYTLVGSSTITCtENGGWSPPPPTCE 57
CCP smart00032
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ...
105-156 1.61e-07

Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.


Pssm-ID: 214478  Cd Length: 56  Bit Score: 50.60  E-value: 1.61e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 131888529   105 TLENGKVFLTGGDLPAldGARVDFRCDPDFHLVGSSRSIC-SQGQWSTPKPHC 156
Cdd:smart00032   6 DIENGTVTSSSGTYSY--GDTVTYSCDPGYTLIGSSTITClENGTWSPPPPTC 56
7tmC_mGluR4 cd15452
metabotropic glutamate receptor 4 in group 3, member of the class C family of ...
661-915 2.50e-07

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  Cd Length: 327  Bit Score: 53.45  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 661 VCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETf 740
Cdd:cd15452   66 TCSLRRIFLGLGMSISYAALLTKTNRIYRIFEQGKRSVSAPRFISPASQLVITFSLISLQLLGVCVWFLVDPSHSVVDY- 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 741 akeEPKEDIDVSILPQLEHCSSKKMNtwLGIFYGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLITAP 820
Cdd:cd15452  145 ---EDQRTPDPQFARGVLKCDISDLS--LICLLGYSMLLMVTCTVYAIKTRGVP-ETFNEAKPIGFTMYTTCIIWLAFIP 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 821 VTMILSSQQDAAF---AFASLAIVFSSYITLVVLFVPKMRRLITRGEW----QSEAQDTMKTGSSTNN----------NE 883
Cdd:cd15452  219 IFFGTSQSAEKMYiqtTTLTISVSLSASVSLGMLYMPKVYVILFHPEQnvpkRKRSLKAVVTAATMSNkftqkgsfrpNG 298
                        250       260       270
                 ....*....|....*....|....*....|..
gi 131888529 884 EEKSRLLekENRELEKiIAEKEERVSELRHQL 915
Cdd:cd15452  299 EAKSELC--ENLETQA-LATKQTYVSYSNHAI 327
PHA02927 PHA02927
secreted complement-binding protein; Provisional
62-178 1.30e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943  Cd Length: 263  Bit Score: 50.81  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  62 IEYVCRGEREVVGPKVRKCLANGSWTDMDTPSR--CVRICSKSYLTLENGKvfLTGGDLPALDGARVDFRCDPDFHLVGS 139
Cdd:PHA02927 108 ITYSCNSGYQLIGESKSYCELGSTGSMVWNPEApiCESVKCQSPPSISNGR--HNGYEDFYTDGSVVTYSCNSGYSLIGN 185
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 131888529 140 SRSICSQGQWSTPkPHCQVNRTPHSERRAVYIGALFPMS 178
Cdd:PHA02927 186 SGVLCSGGEWSDP-PTCQIVKCPHPTISNGYLSSGFKRS 223
PBP1_alkylbenzenes_like cd06360
Type I periplasmic binding component of active transport systems that are predicted be ...
171-481 1.32e-06

Type I periplasmic binding component of active transport systems that are predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; This group includes the type I periplasmic binding component of active transport systems that are predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; their substrate specificity is not well characterized, however.


Pssm-ID: 107355  Cd Length: 336  Bit Score: 51.16  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRrdiLPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 249
Cdd:cd06360    2 VGLLLPYSGTYaALGEDITRGFELALQEAGGK---LGGREVEFVVEDDEAKPDVAVEKARKLIEQDKVDVVVGPVHSGEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 250 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERV 329
Cdd:cd06360   79 LAMVKVLREPGTPLINPNAGADDLTGRLCAPNFFRTSFSNAQWAAPMGKYAADDGYKKVVTVAWDYAFGYEVVEGFKEAF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 330 KEAGIEITFRQ-SFF--SDPAVPVKNLKRQDARIIVGLFYETEARKvFCEVYKErlFGKKYVWFLIGwyadNWFKTyDPS 406
Cdd:cd06360  159 TEAGGKIVKELwVPFgtSDFASYLAQIPDDVPDAVFVFFAGGDAIK-FVKQYDA--AGLKAKIPLIG----SGFLT-DGT 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 131888529 407 incTVEEMTEAVEGHITTeivmLNPANTrsISNMTSQEFVEKLTKRLKRHPEE--TGGfqeaplaYDAIWALALALN 481
Cdd:cd06360  231 ---TLGAAGEAAEGVITA----LHYADT--LDNPANQAFVKAYRAAYPDTPSVyaVQG-------YDAGQALILALE 291
7tmC_mGluR8 cd15454
metabotropic glutamate receptor 8 in group 3, member of the class C family of ...
660-894 1.57e-06

