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Conserved domains on  [gi|340707854|pdb|3QEK|A]
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Chain A, NMDA glutamate receptor subunit

Protein Classification

ABC transporter substrate-binding protein( domain architecture ID 10157238)

ABC transporter substrate-binding protein may function in transport of sugar substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
 4-383 0e+00

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


:

Pssm-ID: 380602  Cd Length: 364  Bit Score: 540.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        4 KIVNIGAVLSTKKHEQIFREAVNQANKRHF-TRKIQLQATSVTHRPNAIQ*ALSVCEDLISSQVYAILVSHPPAPTDhLT 82
Cdd:cd06379   1 KIFNIGAVLSSPKHEEIFREAVNEVNAHSHlPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVIVSHPPTPSD-LS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       83 PTPISYTAGFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETL 162
Cdd:cd06379  80 PTSVSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      163 LEGKESkskkrnyenldqlsydnkrgpKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TG 242
Cdd:cd06379 160 AETKDI---------------------KIEKVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTG 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      243 AGYVWLVGEREisgSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFE*-ENITDPPRGCVGNTNIWKTGPLF 321
Cdd:cd06379 219 AGYVWIVTEQA---LAASNVPDGVLGLQLIHGKNESAHIRDSVSVVAQAIRELFRSsENITDPPVDCRDDTNIWKSGQKF 295

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3QEK_A      322 KRVL*SSKYPDGVTGRIEFNEDGDRKFAQYSI*NLQN-RKLVQVGIFNG------SYIIQNDRKIIWPG 383
Cdd:cd06379 296 FRVLKSVKLSDGRTGRVEFNDKGDRIGAEYDIINVQNpRKLVQVGIYVGsqrptkSLLSLNDRKIIWPG 364
 
Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
 4-383 0e+00

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


Pssm-ID: 380602  Cd Length: 364  Bit Score: 540.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        4 KIVNIGAVLSTKKHEQIFREAVNQANKRHF-TRKIQLQATSVTHRPNAIQ*ALSVCEDLISSQVYAILVSHPPAPTDhLT 82
Cdd:cd06379   1 KIFNIGAVLSSPKHEEIFREAVNEVNAHSHlPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVIVSHPPTPSD-LS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       83 PTPISYTAGFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETL 162
Cdd:cd06379  80 PTSVSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      163 LEGKESkskkrnyenldqlsydnkrgpKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TG 242
Cdd:cd06379 160 AETKDI---------------------KIEKVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTG 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      243 AGYVWLVGEREisgSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFE*-ENITDPPRGCVGNTNIWKTGPLF 321
Cdd:cd06379 219 AGYVWIVTEQA---LAASNVPDGVLGLQLIHGKNESAHIRDSVSVVAQAIRELFRSsENITDPPVDCRDDTNIWKSGQKF 295

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3QEK_A      322 KRVL*SSKYPDGVTGRIEFNEDGDRKFAQYSI*NLQN-RKLVQVGIFNG------SYIIQNDRKIIWPG 383
Cdd:cd06379 296 FRVLKSVKLSDGRTGRVEFNDKGDRIGAEYDIINVQNpRKLVQVGIYVGsqrptkSLLSLNDRKIIWPG 364
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 21-357 5.83e-37

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


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 136.75  E-value: 5.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A         21 FREAVNQANKRH---FTRKIQLQatsVTHRPNAIQ*ALSVCEDLISSQVYAILvshppAPTDHLTPTPISYTAGFYRIPV 97
Cdd:pfam01094   6 VRLAVEDINADPgllPGTKLEYI---ILDTCCDPSLALAAALDLLKGEVVAII-----GPSCSSVASAVASLANEWKVPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A         98 IGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETLLEgkeskskkrnyEN 177
Cdd:pfam01094  78 ISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALR-----------ER 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        178 LDQLSYDNKRGPKADkvlqfepgTKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TGAGYVWLVGEREISGS 257
Cdd:pfam01094 147 GIRVAYKAVIPPAQD--------DDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        258 ALRYAP-----DGIIGLQLINGKNES---------------------------AHISDAVAVVAQAIHELfe*eNITDPP 305
Cdd:pfam01094 219 VILNPStleaaGGVLGFRLHPPDSPEfseffweklsdekelyenlgglpvsygALAYDAVYLLAHALHNL----LRDDKP 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
3QEK_A        306 RGCVGNTNIWKTGPLFKRVL*SSKYpDGVTGRIEFNEDGDRKFAQYSI*NLQ 357
Cdd:pfam01094 295 GRACGALGPWNGGQKLLRYLKNVNF-TGLTGNVQFDENGDRINPDYDILNLN 345
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
 93-345 2.34e-06

