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Conserved domains on  [gi|530399104|ref|XP_005253408|]
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glutamate receptor ionotropic, NMDA 2B isoform X1 [Homo sapiens]

Protein Classification

Periplasmic_Binding_Protein_Type_2 and NMDAR2_C domain-containing protein( domain architecture ID 10403469)

Periplasmic_Binding_Protein_Type_2 and NMDAR2_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NMDAR2_C pfam10565
N-methyl D-aspartate receptor 2B3 C-terminus; This domain is found at the C-terminus of many ...
102-746 0e+00

N-methyl D-aspartate receptor 2B3 C-terminus; This domain is found at the C-terminus of many NMDA-receptor proteins, many of which also carry the Ligated ion-channel family pfam00060 further upstream as well as the ANF_receptor family pfam01094. This region is predicted to be a large extra-cellular domain of the NMDA receptor proteins, being highly hydrophilic, and is thought to be integrally involved in the function of the receptor. The region also carries a number of potential N-glycosylation sites.


:

Pssm-ID: 463148  Cd Length: 634  Bit Score: 766.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  102 HLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSvmnSPTATMNNTHSNILRLLRTAKNMANLSGVNG--S 179
Cdd:pfam10565   1 HLFYWKLRFCFTGVCSGRPGLLFSISRGIYSCIHGVHIEEKKK---SPDFTFNNTQSNMLKLLRTAKNMTNMSNLNGsnS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  180 PQSALDFIRRESSVYDISEHRRSFTHSDCKSYnnpPCEENLFSDYISEVERTFGNLQLKDSNVYQ-----DHYHHHHRPH 254
Cdd:pfam10565  78 PKRALDFIQRGSLIMDMVEDKGNLVHSDNRSY---QPKDNLFSDNISELQRFFGNRHKDNLNNYVfqgqhPLTLNESNPN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  255 SIGSASSIDGlydcdnPPFTTQSRSISKKPLDIGL--PSSKHSQLSDLYGKFSFKSDRYSGhDDLIRSDVSDISTHTVTY 332
Cdd:pfam10565 155 TVEVAVSAEG------GKFNSKPRQLWKKSVETLRqsQSSFPEGLAEEYGKFSFKSQRYLP-EENIHSDVSDISSRAVSY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  333 GNIEGNAakrRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPprspdHKRYFRDKEGLRD-----FYLDQFRTKENSPH 407
Cdd:pfam10565 228 KDPENNA---KHHKPKDNLKKRSVSSKYPRDCSEVELSYLKRK-----QHGSPRDKIYTIDsdkpsFHLDQPRYRENVGL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  408 WEHVDLTDIYKERSDDFKRDSVSGGGPctNRSHI-----------------KHGTGDKHGVVS---GVPAPWEKNLTnve 467
Cdd:pfam10565 300 WEDLDYPDIYQDHNDNYRKDGAPGLHL--NRSPLhhedslpnddqyklyskHYSLKEKNGGASpseSNDRYRQNSTH--- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  468 wedrsggnfCRSCPSKLHNYSttvtGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAApVAVTSNASTTKYPQSP 547
Cdd:pfam10565 375 ---------CRSCLSKLPNYS----GHYTGRSPYNRCDACLHMGNLYDISEDQMLQEAINPAT-HAGGKGHSEDMFGHYW 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  548 TNSKA---QKKNRNKLRRQHSYDTFVDLQKEEAALAP-RSVSLKDKGRFMDGSPYAHMFEMSAgESTFANNKSSVPtagh 623
Cdd:pfam10565 441 PQSDAlhvQKKNRLRLSRQHSYDNIVDKPKEIDLGRPaRSVSLKEKDRFLEDSPYANMFEMRS-EKLLGSRSSLLN---- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  624 hhHNNPGGGYmlSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVagASKARPD--FRALVTNKPVVSALHGavp 701
Cdd:pfam10565 516 --HNLEESKR--SKSLYPDHVSDNPFLPSFRDDQRLLHGRSSSDIYKQSA--PSKGRNDnyFRSSVKSTASYCSRDG--- 586
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 530399104  702 aRFQKDICIGNQSNPCVPNNKN----PRAFNGSSNGHVYEKLSSIESDV 746
Cdd:pfam10565 587 -RVPNDMYISEHVMPYVANKNSlysaPRVFNSCSNRRVYKKMPSIESDV 634
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
1-65 5.91e-38

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd13718:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 283  Bit Score: 142.86  E-value: 5.91e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530399104   1 MAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHN 65
Cdd:cd13718  219 MAGQDEGCKLVTIGSGKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLTGICHN 283
 
Name Accession Description Interval E-value
NMDAR2_C pfam10565
N-methyl D-aspartate receptor 2B3 C-terminus; This domain is found at the C-terminus of many ...
102-746 0e+00

N-methyl D-aspartate receptor 2B3 C-terminus; This domain is found at the C-terminus of many NMDA-receptor proteins, many of which also carry the Ligated ion-channel family pfam00060 further upstream as well as the ANF_receptor family pfam01094. This region is predicted to be a large extra-cellular domain of the NMDA receptor proteins, being highly hydrophilic, and is thought to be integrally involved in the function of the receptor. The region also carries a number of potential N-glycosylation sites.


