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Conserved domains on  [gi|4504125|ref|NP_000824|]
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glutamate receptor ionotropic, NMDA 2A isoform 1 precursor [Homo sapiens]

Protein Classification

glutamate receptor ionotropic, NMDA 2( domain architecture ID 10157231)

glutamate receptor ionotropic, NMDA 2 is a component of NMDA (N-methyl-D-aspartate) receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium

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 ...
839-1464 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: 1066.36  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     839 HLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISSMSNMNssRMDSP 918
Cdd:pfam10565    1 HLFYWKLRFCFTGVCSGRPGLLFSISRGIYSCIHGVHIEEKKKSPDFTFNNTQSNMLKLLRTAKNMTNMSNLN--GSNSP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     919 KRAADFIQRGSLIMDMVSDKGNLMYSDNRSFQGKESIFGDNMNELQTFVANRQKDNLNNYVFQGQHPLTLNESNPNTVEV 998
Cdd:pfam10565   79 KRALDFIQRGSLIMDMVEDKGNLVHSDNRSYQPKDNLFSDNISELQRFFGNRHKDNLNNYVFQGQHPLTLNESNPNTVEV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     999 AVSTE-SKANSRPRQLWKKSVDSIRQdslsqNPVSQRDEATAENRTHSLKSPRYLPEEMAHSDISETSNRATCHREPD-N 1076
Cdd:pfam10565  159 AVSAEgGKFNSKPRQLWKKSVETLRQ-----SQSSFPEGLAEEYGKFSFKSQRYLPEENIHSDVSDISSRAVSYKDPEnN 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1077 SKNHKTKDNF-KRSVASKYPKDCSEVERTYLKTK-SSSPRDKIYTIDGEKePGFHLDPPQFVENVTLPENVDFPDPYQDP 1154
Cdd:pfam10565  234 AKHHKPKDNLkKRSVSSKYPRDCSEVELSYLKRKqHGSPRDKIYTIDSDK-PSFHLDQPRYRENVGLWEDLDYPDIYQDH 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1155 SENFRK-GDSTLPMNRNPLHNEEGLSNNDQYKLYSKHFTLKDKG--SPHSETSERYRQNSTHCRSCLSNMPTYSGHFTMR 1231
Cdd:pfam10565  313 NDNYRKdGAPGLHLNRSPLHHEDSLPNDDQYKLYSKHYSLKEKNggASPSESNDRYRQNSTHCRSCLSKLPNYSGHYTGR 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1232 SPF-KCDACLRMGNLYDIDEDQMLQETGNPAT-------GEQVYQQDWAQNNALQLQK-NKLRISRQHSYDNIVDKPREL 1302
Cdd:pfam10565  393 SPYnRCDACLHMGNLYDISEDQMLQEAINPAThaggkghSEDMFGHYWPQSDALHVQKkNRLRLSRQHSYDNIVDKPKEI 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1303 DLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGRC 1382
Cdd:pfam10565  473 DLGRPARSVSLKEKDRFLEDSPYANMFEMRSEKLLGSRSSLLNHNLEESKRSKSLYPDHVSDNPFLPSFRDDQRLLHGRS 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1383 PSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIES 1462
Cdd:pfam10565  553 SSDIYKQSAPSKGRNDNYFRSSVKSTASYCSRDGRVPNDMYISEHVMPYVANKNSLYSAPRVFNSCSNRRVYKKMPSIES 632

                   ..
gi 4504125    1463 DV 1464
Cdd:pfam10565  633 DV 634
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
32-387 0e+00

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: 603.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    32 PALNIAVMLGHSHdvTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQ 111
Cdd:cd06378    1 PSLNIAVILPGTS--FEVRIRSRLEPDAFHGLPFEVSPITVLMNDTNPKSILTQICDLLSGRKVHGIVFEDDTDQEAVAQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   112 MLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTV 191
Cdd:cd06378   79 ILDFISLQTYLPILGISGGSANVLLDKEEGSTFLQLGPSIEQQATVMLNILEEYDWHQFSVVTSLFPGYRDFVDAIRSTI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   192 DNSFVGWDMQNVITLDTSF--EDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIP 269
Cdd:cd06378  159 DNSFVGWELQDVLTLDMSNdgSDAKTLRQLKKIEAQVILLYCTKEEAQYIFEAAEEAGLTGYGYVWIVPSLVLGNTDPPP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   270 KEFPSGLISVSYDDWDYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGKDLS 349
Cdd:cd06378  239 AEFPVGLISVHFDTWDYSLRARVRDGVAIIATGAEAMLSEHGFLPEPKSDCYAPNETREPANETLHRYLINVTWEGRDLS 318
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 4504125   350 FTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRH 387
Cdd:cd06378  319 FNEDGYLVNPELVIINLNRERLWEKVGKWESGSLQMKY 356
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
403-802 0e+00

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: 551.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   403 DNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNST--NEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLV 480
Cdd:cd13718    1 KFHLKIVTLEEAPFVIVEPVDPLTGTCMRNTVPCRKQLNHENSTdaDENRYVKKCCKGFCIDILKKLAKDVGFTYDLYLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   481 TNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNgtvspsaflepfsasvwvm 560
Cdd:cd13718   81 TNGKHGKKINGVWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMVARSN------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   561 mfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnnsvpvqnpkgttskimvsvwaffavi 640
Cdd:cd13718      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   641 flasytanlaafmiqeefvdQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSL 720
Cdd:cd13718  142 --------------------QVSGLSDKKFQRPHDQSPPFRFGTVPNGSTERNIRNNYPEMHQYMRKYNQKGVEDALVSL 201
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   721 KTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGIC 800
Cdd:cd13718  202 KTGKLDAFIYDAAVLNYMAGQDEGCKLVTIGSGKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLTGIC 281

                 ..
gi 4504125   801 HN 802
Cdd:cd13718  282 HN 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 ...
839-1464 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: 1066.36  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     839 HLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISSMSNMNssRMDSP 918
Cdd:pfam10565    1 HLFYWKLRFCFTGVCSGRPGLLFSISRGIYSCIHGVHIEEKKKSPDFTFNNTQSNMLKLLRTAKNMTNMSNLN--GSNSP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     919 KRAADFIQRGSLIMDMVSDKGNLMYSDNRSFQGKESIFGDNMNELQTFVANRQKDNLNNYVFQGQHPLTLNESNPNTVEV 998
Cdd:pfam10565   79 KRALDFIQRGSLIMDMVEDKGNLVHSDNRSYQPKDNLFSDNISELQRFFGNRHKDNLNNYVFQGQHPLTLNESNPNTVEV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     999 AVSTE-SKANSRPRQLWKKSVDSIRQdslsqNPVSQRDEATAENRTHSLKSPRYLPEEMAHSDISETSNRATCHREPD-N 1076
Cdd:pfam10565  159 AVSAEgGKFNSKPRQLWKKSVETLRQ-----SQSSFPEGLAEEYGKFSFKSQRYLPEENIHSDVSDISSRAVSYKDPEnN 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1077 SKNHKTKDNF-KRSVASKYPKDCSEVERTYLKTK-SSSPRDKIYTIDGEKePGFHLDPPQFVENVTLPENVDFPDPYQDP 1154
Cdd:pfam10565  234 AKHHKPKDNLkKRSVSSKYPRDCSEVELSYLKRKqHGSPRDKIYTIDSDK-PSFHLDQPRYRENVGLWEDLDYPDIYQDH 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1155 SENFRK-GDSTLPMNRNPLHNEEGLSNNDQYKLYSKHFTLKDKG--SPHSETSERYRQNSTHCRSCLSNMPTYSGHFTMR 1231
Cdd:pfam10565  313 NDNYRKdGAPGLHLNRSPLHHEDSLPNDDQYKLYSKHYSLKEKNggASPSESNDRYRQNSTHCRSCLSKLPNYSGHYTGR 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1232 SPF-KCDACLRMGNLYDIDEDQMLQETGNPAT-------GEQVYQQDWAQNNALQLQK-NKLRISRQHSYDNIVDKPREL 1302
Cdd:pfam10565  393 SPYnRCDACLHMGNLYDISEDQMLQEAINPAThaggkghSEDMFGHYWPQSDALHVQKkNRLRLSRQHSYDNIVDKPKEI 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1303 DLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGRC 1382
Cdd:pfam10565  473 DLGRPARSVSLKEKDRFLEDSPYANMFEMRSEKLLGSRSSLLNHNLEESKRSKSLYPDHVSDNPFLPSFRDDQRLLHGRS 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1383 PSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIES 1462
Cdd:pfam10565  553 SSDIYKQSAPSKGRNDNYFRSSVKSTASYCSRDGRVPNDMYISEHVMPYVANKNSLYSAPRVFNSCSNRRVYKKMPSIES 632

                   ..
gi 4504125    1463 DV 1464
Cdd:pfam10565  633 DV 634
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
32-387 0e+00

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: 603.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    32 PALNIAVMLGHSHdvTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQ 111
Cdd:cd06378    1 PSLNIAVILPGTS--FEVRIRSRLEPDAFHGLPFEVSPITVLMNDTNPKSILTQICDLLSGRKVHGIVFEDDTDQEAVAQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   112 MLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTV 191
Cdd:cd06378   79 ILDFISLQTYLPILGISGGSANVLLDKEEGSTFLQLGPSIEQQATVMLNILEEYDWHQFSVVTSLFPGYRDFVDAIRSTI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   192 DNSFVGWDMQNVITLDTSF--EDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIP 269
Cdd:cd06378  159 DNSFVGWELQDVLTLDMSNdgSDAKTLRQLKKIEAQVILLYCTKEEAQYIFEAAEEAGLTGYGYVWIVPSLVLGNTDPPP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   270 KEFPSGLISVSYDDWDYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGKDLS 349
Cdd:cd06378  239 AEFPVGLISVHFDTWDYSLRARVRDGVAIIATGAEAMLSEHGFLPEPKSDCYAPNETREPANETLHRYLINVTWEGRDLS 318
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 4504125   350 FTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRH 387
Cdd:cd06378  319 FNEDGYLVNPELVIINLNRERLWEKVGKWESGSLQMKY 356
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
403-802 0e+00