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


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 48.77  E-value: 2.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       93 YRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE*-*RLFNWNHVILIVSDDHEGRAAQKKLETLLEgkesksk 171
Cdd:COG0683  94 AGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADYlAKKLGAKKVALLYDDYAYGQGLAAAFKAALK------- 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      172 krnyenldqlsydnKRGPKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TGAGYVWLVGE 251
Cdd:COG0683 167 --------------AAGGEVVGEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGLKGPLNKAFVKA 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      252 -REISGSalryAPDGIiglqlingkneSAHISDAVAVVAQAIhelfE*ENITDPPRgcvgntniwktgplFKRVL*SSKY 330
Cdd:COG0683 233 yKAKYGR----EPSSY-----------AAAGYDAALLLAEAI----EKAGSTDREA--------------VRDALEGLKF 279

                       250
                ....*....|....*
3QEK_A      331 pDGVTGRIEFNEDGD 345
Cdd:COG0683 280 -DGVTGPITFDPDGQ 293
 
Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
 4-383 0e+00

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


Pssm-ID: 380602  Cd Length: 364  Bit Score: 540.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        4 KIVNIGAVLSTKKHEQIFREAVNQANKRHF-TRKIQLQATSVTHRPNAIQ*ALSVCEDLISSQVYAILVSHPPAPTDhLT 82
Cdd:cd06379   1 KIFNIGAVLSSPKHEEIFREAVNEVNAHSHlPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVIVSHPPTPSD-LS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       83 PTPISYTAGFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETL 162
Cdd:cd06379  80 PTSVSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      163 LEGKESkskkrnyenldqlsydnkrgpKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TG 242
Cdd:cd06379 160 AETKDI---------------------KIEKVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTG 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      243 AGYVWLVGEREisgSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFE*-ENITDPPRGCVGNTNIWKTGPLF 321
Cdd:cd06379 219 AGYVWIVTEQA---LAASNVPDGVLGLQLIHGKNESAHIRDSVSVVAQAIRELFRSsENITDPPVDCRDDTNIWKSGQKF 295

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
3QEK_A      322 KRVL*SSKYPDGVTGRIEFNEDGDRKFAQYSI*NLQN-RKLVQVGIFNG------SYIIQNDRKIIWPG 383
Cdd:cd06379 296 FRVLKSVKLSDGRTGRVEFNDKGDRIGAEYDIINVQNpRKLVQVGIYVGsqrptkSLLSLNDRKIIWPG 364
PBP1_iGluR_NMDA cd06367
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic ...
 4-376 1.18e-166

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


Pssm-ID: 380590 [Multi-domain]  Cd Length: 357  Bit Score: 470.18  E-value: 1.18e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        4 KIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLQATSVTH-RPNAIQ*ALSVCEDLISSQVYAILVSHPPAPTDhlT 82
Cdd:cd06367   1 PSVNIGAILGTKKEVAIKDEAEKDDFHHHFTLPVQLRVELVTMpEPDPKSIITRICDLLSDSKVQGVVFSDDTDQEA--I 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       83 PTPISYTAGFYRIPVIGLTTR*SIY-SDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLET 161
Cdd:cd06367  79 AQILDFIAAQTLTPVLGLHGRSSMImADKSEHSMFLQFGPPIEQQASVMLNIMEEYDWYIVSLVTTYFPGYQDFVNKLRS 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      162 LLEGKESkskkrnyenldqlsydnkrgpKADKVLQFEPGT----KNLTALLLEAKELEARVIILSASEDDATAVYKSAA* 237
Cdd:cd06367 159 TIENSGW---------------------ELEEVLQLDMSLddgdSKLQAQLKKLQSPEARVILLYCTKEEATYVFEVAAS 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      238 LD*TGAGYVWLVGEREI-SGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFE*EN-ITDPPRGCVGNTNIW 315
Cdd:cd06367 218 VGLTGYGYTWLVGSLVAgTDTVPAEFPTGLISLSYDEWYNLPARIRDGVAIVATAASEMLSEHEqIPDPPSSCVNNQEIR 297

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3QEK_A      316 K-TGPLFKRVL*SSKYpdgVTGRIEFNEDGDRKFAQYSI*NLQN-RKLVQVGIFNGSYIIQND 376
Cdd:cd06367 298 KyTGPMLKRYLINVTF---EGRDLSFSEDGYQMHPKLVIILLNNeRKWERVGKWKDSSLIMND 357
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
 7-375 2.30e-80

