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Conserved domains on  [gi|1622942472|ref|XP_028704836|]
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glutamate receptor ionotropic, delta-2 isoform X2 [Macaca mulatta]

Protein Classification

substrate-binding domain-containing protein; glutamate ABC transporter substrate-binding protein( domain architecture ID 10157287)

substrate-binding domain-containing protein similar to ionotropic glutamate receptor receptor (iGluR) subtypes, which contain the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain that is structurally homologous to the periplasmic-binding fold type 1 (PBP1), and the C-terminal ligand-binding domain that belongs to the PBP2 fold| glutamate ABC transporter substrate-binding protein functions as the initial receptor in the ABC transport of glutamate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
28-429 0e+00

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family. 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. 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. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 are closer related 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 tumor necrosis factor family that is secreted from cerebellar granule cells.


:

Pssm-ID: 380614 [Multi-domain]  Cd Length: 402  Bit Score: 879.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06391     1 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06391    81 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 267
Cdd:cd06391   161 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 268 VDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 347
Cdd:cd06391   241 VDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 348 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 427
Cdd:cd06391   321 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 400

                  ..
gi 1622942472 428 SL 429
Cdd:cd06391   401 SL 402
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
440-806 0e+00

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: 535.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 440 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 519
Cdd:cd13731     1 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgs 599
Cdd:cd13731    81 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAE---------------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPY 679
Cdd:cd13731   115 ----------------------------------------------------------------SIQSLQDLSKQTDIPY 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 680 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 759
Cdd:cd13731   131 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 210
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 806
Cdd:cd13731   211 TVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 257
 
Name Accession Description Interval E-value
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
28-429 0e+00

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family. 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. 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. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 are closer related 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 tumor necrosis factor family that is secreted from cerebellar granule cells.


Pssm-ID: 380614 [Multi-domain]  Cd Length: 402  Bit Score: 879.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06391     1 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06391    81 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 267
Cdd:cd06391   161 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 268 VDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 347
Cdd:cd06391   241 VDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 348 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 427
Cdd:cd06391   321 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 400

                  ..
gi 1622942472 428 SL 429
Cdd:cd06391   401 SL 402
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
440-806 0e+00

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: 535.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 440 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 519
Cdd:cd13731     1 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgs 599
Cdd:cd13731    81 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAE---------------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPY 679
Cdd:cd13731   115 ----------------------------------------------------------------SIQSLQDLSKQTDIPY 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 680 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 759
Cdd:cd13731   131 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 210
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 806
Cdd:cd13731   211 TVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 257
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
566-841 5.26e-80

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: 259.93  E-value: 5.26e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 566 DLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMT---STTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFAL 642
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPLETeenRFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 643 IVISSYTANLAAFLTITRIESSIQSLQDLSKQTEIPYGTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSEnnv 722
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNE--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 723 lesqAGIQKVKYGNYAFVWDAavLEYVAINDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKH 802
Cdd:pfam00060 158 ----EGVALVRNGIYAYALLS--ENYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEK 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622942472 803 KWWPKNGQCDLYSSVDTKQKggaLDIKSFAGVFCILAAG 841
Cdd:pfam00060 232 KWWPKSGECDSKSSASSSSQ---LGLKSFAGLFLILGIG 267
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
664-807 3.95e-46

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: 161.30  E-value: 3.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  664 SIQSLQDLSKQTEIPYGTVLDSAVYEHVRMKGLNPferdsmYSQMWRMINRSngsENNVLESQAGIQKVKYGNYAFVWDA 743
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPE------YSRMWPYMKSP---EVFVKSYAEGVQRVRVSNYAFIMES 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942472  744 AVLEYVAINDpdCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPK 807
Cdd:smart00079  72 PYLDYELSRN--CDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
41-404 3.75e-41

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: 154.85  E-value: 3.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  41 DEVFRTAVGDLNQNEEILQTEKITFSVtfVDGNNPFQAVQEAC-ELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLfi 119
Cdd:pfam01094   3 LLAVRLAVEDINADPGLLPGTKLEYII--LDTCCDPSLALAAAlDLLKGEVVAIIGPSCSSVASAVASLANEWKVPLI-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 120 qrSTAGTPRSGCGLTRSnrndDYTLSVRPP-VYLNDVILRVVTEYAWQKFIIFY-DSEYDIRGIQEFLDKVSQQGMDVAL 197
Cdd:pfam01094  79 --SYGSTSPALSDLNRY----PTFLRTTPSdTSQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 198 QKV---ENNINKMITTLfdtmrieeLNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELV 274
Cdd:pfam01094 153 KAVippAQDDDEIARKL--------LKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSLVILNPS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 275 -RRSIGRLTIIRQTFPVPQNISQrcFRgNHRISSTLCDPKDPFAQNMeISNLYIYDTVLLLANAFHKKLEDRKWHSmasl 353
Cdd:pfam01094 225 tLEAAGGVLGFRLHPPDSPEFSE--FF-WEKLSDEKELYENLGGLPV-SYGALAYDAVYLLAHALHNLLRDDKPGR---- 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622942472 354 SCIRknSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTN 404
Cdd:pfam01094 297 ACGA--LGPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLN 345
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
443-556 8.13e-16