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  Cd Length: 311  Bit Score: 50.79  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 660 FVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIET 739
Cdd:cd15454   65 GICSFRRVFLGLGMCFSYAALLTKTNRIHRIFEQGKKSVTAPKFISPASQLVITFSLISVQLLGVFVWFAVDPPHTIVDY 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 740 FAKEEPKEDIDVSILpqleHCSSKKMNTWLGIfyGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLITA 819
Cdd:cd15454  145 GEQRTLDPEKARGVL----KCDISDLSLICSL--GYSILLMVTCTVYAIKTRGVP-ETFNEAKPIGFTMYTTCIIWLAFI 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 820 PVtmILSSQQDAAFAFA-----SLAIVFSSYITLVVLFVPKMRRLITRGEwqSEAQDTMKTGSSTNNNEEEKSRLLEKEN 894
Cdd:cd15454  218 PI--FFGTAQSAERMYIqtttlTISMSLSASVSLGMLYMPKVYIIIFHPE--QNVQKRKRSFKAVVTAATMQSKLIQKGN 293
PBP1_CaSR cd06364
Ligand-binding domain of the CaSR calcium-sensing receptor, which is a member of the family C ...
246-390 4.00e-06

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; 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: 107359  Cd Length: 510  Bit Score: 50.41  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 246 SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDL 325
Cdd:cd06364  128 SGVSTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKF 207
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 326 EERVKEAGIEITFRQ--SFFSDPAV---PVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKkyVWF 390
Cdd:cd06364  208 REEAEERDICIDFSEliSQYSDEEEiqrVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGK--IWL 275
PHA02927 PHA02927
secreted complement-binding protein; Provisional
62-162 4.11e-06

secreted complement-binding protein; Provisional


Pssm-ID: 222943  Cd Length: 263  Bit Score: 49.27  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529  62 IEYVCRG--EREVVGPKVRKCLANGsWTDMDtpsRCVRICSKSYLTLENGKVFLTGGDLpaldGARVDFRCDPDFHLVGS 139
Cdd:PHA02927  50 IEYLCLPgyRKQKMGPIYAKCTGTG-WTLFN---QCIKRRCPSPRDIDNGQLDIGGVDF----GSSITYSCNSGYQLIGE 121
                         90       100
                 ....*....|....*....|....*...
gi 131888529 140 SRSICSQGQ-----WSTPKPHCQVNRTP 162
Cdd:PHA02927 122 SKSYCELGStgsmvWNPEAPICESVKCQ 149
PBP1_iGluR_AMPA cd06380
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the AMPA receptor; ...
446-566 1.35e-05

N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the AMPA receptor; N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor, a member of the glutamate-receptor ion channels (iGluRs). AMPA receptors are the major mediators of excitatory synaptic transmission in the central nervous system. While this N-terminal domain belongs to the periplasmic-binding fold type I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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. AMPA receptors consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important roles in mediating the rapid excitatory synaptic current.