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


Pssm-ID: 380493 [Multi-domain]  Cd Length: 332  Bit Score: 249.64  E-value: 2.30e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        7 NIGAVL-------STKKHEQIFREAVNQANKRHF-TRKIQLQATSVTHRPNAIQ*ALSVCEDLISSQVYAILVSHPPAPT 78
Cdd:cd06269   1 TIGALLpvhdyleSGAKVLPAFELALSDVNSRPDlLPKTTLGLAIRDSECNPTQALLSACDLLAAAKVVAILGPGCSASA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       79 DhltptPISYTAGFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKK 158
Cdd:cd06269  81 A-----PVANLARHWDIPVLSYGATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEG 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      159 LETLLEGKESkskkrnyenldqlsydnkrgpKADKVLQFEPG-TKNLTALLLEAKELEARVIILSASEDDATAVYKSAA* 237
Cdd:cd06269 156 LEELFQEKGG---------------------LITSRQSFDENkDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKR 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      238 LD*TGAGYVWLVGEREIS-----GSALRYAPDGIIGLQLINGKNEsahisdavavvaqaihelfE*ENITDPPRGCVGNT 312
Cdd:cd06269 215 LDMTSKDYVWFVIDGEASssdehGDEARQAAEGAITVTLIFPVVK-------------------EFLKFSMELKLKSSKR 275

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3QEK_A      313 NIWKTGPLFKRVL*SSKYpDGVTgriefnedGDRKFaQYSI*NLQN---RKLVQVGIFNGS-YIIQN 375
Cdd:cd06269 276 KQGLNEEYELNNFAAFFY-DAVL--------ADRPG-QFSIINLQYteaGDYRKVGTWDSEgGLNMS 332
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 21-357 5.83e-37

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


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 136.75  E-value: 5.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A         21 FREAVNQANKRH---FTRKIQLQatsVTHRPNAIQ*ALSVCEDLISSQVYAILvshppAPTDHLTPTPISYTAGFYRIPV 97
Cdd:pfam01094   6 VRLAVEDINADPgllPGTKLEYI---ILDTCCDPSLALAAALDLLKGEVVAII-----GPSCSSVASAVASLANEWKVPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A         98 IGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETLLEgkeskskkrnyEN 177
Cdd:pfam01094  78 ISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALR-----------ER 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        178 LDQLSYDNKRGPKADkvlqfepgTKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TGAGYVWLVGEREISGS 257
Cdd:pfam01094 147 GIRVAYKAVIPPAQD--------DDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        258 ALRYAP-----DGIIGLQLINGKNES---------------------------AHISDAVAVVAQAIHELfe*eNITDPP 305
Cdd:pfam01094 219 VILNPStleaaGGVLGFRLHPPDSPEfseffweklsdekelyenlgglpvsygALAYDAVYLLAHALHNL----LRDDKP 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
3QEK_A        306 RGCVGNTNIWKTGPLFKRVL*SSKYpDGVTGRIEFNEDGDRKFAQYSI*NLQ 357
Cdd:pfam01094 295 GRACGALGPWNGGQKLLRYLKNVNF-TGLTGNVQFDENGDRINPDYDILNLN 345
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
 84-383 1.96e-19

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


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 88.84  E-value: 1.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       84 TPISYTAGFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETLL 163
Cdd:cd06366  84 EPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLEELL 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      164 EgkeskskKRNYENLDQLSYdnkrgpkadkvLQFEPGT--KNLtallleaKELEARVIILSASEDDATAVYKSAA*LD*T 241
Cdd:cd06366 164 E-------EANITIVATESF-----------SSEDPTDqlENL-------KEKDARIIIGLFYEDAARKVFCEAYKLGMY 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      242 GAGYVWL-----------VGEREISGS------------ALRYAPDGIIGLQLINGK--------------NESAHIS-- 282
Cdd:cd06366 219 GPKYVWIlpgwyddnwwdVPDNDVNCTpeqmlealeghfSTELLPLNPDNTKTISGLtaqeflkeylerlsNSNYTGSpy 298

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      283 -----DAVAVVAQAIHELFE*ENITDPPRGCVGNTNIwKTGPLFKRVL*SSKYpDGVTGRIEFNEDGDRKfAQYSI*NLQ 357
Cdd:cd06366 299 apfayDAVWAIALALNKTIEKLAEYNKTLEDFTYNDK-EMADLFLEAMNSTSF-EGVSGPVSFDSKGDRL-GTVDIEQLQ 375

                       330       340
                ....*....|....*....|....*....
3QEK_A      358 NRKLVQVGIFN---GSYIIQNDRKIIWPG 383
Cdd:cd06366 376 GGSYVKVGLYDpnaDSLLLLNESSIVWPG 404
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
 6-366 6.53e-17