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: 77.33  E-value: 8.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLE-EPFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGI 521
Cdd:COG0834     1 LRVGVDPDyPPFSFRDED-----GKLVGFDVDLARAIAKRLGLKVEFVPVP------------WDRLIPALQSGKVDLII 63
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTV 556
Cdd:COG0834    64 AGMTITPEREKQVDFSDPYYTSGQVLLVRKDNSGI 98
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
452-553 9.74e-06

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 48.18  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:PRK11260   53 PFSFQGED-----GKLTGFEVEFAEALAKHLGVKASLKPTK------------WDGMLASLDSKRIDVVINQVTISDERK 115
                          90       100
                  ....*....|....*....|..
gi 1622942472 532 NVVDFTTRYMDYSVGVLLRRAE 553
Cdd:PRK11260  116 KKYDFSTPYTVSGIQALVKKGN 137
 
Name Accession Description Interval E-value
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
28-429 0e+00

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family. 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. 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. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 are closer related 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 tumor necrosis factor family that is secreted from cerebellar granule cells.


Pssm-ID: 380614 [Multi-domain]  Cd Length: 402  Bit Score: 879.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06391     1 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06391    81 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 267
Cdd:cd06391   161 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 268 VDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 347
Cdd:cd06391   241 VDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSSLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 348 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 427
Cdd:cd06391   321 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 400

                  ..
gi 1622942472 428 SL 429
Cdd:cd06391   401 SL 402
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
28-429 0e+00

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family of delta receptors, GluRdelta1 and GluRdelta2; This CD represents the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family of delta receptors, GluRdelta1 and GluRdelta2. 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. 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. Phylogenetic 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: 380604 [Multi-domain]  Cd Length: 401  Bit Score: 860.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06381     1 HIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06381    81 LTDAMHIPHLFVQRNPGGSPRTACHLNPSPDGEAYTLASRPPVRLNDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFLDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 267
Cdd:cd06381   161 ASRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNRYRDTLRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEISD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 268 VDVQELVRRSIGRLTIIRQTFPvPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 347
Cdd:cd06381   241 PEILDLVHSALGRMTVVRQIFP-SAKDNQKCFRNNHRISSLLCDPQEGYLQMLQISNLYLYDSVLMLANAFHRKLEDRKW 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 348 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 427
Cdd:cd06381   320 HSMASLNCIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDSSNPYVQFEILGTTYSETFGKDMRKLATWDSEKGLNG 399

                  ..
gi 1622942472 428 SL 429
Cdd:cd06381   400 SL 401
PBP1_iGluR_delta_1 cd06392
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 ...
28-429 0e+00

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family. 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. 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. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 may be closer related to non-NMDA receptors. In contrast to GluRdelta2, GluRdelta1 is expressed in many areas in the developing CNS, including the hippocampus and the caudate putamen. 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: 380615  Cd Length: 402  Bit Score: 638.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06392     1 HIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06392    81 LTDAMHIPHLFVQRNSGGSPRTACHLNPSPEGEEYTLAARPPVRLNDVMLKLVTELRWQKFIVFYDSEYDIRGLQSFLDQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 267
Cdd:cd06392   161 ASRLGLDVSLQKVDRNISRVFTNLFTTMKTEELNRYRDTLRRAILLLSPRGAQSFINEAVETNLASKDSHWVFVNEEISD 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 268 VDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKW 347
Cdd:cd06392   241 PEILELVHSALGRMTVIRQIFPLSKDNNQRCMRNNHRISSLLCDPQEGYLQMLQVSNLYLYDSVLMLANAFHRKLEDRKW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 348 HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNG 427
Cdd:cd06392   321 HSMASLNCIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDGANPYVQFEILGTSYSETFGKDVRRLATWDSEKGLNG 400

                  ..
gi 1622942472 428 SL 429
Cdd:cd06392   401 SL 402
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
440-806 0e+00