Pssm-ID: 107375  Cd Length: 382  Bit Score: 48.46  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 446 VEKLTKRLKR-HPEETGGFQ------EAPLAYDAIWALALALNKTSGGGGRSGVRLeDFNYNNQTIT------------D 506
Cdd:cd06380  250 VQKFLQRWKKlDPREWPGAGtspikyTAALAHDAVLVMAEAFRSLRRQRGSGRHRI-DISRRGNGGDclanpavpwehgI 328
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 131888529 507 QIYRAMNSSSFEGVSGHVVFDASGSRMAWTL-IEQLQGGSYKKIGYydstkddlsWSKTDK 566
Cdd:cd06380  329 DIERALKKVQFEGLTGNVQFDEFGQRTNYTLdVVELKTRGLRKVGY---------WNEDDG 380
7tmC_mGluR6 cd15453
metabotropic glutamate receptor 6 in group 3, member of the class C family of ...
661-864 2.82e-05

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  Cd Length: 273  Bit Score: 46.95  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 661 VCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETF 740
Cdd:cd15453   66 VCAFRRLFLGLGTTLSYSALLTKTNRIYRIFEQGKRSVTPPPFISPTSQLVITFSLTSLQVVGVIAWLGAQPPHSVIDYE 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 741 AKEEPKEDIDVSILpqleHCSSKKMNTwLGIFyGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLITAP 820
Cdd:cd15453  146 EQRTVDPEQARGVL----KCDMSDLSL-IGCL-GYSLLLMVTCTVYAIKARGVP-ETFNEAKPIGFTMYTTCIIWLAFVP 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 131888529 821 VtmILSSQQDAAFAFA-----SLAIVFSSYITLVVLFVPKMRRLITRGE 864
Cdd:cd15453  219 I--FFGTAQSAEKIYIqtttlTVSLSLSASVSLGMLYVPKTYVILFHPE 265
PBP1_SBP_like_3 cd06329
Periplasmic solute-binding domain of active transport proteins; Periplasmic solute-binding ...
171-289 2.91e-05

Periplasmic solute-binding domain of active transport proteins; Periplasmic solute-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: 107324  Cd Length: 342  Bit Score: 47.29  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLyELLYNDPIKIILMPGCSSVS 249
Cdd:cd06329    2 IGVIDPLSGPFaSLGELVRRGLQLAADEINAKGGVD-GRPIELVEEDNKGSPQEALRKA-QKAIDDGVRLVVQGNSSSVA 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 131888529 250 TLVAEAARMWNL-------IVLSYGSSSPALSNRQRFPTFFRTHPSA 289
Cdd:cd06329   80 LALTEAVRKHNQrnpgkevLYLNYASVAPALTGEKCSFWHFRTDANT 126
7tmC_mGluR_group3 cd15286
metabotropic glutamate receptors in group 3, member of the class C family of ...
597-864 5.10e-05

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: 45.95  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 597 LSSLGIV-LAVVCLSFNIYNsHVRYIQNSQPNLNNLTAVGCSLALAAVFPLgldgyhIGRSQFPfVCQARLWLLGLGFSL 675
Cdd:cd15286    9 LAVLGIIaTLFVLVTFVRYN-DTPIVRASGRELSYVLLTGIFLCYAITFLM------VAEPGVG-VCSLRRLFLGLGMSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 676 GYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEP---------K 746
Cdd:cd15286   81 SYAALLTKTNRIYRIFEQGKKSVTPPRFISPTSQLVITFSLISVQLLGVLAWFAVDPPHALIDYEEGRTPdpeqargvlR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 747 EDI-DVSILPQLehcsskkmntwlgifyGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLITAPVTMIL 825
Cdd:cd15286  161 CDMsDLSLICCL----------------GYSLLLMVTCTVYAIKARGVP-ETFNEAKPIGFTMYTTCIVWLAFIPIFFGT 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 131888529 826 SSQQDAAF---AFASLAIVFSSYITLVVLFVPKMRRLITRGE 864
Cdd:cd15286  224 AQSAEKLYiqtATLTVSMSLSASVSLGMLYMPKVYVILFHPE 265
PBP1_ABC-type_HAAT_like cd06333
Type I periplasmic binding component of ABC (ATPase Binding Cassette)-type transport systems ...
171-363 6.09e-05

Type I periplasmic binding component of ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in uptake of amino acids; This subgroup includes the type I periplasmic binding component of ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in uptake of amino acids. Members of this subgroup are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine-binding protein (LIVBP); their ligand specificity has not been determined experimentally, however.