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of NMDA receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR2 subunit of NMDA receptor family. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 380601  Cd Length: 356  Bit Score: 81.19  E-value: 6.53e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        6 VNIGAVLSTKKHEQIFREAVNQANkRHFTRKIQLQATSVTHRPNAIQ*ALSVCEDLISSQVYAILVShppAPTDHLTPTP 85
Cdd:cd06378   3 LNIAVILPGTSFEVRIRSRLEPDA-FHGLPFEVSPITVLMNDTNPKSILTQICDLLSGRKVHGIVFE---DDTDQEAVAQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       86 ISY---TAGFYRIPVIGLTTR*SIySDKSIHLSFLRTVPPYSHQALVWFE**RLFNWnHVILIVSDDHEG-RAAQKKLET 161
Cdd:cd06378  79 ILDfisLQTYLPILGISGGSANVL-LDKEEGSTFLQLGPSIEQQATVMLNILEEYDW-HQFSVVTSLFPGyRDFVDAIRS 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      162 LLEGKESKSKKRNYENLDqLSYDnkrgpkadkvlqfEPGTKNLTALlleaKELEARVIILSASEDDATAVYKSAA*LD*T 241
Cdd:cd06378 157 TIDNSFVGWELQDVLTLD-MSND-------------GSDAKTLRQL----KKIEAQVILLYCTKEEAQYIFEAAEEAGLT 218

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      242 GAGYVWLVgereiSGSAL---RYAPD----GIIGLqLINGKNES--AHISDAVAVVAQAIHELFE*EN-ITDPPRGCVG- 310
Cdd:cd06378 219 GYGYVWIV-----PSLVLgntDPPPAefpvGLISV-HFDTWDYSlrARVRDGVAIIATGAEAMLSEHGfLPEPKSDCYAp 292

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
3QEK_A      311 NTNIWKTGPLFKRVL*SSKY--PDgvtgrIEFNEDGDRKFAQYSI*NLQN-RKLVQVGI 366
Cdd:cd06378 293 NETREPANETLHRYLINVTWegRD-----LSFNEDGYLVNPELVIINLNReRLWEKVGK 346
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
 91-357 2.72e-13

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


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 70.79  E-value: 2.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       91 GFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETLLegkesks 170
Cdd:cd06362 128 RLFKIPQISYASTSDELSDKERYPYFLRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGSYGEEGYKAFKKLA------- 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      171 KKRN-----YENLDQLSYDNkrgpKADKVLQfepgtknltaLLLEAKelEARVIILSASEDDATAVYKSAA*LD*TGaGY 245
Cdd:cd06362 201 RKAGiciaeSERISQDSDEK----DYDDVIQ----------KLLQKK--NARVVVLFADQEDIRGLLRAAKRLGASG-RF 263

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      246 VWL----VGEREIS-GSALRYAPDGI-IGL-------------------------------------------------- 269
Cdd:cd06362 264 IWLgsdgWGTNIDDlKGNEDVALGALtVQPyseevprfddyfksltpsnntrnpwfrefwqelfqcsfrpsrenscnddk 343

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      270 QLINGKNESAHIS------DAVAVVAQAIHELFE*ENITDPPRGCVGNTNIWKtGPLFKRVL*SSKYPDGVTGRIEFNED 343
Cdd:cd06362 344 LLINKSEGYKQESkvsfviDAVYAFAHALHKMHK-DLCPGDTGLCQDLMKCID-GSELLEYLLNVSFTGEAGGEIRFDEN 421

                       330
                ....*....|....
3QEK_A      344 GDRKfAQYSI*NLQ 357
Cdd:cd06362 422 GDGP-GRYDIMNFQ 434
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
 93-285 5.69e-11

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


Pssm-ID: 380573  Cd Length: 350  Bit Score: 63.08  E-value: 5.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       93 YRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETLLEGKE---SK 169
Cdd:cd06350 117 FKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVSTVYSDDDYGRSGIEAFEREAKERGiciAQ 196

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      170 SKKRNYENLDQlsydnkrgpKADKVLQfepgtknltalLLEAKElEARVIILSASEDDATAVYKSAA*LD*TgaGYVWLV 249
Cdd:cd06350 197 TIVIPENSTED---------EIKRIID-----------KLKSSP-NAKVVVLFLTESDARELLKEAKRRNLT--GFTWIG 253

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
3QEK_A      250 ----GEREISGSALRYAPDGIIGLQL----ING-----KNESAHISDAV 285
Cdd:cd06350 254 sdgwGDSLVILEGYEDVLGGAIGVVPrskeIPGfddylKSYAPYVIDAV 302
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
 7-368 2.02e-10