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: 551.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   403 DNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNST--NEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLV 480
Cdd:cd13718    1 KFHLKIVTLEEAPFVIVEPVDPLTGTCMRNTVPCRKQLNHENSTdaDENRYVKKCCKGFCIDILKKLAKDVGFTYDLYLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   481 TNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNgtvspsaflepfsasvwvm 560
Cdd:cd13718   81 TNGKHGKKINGVWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMVARSN------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   561 mfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnnsvpvqnpkgttskimvsvwaffavi 640
Cdd:cd13718      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   641 flasytanlaafmiqeefvdQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSL 720
Cdd:cd13718  142 --------------------QVSGLSDKKFQRPHDQSPPFRFGTVPNGSTERNIRNNYPEMHQYMRKYNQKGVEDALVSL 201
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   721 KTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGIC 800
Cdd:cd13718  202 KTGKLDAFIYDAAVLNYMAGQDEGCKLVTIGSGKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLTGIC 281

                 ..
gi 4504125   801 HN 802
Cdd:cd13718  282 HN 283
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
554-827 1.54e-82

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: 271.87  E-value: 1.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     554 SASVWVMMFVMLLIVsAIAVFVFEYFSPVGYNRNLAKgkapHGPSFTIGKAIWLLWGLVFNNSvPVQNPKGTTSKIMVSV 633
Cdd:pfam00060    1 SLEVWLGILVAFLIV-GVVLFLLERFSPYEWRGPLET----EENRFTLSNSLWFSFGALVQQG-HRENPRSLSGRIVVGV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     634 WAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYsppFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGV 713
Cdd:pfam00060   75 WWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEY---GTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     714 EDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELET 793
Cdd:pfam00060  152 KDALNEEGVALVRNGIYAYALLSENYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEK 231
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 4504125     794 LWLTGI--CHNEKNEVMSSQLDIDNMAGVFYMLAAA 827
Cdd:pfam00060  232 KWWPKSgeCDSKSSASSSSQLGLKSFAGLFLILGIG 267
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
662-798 2.23e-24

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: 100.06  E-value: 2.23e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125      662 VTGLSDKKFQrphdysPPFRFGTVPNGSTERNIRNN--------YPYMHQ--YMTKFNQKGVEDALVSLktgklDAFIYD 731
Cdd:smart00079    2 ITSVEDLAKQ------TKIEYGTQDGSSTLAFFKRSgnpeysrmWPYMKSpeVFVKSYAEGVQRVRVSN-----YAFIME 70
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504125      732 AAVLNYKAGRDegCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTG 798
Cdd:smart00079   71 SPYLDYELSRN--CDLMTVGE--EFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
457-796 6.36e-13

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 69.62  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTngkhgkkvnnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVM 536
Cdd:COG0834   22 VGFDVDLARAIAKRLGLKVEFVPVP-----------WDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPYYTSGQVLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   537 VSRSNGTV-SPSAFlepfsasvwvmmfvmllivsaiavfvfeyfspvgynrnlaKGKaphgpsfTIGkaiwllwglvfnn 615
Cdd:COG0834   91 VRKDNSGIkSLADL----------------------------------------KGK-------TVG------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   616 svpVQnpKGTTskimvsvwaffaviflasytanlaafmiQEEFVDqvtglsdkkfqrphDYSPPFRFGTVPNgsternir 695
Cdd:COG0834  111 ---VQ--AGTT----------------------------YEEYLK--------------KLGPNAEIVEFDS-------- 135
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   696 nnypymhqymtkfnqkgVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGyiFATTGYGIALQKGSP-WKRQ 774
Cdd:COG0834  136 -----------------YAEALQALASGRVDAVVTDEPVAAYLLAKNPGDDLKIVGEP--LSGEPYGIAVRKGDPeLLEA 196
                        330       340
                 ....*....|....*....|..
gi 4504125   775 IDLALLQFVGDGEMEELETLWL 796
Cdd:COG0834  197 VNKALAALKADGTLDKILEKWF 218
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
108-256 8.85e-08

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: 55.85  E-value: 8.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     108 AVAQMLDFISSHTFVPILGiHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTtIFPGY-REFISF 186
Cdd:pfam01094   61 SVASAVASLANEWKVPLIS-YGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIY-SDDDYgESGLQA 138
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504125     187 VKTTVDNSFVGWDMQNVITLDTSFEDAKTQV-QLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWI 256
Cdd:pfam01094  139 LEDALRERGIRVAYKAVIPPAQDDDEIARKLlKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWI 209
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
458-544 8.39e-05

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 45.89  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    458 GFCIDILKKLSRTVKFTYDLylvtngkhgKKVNnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:PRK09495   48 GFDIDLWAAIAKELKLDYTL---------KPMD--FSGIIPALQTKNVDLALAGITITDERKKAIDFSDGYYKSGLLVMV 116

                  ....*..
gi 4504125    538 SRSNGTV 544
Cdd:PRK09495  117 KANNNDI 123
 
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 ...
839-1464 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: 1066.36  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     839 HLFYWKLRFCFTGVCSDRPGLLFSISRGIYSCIHGVHIEEKKKSPDFNLTGSQSNMLKLLRSAKNISSMSNMNssRMDSP 918
Cdd:pfam10565    1 HLFYWKLRFCFTGVCSGRPGLLFSISRGIYSCIHGVHIEEKKKSPDFTFNNTQSNMLKLLRTAKNMTNMSNLN--GSNSP 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     919 KRAADFIQRGSLIMDMVSDKGNLMYSDNRSFQGKESIFGDNMNELQTFVANRQKDNLNNYVFQGQHPLTLNESNPNTVEV 998
Cdd:pfam10565   79 KRALDFIQRGSLIMDMVEDKGNLVHSDNRSYQPKDNLFSDNISELQRFFGNRHKDNLNNYVFQGQHPLTLNESNPNTVEV 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     999 AVSTE-SKANSRPRQLWKKSVDSIRQdslsqNPVSQRDEATAENRTHSLKSPRYLPEEMAHSDISETSNRATCHREPD-N 1076
Cdd:pfam10565  159 AVSAEgGKFNSKPRQLWKKSVETLRQ-----SQSSFPEGLAEEYGKFSFKSQRYLPEENIHSDVSDISSRAVSYKDPEnN 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1077 SKNHKTKDNF-KRSVASKYPKDCSEVERTYLKTK-SSSPRDKIYTIDGEKePGFHLDPPQFVENVTLPENVDFPDPYQDP 1154
Cdd:pfam10565  234 AKHHKPKDNLkKRSVSSKYPRDCSEVELSYLKRKqHGSPRDKIYTIDSDK-PSFHLDQPRYRENVGLWEDLDYPDIYQDH 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1155 SENFRK-GDSTLPMNRNPLHNEEGLSNNDQYKLYSKHFTLKDKG--SPHSETSERYRQNSTHCRSCLSNMPTYSGHFTMR 1231
Cdd:pfam10565  313 NDNYRKdGAPGLHLNRSPLHHEDSLPNDDQYKLYSKHYSLKEKNggASPSESNDRYRQNSTHCRSCLSKLPNYSGHYTGR 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1232 SPF-KCDACLRMGNLYDIDEDQMLQETGNPAT-------GEQVYQQDWAQNNALQLQK-NKLRISRQHSYDNIVDKPREL 1302
Cdd:pfam10565  393 SPYnRCDACLHMGNLYDISEDQMLQEAINPAThaggkghSEDMFGHYWPQSDALHVQKkNRLRLSRQHSYDNIVDKPKEI 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1303 DLSRPSRSISLKDRERLLEGNFYGSLFSVPSSKLSGKKSSLFPQGLEDSKRSKSLLPDHTSDNPFLHSHRDDQRLVIGRC 1382
Cdd:pfam10565  473 DLGRPARSVSLKEKDRFLEDSPYANMFEMRSEKLLGSRSSLLNHNLEESKRSKSLYPDHVSDNPFLPSFRDDQRLLHGRS 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    1383 PSDPYKHSLPSQAVNDSYLRSSLRSTASYCSRDSRGHNDVYISEHVMPYAANKNNMYSTPRVLNSCSNRRVYKKMPSIES 1462
Cdd:pfam10565  553 SSDIYKQSAPSKGRNDNYFRSSVKSTASYCSRDGRVPNDMYISEHVMPYVANKNSLYSAPRVFNSCSNRRVYKKMPSIES 632

                   ..
gi 4504125    1463 DV 1464
Cdd:pfam10565  633 DV 634
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
32-387 0e+00

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: 603.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    32 PALNIAVMLGHSHdvTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQ 111
Cdd:cd06378    1 PSLNIAVILPGTS--FEVRIRSRLEPDAFHGLPFEVSPITVLMNDTNPKSILTQICDLLSGRKVHGIVFEDDTDQEAVAQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   112 MLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTV 191
Cdd:cd06378   79 ILDFISLQTYLPILGISGGSANVLLDKEEGSTFLQLGPSIEQQATVMLNILEEYDWHQFSVVTSLFPGYRDFVDAIRSTI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   192 DNSFVGWDMQNVITLDTSF--EDAKTQVQLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGNTELIP 269
Cdd:cd06378  159 DNSFVGWELQDVLTLDMSNdgSDAKTLRQLKKIEAQVILLYCTKEEAQYIFEAAEEAGLTGYGYVWIVPSLVLGNTDPPP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   270 KEFPSGLISVSYDDWDYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGKDLS 349
Cdd:cd06378  239 AEFPVGLISVHFDTWDYSLRARVRDGVAIIATGAEAMLSEHGFLPEPKSDCYAPNETREPANETLHRYLINVTWEGRDLS 318
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 4504125   350 FTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTLSLRH 387
Cdd:cd06378  319 FNEDGYLVNPELVIINLNRERLWEKVGKWESGSLQMKY 356
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
403-802 0e+00