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: 535.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 440 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 519
Cdd:cd13731     1 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgs 599
Cdd:cd13731    81 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAE---------------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPY 679
Cdd:cd13731   115 ----------------------------------------------------------------SIQSLQDLSKQTDIPY 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 680 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 759
Cdd:cd13731   131 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 210
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 806
Cdd:cd13731   211 TVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 257
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
440-806 2.51e-171

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: 497.83  E-value: 2.51e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 440 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 519
Cdd:cd13716     1 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHKYGSQQEDGTWNGLIGELVFKRADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgs 599
Cdd:cd13716    81 GISALTITPERENVVDFTTRYMDYSVGVLLRKAE---------------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPY 679
Cdd:cd13716   115 ----------------------------------------------------------------SIQSLQDLSKQTDIPY 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 680 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 759
Cdd:cd13716   131 GTVLDSAVYEYVRSKGTNPFERDSMYSQMWRMINRSNGSENNVSESSEGIRKVKYGNYAFVWDAAVLEYVAINDDDCSFY 210
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 806
Cdd:cd13716   211 TVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 257
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
440-806 1.24e-125

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: 379.69  E-value: 1.24e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 440 GVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADI 519
Cdd:cd13730     1 GLTLKVVTVLEEPFVMVAENILGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGKYGHQLHNTSWNGMIGELISKRADL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgs 599
Cdd:cd13730    81 AISAITITPERESVVDFSKRYMDYSVGILIKKPE---------------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPY 679
Cdd:cd13730   115 ----------------------------------------------------------------PIRTFQDLSKQVEMSY 130
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 680 GTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFY 759
Cdd:cd13730   131 GTVRDSAVYEYFRAKGTNPLEQDSTFAELWRTISKNGGADNCVSSPSEGIRKAKKGNYAFLWDVAVVEYAALTDDDCSVT 210
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 806
Cdd:cd13730   211 VIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKWWP 257
PBP1_iGluR_N_LIVBP-like cd06351
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
28-428 6.08e-95

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


Pssm-ID: 380574  Cd Length: 348  Bit Score: 303.12  E-value: 6.08e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06351     1 HIGFIFEVNNEPAAKAFEVAVTYLKKNINTRYGLSVQYDSIEANKSNAFVLLEAICNKYATGTPALILDTTKSSINSLTS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIPHLFIQRSTAGTPRsgcglTRSNRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06351    81 ALGAPHISASYGQQGDLRQWR-----DLDEAKQKYLLQVRPPEALRSIVLHLNITNAWIKFVDSYDMEHYKSLLQNIQTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTL-RRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIN 266
Cdd:cd06351   156 AVQNNVIVAIAKVGKREREEQLDINNFFILGTLQSIRMVLeVRPAYFERNFAWHAITQNEVEISSQSDNAHIMFMNPMAY 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 267 DVdVQELVRRSIGRLTIIRQTFPVPQNIsQRCFRGNHRisSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKkledrk 346
Cdd:cd06351   236 DI-LLETVYRDRLGLTRTTYNLNENPMV-QQFIQRWVR--LDEREFPEAKNAELQLSSAFYFDLALRSALAFKE------ 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 347 whsmaslscirknskpwqggrsmletikkggvsglTGELEFGENGGNPNVHFEILGTNYgeelGRGVRKLGCWNPVTGLN 426
Cdd:cd06351   306 -----------------------------------TGYGTFDLQSTQPFNGHSFMKFEM----DINVRKIRGWSEYESVN 346

                  ..
gi 1622942472 427 GS 428
Cdd:cd06351   347 SK 348
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
441-806 1.13e-92

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: 293.32  E-value: 1.13e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 441 VVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIG 520
Cdd:cd13685     2 KTLRVTTILEPPFVMKKRDSLSGNPRFEGYCIDLLEELAKILGFDYEIYLVPDGKYGSRDENGNWNGMIGELVRGEADIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRRaektvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsm 600
Cdd:cd13685    82 VAPLTITAEREEVVDFTKPFMDTGISILMRK------------------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 601 tsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriESSIQSLQDLSKQTEIPYG 680
Cdd:cd13685   113 -------------------------------------------------------------PTPIESLEDLAKQSKIEYG 131
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 681 TVLDSAVYEHVRMKGLNPFERDSmYSQMWRMINRSngseNNVLESQAGIQKVKYGN--YAFVWDAAVLEYVAINdpDCSF 758
Cdd:cd13685   132 TLKGSSTFTFFKNSKNPEYRRYE-YTKIMSAMSPS----VLVASAAEGVQRVRESNggYAFIGEATSIDYEVLR--NCDL 204
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1622942472 759 YTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWP 806
Cdd:cd13685   205 TKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGELEKLKEKWWN 252
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
442-805 5.91e-83