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


Pssm-ID: 380645 [Multi-domain]  Cd Length: 373  Bit Score: 61.86  E-value: 2.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        7 NIGAVL---STKKHEQI--FREAVNQANKRHFTRKIQLqatsVTH----RPNAIQ*ALSVcEDLISS-QVYAILVshppa 76
Cdd:cd19990   1 KIGAILdlnSRVGKEAKvaIEMAVSDFNSDSSSYGTKL----VLHvrdsKGDPLQAASAA-LDLIKNkKVEAIIG----- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       77 PTDHLTPTPISYTAGFYRIPVIGLT-TR*SIYSDKSIHlsFLRTVPPYSHQ-----ALVWFe**rlFNWNHVILIVSDDH 150
Cdd:cd19990  71 PQTSEEASFVAELGNKAQVPIISFSaTSPTLSSLRWPF--FIRMTHNDSSQmkaiaAIVQS-----YGWRRVVLIYEDDD 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      151 EGRAAQKKLETLLEGKESKskkrnYENLDQLSydnkrgPKADKvlqfepgtKNLTALLLEAKELEARVIILSASEDDATA 230
Cdd:cd19990 144 YGSGIIPYLSDALQEVGSR-----IEYRVALP------PSSPE--------DSIEEELIKLKSMQSRVFVVHMSSLLASR 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      231 VYKSAA*LD*TGAGYVWLVGER-----EISGSALRYAPDGIIGL---------------------QLINGKNESAHIS-- 282
Cdd:cd19990 205 LFQEAKKLGMMEKGYVWIVTDGitnllDSLDSSTISSMQGVIGIktyipessefqdfkarfrkkfRSEYPEEENAEPNiy 284

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      283 -----DAVAVVAQAIHELFE*EnitdpprgcvGNTNIWKTGPLFKRVL*SSKYpDGVTGRIEFNEDGDRKFAQYSI*NLQ 357
Cdd:cd19990 285 alrayDAIWALAHAVEKLNSSG----------GNISVSDSGKKLLEEILSTKF-KGLSGEVQFVDGQLAPPPAFEIVNVI 353

                       410
                ....*....|.
3QEK_A      358 NRKLVQVGIFN 368
Cdd:cd19990 354 GKGYRELGFWS 364
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
 91-345 8.24e-10

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


Pssm-ID: 380584 [Multi-domain]  Cd Length: 401  Bit Score: 60.08  E-value: 8.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       91 GFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAqkkLETLLEGKESKS 170
Cdd:cd06361 122 NLQLIPQISYESSAPILSDKLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDDDYGRSA---LESFIIQAEAEN 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      171 -----KKRNYENLDqlsyDNKRGPKADKVLQfepgtknltALLLEAKeleARVIILSASEDDATAVYKSAA*LD*TgagY 245
Cdd:cd06361 199 vciafKEVLPAYLS----DPTMNVRINDTIQ---------TIQSSSQ---VNVVVLFLKPSLVKKLFKEVIERNIS---K 259

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      246 VWLVGEREISGSALRYAPD-----GIIGLQLINGKNESAH----------ISDAVAVVAQAIHELFE*enitdppRGCVG 310
Cdd:cd06361 260 IWIASDNWSTAREILKMPNinkvgKILGFTFKSGNISSFHnylknlliysIQLAVTAIANALRKLCCE-------RGCQD 332

                       250       260       270
                ....*....|....*....|....*....|....*...
3QEK_A      311 NTNI--WKtgpLFKrVL*SSKYPDGvtGR-IEFNEDGD 345
Cdd:cd06361 333 PTAFqpWE---LLK-ELKKVTFTDD--GEtYHFDANGD 364
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
 84-371 2.97e-09

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


Pssm-ID: 380575 [Multi-domain]  Cd Length: 391  Bit Score: 58.14  E-value: 2.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       84 TPISYTAGFYRIPVI--GLTTR*SiySDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEG-RAAQKKLE 160
Cdd:cd06352  83 DAVGRLATYWNIPIItwGAVSASF--LDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDDSKcFSIANDLE 160

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      161 TLLegkeskskkrNYENLDQLSYdnkrgpkadKVLQFEPGTKNLTALLLEAKElEARVIILSASEDDATAVYKSAA*LD* 240
Cdd:cd06352 161 DAL----------NQEDNLTISY---------YEFVEVNSDSDYSSILQEAKK-RARIIVLCFDSETVRQFMLAAHDLGM 220

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      241 TGAGYVWL-VGEREISGS----------------ALRYApDGIIGLQLINGKNE-------------------------- 277
Cdd:cd06352 221 TNGEYVFIfIELFKDGFGgnstdgwerndgrdedAKQAY-ESLLVISLSRPSNPeydnfskevkarakeppfycydasee 299

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      278 -----SAHISDAVAVVAQAIHE-LFE*ENITDpprgcvgNTNIWKtgPLFKRVL*sskypDGVTGRIEFNEDGDRKFaQY 351
Cdd:cd06352 300 evspyAAALYDAVYLYALALNEtLAEGGNYRN-------GTAIAQ--RMWNRTF------QGITGPVTIDSNGDRDP-DY 363