Pssm-ID: 107328  Cd Length: 312  Bit Score: 46.02  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGgwPG---GQACQPAVEMALEDVNSRrDILPDyELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSS 247
Cdd:cd06333    2 IGAILSLTG--PAaslGIPEKKTLELLPDEINAG-GIGGE-KVELIVLDDGSDPTKAVTNARKLIEEDKVDAIIGPSTTP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 248 VSTLVAEAARMWNLIVLSYGSSSPALSNRQRFptFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEE 327
Cdd:cd06333   78 ATMAVAPVAEEAKTPMISLAPAAAIVEPKRKW--VFKTPQNDRLMAEAILADMKKRGVKTVAFIGFSDAYGESGLKELKA 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 131888529 328 RVKEAGIEITFRQSFF-SDPAVPVKNLK----RQDARIIVG 363
Cdd:cd06333  156 LAPKYGIEVVADERYGrTDTSVTAQLLKiraaRPDAVLIWG 196
PBP1_mGluR_groupII cd06375
Ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
246-482 9.10e-05

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: 107370  Cd Length: 458  Bit Score: 45.92  E-value: 9.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 246 SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDL 325
Cdd:cd06375  115 SSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAF 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 326 EERVKEAGIEITFRQSFFSDP------AVPVKNLKRQDARIIVgLFYETE-ARKVFCEVYKerlFGKKYVWFLigwyADN 398
Cdd:cd06375  195 EQEARLRNICIATSEKVGRSAdrksydSVIRKLLQKPNARVVV-LFTRSEdARELLAAAKR---LNASFTWVA----SDG 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 399 WFKTYDPsinctVEEMTEAVEGHITTEI------------VMLNP-ANTRSI-----------SNMTSQEFVEKLTKRLK 454
Cdd:cd06375  267 WGAQESI-----VKGSEDVAEGAITIELashpipdfdryfQSLTPeTNTRNPwfkdfweqkfqCSLQNRDCANTTTNDKE 341
                        250       260       270
                 ....*....|....*....|....*....|
gi 131888529 455 RHPEETGGFQEAPLAY--DAIWALALALNK 482
Cdd:cd06375  342 RLLDKVNYEQESKIMFvvNAVYAMAHALHN 371
PBP1_ABC_ligand_binding_like_14 cd06349
Type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
170-337 1.30e-04

Type I periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems; This subgroup includes the type I 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, 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: 107344  Cd Length: 340  Bit Score: 45.07  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 170 YIGALFPMSG-------GWpggqacQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKyLYELLYNDP-IKIIL 241
Cdd:cd06349    1 LIGVAGPLTGdnaqygtQW------KRAFDLALDEINAAGGVG-GRPLNIVFEDSKSDPRQAVT-IAQKFVADPrIVAVL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 242 MPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFptFFRTHPSATLHNPTRVKL-FEKWGWKKIATIQQTTEVFTS 320
Cdd:cd06349   73 GDFSSGVSMAASPIYQRAGLVQLSPTNSHPDFTKGGDF--IFRNSTSQAIEAPLLADYaVKDLGFKKVAILSVNTDWGRT 150
                        170
                 ....*....|....*..
gi 131888529 321 TLDDLEERVKEAGIEIT 337
Cdd:cd06349  151 SADIFVKAAEKLGGQVV 167
7tmC_mGluR2 cd15447
metabotropic glutamate receptor 2 in group 2, member of the class C family oof ...
661-860 2.43e-04

metabotropic glutamate receptor 2 in group 2, member of the class C family oof 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: 43.76  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 661 VCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPlhrtiETF 740
Cdd:cd15447   66 VCTLRRLGLGTSFAVCYSALLTKTNRIARIFSGAKDGAQRPRFISPASQVAICLALISCQLLVVLIWLLVEA-----PGT 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 741 AKEEPKEDIDVSILpqleHCSSKKMNTWLGIfyGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLITAP 820
Cdd:cd15447  141 RKETAPERRYVVTL----KCNSRDSSMLISL--TYNVLLIILCTLYAFKTRKCP-ENFNEAKFIGFTMYTTCIIWLAFLP 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 131888529 821 VTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLI 860
Cdd:cd15447  214 IFYVTSSDYRVQTTTMCISVSLSGSVVLGCLFAPKLHIIL 253
7tmC_mGluR7 cd15451
metabotropic glutamate receptor 7 in group 3, member of the class C family of ...
661-864 2.97e-04