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: 551.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   403 DNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNST--NEGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLV 480
Cdd:cd13718    1 KFHLKIVTLEEAPFVIVEPVDPLTGTCMRNTVPCRKQLNHENSTdaDENRYVKKCCKGFCIDILKKLAKDVGFTYDLYLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   481 TNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNgtvspsaflepfsasvwvm 560
Cdd:cd13718   81 TNGKHGKKINGVWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMVARSN------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   561 mfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnnsvpvqnpkgttskimvsvwaffavi 640
Cdd:cd13718      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   641 flasytanlaafmiqeefvdQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSL 720
Cdd:cd13718  142 --------------------QVSGLSDKKFQRPHDQSPPFRFGTVPNGSTERNIRNNYPEMHQYMRKYNQKGVEDALVSL 201
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   721 KTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGIC 800
Cdd:cd13718  202 KTGKLDAFIYDAAVLNYMAGQDEGCKLVTIGSGKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLTGIC 281

                 ..
gi 4504125   801 HN 802
Cdd:cd13718  282 HN 283
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
403-796 2.38e-122

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: 381.21  E-value: 2.38e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   403 DNHLSIVTLEEAPFVIVedidpltetcvrntvpcrkfvkinnstnegmnvkKCCKGFCIDILKKLSRTVKFTYDLYLVTN 482
Cdd:cd13687    1 STHLKVVTLEEAPFVYV----------------------------------KCCYGFCIDLLKKLAEDVNFTYDLYLVTD 46
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   483 GKHG---KKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNgtvspsaflepfsasvwv 559
Cdd:cd13687   47 GKFGtvnKSINGEWNGMIGELVSGRADMAVASLTINPERSEVIDFSKPFKYTGITILVKKRN------------------ 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   560 mmfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnnsvpvqnpkgttskimvsvwaffav 639
Cdd:cd13687      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   640 iflasytanlaafmiqeefvdQVTGLSDKKFQRPhdySPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVS 719
Cdd:cd13687  109 ---------------------ELSGINDPRLRNP---SPPFRFGTVPNSSTERYFRRQVELMHRYMEKYNYETVEEAIQA 164
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504125   720 LKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWL 796
Cdd:cd13687  165 LKNGKLDAFIWDSAVLEYEASQDEGCKLVTVGS--LFARSGYGIGLQKNSPWKRNVSLAILQFHESGFMEELDKKWL 239
PBP1_iGluR_NMDA cd06367
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic ...
32-383 1.72e-110

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: 353.47  E-value: 1.72e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    32 PALNIAVMLGHSHDVTERELRTLWGPEQAAGLPLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVAQ 111
Cdd:cd06367    1 PSVNIGAILGTKKEVAIKDEAEKDDFHHHFTLPVQLRVELVTMPEPDPKSIITRICDLLSDSKVQGVVFSDDTDQEAIAQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   112 MLDFISSHTFVPILGIHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTTIFPGYREFISFVKTTV 191
Cdd:cd06367   81 ILDFIAAQTLTPVLGLHGRSSMIMADKSEHSMFLQFGPPIEQQASVMLNIMEEYDWYIVSLVTTYFPGYQDFVNKLRSTI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   192 DNSfvGWDMQNVITLDTSFE--DAKTQVQLKKIHS---SVILLYCSKDEAVLILSEARSLGLTGYDFFWIVPSLVSGnTE 266
Cdd:cd06367  161 ENS--GWELEEVLQLDMSLDdgDSKLQAQLKKLQSpeaRVILLYCTKEEATYVFEVAASVGLTGYGYTWLVGSLVAG-TD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   267 LIPKEFPSGLISVSYDDWdYSLEARVRDGIGILTTAASSMLEKFSYIPEAKASCYGQMERPEVPMHTLHPFMVNVTWDGK 346
Cdd:cd06367  238 TVPAEFPTGLISLSYDEW-YNLPARIRDGVAIVATAASEMLSEHEQIPDPPSSCVNNQEIRKYTGPMLKRYLINVTFEGR 316
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 4504125   347 DLSFTEEGYQVHPRLVVIVLNKDREWEKVGKWENHTL 383
Cdd:cd06367  317 DLSFSEDGYQMHPKLVIILLNNERKWERVGKWKDSSL 353
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
554-827 1.54e-82

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: 271.87  E-value: 1.54e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     554 SASVWVMMFVMLLIVsAIAVFVFEYFSPVGYNRNLAKgkapHGPSFTIGKAIWLLWGLVFNNSvPVQNPKGTTSKIMVSV 633
Cdd:pfam00060    1 SLEVWLGILVAFLIV-GVVLFLLERFSPYEWRGPLET----EENRFTLSNSLWFSFGALVQQG-HRENPRSLSGRIVVGV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     634 WAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYsppFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGV 713
Cdd:pfam00060   75 WWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEY---GTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSV 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     714 EDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELET 793
Cdd:pfam00060  152 KDALNEEGVALVRNGIYAYALLSENYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEK 231
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 4504125     794 LWLTGI--CHNEKNEVMSSQLDIDNMAGVFYMLAAA 827
Cdd:pfam00060  232 KWWPKSgeCDSKSSASSSSQLGLKSFAGLFLILGIG 267
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
404-796 9.94e-74

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: 245.75  E-value: 9.94e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   404 NHLSIVTLEEAPFVIVEDIDPltetcvrntvpcrkfvkinnstneGMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNG 483
Cdd:cd00998    1 KTLKVVVPLEPPFVMFVTGSN------------------------AVTGNGRFEGYCIDLLKELSQSLGFTYEYYLVPDG 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   484 KHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSrsngtvspsaflepfsasvwvmmfv 563
Cdd:cd00998   57 KFGAPVNGSWNGMVGEVVRGEADLAVGPITITSERSVVIDFTQPFMTSGIGIMIP------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   564 mllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnnsvpvqnpkgttskimvsvwaffavifla 643
Cdd:cd00998      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   644 sytanlaafmiqeefvdqVTGLSDKKFQrphdysPPFRFGTVPNGSTERNIRNNYPY------MHQYMTKFNQKGVEDAL 717
Cdd:cd00998  112 ------------------IRSIDDLKRQ------TDIEFGTVENSFTETFLRSSGIYpfyktwMYSEARVVFVNNIAEGI 167
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504125   718 VSLKTGKLDAFIYDAAVLNYKAGRDEgCKLVTIGSGyiFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWL 796
Cdd:cd00998  168 ERVRKGKVYAFIWDRPYLEYYARQDP-CKLIKTGGG--FGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
404-796 6.04e-56

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: 196.04  E-value: 6.04e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   404 NHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEgmnvkKCCKGFCIDILKKLSRTVKFTYDLYLVTNG 483
Cdd:cd13719    2 THLKIVTIHEEPFVYVRPTPSDGTCREEFTVNCPNFNISGRPTVP-----FCCYGYCIDLLIKLARKMNFTYELHLVADG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   484 KHG--KKVNNV----WNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGtvspsaflepfsasv 557
Cdd:cd13719   77 QFGtqERVNNSnkkeWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEIR--------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   558 wvmmfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnnsvpvqnpkgttskimvsvwaff 637
Cdd:cd13719      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   638 aviflasytanlaafmiqeefvdqVTGLSDKKFQRPHDYsppFRFGTVPNGSTERNIRNN--YPYMHQYMTKFNQKGVED 715
Cdd:cd13719  142 ------------------------LTGINDPRLRNPSEK---FIYATVKGSSVDMYFRRQveLSTMYRHMEKHNYETAEE 194
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   716 ALVSLKTGKLDAFIYDAAVLNYKAGRDegCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13719  195 AIQAVRDGKLHAFIWDSSRLEFEASQD--CDLVTAGE--LFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTW 270

                 .
gi 4504125   796 L 796
Cdd:cd13719  271 I 271
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
405-795 6.54e-47

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: 170.03  E-value: 6.54e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   405 HLSIVTLEEAPFVIVEDID-----PLTETCVR-NTVPCRKFVKINNS-----TNEGMNVKKCCKGFCIDILKKLSRTVKF 473
Cdd:cd13720    3 HLRVVTLLEHPFVFTREVDeeglcPAGQLCLDpMTNDSSTLDALFSSlhssnDTVPIKFRKCCYGYCIDLLEKLAEDLGF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   474 TYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSrsngtvspsaflepf 553
Cdd:cd13720   83 DFDLYIVGDGKYGAWRNGRWTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSLGILVR--------------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   554 sasvwvmmfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnnsvpvqnPKgttskimvsv 633
Cdd:cd13720  148 --------------------------------------------------------------------TR---------- 149
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   634 waffaviflasytanlaafmiqeefvDQVTGLSDKKFQRPhdySPPFRFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGV 713
Cdd:cd13720  150 --------------------------DELSGIHDPKLHHP---SQGFRFGTVRESSAEYYVKKSFPEMHEHMRRYSLPNT 200
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   714 EDALVSLKTG--KLDAFIYDAAVLNYKAGRDEGCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEEL 791
Cdd:cd13720  201 PEGVEYLKNDpeKLDAFIMDKALLDYEVSIDADCKLLTVGK--PFAIEGYGIGLPQNSPLTSNISELISQYKSNGFMDLL 278

                 ....
gi 4504125   792 ETLW 795
Cdd:cd13720  279 HDKW 282
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
403-795 7.29e-44