                       330       340
                ....*....|....*....|..
3QEK_A      352 SI*NLQ--NRKLVQVGIFNGSY 371
Cdd:cd06352 364 ALLDLDpsTGKFVVVLTYDGTS 385
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
 91-381 9.02e-09

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


Pssm-ID: 380586 [Multi-domain]  Cd Length: 418  Bit Score: 56.93  E-value: 9.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       91 GFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETLLEGkesks 170
Cdd:cd06363 129 GFFLMPQISYGASSEELSNKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAAN----- 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      171 kkRN----YEnlDQLSYDNKRGPKADKVLqfepgtKNLtallleaKELEARVIILSASEDDATAVYKSAA*LD*TGAgyV 246
Cdd:cd06363 204 --TGicvaYQ--GLIPTDTDPKPKYQDIL------KKI-------NQTKVNVVVVFAPKQAAKAFFEEVIRQNLTGK--V 264

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      247 WLVGEreisGSALRYAPDGIIGLQLING------------------KNESAHISDAVAVVAQAIHELFe*enitdpprGC 308
Cdd:cd06363 265 WIASE----AWSLNDTVTSLPGIQSIGTvlgfaiqtgtlpgfqefiYAFAFSVYAAVYAVAHALHNLL----------GC 330

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      309 vgNTNIWKTGPLFK-----RVL*SSKYP-DGVTgrIEFNEDGDRKFAQYSI*---NLQNRKLVQVGIFNgSYIIQ---ND 376
Cdd:cd06363 331 --NSGACPKGRVVYpwqllEELKKVNFTlLNQT--IRFDENGDPNFGYDIVQwiwNNSSWTFEVVGSYS-TYPIQltiNE 405


                ....*
3QEK_A      377 RKIIW 381
Cdd:cd06363 406 SKIKW 410
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
 93-271 4.47e-08

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


Pssm-ID: 380598 [Multi-domain]  Cd Length: 462  Bit Score: 54.83  E-value: 4.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       93 YRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGraaqkklETLLEGKESKSKK 172
Cdd:cd06375 133 FQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYG-------ETGIEAFEQEARL 205

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      173 RNYenldQLSYDNKRGPKADKVLqFEPGTKNLTallleaKELEARVIILSASEDDATAVYKSAA*LD*tgAGYVWLV--- 249
Cdd:cd06375 206 RNI----CIATAEKVGRSADRKS-FDGVIRELL------QKPNARVVVLFTRSDDARELLAAAKRLN---ASFTWVAsdg 271

                       170       180
                ....*....|....*....|...
3QEK_A      250 -GEREISGSALRYAPDGIIGLQL 271
Cdd:cd06375 272 wGAQESIVKGSEDVAEGAITLEL 294
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
 201-357 5.17e-07

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 subunits of Kainate receptor; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 subunits of Kainate receptor. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. There are five types of kainate receptors, GluR5, GluR6, GluR7, KA1, and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMPA receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined.


Pssm-ID: 380616  Cd Length: 379  Bit Score: 51.06  E-value: 5.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      201 TKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TGAGYVWLVGEREISGSALRYAPD---GIIGLQLINGKN- 276
Cdd:cd06394 174 SRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDdqsNILGFSMFNTSHp 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      277 ---------------------------ESAHISDAVAVVAQAIHELFE*ENITDPPRGCvGNTNIWKTGPLFKRVL*SSK 329
Cdd:cd06394 254 fylefvrslnmswrencdastypgpalSSALMFDAVHVVVSAVRELNRSQEIGVKPLSC-TSAQIWQHGTSLMNYLRMVE 332

                       170       180
                ....*....|....*....|....*...
3QEK_A      330 YpDGVTGRIEFNEDGDRkfAQYSI*NLQ 357
Cdd:cd06394 333 Y-DGLTGRVEFNSKGQR--TNYTLRILE 357
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
 86-166 1.30e-06

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


Pssm-ID: 380587 [Multi-domain]  Cd Length: 473  Bit Score: 49.95  E-value: 1.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       86 ISYTAGFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQA-----LVwfe**RLFNWNHVILIVSDDHEGRAAQKKLE 160
Cdd:cd06364 116 VARTLGLFYIPQVSYFASCACLSDKKQFPSFLRTIPSDYYQSralaqLV-----KHFGWTWVGAIASDDDYGRNGIKAFL 190


                ....*.
3QEK_A      161 TLLEGK 166
Cdd:cd06364 191 EEAEKL 196
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
 7-368 1.45e-06

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors, non-NMDA ionotropic receptors which respond to the neurotransmitter glutamate. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Kainate receptors have five subunits, GluR5, GluR6, GluR7, KA1 and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined.