Pssm-ID: 463148  Cd Length: 634  Bit Score: 766.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  102 HLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSvmnSPTATMNNTHSNILRLLRTAKNMANLSGVNG--S 179
Cdd:pfam10565   1 HLFYWKLRFCFTGVCSGRPGLLFSISRGIYSCIHGVHIEEKKK---SPDFTFNNTQSNMLKLLRTAKNMTNMSNLNGsnS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  180 PQSALDFIRRESSVYDISEHRRSFTHSDCKSYnnpPCEENLFSDYISEVERTFGNLQLKDSNVYQ-----DHYHHHHRPH 254
Cdd:pfam10565  78 PKRALDFIQRGSLIMDMVEDKGNLVHSDNRSY---QPKDNLFSDNISELQRFFGNRHKDNLNNYVfqgqhPLTLNESNPN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  255 SIGSASSIDGlydcdnPPFTTQSRSISKKPLDIGL--PSSKHSQLSDLYGKFSFKSDRYSGhDDLIRSDVSDISTHTVTY 332
Cdd:pfam10565 155 TVEVAVSAEG------GKFNSKPRQLWKKSVETLRqsQSSFPEGLAEEYGKFSFKSQRYLP-EENIHSDVSDISSRAVSY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  333 GNIEGNAakrRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPprspdHKRYFRDKEGLRD-----FYLDQFRTKENSPH 407
Cdd:pfam10565 228 KDPENNA---KHHKPKDNLKKRSVSSKYPRDCSEVELSYLKRK-----QHGSPRDKIYTIDsdkpsFHLDQPRYRENVGL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  408 WEHVDLTDIYKERSDDFKRDSVSGGGPctNRSHI-----------------KHGTGDKHGVVS---GVPAPWEKNLTnve 467
Cdd:pfam10565 300 WEDLDYPDIYQDHNDNYRKDGAPGLHL--NRSPLhhedslpnddqyklyskHYSLKEKNGGASpseSNDRYRQNSTH--- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  468 wedrsggnfCRSCPSKLHNYSttvtGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAApVAVTSNASTTKYPQSP 547
Cdd:pfam10565 375 ---------CRSCLSKLPNYS----GHYTGRSPYNRCDACLHMGNLYDISEDQMLQEAINPAT-HAGGKGHSEDMFGHYW 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  548 TNSKA---QKKNRNKLRRQHSYDTFVDLQKEEAALAP-RSVSLKDKGRFMDGSPYAHMFEMSAgESTFANNKSSVPtagh 623
Cdd:pfam10565 441 PQSDAlhvQKKNRLRLSRQHSYDNIVDKPKEIDLGRPaRSVSLKEKDRFLEDSPYANMFEMRS-EKLLGSRSSLLN---- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  624 hhHNNPGGGYmlSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVagASKARPD--FRALVTNKPVVSALHGavp 701
Cdd:pfam10565 516 --HNLEESKR--SKSLYPDHVSDNPFLPSFRDDQRLLHGRSSSDIYKQSA--PSKGRNDnyFRSSVKSTASYCSRDG--- 586
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 530399104  702 aRFQKDICIGNQSNPCVPNNKN----PRAFNGSSNGHVYEKLSSIESDV 746
Cdd:pfam10565 587 -RVPNDMYISEHVMPYVANKNSlysaPRVFNSCSNRRVYKKMPSIESDV 634
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
1-65 5.91e-38

The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the NR2 subunit of NMDA receptor family. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors 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: 270436 [Multi-domain]  Cd Length: 283  Bit Score: 142.86  E-value: 5.91e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530399104   1 MAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHN 65
Cdd:cd13718  219 MAGQDEGCKLVTIGSGKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLTGICHN 283
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
1-90 1.03e-25

Ligand-gated ion channel; This family includes the four transmembrane regions of the ionotropic glutamate receptors and NMDA receptors.