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: 271.48  E-value: 5.91e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVTVLEEPFVMVSENvlgKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGI 521
Cdd:cd13717     3 VYRIGTVESPPFVYRDRD---GSPIWEGYCIDLIEEISEILNFDYEIVEPEDGKFGTMDENGEWNGLIGDLVRKEADIAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYsVG--VLLRRAEKTVDMFACLAPFDLSLWaciagtvllvgllvyllnwlnpprlqmgs 599
Cdd:cd13717    80 AALSVMAEREEVVDFTVPYYDL-VGitILMKKPERPTSLFKFLTVLELEVW----------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mTSTTLYNSMWFVYGSFVQQGG-EVPyTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTEIP 678
Cdd:cd13717   130 -REFTLKESLWFCLTSLTPQGGgEAP-KNLSGRLLVATWWLFVFIIIASYTANLAAFLTVSRLQTPVESLDDLARQYKIQ 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 679 YGTVLDSAVYEH-VRMKG-----------------LNPFERDSM----------YSQMWRMINRSNGSENnvleSQAGIQ 730
Cdd:cd13717   208 YTVVKNSSTHTYfERMKNaedtlyemwkdmslndsLSPVERAKLavwdypvsekYTKIYQAMQEAGLVAN----AEEGVK 283
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942472 731 KVKYGN---YAFVWDAAVLEYVAINDpdCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd13717   284 RVRESTsagFAFIGDATDIKYEILTN--CDLQEVGEEFSRKPYAIAVQQGSPLKDELNYAILELQNDRFLEKLKAKWW 359
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
566-841 5.26e-80

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: 259.93  E-value: 5.26e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 566 DLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMT---STTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFAL 642
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPLETeenRFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 643 IVISSYTANLAAFLTITRIESSIQSLQDLSKQTEIPYGTVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSNGSEnnv 722
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNE--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 723 lesqAGIQKVKYGNYAFVWDAavLEYVAINDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKH 802
Cdd:pfam00060 158 ----EGVALVRNGIYAYALLS--ENYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEK 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1622942472 803 KWWPKNGQCDLYSSVDTKQKggaLDIKSFAGVFCILAAG 841
Cdd:pfam00060 232 KWWPKSGECDSKSSASSSSQ---LGLKSFAGLFLILGIG 267
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
443-805 6.10e-75

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: 250.38  E-value: 6.10e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMV--SENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIG 520
Cdd:cd13723     4 LIVTTVLEEPFVMFrkSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKT-VDMFACLAPFDLSLWACI------AGTVLLVGLLVYLLNWLNPP 593
Cdd:cd13723    84 VAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTnPSVFSFLNPLSPDIWMYVllaylgVSCVLFVIARFSPYEWYDAH 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 594 RLQMGSMT---STTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQD 670
Cdd:cd13723   164 PCNPGSEVvenNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 671 LSKQTEIPYGTVLDSAVYEHVRMKGLNPFERdsmysqMWRMInrSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYva 750
Cdd:cd13723   244 LAKQTKIEYGAVKDGATMTFFKKSKISTFEK------MWAFM--SSKPSALVKNNEEGIQRALTADYALLMESTTIEY-- 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622942472 751 INDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd13723   314 VTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWW 368
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
28-429 8.09e-69

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-aspartate) subtypes of ionotropic glutamate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-asparate) subtypes of ionotropic 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. Glutamate mediates the majority of excitatory synaptic transmission in the central nervous system via two broad classes of ionotropic receptors, characterized by their response to glutamate agonists: N-methyl-D-aspartate (NMDA) and non-NMDA receptors. NMDA receptors have intrinsically slow kinetics, are highly permeable to Ca2+, and are blocked by extracellular Mg2+ in a voltage-dependent manner. Non-NMDA receptors have faster kinetics, are most often only weakly permeable to Ca2+, and are not blocked by extracellular Mg2+. While non-NMDA receptors typically mediate excitatory synaptic responses at resting membrane potentials, NMDA receptors contribute several forms of synaptic plasticity and are thought to play an important role in the development of synaptic pathways. Non-NMDA receptors include alpha-amino-3-hydroxy-5-methyl-4-isoxazole proprionate (AMPA) and kainate receptors.