Pssm-ID: 380605  Cd Length: 335  Bit Score: 49.53  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A        7 NIGAVL--STKKHEQIFREAVNQANKRHFTRKIQLQATSV-THRPNAIQ*ALSVCeDLISSQVYAILvshppAPTDHLTP 83
Cdd:cd06382   1 RIGGIFdeDDEDLEIAFKYAVDRINRERTLPNTKLVPDIErVPRDDSFEASKKVC-ELLEEGVAAIF-----GPSSPSSS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       84 TPISYTAGFYRIPVIglTTR*SIYSDKSIHLSFlrTVPPySHQAL--VWFE**RLFNWNHVILIVSDDHEGRAAQKKLet 161
Cdd:cd06382  75 DIVQSICDALEIPHI--ETRWDPKESNRDTFTI--NLYP-DPDALskAYADLVKSLNWKSFTILYEDDEGLIRLQELL-- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      162 llegkesKSKKRNYENLdqlsydnkrgpkadKVLQFEPGtKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*T 241
Cdd:cd06382 148 -------KLPKPKDIPI--------------TVRQLDPG-DDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGML 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      242 GAGYVWLVGEREIS---GSALRYAPDGIIGLQLINGKNESahisdavavVAQAIHELFE*ENITDPPRGcvgNTNIWKTG 318
Cdd:cd06382 206 TEYYHYILTNLDLHtldLEPFKYSGANITGFRLVDPENPE---------VKNVLKDWSKREKEGFNKDI---GPGQITTE 273

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
3QEK_A      319 P--------LFKRVL*sskypDGVTGRIEFNEDGDRKFAQYSI*NLQNRKLVQVGIFN 368
Cdd:cd06382 274 TalmydavnLFANALK-----EGLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGTWN 326
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
 93-345 2.34e-06

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


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 48.77  E-value: 2.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       93 YRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE*-*RLFNWNHVILIVSDDHEGRAAQKKLETLLEgkesksk 171
Cdd:COG0683  94 AGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADYlAKKLGAKKVALLYDDYAYGQGLAAAFKAALK------- 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      172 krnyenldqlsydnKRGPKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAA*LD*TGAGYVWLVGE 251
Cdd:COG0683 167 --------------AAGGEVVGEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGLKGPLNKAFVKA 232

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      252 -REISGSalryAPDGIiglqlingkneSAHISDAVAVVAQAIhelfE*ENITDPPRgcvgntniwktgplFKRVL*SSKY 330
Cdd:COG0683 233 yKAKYGR----EPSSY-----------AAAGYDAALLLAEAI----EKAGSTDREA--------------VRDALEGLKF 279

                       250
                ....*....|....*
3QEK_A      331 pDGVTGRIEFNEDGD 345
Cdd:COG0683 280 -DGVTGPITFDPDGQ 293
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
 93-376 7.44e-06

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


Pssm-ID: 380597 [Multi-domain]  Cd Length: 474  Bit Score: 47.72  E-value: 7.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       93 YRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETL--LEGKESKS 170
Cdd:cd06374 141 FHIPQIGYSATSIDLSDKSLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELaaEEGICIAH 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      171 KKRNYENLDQLSYDN------KRGPKADKVLQFEPGTkNLTALLLEAKELEAR---VIILS---ASEDDATAVYKSAA*- 237
Cdd:cd06374 221 SDKIYSNAGEEEFDRllrklmNTPNKARVVVCFCEGE-TVRGLLKAMRRLNATghfLLIGSdgwADRKDVVEGYEDEAAg 299

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      238 -------------LD--------*TGAGYVWLvgeRE---------ISGSalryaPDGIIGLQLINGKNESAHIS----- 282
Cdd:cd06374 300 gitikihspevesFDeyyfnlkpETNSRNPWF---REfwqhrfdcrLPGH-----PDENPYFKKCCTGEESLLGNyvqds 371

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      283 ------DAVAVVAQAIHELFE*ENITDPPRGCVGNTNIwkTGPLFKRVL*SSKYPDGVTGRIEFNEDGDRKfAQYSI*NL 356
Cdd:cd06374 372 klgfviNAIYAMAHALHRMQEDLCGGYSVGLCPAMLPI--NGSLLLDYLLNVSFVGVSGDTIMFDENGDPP-GRYDIMNF 448

                       330       340
                ....*....|....*....|....*
3QEK_A      357 QNRK-----LVQVGIFNGSYIIQND 376
Cdd:cd06374 449 QKTGegsydYVQVGSWKNGSLKMDD 473
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
 91-381 2.32e-05