Pssm-ID: 459656 [Multi-domain]  Cd Length: 267  Bit Score: 107.01  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104    1 MAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGI--CHNEKNEVMSSQLDID 78
Cdd:pfam00060 176 NYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSgeCDSKSSASSSSQLGLK 255
                          90
                  ....*....|..
gi 530399104   79 NMAGVFYMLGAA 90
Cdd:pfam00060 256 SFAGLFLILGIG 267
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
8-61 4.58e-10

Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic homologues are represented by a separate alignment: PBPb


Pssm-ID: 197504 [Multi-domain]  Cd Length: 133  Bit Score: 58.07  E-value: 4.58e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530399104     8 CKLVTIGSgkVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTG 61
Cdd:smart00079  82 CDLMTVGE--EFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
 
Name Accession Description Interval E-value
NMDAR2_C pfam10565
N-methyl D-aspartate receptor 2B3 C-terminus; This domain is found at the C-terminus of many ...
102-746 0e+00

N-methyl D-aspartate receptor 2B3 C-terminus; This domain is found at the C-terminus of many NMDA-receptor proteins, many of which also carry the Ligated ion-channel family pfam00060 further upstream as well as the ANF_receptor family pfam01094. This region is predicted to be a large extra-cellular domain of the NMDA receptor proteins, being highly hydrophilic, and is thought to be integrally involved in the function of the receptor. The region also carries a number of potential N-glycosylation sites.


Pssm-ID: 463148  Cd Length: 634  Bit Score: 766.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  102 HLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSvmnSPTATMNNTHSNILRLLRTAKNMANLSGVNG--S 179
Cdd:pfam10565   1 HLFYWKLRFCFTGVCSGRPGLLFSISRGIYSCIHGVHIEEKKK---SPDFTFNNTQSNMLKLLRTAKNMTNMSNLNGsnS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  180 PQSALDFIRRESSVYDISEHRRSFTHSDCKSYnnpPCEENLFSDYISEVERTFGNLQLKDSNVYQ-----DHYHHHHRPH 254
Cdd:pfam10565  78 PKRALDFIQRGSLIMDMVEDKGNLVHSDNRSY---QPKDNLFSDNISELQRFFGNRHKDNLNNYVfqgqhPLTLNESNPN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  255 SIGSASSIDGlydcdnPPFTTQSRSISKKPLDIGL--PSSKHSQLSDLYGKFSFKSDRYSGhDDLIRSDVSDISTHTVTY 332
Cdd:pfam10565 155 TVEVAVSAEG------GKFNSKPRQLWKKSVETLRqsQSSFPEGLAEEYGKFSFKSQRYLP-EENIHSDVSDISSRAVSY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  333 GNIEGNAakrRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPprspdHKRYFRDKEGLRD-----FYLDQFRTKENSPH 407
Cdd:pfam10565 228 KDPENNA---KHHKPKDNLKKRSVSSKYPRDCSEVELSYLKRK-----QHGSPRDKIYTIDsdkpsFHLDQPRYRENVGL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  408 WEHVDLTDIYKERSDDFKRDSVSGGGPctNRSHI-----------------KHGTGDKHGVVS---GVPAPWEKNLTnve 467
Cdd:pfam10565 300 WEDLDYPDIYQDHNDNYRKDGAPGLHL--NRSPLhhedslpnddqyklyskHYSLKEKNGGASpseSNDRYRQNSTH--- 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  468 wedrsggnfCRSCPSKLHNYSttvtGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAApVAVTSNASTTKYPQSP 547
Cdd:pfam10565 375 ---------CRSCLSKLPNYS----GHYTGRSPYNRCDACLHMGNLYDISEDQMLQEAINPAT-HAGGKGHSEDMFGHYW 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  548 TNSKA---QKKNRNKLRRQHSYDTFVDLQKEEAALAP-RSVSLKDKGRFMDGSPYAHMFEMSAgESTFANNKSSVPtagh 623
Cdd:pfam10565 441 PQSDAlhvQKKNRLRLSRQHSYDNIVDKPKEIDLGRPaRSVSLKEKDRFLEDSPYANMFEMRS-EKLLGSRSSLLN---- 515
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104  624 hhHNNPGGGYmlSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVagASKARPD--FRALVTNKPVVSALHGavp 701
Cdd:pfam10565 516 --HNLEESKR--SKSLYPDHVSDNPFLPSFRDDQRLLHGRSSSDIYKQSA--PSKGRNDnyFRSSVKSTASYCSRDG--- 586
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*....
gi 530399104  702 aRFQKDICIGNQSNPCVPNNKN----PRAFNGSSNGHVYEKLSSIESDV 746
Cdd:pfam10565 587 -RVPNDMYISEHVMPYVANKNSlysaPRVFNSCSNRRVYKKMPSIESDV 634
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
1-65 5.91e-38

The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the NR2 subunit of NMDA receptor family. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors 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: 270436 [Multi-domain]  Cd Length: 283  Bit Score: 142.86  E-value: 5.91e-38
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530399104   1 MAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHN 65
Cdd:cd13718  219 MAGQDEGCKLVTIGSGKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLTGICHN 283
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
1-90 1.03e-25

Ligand-gated ion channel; This family includes the four transmembrane regions of the ionotropic glutamate receptors and NMDA receptors.