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: 160.04  E-value: 7.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   403 DNHLSIVTLEEAPFVIVEDiDPLTetcvrntvpcrkfvkinnsTNEGMnvkkccKGFCIDILKKLSRTVKFTYDLYLVTN 482
Cdd:cd13685    1 NKTLRVTTILEPPFVMKKR-DSLS-------------------GNPRF------EGYCIDLLEELAKILGFDYEIYLVPD 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   483 GKHGKKV-NNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSngtvspsaflepfsasvwvmm 561
Cdd:cd13685   55 GKYGSRDeNGNWNGMIGELVRGEADIAVAPLTITAEREEVVDFTKPFMDTGISILMRKP--------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   562 fvmllivsaiavfvfeyfSPVGYNRNLAKgkaphgpsftigkaiwllwglvfnnsvpvqnpkgtTSKImvsvwaffavif 641
Cdd:cd13685  114 ------------------TPIESLEDLAK-----------------------------------QSKI------------ 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   642 lasytanlaafmiqeefvdqvtglsdkkfqrphdysppfRFGTVPNGSTERNIRN--NYPYMHQYMTKFNQKGVEDALVS 719
Cdd:cd13685  129 ---------------------------------------EYGTLKGSSTFTFFKNskNPEYRRYEYTKIMSAMSPSVLVA 169
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   720 --------LKTGKLD-AFIYDAAVLNYKAGRDegCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEE 790
Cdd:cd13685  170 saaegvqrVRESNGGyAFIGEATSIDYEVLRN--CDLTKVGE--VFSEKGYGIAVQQGSPLRDELSLAILELQESGELEK 245

                 ....*
gi 4504125   791 LETLW 795
Cdd:cd13685  246 LKEKW 250
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
457-795 9.64e-43

GluR7 subtype of kainate receptor, 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: 270441 [Multi-domain]  Cd Length: 369  Bit Score: 161.01  E-value: 9.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNN-VWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISV 535
Cdd:cd13723   31 EGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKgQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   536 MVSRSNGTvSPS--AFLEPFSASVWVMMFVMLLIVSAIaVFVFEYFSPVGY--NRNLAKGKAPHGPSFTIGKAIWLLWGL 611
Cdd:cd13723  111 LYRKPNGT-NPSvfSFLNPLSPDIWMYVLLAYLGVSCV-LFVIARFSPYEWydAHPCNPGSEVVENNFTLLNSFWFGMGS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   612 VFNNSVPVQnPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYsppfrfGTVPNGST- 690
Cdd:cd13723  189 LMQQGSELM-PKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEY------GAVKDGATm 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   691 ---ERNIRNNYPYMHQYMT-------KFNQKGVEDALVSLKtgkldAFIYDAAVLNYKAGRDegCKLVTIGSgyIFATTG 760
Cdd:cd13723  262 tffKKSKISTFEKMWAFMSskpsalvKNNEEGIQRALTADY-----ALLMESTTIEYVTQRN--CNLTQIGG--LIDSKG 332
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 4504125   761 YGIALQKGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13723  333 YGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKW 367
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
403-795 1.54e-41

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: 157.08  E-value: 1.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   403 DNHLSIVTLEEAPFVIVEDIDPLTetcvrntvpcrkfvkinnstnegmnvkkcCKGFCIDILKKLSRTVKFTYDLYLVTN 482
Cdd:cd13717    1 RRVYRIGTVESPPFVYRDRDGSPI-----------------------------WEGYCIDLIEEISEILNFDYEIVEPED 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   483 GKHGKKVNN-VWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVE-TGISVMVSRSNGTVSPSAFLEPFSASVWVM 560
Cdd:cd13717   52 GKFGTMDENgEWNGLIGDLVRKEADIALAALSVMAEREEVVDFTVPYYDlVGITILMKKPERPTSLFKFLTVLELEVWRE 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   561 mfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsFTIGKAIWLLWGlvfnnSVPVQN----PKGTTSKIMVSVWAF 636
Cdd:cd13717  132 --------------------------------------FTLKESLWFCLT-----SLTPQGggeaPKNLSGRLLVATWWL 168
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   637 FAVIFLASYTANLAAFMIQEEFVDQVTGLSDKKFQRPHDYSPpfrfgtVPNGSTER---NIRNN---------------- 697
Cdd:cd13717  169 FVFIIIASYTANLAAFLTVSRLQTPVESLDDLARQYKIQYTV------VKNSSTHTyfeRMKNAedtlyemwkdmslnds 242
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   698 -------------YPYMHQYmTKFNQKGVEDALVSLKTGKLD----------AFIYDAAVLNYKAGRDegCKLVTIGSgy 754
Cdd:cd13717  243 lspveraklavwdYPVSEKY-TKIYQAMQEAGLVANAEEGVKrvrestsagfAFIGDATDIKYEILTN--CDLQEVGE-- 317
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 4504125   755 IFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13717  318 EFSRKPYAIAVQQGSPLKDELNYAILELQNDRFLEKLKAKW 358
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
405-539 9.77e-35

Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the S1 domain, is the luminal domain just upstream of the first, M1, transmembrane region of transmembrane ion-channel proteins, and it binds L-glutamate and glycine. It is found in association with Lig_chan, pfam00060.


Pssm-ID: 463166 [Multi-domain]  Cd Length: 111  Bit Score: 128.79  E-value: 9.77e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     405 HLSIVTLEEAPFVIvedidpltetcvrntvpcRKFVKINNSTnegmnvkkcCKGFCIDILKKLSRTVKFTYDLYLVTNGK 484
Cdd:pfam10613    2 TLIVTTILEPPFVM------------------LKENLEGNDR---------YEGFCIDLLKELAEILGFKYEIRLVPDGK 54
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 4504125     485 HG--KKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSR 539
Cdd:pfam10613   55 YGslDPTTGEWNGMIGELIDGKADLAVAPLTITSEREKVVDFTKPFMTLGISILMKK 111
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
405-795 4.41e-30

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: 120.33  E-value: 4.41e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   405 HLSIVTLEEAPFVIV-EDIDPLTetcvrntvpcrkfvkiNNSTNEGmnvkkcckgFCIDILKKLSRTVKFTYDLYLVTNG 483
Cdd:cd13714    3 TLIVTTILEEPYVMLkESAKPLT----------------GNDRFEG---------FCIDLLKELAKILGFNYTIRLVPDG 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   484 KHGK--KVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNgtvspsaflePFsasvwvmm 561
Cdd:cd13714   58 KYGSydPETGEWNGMVRELIDGRADLAVADLTITYERESVVDFTKPFMNLGISILYRKPT----------PI-------- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   562 fvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvfnNSVpvqnpkgttskimvsvwaffavif 641
Cdd:cd13714  120 -----------------------------------------------------ESA------------------------ 122
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   642 lasytanlaafmiqEEFVDQVTglsdkkfqrphdysppFRFGTVPNGST-----ERNIRNNYPYMHQYM-------TKFN 709
Cdd:cd13714  123 --------------DDLAKQTK----------------IKYGTLRGGSTmtffrDSNISTYQKMWNFMMsakpsvfVKSN 172
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   710 QKGVEDAlvslKTGKLdAFIYDAAVLNYKAGRDegCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEME 789
Cdd:cd13714  173 EEGVARV----LKGKY-AFLMESTSIEYVTQRN--CNLTQIGG--LLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLE 243

                 ....*.
gi 4504125   790 ELETLW 795
Cdd:cd13714  244 MLKNKW 249
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
457-795 4.01e-29

The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the KA1 subunit of kainate receptor. While this ligand-binding domain is structurally homologous to the periplasmic binding fold type II superfamily, the N_terminal domain of kainate receptors belongs to the periplasmic-binding fold type I. 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 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: 270442 [Multi-domain]  Cd Length: 333  Bit Score: 120.12  E-value: 4.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHG-KKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISV 535
Cdd:cd13724   31 EGFCVDMLKELAEILRFNYKIRLVGDGVYGvPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   536 M----VSRSNGTVSpsaFLEPFSASVWVMMFVMLLIVSAIAVFV-----FEYFSPvgynRNLAKGKAPHG-PSFTIGKAI 605
Cdd:cd13724  111 LyrvhMGRKPGYFS---FLDPFSPGVWLFMLLAYLAVSCVLFLVarltpYEWYSP----HPCAQGRCNLLvNQYSLGNSL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   606 WLLWGLVFNNSVPVQNPkgttskimvsvwaffaviflasytanlaafmiqeefVDQVTGLSDKKfqrphdyspPFRFGTV 685
Cdd:cd13724  184 WFPVGGFMQQGSTIAPP------------------------------------IESVDDLADQT---------AIEYGTI 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   686 PNGSTERNIRNN--------YPYMHQYMTKFNQKGVEDALVSLKTGKLdAFIYDAAVLNYKagRDEGCKLVTIGSgyIFA 757
Cdd:cd13724  219 HGGSSMTFFQNSryqtyqrmWNYMYSKQPSVFVKSTEEGIARVLNSNY-AFLLESTMNEYY--RQRNCNLTQIGG--LLD 293
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 4504125   758 TTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13724  294 TKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKW 331
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
662-798 2.23e-24

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: 100.06  E-value: 2.23e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125      662 VTGLSDKKFQrphdysPPFRFGTVPNGSTERNIRNN--------YPYMHQ--YMTKFNQKGVEDALVSLktgklDAFIYD 731
Cdd:smart00079    2 ITSVEDLAKQ------TKIEYGTQDGSSTLAFFKRSgnpeysrmWPYMKSpeVFVKSYAEGVQRVRVSN-----YAFIME 70
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4504125      732 AAVLNYKAGRDegCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTG 798
Cdd:smart00079   71 SPYLDYELSRN--CDLMTVGE--EFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
458-539 7.30e-23

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtypes of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This family represents the ligand-binding domain of the AMPA receptor subunits, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270433 [Multi-domain]  Cd Length: 261  Bit Score: 99.74  E-value: 7.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRTVKFTYDLYLVTNGKHGKK--VNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISV 535
Cdd:cd13715   34 GYCVDLADEIAKHLGIKYELRIVKDGKYGARdaDTGIWNGMVGELVRGEADIAIAPLTITLVRERVIDFSKPFMSLGISI 113

                 ....
gi 4504125   536 MVSR 539
Cdd:cd13715  114 MIKK 117
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
406-795 5.98e-22

The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the delta1 receptor of an orphan glutamate receptor family. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of delta receptors belongs to the periplasmic-binding fold type I. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRdelta2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans.