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


Pssm-ID: 380588 [Multi-domain]  Cd Length: 464  Bit Score: 46.10  E-value: 2.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       91 GFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDD----HEGRAAQKKL------- 159
Cdd:cd06365 121 GLYKYPQISYGAFDPLLSDKVQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDDdygeQFSQDLKKEMekngicv 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      160 ---ETLLEGKESKSKKRNYENLDQLSydnkrgpkadkvlqfepgtknltallleakeleARVIILSASEDDATAVykSAA 236
Cdd:cd06365 201 afvEKIPTNSSLKRIIKYINQIIKSS---------------------------------ANVIIIYGDTDSLLEL--LFR 245

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      237 *LD*TGAGYVWLV-------------------G-------EREISG--------SALRYaPDGII--------------- 267
Cdd:cd06365 246 LWEQLVTGKVWITtsqwdistlpfefylnlfnGtlgfsqhSGEIPGfkeflqsvHPSKY-PEDIFlktlwesyfnckwpd 324

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      268 ----GLQLINGKNE----------------SAHISDAVAVVAQAIHELFE*EnITDPPRGCVGNTNI--WKTGPLFKRVl 325
Cdd:cd06365 325 qnckSLQNCCGNESletldvhsfdmtmsrlSYNVYNAVYAVAHALHEMLLCQ-PKTGPGNCSDRRNFqpWQLHHYLKKV- 402

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3QEK_A      326 *ssKYPDGVTGRIEFNEDGDRKfAQYSI*NLQNR-----KLVQVGIF-----NGSYIIQNDRKIIW 381
Cdd:cd06365 403 ---QFTNPAGDEVNFDEKGDLP-TKYDILNWQIFpngtgTKVKVGTFdpsapSGQQLIINDSMIEW 464
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
 85-247 3.42e-04

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


Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 42.54  E-value: 3.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       85 PISYTAGFYRIPVI-------GLTTR*SIYSdksiHLSflRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEgraaQK 157
Cdd:cd06386  87 PVARLASHWNLPMLsagalaaGFSHKDSEYS----HLT--RVAPAYAKMGEMFLALFRHHHWSRAFLVYSDDKL----ER 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      158 KLETLLEGKESKSKKRNYeNLDQLSYDNKRGPKADKVLQfepgtknltalLLEAKEleaRVIILSASEDDATAVYKSAA* 237
Cdd:cd06386 157 NCYFTLEGVHEVFQEEGL-HTSIYSFDETKDLDLEEIVR-----------NIQASE---RVVIMCASSDTIRSIMLVAHR 221

                       170
                ....*....|
3QEK_A      238 LD*TGAGYVW 247
Cdd:cd06386 222 HGMTNGDYAF 231
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
 84-226 6.89e-04

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


Pssm-ID: 380596 [Multi-domain]  Cd Length: 394  Bit Score: 41.49  E-value: 6.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A       84 TPISYTAGFYRIPVIGLTTR*SIYSDKSIHLSFLRTVPPYSHQALVWFE**RLFNWNHVILIVSDDHEGRAAQKKLETLL 163
Cdd:cd06373  81 APVARYAGHWNVPVLTAGGLAAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVALLYHDNLRRKAGNSNCYFTL 160

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3QEK_A      164 EG-----KESKSKkrnyenlDQLSYDnkrgpkadkvlQFEPGTKNLTALLLEAKeLEARVIILSASED 226
Cdd:cd06373 161 EGifnalTGERDS-------IHKSFD-----------EFDETKDDFEILLKRVS-NSARIVILCASPD 209
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
 283-353 4.24e-03

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


Pssm-ID: 380565 [Multi-domain]  Cd Length: 334  Bit Score: 38.66  E-value: 4.24e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3QEK_A      283 DAVAVVAQAIhelfE*ENITDPprgcvgntniwktgplfKRV---L*SSKYpDGVTGRIEFNEDGDRKFAQYSI 353
Cdd:cd06342 280 DAAQVLLAAI----EKAGSTDR-----------------AAVaaaLRATDF-DGVTGTISFDAKGDLTGPAFTV 331
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
 275-366 9.39e-03

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 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. 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: 380603 [Multi-domain]  Cd Length: 390  Bit Score: 37.64  E-value: 9.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3QEK_A      275 KNESAHISDAVAVVAQA-----------IHELFE*ENITDPPRG--C-VGNTNIWKTGPLFKRVL*SSKYpDGVTGRIEF 340
Cdd:cd06380 274 PYEAALAVDAVLVIAEAfqsllrqnddiFRFTFHGELYNNGSKGidCdPNPPLPWEHGKAIMKALKKVRF-EGLTGNVQF 352

                        90       100
                ....*....|....*....|....*....
3QEK_A      341 NEDGDRKfaQYSI*NLQ---NRKLVQVGI 366
Cdd:cd06380 353 DDFGQRK--NYTLDVIEltsNRGLRKIGT 379
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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