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: 43.86  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 661 VCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETf 740
Cdd:cd15451   66 VCSFRRIFLGLGMCISYAALLTKTNRIYRIFEQGKKSVTAPRLISPTSQLAITSSLISVQLLGVLIWFAVDPPNIIIDY- 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 741 akeepkeDIDVSILPQLEHCSSKKMNTWLGIF--YGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLIT 818
Cdd:cd15451  145 -------DEQKTMNPEQARGVLKCDITDLQIIcsLGYSILLMVTCTVYAIKTRGVP-ENFNEAKPIGFTMYTTCIVWLAF 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 131888529 819 APVtmILSSQQDAAFAFA-----SLAIVFSSYITLVVLFVPKMRRLITRGE 864
Cdd:cd15451  217 IPI--FFGTAQSAEKLYIqtttlTISMNLSASVALGMLYMPKVYIIIFHPE 265
7tmC_mGluRs_group2_3 cd15934
metabotropic glutamate receptors in group 2 and 3, member of the class C family of ...
596-856 4.84e-04

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: 42.60  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 596 VLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLgldgyhIGRSQfPFVCQARLWLLGLGFSL 675
Cdd:cd15934    8 VFALLGILATLFVIVVFIRYNDTPVVKASGRELSYVLLTGILLCYLMTFVL------LAKPS-VITCALRRLGLGLGFSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 676 GYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETfakeepkEDIDVSILp 755
Cdd:cd15934   81 CYAALLTKTNRISRIFNSGKRSAKRPRFISPKSQLVICLGLISVQLIGVLVWLVVEPPGTRIDY-------PRRDQVVL- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 756 qleHCSSKKMNTWLGIFYgykglllllGIFL-------AYETKSVStEKINDHRAVGMAIYNVAVLCLitAPVTMILSSQ 828
Cdd:cd15934  153 ---KCKISDSSLLISLVY---------NMLLiilctvyAFKTRKIP-ENFNEAKFIGFTMYTTCIIWL--AFVPIYFGTS 217
                        250       260       270
                 ....*....|....*....|....*....|
gi 131888529 829 QDAAFAFASL--AIVFSSYITLVVLFVPKM 856
Cdd:cd15934  218 NDFKIQTTTLcvSISLSASVALGCLFAPKV 247
PRK15404 PRK15404
leucine ABC transporter subunit substrate-binding protein LivK; Provisional
171-338 8.90e-04

leucine ABC transporter subunit substrate-binding protein LivK; Provisional


Pssm-ID: 237959  Cd Length: 369  Bit Score: 42.32  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGgwPGGQ---ACQPAVEMALEDVNSRRDILPDyELKLIHHDSKCDPGQATKYLYELLyNDPIKIILMPGCSS 247
Cdd:PRK15404  28 IAIVGPMSG--PVAQygdMEFTGARQAIEDINAKGGIKGD-KLEGVEYDDACDPKQAVAVANKVV-NDGIKYVIGHLCSS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 248 vSTLvaEAARMWN---LIVLSYGSSSPALSNRqRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATI---QQTTE-VFT 319
Cdd:PRK15404 104 -STQ--PASDIYEdegILMITPAATAPELTAR-GYQLIFRTIGLDSDQGPTAAKyILEKVKPKRIAVLhdkQQYGEgLAR 179
                        170
                 ....*....|....*....
gi 131888529 320 STLDDLeervKEAGIEITF 338
Cdd:PRK15404 180 SVKDGL----KKAGANVVF 194
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
881-926 1.65e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organisms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 313442  Cd Length: 187  Bit Score: 40.61  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 131888529  881 NNEEEKSRL------LEKENRELEKIIAEKEERVSELRHQLQSRQQIRSRRH 926
Cdd:pfam10211 116 QAEQGKSELekkiadLEEEKEELEKQVAELKAKCEAIEKREEERRQAEEKKH 167
PBP1_SBP_like_1 cd06327
Periplasmic solute-binding domain of active transport proteins that belong to the type I ...
171-336 1.94e-03