Pssm-ID: 459656 [Multi-domain]  Cd Length: 267  Bit Score: 107.01  E-value: 1.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530399104    1 MAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGI--CHNEKNEVMSSQLDID 78
Cdd:pfam00060 176 NYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSgeCDSKSSASSSSQLGLK 255
                          90
                  ....*....|..
gi 530399104   79 NMAGVFYMLGAA 90
Cdd:pfam00060 256 SFAGLFLILGIG 267
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
1-59 1.02e-24

The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; The ligand-binding domain of the ionotropic NMDA subtype is structurally homologous to the periplasmic-binding fold type II superfamily, while the N-terminal domain belongs to the periplasmic-binding fold type I. 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: 270405 [Multi-domain]  Cd Length: 239  Bit Score: 103.49  E-value: 1.02e-24
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530399104   1 MAGRDEGCKLVTIGSgkVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWL 59
Cdd:cd13687  183 EASQDEGCKLVTVGS--LFARSGYGIGLQKNSPWKRNVSLAILQFHESGFMEELDKKWL 239
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
2-59 5.72e-12

The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic binding protein type II superfamily; This subfamily represents the ligand binding of ionotropic glutamate receptors. iGluRs are heterotetrameric ion channels that comprises of three functionally distinct subtypes based on their pharmacology and structural similarities: AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid), NMDA (N-methyl-D-aspartate), and kainate receptors. All three types of channels are also activated by the physiological neurotransmitter, glutamate. iGluRs are concentrated at postsynaptic sites, where they exert a variety of different functions. While this ligand-binding domain of iGluRs is structurally homologous to the periplasmic binding fold type II superfamily, the N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain belongs to the periplasmic-binding fold type I.


Pssm-ID: 270219 [Multi-domain]  Cd Length: 243  Bit Score: 66.24  E-value: 5.72e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530399104   2 AGRDEgCKLVTIGSGkvFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWL 59
Cdd:cd00998  189 ARQDP-CKLIKTGGG--FGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
8-61 4.58e-10

Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic homologues are represented by a separate alignment: PBPb


Pssm-ID: 197504 [Multi-domain]  Cd Length: 133  Bit Score: 58.07  E-value: 4.58e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530399104     8 CKLVTIGSgkVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTG 61
Cdd:smart00079  82 CDLMTVGE--EFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
8-58 1.64e-08

The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily; This subfamily represents the ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate receptors including AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) receptors (GluR1-4), kainate receptors (GluR5-7 and KA1/2), and orphan receptors delta 1/2. iGluRs form tetrameric ligand-gated ion channels, which are concentrated at postsynaptic sites in excitatory synapses where they fulfill a variety of different functions. While this ligand-binding domain of iGluRs is structurally homologous to the periplasmic binding fold type II superfamily, the N-terminal leucine/isoleucine/valine#binding protein (LIVBP)-like domain belongs to the periplasmic-binding fold type I.


Pssm-ID: 270403 [Multi-domain]  Cd Length: 252  Bit Score: 56.04  E-value: 1.64e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530399104   8 CKLVTIGSgkVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALW 58
Cdd:cd13685  202 CDLTKVGE--VFSEKGYGIAVQQGSPLRDELSLAILELQESGELEKLKEKW 250
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
2-59 1.70e-08

The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand binding domain of the NR1, an essential channel-forming subunit of the NMDA receptor. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors 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: 270437 [Multi-domain]  Cd Length: 277  Bit Score: 56.60  E-value: 1.70e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530399104   2 AGRDegCKLVTIGSgkVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWL 59
Cdd:cd13719  218 ASQD--CDLVTAGE--LFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWI 271
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
8-58 4.74e-05

The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270435 [Multi-domain]  Cd Length: 360  Bit Score: 46.14  E-value: 4.74e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530399104   8 CKLVTIGsgKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALW 58
Cdd:cd13717  310 CDLQEVG--EEFSRKPYAIAVQQGSPLKDELNYAILELQNDRFLEKLKAKW 358
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
8-58 2.49e-04

Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270432 [Multi-domain]  Cd Length: 251  Bit Score: 43.29  E-value: 2.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530399104   8 CKLVTIGSgkVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALW 58
Cdd:cd13714  201 CNLTQIGG--LLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKW 249
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
5-58 4.57e-03

The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the NR3 subunit of NMDA receptor family. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors 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: 270438 [Multi-domain]  Cd Length: 283  Bit Score: 39.84  E-value: 4.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530399104   5 DEGCKLVTIGsgKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALW 58
Cdd:cd13720  231 DADCKLLTVG--KPFAIEGYGIGLPQNSPLTSNISELISQYKSNGFMDLLHDKW 282
 
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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