Pssm-ID: 270448 [Multi-domain]  Cd Length: 257  Bit Score: 96.95  E-value: 5.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   406 LSIVTLEEAPFVIV-EDIdpltetcvrntvpcrkfvkinnstnegMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGK 484
Cdd:cd13730    4 LKVVTVLEEPFVMVaENI---------------------------LGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGK 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   485 HGKKVNN-VWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSR----------------SNGTVSPS 547
Cdd:cd13730   57 YGHQLHNtSWNGMIGELISKRADLAISAITITPERESVVDFSKRYMDYSVGILIKKpepirtfqdlskqvemSYGTVRDS 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   548 AflepfsasvwvmmfvmllivsaiavfVFEYFSpvgynrnlAKGKAPHGPSFTIGKaiwlLWGLVFNNSvpvqnpkGTTS 627
Cdd:cd13730  137 A--------------------------VYEYFR--------AKGTNPLEQDSTFAE----LWRTISKNG-------GADN 171
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   628 KImvsvwaffaviflasytanlaafmiqeefvdqvtglsdkkfqrphdysppfrfgTVPNGSTERNIRNNYpymhqymtk 707
Cdd:cd13730  172 CV------------------------------------------------------SSPSEGIRKAKKGNY--------- 188
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   708 fnqkgvedalvslktgkldAFIYDAAVLNYKAGRDEGCKLVTIGSGyiFATTGYGIALQKGSPWKRQIDLALLQFVGDGE 787
Cdd:cd13730  189 -------------------AFLWDVAVVEYAALTDDDCSVTVIGNS--ISSKGYGIALQHGSPYRDLFSQRILELQDTGD 247

                 ....*...
gi 4504125   788 MEELETLW 795
Cdd:cd13730  248 LDVLKQKW 255
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
406-795 1.15e-21

The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the delta-2 receptor of an orphan glutamate receptor family. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of delta receptors belongs to the periplasmic-binding fold type I. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRalpha2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans.


Pssm-ID: 270449 [Multi-domain]  Cd Length: 257  Bit Score: 96.25  E-value: 1.15e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   406 LSIVTLEEAPFVIVedidpltetcvrntvpcrkfvkinnSTNEGMNVKKCcKGFCIDILKKLSRTVKFTYDLYLVTNGKH 485
Cdd:cd13731    4 LRVVTVLEEPFVMV-------------------------SENVLGKPKKY-QGFSIDVLDALSNYLGFNYEIYVAPDHKY 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   486 GK-KVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVSpsafLEPFSasvwvmmfvm 564
Cdd:cd13731   58 GSpQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAESIQS----LQDLS---------- 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   565 llivsaiavfvfeyfspvgynrnlakgkaphgpsftigKAIWLLWGLVFNNSVpvqnpkgttskimvsvwaffaviflas 644
Cdd:cd13731  124 --------------------------------------KQTDIPYGTVLDSAV--------------------------- 138
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   645 ytanlaafmiqeefVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGStERNIRNnypymhqymtkfNQKGVEdalvSLKTGK 724
Cdd:cd13731  139 --------------YEHVRMKGLNPFERDSMYSQMWRMINRSNGS-ENNVLE------------SQAGIQ----KVKYGN 187
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504125   725 LdAFIYDAAVLNYKAGRDEGCKLVTIGSGyiFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13731  188 Y-AFVWDAAVLEYVAINDPDCSFYTVGNT--VADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 255
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
406-795 1.86e-20

The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily; This subfamily represents the ligand-binding domain of an orphan family of delta receptors, GluRdelta1 and GluRdelta2. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of iGluRs belongs to the periplasmic-binding fold type I. Although the delta receptors are members of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRalpha2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans.


Pssm-ID: 270434 [Multi-domain]  Cd Length: 257  Bit Score: 92.60  E-value: 1.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   406 LSIVTLEEAPFVIV-EDIdpltetcvrntvpcrkfvkinnstnegMNVKKCCKGFCIDILKKLSRTVKFTYDLYLVTNGK 484
Cdd:cd13716    4 LRVVTVLEEPFVMVsENV---------------------------LGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHK 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   485 HGKKV-NNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMVSRSngtvspsaflepfsasvwvmmfv 563
Cdd:cd13716   57 YGSQQeDGTWNGLIGELVFKRADIGISALTITPERENVVDFTTRYMDYSVGVLLRKA----------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   564 mllivSAIAVFvfeyfspvgynRNLAkgkaphgpsftigKAIWLLWGLVFNNSVpvqnpkgttskimvsvwaffavifla 643
Cdd:cd13716  114 -----ESIQSL-----------QDLS-------------KQTDIPYGTVLDSAV-------------------------- 138
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   644 sytanlaafmiqeefVDQVTGLSDKKFQRPHDYSPPFRFGTVPNGStERNIRNnypymhqymtkfNQKGVEDAlvslKTG 723
Cdd:cd13716  139 ---------------YEYVRSKGTNPFERDSMYSQMWRMINRSNGS-ENNVSE------------SSEGIRKV----KYG 186
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4504125   724 KLdAFIYDAAVLNYKAGRDEGCKLVTIGSGyiFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13716  187 NY-AFVWDAAVLEYVAINDDDCSFYTVGNT--VADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 255
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-539 2.85e-19

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR1 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR1, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270447 [Multi-domain]  Cd Length: 260  Bit Score: 89.31  E-value: 2.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNN--VWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGIS 534
Cdd:cd13729   31 EGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPEtkMWNGMVGELVYGKADVAVAPLTITLVREEVIDFSKPFMSLGIS 110

                 ....*
gi 4504125   535 VMVSR 539
Cdd:cd13729  111 IMIKK 115
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
457-541 2.87e-18

GluR6 subtype of kainate receptor, 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: 270439 [Multi-domain]  Cd Length: 251  Bit Score: 86.23  E-value: 2.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGKK--VNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGIS 534
Cdd:cd13721   31 EGYCIDLLRELSTILGFTYEIRLVEDGKYGAQddVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGIS 110

                 ....*..
gi 4504125   535 VMVSRSN 541
Cdd:cd13721  111 ILYRKGT 117
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-539 3.00e-18

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR4 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR4, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I.The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270445 [Multi-domain]  Cd Length: 259  Bit Score: 86.24  E-value: 3.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNN--VWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGIS 534
Cdd:cd13727   31 EGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDPEtkIWNGMVGELVYGKAEIAVAPLTITLVREEVIDFSKPFMSLGIS 110

                 ....*
gi 4504125   535 VMVSR 539
Cdd:cd13727  111 IMIKK 115
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
442-501 7.82e-18

Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the S1 domain, is the luminal domain just upstream of the first, M1, transmembrane region of transmembrane ion-channel proteins, and it binds L-glutamate and glycine. It is found in association with Lig_chan.


Pssm-ID: 214911 [Multi-domain]  Cd Length: 62  Bit Score: 78.83  E-value: 7.82e-18
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504125      442 INNSTNEGMNvkKCCKGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKV-NNVWNGMIGEVV 501
Cdd:smart00918    4 MLKESPDGGN--DRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLpNGSWNGMVGELV 62
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-539 9.74e-18

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR2 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR2, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270444 [Multi-domain]  Cd Length: 259  Bit Score: 84.69  E-value: 9.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGKK--VNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGIS 534
Cdd:cd13726   31 EGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARdaDTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSLGIS 110

                 ....*
gi 4504125   535 VMVSR 539
Cdd:cd13726  111 IMIKK 115
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-539 2.48e-17

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR3 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR3, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current


Pssm-ID: 270446 [Multi-domain]  Cd Length: 259  Bit Score: 83.59  E-value: 2.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGKK--VNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGIS 534
Cdd:cd13728   31 EGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARdpETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGIS 110

                 ....*
gi 4504125   535 VMVSR 539
Cdd:cd13728  111 IMIKK 115
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
457-795 1.46e-16

The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the KA2 subunit of kainate receptor. While this ligand-binding domain is structurally homologous to the periplasmic binding fold type II superfamily, the N_terminal domain of kainate receptors belongs to the periplasmic-binding fold type I. 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 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: 270443 [Multi-domain]  Cd Length: 250  Bit Score: 80.90  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGK-KVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISV 535
Cdd:cd13725   31 EGFCVDMLRELAELLRFRYRLRLVEDGLYGApEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   536 MvsrsngtvspsaflepfsasvwvmmfvmllivsaiavfvfeyfspvgynrnlakgkaphgpsftigkaiwllwglvFNN 615
Cdd:cd13725  111 L----------------------------------------------------------------------------YRV 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   616 SVPVQNPkgttskimvsvwaffaviflasytanlaafmiqEEFVDQVTglsdkkfqrphdysppFRFGTVPNGSTERNIR 695
Cdd:cd13725  115 HMPVESA---------------------------------DDLADQTN----------------IEYGTIHAGSTMTFFQ 145
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   696 NN----YPYMHQYMtKFNQKGV-----EDALVSLKTGKLdAFIYDAAVLNYKAGRDegCKLVTIGSgyIFATTGYGIALQ 766
Cdd:cd13725  146 NSryqtYQRMWNYM-QSKQPSVfvkstEEGIARVLNSRY-AFLLESTMNEYHRRLN--CNLTQIGG--LLDTKGYGIGMP 219
                        330       340
                 ....*....|....*....|....*....
gi 4504125   767 KGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13725  220 LGSPFRDEITLAILQLQENNRLEILKRKW 248
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
457-541 4.28e-16

GluR5 subtype of kainate receptor, 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: 270440 [Multi-domain]  Cd Length: 250  Bit Score: 79.71  E-value: 4.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNN-VWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISV 535
Cdd:cd13722   31 EGYCLDLLKELSNILGFLYDVKLVPDGKYGAQNDKgEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTLGISI 110

                 ....*.
gi 4504125   536 MVSRSN 541
Cdd:cd13722  111 LYRKGT 116
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
457-796 6.36e-13

ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino acid transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 69.62  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLYLVTngkhgkkvnnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVM 536
Cdd:COG0834   22 VGFDVDLARAIAKRLGLKVEFVPVP-----------WDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPYYTSGQVLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   537 VSRSNGTV-SPSAFlepfsasvwvmmfvmllivsaiavfvfeyfspvgynrnlaKGKaphgpsfTIGkaiwllwglvfnn 615
Cdd:COG0834   91 VRKDNSGIkSLADL----------------------------------------KGK-------TVG------------- 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   616 svpVQnpKGTTskimvsvwaffaviflasytanlaafmiQEEFVDqvtglsdkkfqrphDYSPPFRFGTVPNgsternir 695
Cdd:COG0834  111 ---VQ--AGTT----------------------------YEEYLK--------------KLGPNAEIVEFDS-------- 135
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   696 nnypymhqymtkfnqkgVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGyiFATTGYGIALQKGSP-WKRQ 774
Cdd:COG0834  136 -----------------YAEALQALASGRVDAVVTDEPVAAYLLAKNPGDDLKIVGEP--LSGEPYGIAVRKGDPeLLEA 196
                        330       340
                 ....*....|....*....|..
gi 4504125   775 IDLALLQFVGDGEMEELETLWL 796
Cdd:COG0834  197 VNKALAALKADGTLDKILEKWF 218
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
712-796 3.75e-12

Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate receptor domain GluR0. These domains are found in the GluR0 proteins that have been shown to function as prokaryotic 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. The GluR0 proteins belong to the PBP2 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: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 67.36  E-value: 3.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   712 GVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSgyIFATTGYGIALQKGSPWKRQIDLALLQFVGDGEMEEL 791
Cdd:cd00997  135 NLEAAYTALQDKDADAVVFDAPVLRYYAAHDGNGKAEVTGS--VFLEENYGIVFPTGSPLRKPINQALLNLREDGTYDEL 212

                 ....*
gi 4504125   792 ETLWL 796
Cdd:cd00997  213 YEKWF 217
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
458-795 3.10e-10

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, 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 majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. 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.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 61.50  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRTVKFTYDLylvtngkhgkkVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:cd13530   24 GFDVDLANAIAKRLGVKVEF-----------VDTDFDGLIPALQSGKIDVAISGMTITPERAKVVDFSDPYYYTGQVLVV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   538 SRSNGTVSPSAFLepfsasvwvmmfvmllivsaiavfvfeyfspvgynrnlaKGKaphgpsfTIGkaiwllwglvfnnsv 617
Cdd:cd13530   93 KKDSKITKTVADL---------------------------------------KGK-------KVG--------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   618 pVQnpKGTTskimvsvwaffaviflasytanlaafmiQEEFVDQVTGLSDKKFqrphdysppfrfgtvpngsternirnn 697
Cdd:cd13530  112 -VQ--AGTT----------------------------GEDYAKKNLPNAEVVT--------------------------- 133
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   698 YPYmhqymtkfnqkgVEDALVSLKTGKLDAFIYDAAVLNYkAGRDEGCKLVTIgsGYIFATTGYGIALQKG-SPWKRQID 776
Cdd:cd13530  134 YDN------------YPEALQALKAGRIDAVITDAPVAKY-YVKKNGPDLKVV--GEPLTPEPYGIAVRKGnPELLDAIN 198
                        330
                 ....*....|....*....
gi 4504125   777 LALLQFVGDGEMEELETLW 795
Cdd:cd13530  199 KALAELKADGTLDKLLEKW 217
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
457-796 1.33e-09

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 60.00  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     457 KGFCIDILKKLSRT--VKFTYdlylvtngkhgkkVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGIS 534
Cdd:pfam00497   22 VGFDVDLAKAIAKRlgVKVEF-------------VPVSWDGLIPALQSGKVDLIIAGMTITPERAKQVDFSDPYYYSGQV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     535 VMVSRSNGTVSPSAFLEpfsasvwvmmfvmllivsaiavfvfeyfspvgynrnlAKGKaphgpsfTIGkaiwllwglvfn 614
Cdd:pfam00497   89 ILVRKKDSSKSIKSLAD-------------------------------------LKGK-------TVG------------ 112
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     615 nsvpVQnpKGTTskimvsvwaffaviflasytanlaafmiQEEFVDqvtglsdkkfqrphdysppfrfgtvpngsterNI 694
Cdd:pfam00497  113 ----VQ--KGST----------------------------AEELLK--------------------------------NL 126
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     695 RNNYPYMHQYmtkfnqKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSgyIFATTGYGIALQKGSP-WKR 773
Cdd:pfam00497  127 KLPGAEIVEY------DDDAEALQALANGRVDAVVADSPVAAYLIKKNPGLNLVVVGE--PLSPEPYGIAVRKGDPeLLA 198
                          330       340
                   ....*....|....*....|...
gi 4504125     774 QIDLALLQFVGDGEMEELETLWL 796
Cdd:pfam00497  199 AVNKALAELKADGTLAKIYEKWF 221
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
86-320 2.30e-09

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: 61.20  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    86 VCDLMSGARIHGLVFG---DDTDQEAVAqmLDFISSHTFVPILGIHGGASmIMADKDPTSTFFQFGASIQQQATVMLKIM 162
Cdd:cd06379   55 VCEDLIASQVYAVIVShppTPSDLSPTS--VSYTAGFYRIPVIGISARDS-AFSDKNIHVSFLRTVPPYSHQADVWAEML 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   163 QDYDWHVFSLVTTIFPGYREFIS-FVKTTVDNSFVgwdMQNVITLDTSFEDAKTQVQ-LKKIHSSVILLYCSKDEAVLIL 240
Cdd:cd06379  132 RHFEWKQVIVIHSDDQDGRALLGrLETLAETKDIK---IEKVIEFEPGEKNFTSLLEeMKELQSRVILLYASEDDAEIIF 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   241 SEARSLGLTGYDFFWIVpslvsGNTELIPKEFPSGLISV----SYDDwdyslEARVRDGIGILTTAASSMLEKFSYIPEA 316
Cdd:cd06379  209 RDAAMLNMTGAGYVWIV-----TEQALAASNVPDGVLGLqlihGKNE-----SAHIRDSVSVVAQAIRELFRSSENITDP 278

                 ....
gi 4504125   317 KASC 320
Cdd:cd06379  279 PVDC 282
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
458-551 8.41e-09

Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; This periplasmic substrate-binding component serves as an initial receptor in the ABC transport of glutamine in bacteria and eukaryota. GlnH belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270216 [Multi-domain]  Cd Length: 218  Bit Score: 57.29  E-value: 8.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRTVKFTYDLylvtngkhgKKVNnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:cd00994   23 GFDIDLWEAIAKEAGFKYEL---------QPMD--FKGIIPALQTGRIDIAIAGITITEERKKVVDFSDPYYDSGLAVMV 91
                         90
                 ....*....|....
gi 4504125   538 SRSNGTVSPSAFLE 551
Cdd:cd00994   92 KADNNSIKSIDDLA 105
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
681-796 1.01e-08

Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold; This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270406 [Multi-domain]  Cd Length: 238  Bit Score: 57.65  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   681 RFGTVPNGSTERNIRNNYPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVL-NYKAGRDEGCKLVTIgsGYIFATT 759
Cdd:cd13688  123 TVGVTAGTTTEDALRTVNPLAGLQASVVPVKDHAEGFAALETGKADAFAGDDILLaGLAARSKNPDDLALI--PRPLSYE 200
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 4504125   760 GYGIALQKGSP-WKRQIDLALLQFVGDGEMEELETLWL 796
Cdd:cd13688  201 PYGLMLRKDDPdFRLLVDRALAQLYQSGEIEKLYDKWF 238
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
108-256 8.85e-08

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: 55.85  E-value: 8.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125     108 AVAQMLDFISSHTFVPILGiHGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDWHVFSLVTtIFPGY-REFISF 186
Cdd:pfam01094   61 SVASAVASLANEWKVPLIS-YGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIY-SDDDYgESGLQA 138
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4504125     187 VKTTVDNSFVGWDMQNVITLDTSFEDAKTQV-QLKKIHSSVILLYCSKDEAVLILSEARSLGLTGYDFFWI 256
Cdd:pfam01094  139 LEDALRERGIRVAYKAVIPPAQDDDEIARKLlKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWI 209
PBP1_iGluR_NMDA_NR3 cd06377
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of ...
48-390 2.66e-07

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of NMDA receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR3 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: 380600 [Multi-domain]  Cd Length: 373  Bit Score: 54.75  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    48 ERELRTLWGPEQaaglpLDVNVVALLMNRTDPKSLITHVCDLMSGARIHGLVFGDDTDQEAVaqMLDFISSHTFVPILGI 127
Cdd:cd06377   30 AVDLPTGLLPYN-----LSLEVVVAAPWARDPASLTRSLCHSVVVQGVAALLAFPQSRGELL--QLDFLSAALEIPVVSI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   128 hggASMIMADKDPTSTFFQFGASIQQQAT----VMLKIMQDYDWHVFSLVT--TIFPGyrefiSFVKTTVDNS-FVGWDM 200
Cdd:cd06377  103 ---LRREFPRPLRSQNPFHLQLDLQSSLEsledVLVSLLQANSWEDVSLLLcqPWDPT-----SFLLLWQNNSqFHLGTV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   201 QNVITLDTSFEDAKTQVQLKKIH---SSVILLYCSKDEAVLILSEARSLGLTgyDFFWIVPSlvSGNTELIPKE-FPSGL 276
Cdd:cd06377  175 LNLSVLDESDLQRSLQQHLESLKdpsPAIVMFGCDAARARRVFEAAPPGGLP--EFHWLLGT--PLPVEELPTEgLPPGL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   277 IS---VSyddwDYSLEARVRDGIGILTTAASSM---LEKFSYIPeAKASCygqMER----PEVPMHTLHPFMVNVTWDGK 346
Cdd:cd06377  251 LAlgeTS----RPSLEAYVQDAVELVARALSSAalvHPELALLP-ATVNC---NDLktggSESSGQYLSRFLANTSFQGR 322
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 4504125   347 DLSFTEEGY-QVHP--RLVVIVLNKDR----EWEKVGKWENHTLSLRHAVW 390
Cdd:cd06377  323 TGTVWVTGSsQVHSerHFKVWSLRRDPlgapTWATVGSWQDGKLDMEPGAW 373
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
437-537 3.59e-07

Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily contains the 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 PBP2 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: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 52.91  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   437 RKFVKINNSTNEGMNvkkCCKGFCIDI----LKKLSRTVkfTYDLYLVTNGKHgkkvnnvWNGMIGEVVYQRAVMAVGSL 512
Cdd:cd13686   14 KEFVKVTRDPITNST---SVTGFCIDVfeaaVKRLPYAV--PYEFIPFNDAGS-------YDDLVYQVYLKKFDAAVGDI 81
                         90       100
                 ....*....|....*....|....*
gi 4504125   513 TINEERSEVVDFSVPFVETGISVMV 537
Cdd:cd13686   82 TITANRSLYVDFTLPYTESGLVMVV 106
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
458-547 1.38e-06

Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270431 [Multi-domain]  Cd Length: 218  Bit Score: 50.75  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRtvkftydlylvtngKHGKKVNNV---WNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGIS 534
Cdd:cd13713   24 GFDVDVAKAIAK--------------RLGVKVEPVttaWDGIIAGLWAGRYDIIIGSMTITEERLKVVDFSNPYYYSGAQ 89
                         90
                 ....*....|...
gi 4504125   535 VMVSRSNGTVSPS 547
Cdd:cd13713   90 IFVRKDSTITSLA 102
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
86-257 1.49e-06

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: 52.03  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    86 VCDLMSGARIHGLVFGDdtdQEAVAQMLDFISSHTFVPILGIhGGASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDY 165
Cdd:cd06269   59 ACDLLAAAKVVAILGPG---CSASAAPVANLARHWDIPVLSY-GATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   166 DWHVFSLV-TTIFPGYREFISFVKttvdnsfVGWDMQNVITLDTSFEDAKTQ---VQLKKIHSS---VILLYCSKDEAVL 238
Cdd:cd06269  135 GWNKVVLIySDDEYGEFGLEGLEE-------LFQEKGGLITSRQSFDENKDDdltKLLRNLRDTearVIILLASPDTARS 207
                        170
                 ....*....|....*....
gi 4504125   239 ILSEARSLGLTGYDFFWIV 257
Cdd:cd06269  208 LMLEAKRLDMTSKDYVWFV 226
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
458-547 2.07e-06

Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold; This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270407 [Multi-domain]  Cd Length: 229  Bit Score: 50.69  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRT--VKFTYdlylvtngkhgKKVNNvwNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISV 535
Cdd:cd13689   33 GFDVDLCKAIAKKlgVKLEL-----------KPVNP--AARIPELQNGRVDLVAANLTYTPERAEQIDFSDPYFVTGQKL 99
                         90
                 ....*....|..
gi 4504125   536 MVSRSNGTVSPS 547
Cdd:cd13689  100 LVKKGSGIKSLK 111
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
700-796 2.36e-06

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises 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.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 50.28  E-value: 2.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   700 YMHQYMTKFNQKG-------VEDALVSLKTGKLDAFIYDAAVLNYKAgRDEGCKLVTIgSGYIFATTGYGIALQKGSPW- 771
Cdd:cd13704  118 IMHEYLKERGLGInlvlvdsPEEALRLLASGKVDAAVVDRLVGLYLI-KELGLTNVKI-VGPPLLPLKYCFAVRKGNPEl 195
                         90       100
                 ....*....|....*....|....*
gi 4504125   772 KRQIDLALLQFVGDGEMEELETLWL 796
Cdd:cd13704  196 LAKLNEGLAILKASGEYDEIYEKWF 220
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
714-796 1.01e-05

Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), 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 majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. 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.


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 48.34  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   714 EDALVSLKTGKLDAFIYDaAVLNYKAGRDEGCKLVTIGSgyIFATTGYGIALQKGSP-WKRQIDLALLQFVGDGEMEELE 792
Cdd:cd13629  141 AAAVLEVVNGKADAFIYD-QPTPARFAKKNDPTLVALLE--PFTYEPLGFAIRKGDPdLLNWLNNFLKQIKGDGTLDELY 217

                 ....
gi 4504125   793 TLWL 796
Cdd:cd13629  218 DKWF 221
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
685-796 1.24e-05

Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold; This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 48.07  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   685 VPNGST-ERNIRNNYPYMHqyMTKFNQKGveDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFAttgYGI 763
Cdd:cd01000  122 VLQGSTaEAALRKAAPEAQ--LLEFDDYA--EAFQALESGRVDAMATDNSLLAGWAAENPDDYVILPKPFSQEP---YGI 194
                         90       100       110
                 ....*....|....*....|....*....|....
gi 4504125   764 ALQKGSP-WKRQIDLALLQFVGDGEMEELETLWL 796
Cdd:cd01000  195 AVRKGDTeLLKAVNATIAKLKADGELAEIYKKWL 228
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
660-795 2.64e-05

Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 periplasmic binding protein; This periplasmic substrate component serves as an initial receptor in the ABC transport of glutamine in eubacteria and archaea. After binding the alanine with high affinity, this domain Interacts 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. This alanine specific domain belong to the PBP2 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: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 47.08  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   660 DQVTGLSDKKFQRPHDYSPpFRFGtVPNGST-ERNIRNNYPYMHQYMTKFNQKgVEDALVSLKTGKLD-AFIYDAAVLNY 737
Cdd:cd13628   89 DTIVS*KDRKIKQLQDLNG-KSLG-VQLGTIqEQLIKELSQPYPGLKTKLYNR-VNELVQALKSGRVDaAIVEDIVAETF 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 4504125   738 KAGRDEgcklvTIGSGYIFAT-TGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLW 795
Cdd:cd13628  166 AQKKN*-----LLESRYIPKEaDGSAIAFPKGSPLRDDFNRWLKEMGDSGELELMVRRW 219
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
458-541 4.07e-05

Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 periplasmic binding protein fold; This group includes the periplasmic substrate-binding protein ArtJ of the ATP-binding cassette (ABC) transport system from the thermophilic bacterium Geobacillus stearothermophilus, which is specific for arginine, lysine, and histidine. ArtJ belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270342 [Multi-domain]  Cd Length: 219  Bit Score: 46.33  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRTVKFTYDLylvtngkhgkkVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:cd13624   24 GFDIDLIKAIAKEAGFEVEF-----------KNMAFDGLIPALQSGKIDIIISGMTITEERKKSVDFSDPYYEAGQAIVV 92

                 ....
gi 4504125   538 SRSN 541
Cdd:cd13624   93 RKDS 96
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
458-546 6.78e-05

Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in PBPe


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 45.78  E-value: 6.78e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125      458 GFCIDILKKLSRTVKFTYDLYLVTngkhgkkvnnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:smart00062   24 GFDVDLAKAIAKELGLKVEFVEVS-----------FDSLLTALKSGKIDVVAAGMTITPERAKQVDFSDPYYRSGQVILV 92

                    ....*....
gi 4504125      538 SRSNGTVSP 546
Cdd:smart00062   93 RKDSPIKSL 101
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
684-796 7.25e-05

Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein fold; This group includes periplasmic glutamate-binding domain GluB from Corynebacterium efficiens and its related proteins. The GluB domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270408 [Multi-domain]  Cd Length: 231  Bit Score: 45.72  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   684 TVPNGSTERNIRNNYPyMHQYMTKFNQkgvEDALVSLKTGKLDAFIYDAAVL-NYKAGRDEGCKLVTIGsgyiFATTGYG 762
Cdd:cd13690  124 TAAGSTSADNLKKNAP-GATIVTRDNY---SDCLVALQQGRVDAVSTDDAILaGFAAQDPPGLKLVGEP----FTDEPYG 195
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 4504125   763 IALQKGSP-WKRQIDLALLQFVGDGEMEELETLWL 796
Cdd:cd13690  196 IGLPKGDDeLVAFVNGALEDMRADGTWQALFDRWL 230
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
458-544 8.39e-05

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 45.89  E-value: 8.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    458 GFCIDILKKLSRTVKFTYDLylvtngkhgKKVNnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:PRK09495   48 GFDIDLWAAIAKELKLDYTL---------KPMD--FSGIIPALQTKNVDLALAGITITDERKKAIDFSDGYYKSGLLVMV 116

                  ....*..
gi 4504125    538 SRSNGTV 544
Cdd:PRK09495  117 KANNNDI 123
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
143-287 1.37e-04

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: 45.75  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   143 TFFQFGASIQQQATVMLKIMQDYDWhvfSLVTTIFP----GYREFISFVKTTVDNSFVgwdmqnvITLDTSFEDAKTQVQ 218
Cdd:cd06350  139 YFLRTVPSDTLQAKAIADLLKHFNW---NYVSTVYSdddyGRSGIEAFEREAKERGIC-------IAQTIVIPENSTEDE 208
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4504125   219 LKKI--------HSSVILLYCSKDEAVLILSEARSLGLTGydFFWIVPSLVSGNTELI--PKEFPSGLISVSYDDWDYS 287
Cdd:cd06350  209 IKRIidklksspNAKVVVLFLTESDARELLKEAKRRNLTG--FTWIGSDGWGDSLVILegYEDVLGGAIGVVPRSKEIP 285
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
507-537 1.60e-04

Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold; This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 44.61  E-value: 1.60e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 4504125   507 MAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:cd01000   73 LIIATMTITPERAKEVDFSVPYYADGQGLLV 103
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
715-795 1.99e-04

The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270414 [Multi-domain]  Cd Length: 227  Bit Score: 44.68  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   715 DALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTgYGIALQKGSP-WKRQIDLALLQFVGDGEMEELET 793
Cdd:cd13696  146 DAILALKQGQADAMVEDNTVANYKASSGQFPSLEIAGEAPYPLDY-VAIGVRKGDYdWLRYLNLFVFQQNASGRYAELYQ 224

                 ..
gi 4504125   794 LW 795
Cdd:cd13696  225 KW 226
PBP2_GlnP cd13619
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ...
457-545 3.87e-04

Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold protein superfamily; Periplasmic glutamine binding domain GlnP serves as an initial receptor in the ABC transport of glutamine in eubacteria. GlnP belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270337 [Multi-domain]  Cd Length: 220  Bit Score: 43.46  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLylvtngkhgKKVNnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVM 536
Cdd:cd13619   23 VGIDVDLLNAIAKDQGFKVEL---------KPMG--FDAAIQAVQSGQADGVIAGMSITDERKKTFDFSDPYYDSGLVIA 91

                 ....*....
gi 4504125   537 VSRSNGTVS 545
Cdd:cd13619   92 VKKDNTSIK 100
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
457-547 1.09e-03

Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 periplasmic binding protein fold; This subgroup includes the periplasmic binding component of ABC transporter involved in uptake of mimosine MidA and its similar proteins. This periplasmic binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270225 [Multi-domain]  Cd Length: 230  Bit Score: 42.23  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLylvtngkhgkkVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFsVPFVETGISVM 536
Cdd:cd01004   25 IGFDVDLAKAIAKRLGLKVEI-----------VNVSFDGLIPALQSGRYDIIMSGITDTPERAKQVDF-VDYMKDGLGVL 92
                         90
                 ....*....|.
gi 4504125   537 VSRSNGTVSPS 547
Cdd:cd01004   93 VAKGNPKKIKS 103
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
681-796 1.54e-03

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 41.75  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   681 RFGTVPNGSTERNIRNNYPYMHQYMTKfnqkGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEgcklvtIGSGYIFATTG 760
Cdd:cd01007  111 RVAVVKGYALEELLRERYPNINLVEVD----STEEALEAVASGEADAYIGNLAVASYLIQKYG------LSNLKIAGLTD 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 4504125   761 Y----GIALQKGSP-WKRQIDLALLQfVGDGEMEELETLWL 796
Cdd:cd01007  181 YpqdlSFAVRKDWPeLLSILNKALAS-ISPEERQAIRNKWL 220
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
88-257 1.62e-03

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: 42.60  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125    88 DLMSGARIHGLVfGDDTDQEA--VAQmldfISSHTFVPILGIhggasmimADKDPTST------FFQFGASIQQQATVML 159
Cdd:cd19990   58 DLIKNKKVEAII-GPQTSEEAsfVAE----LGNKAQVPIISF--------SATSPTLSslrwpfFIRMTHNDSSQMKAIA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   160 KIMQDYDWHVFSLVTTIFPGYREFISFVKTTVDNsfVGWDMQNVITLDTSFEDAKTQVQLKKI---HSSVILLYCSKDEA 236
Cdd:cd19990  125 AIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQE--VGSRIEYRVALPPSSPEDSIEEELIKLksmQSRVFVVHMSSLLA 202
                        170       180
                 ....*....|....*....|.
gi 4504125   237 VLILSEARSLGLTGYDFFWIV 257
Cdd:cd19990  203 SRLFQEAKKLGMMEKGYVWIV 223
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
458-540 1.68e-03

Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), 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 majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. 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.


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 41.79  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLS----RTVKFtydlylvtngkhgkkVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGI 533
Cdd:cd13629   24 GFDVDLAKALAkdlgVKVEF---------------VNTAWDGLIPALQTGKFDLIISGMTITPERNLKVNFSNPYLVSGQ 88

                 ....*..
gi 4504125   534 SVMVSRS 540
Cdd:cd13629   89 TLLVNKK 95
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
458-541 2.29e-03

Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 periplasmic binding fold protein superfamily; This family comprises of the periplasmic-binding protein component (GltS) of an ABC transporter specific for glutamate or arginine from Lactococcus lactis, as well as its closely related proteins. The GltS domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis


Pssm-ID: 270338 [Multi-domain]  Cd Length: 227  Bit Score: 41.17  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRTvkftydlylvtNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVMV 537
Cdd:cd13620   31 GADIDIAKAIAKE-----------LGVKLEIKSMDFDNLLASLQSGKVDMAISGMTPTPERKKSVDFSDVYYEAKQSLLV 99

                 ....
gi 4504125   538 SRSN 541
Cdd:cd13620  100 KKAD 103
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
507-545 2.60e-03

Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein fold; This group includes periplasmic glutamate-binding domain GluB from Corynebacterium efficiens and its related proteins. The GluB domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270408 [Multi-domain]  Cd Length: 231  Bit Score: 41.10  E-value: 2.60e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 4504125   507 MAVGSLTINEERSEVVDFSVPFVETGISVMVSRSNGTVS 545
Cdd:cd13690   74 LVVATYSITPERRKQVDFAGPYYTAGQRLLVRAGSKIIT 112
PBP2_Arg_STM4351 cd13700
Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding ...
639-796 2.69e-03

Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding protein fold; This group includes domains similar to Escherichia coli arginine third transport system. STM4351 is the high arginine specific periplasmic-binding protein of ABC transport system. STM4351 belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270418 [Multi-domain]  Cd Length: 222  Bit Score: 40.89  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   639 VIFLASYTANLAAFMIQEEFVDQVTGLSDKKFqrphdysppfrfgTVPNGST-ERNIRNNYPymhQYMTKfNQKGVEDAL 717
Cdd:cd13700   79 VSFSTPYYENSAVVIAKKDTYKTFADLKGKKI-------------GVQNGTThQKYLQDKHK---EITTV-SYDSYQNAF 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   718 VSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVT--IGSGYIFAtTGYGIALQKGSP-WKRQIDLALLQFVGDGEMEELETL 794
Cdd:cd13700  142 LDLKNGRIDGVFGDTAVVAEWLKTNPDLAFVGekVTDPNYFG-TGLGIAVRKDNQaLLEKLNAALAAIKANGEYQKIYDK 220

                 ..
gi 4504125   795 WL 796
Cdd:cd13700  221 WF 222
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
458-539 3.08e-03

Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and related proteins; the type 2 periplasmic-binding protein fold; This family comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270222 [Multi-domain]  Cd Length: 228  Bit Score: 40.74  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRTVKFTYDLylvtngkhgkkVNNVWNGMIGEVVYQR--AVMAvgSLTINEERSEVVDFSVPFVETGISV 535
Cdd:cd01001   26 GFDIDLANALCKRMKVKCEI-----------VTQPWDGLIPALKAGKydAIIA--SMSITDKRRQQIDFTDPYYRTPSRF 92

                 ....
gi 4504125   536 MVSR 539
Cdd:cd01001   93 VARK 96
PBP2_OccT_like cd13699
Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding ...
457-551 3.16e-03

Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding protein fold; This group includes periplasmic octopine-binding protein and related proteins. This group belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270417 [Multi-domain]  Cd Length: 211  Bit Score: 40.82  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   457 KGFCIDILKKLSRTVKFTYDLylvtngkhgkkVNNVWNGMIGEVVYQR--AVMAvgSLTINEERSEVVDFSVPFVETGIS 534
Cdd:cd13699   25 GGFEIDLANVLCERMKVKCTF-----------VVQDWDGMIPALNAGKfdVIMD--AMSITAERKKVIDFSTPYAATPNS 91
                         90       100
                 ....*....|....*....|
gi 4504125   535 VMVSR---SNGTVSpSAFLE 551
Cdd:cd13699   92 FAVVTigvQSGTTY-AKFIE 110
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
715-795 5.04e-03

Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 periplasmic binding protein fold; This subgroup includes the periplasmic binding component of ABC transporter involved in uptake of mimosine MidA and its similar proteins. This periplasmic binding domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises 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. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270225 [Multi-domain]  Cd Length: 230  Bit Score: 40.30  E-value: 5.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   715 DALVSLKTGKLDAFIYDAAVLNYKAGRDEGcKLVTIGSGYIFATTgYGIALQKGSPWKRQ-IDLALLQFVGDGEMEELET 793
Cdd:cd01004  149 DALQALRSGRADAYLSDSPTAAYAVKQSPG-KLELVGEVFGSPAP-IGIAVKKDDPALADaVQAALNALIADGTYKKILK 226

                 ..
gi 4504125   794 LW 795
Cdd:cd01004  227 KW 228
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
458-541 6.13e-03

Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 periplasmic binding protein; This periplasmic substrate component serves as an initial receptor in the ABC transport of glutamine in eubacteria and archaea. After binding the alanine with high affinity, this domain Interacts 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. This alanine specific domain belong to the PBP2 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: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 39.76  E-value: 6.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   458 GFCIDILKKLSRTVKFTYDlylVTNGKhgkkvnnvWNGMIGEVVYQRAVMAVGSLTINEERSEVVDFSVPFVETGISVmV 537
Cdd:cd13628   25 GFDIELAKTIAKKLGLKLQ---IQEYD--------FNGLIPALASGQADLALAGITPTPERKKVVDFSEPYYEASDTI-V 92

                 ....
gi 4504125   538 SRSN 541
Cdd:cd13628   93 S*KD 96
PBP1_GC_G-like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
110-287 7.14e-03

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


Pssm-ID: 380595 [Multi-domain]  Cd Length: 390  Bit Score: 40.55  E-value: 7.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   110 AQMLDFISSHTFVPILGIHGgASMIMADKDPTSTFFQFGASIQQQATVMLKIMQDYDW-HVfslvtTIFPGYREFISFVK 188
Cdd:cd06372   81 AEVTGLLASEWNIPMFGFVG-QSPKLDDRDVYDTYVKLVPPLQRIGEVLVKTLQFFGWtHV-----AMFGGSSATSTWDK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4504125   189 -----TTVDNSF-VGWDMQNVITLDTSFEDAkTQVQLKKIHS--SVILLYCSKDEAVLILSEARSLGLTGYDFFWIV--- 257
Cdd:cd06372  155 vdelwKSVENQLkFNFNVTAKVKYDTSNPDL-LQENLRYISSvaRVIVLICSSEDARSILLEAEKLGLMDGEYVFFLlqq 233
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 4504125   258 -------PSLVSGNTELIPKEFPSG-LISV-SYDDWDYS 287
Cdd:cd06372  234 fedsfwkEVLNDEKNQVFLKAYEMVfLIAQsSYGTYGYS 272
 
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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