Periplasmic solute-binding domain of active transport proteins that belong to the type I periplasmic binding fold protein family; Periplasmic solute-binding domain of active transport proteins that belong to the type I periplasmic binding fold protein family. Solute binding proteins are the primary specific receptors that initiate uptake of a broad range of solutes, including amino acids, peptides and inorganic ions. The members are predicted to have a similar function to an active transport system for short chain amides and urea by sequence comparison and phylogenetic analysis. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus may also be involved in transport of amino acids.


Pssm-ID: 107322  Cd Length: 334  Bit Score: 41.39  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 171 IGALFPMSGGW--PGGQACQPAVEMALEDVNsrrDILPDYELKLIHHDSKCDPGQATKYLYELLYNDpiKIILMPGC--S 246
Cdd:cd06327    2 IGVLTDMSGVYadAEGKGSVEAAELAVEDFG---GGVLGRPIELVVADHQNKADVAAAKAREWIDRD--GVDMIVGGpnS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 247 SVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSAT-LHNPTRVKLFEKWGwKKIATIQQTTEVFTSTLDDL 325
Cdd:cd06327   77 AVALAVQEVAREKKKIYIVTGAGSDDLTGKDCSPYTFHWAYDTYmLANGTAPALVKAGG-KKWFFLTADYAFGHSLERDA 155
                        170
                 ....*....|.
gi 131888529 326 EERVKEAGIEI 336
Cdd:cd06327  156 RKVVKANGGKV 166
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR1 subunit ...
508-568 2.56e-03

N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR1 subunit of the AMPA receptor; N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR1 subunit of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor. The AMPA receptor is a member of the glutamate-receptor ion channels (iGluRs) which are the major mediators of excitatory synaptic transmission in the central nervous system. AMPA receptors are composed of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current. Furthermore, this N-terminal domain of the iGluRs has homology with LIVBP, a bacterial periplasmic binding protein, as well as with the structurally related glutamate-binding domain of the G-protein-coupled metabotropic receptors (mGluRs).


Pssm-ID: 107385  Cd Length: 364  Bit Score: 41.08  E-value: 2.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 131888529 508 IYRAMNSSSFEGVSGHVVFDASGSRMAWTL-IEQLQGGSYKKIGYydstkddlsWSKTDKWI 568
Cdd:cd06390  312 IQRALQQVRFEGLTGNVQFNEKGRRTNYTLhVIEMKHDGIRKIGY---------WNEDEKLV 364
7tmC_mGluR3 cd15448
metabotropic glutamate receptor 3 in group 2, member of the class C family of ...
597-856 3.69e-03

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: 39.93  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 597 LSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFplgldgYHIGRSQfPFVCQARLWLLGLGFSLG 676
Cdd:cd15448    9 IACLGFICTCMVITVFIKHNNTPLVKASGRELCYILLFGVFLSYCMTF------FFIAKPS-PVICTLRRLGLGTSFAVC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 677 YGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVD-PLHRTietFAKEEPKEDIdvsilp 755
Cdd:cd15448   82 YSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLSLILVQIVVVSVWLILEaPGTRR---YTLPEKRETV------ 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 131888529 756 qLEHCSSKKMNTWLGIfyGYKGLLLLLGIFLAYETKSVStEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAF 835
Cdd:cd15448  153 -ILKCNVKDSSMLISL--TYDVVLVILCTVYAFKTRKCP-ENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTT 228
                        250       260
                 ....*....|....*....|.
gi 131888529 836 ASLAIVFSSYITLVVLFVPKM 856
Cdd:cd15448  229 MCISVSLSGFVVLGCLFAPKV 249
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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