Pssm-ID: 380591 [Multi-domain]  Cd Length: 339  Bit Score: 232.26  E-value: 8.09e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDES-AKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQ 106
Cdd:cd06368     1 KIGAIFNEVnDAHERAAFRYAVERLNTNIVKLAYFRITYSIEAIDSNSHFDATDKACDLLEKGVVAIVGPSSSDSNNALQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 107 SLADAMHIPHLFIQRSTAGtprsgcgltrsnRNDDYTLSVRPPVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLD 186
Cdd:cd06368    81 SICDALDVPHITVHDDPRL------------SKSQYSLSLYPRNQLSQAVSDLLKYWRWKRFVLVYDDDDRLRRLQELLE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 187 KVSQQGMDVALQKVENNInkmittlFDTMRIEELNRYRDTLRRAILV-MNPATAKSFITEVVETNLVAFDCHWIIINEEI 265
Cdd:cd06368   149 AARFSKRFVSVRKVDLDY-------KTLDETPLLKRKDCSLFSRILIdLSPEKAYTFLLQALEMGMTIELYHYFLTTMDL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 266 NDVDVQELVRRSIGRLTIIRQTFPVPQNIS--QRCFRGNHRISSTLCDPKDPfaQNMEISNLYIYDTVLLLANAFHKkle 343
Cdd:cd06368   222 SLLLDLELFRYNHANITGFQLVDNNSMYKEdiNRLAFNWSRFRQHIKIESNL--RGPPYEAALMFDAVLLLADAFRR--- 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 344 drkwhsmaslscirknskpwqggrsmletikkggvsglTGELEFGENGGNPNVHFEILGTNYGeelgrGVRKLGCWNPVT 423
Cdd:cd06368   297 --------------------------------------TGDLRFNGTGLRSNFTLRILELGYG-----GLRKIGFWDSNT 333

                  ....*.
gi 1622942472 424 GLNGSL 429
Cdd:cd06368   334 RLAMNL 339
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
441-805 4.14e-58

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: 199.69  E-value: 4.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 441 VVLRVVTVLEEPFVMV--SENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQED-GTWNGLVGELVFKRA 517
Cdd:cd13714     2 KTLIVTTILEEPYVMLkeSAKPLTGNDRFEGFCIDLLKELAKILGFNYTIRLVPDGKYGSYDPEtGEWNGMVRELIDGRA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 518 DIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqm 597
Cdd:cd13714    82 DLAVADLTITYERESVVDFTKPFMNLGISILYRKPT-------------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 598 gsmtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEI 677
Cdd:cd13714   118 ------------------------------------------------------------------PIESADDLAKQTKI 131
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 678 PYGTVLDSAVYEhvrmkglnpFERDSMYSQMWRMINRSNGSENNVLES--QAGIQKVKYGNYAFVWDAAVLEYVAINdpD 755
Cdd:cd13714   132 KYGTLRGGSTMT---------FFRDSNISTYQKMWNFMMSAKPSVFVKsnEEGVARVLKGKYAFLMESTSIEYVTQR--N 200
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622942472 756 CSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd13714   201 CNLTQIGGLLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKWW 250
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
443-805 5.73e-53

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: 184.88  E-value: 5.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMVSENVLGKP--KKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPqEDGTWNGLVGELVFKRADIG 520
Cdd:cd00998     3 LKVVVPLEPPFVMFVTGSNAVTgnGRFEGYCIDLLKELSQSLGFTYEYYLVPDGKFGAP-VNGSWNGMVGEVVRGEADLA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRraektvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsm 600
Cdd:cd00998    82 VGPITITSERSVVIDFTQPFMTSGIGIMIP-------------------------------------------------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 601 tsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriessIQSLQDLSKQTEIPYG 680
Cdd:cd00998   112 ----------------------------------------------------------------IRSIDDLKRQTDIEFG 127
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 681 TVLDSAVYEHVRMKGLNPFERDSMYSQMWRMINRSngsennvleSQAGIQKVKYGN-YAFVWDAAVLEYVAINDPdCSFY 759
Cdd:cd00998   128 TVENSFTETFLRSSGIYPFYKTWMYSEARVVFVNN---------IAEGIERVRKGKvYAFIWDRPYLEYYARQDP-CKLI 197
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd00998   198 KTGGGFGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
28-333 3.94e-52

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: 185.70  E-value: 3.94e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFD-----ESAKKDDEVFRTAVGDLNQNEEILQteKITFSVTFVDG-NNPFQAVQEACELM-NQGILALVSSIGCT 100
Cdd:cd06269     1 TIGALLPvhdylESGAKVLPAFELALSDVNSRPDLLP--KTTLGLAIRDSeCNPTQALLSACDLLaAAKVVAILGPGCSA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 101 SAGSLQSLADAMHIPHLFIQRSTAGTPRSgcgltrsnRNDDYTLSVRPP-VYLNDVILRVVTEYAWQKFIIFY-DSEYDI 178
Cdd:cd06269    79 SAAPVANLARHWDIPVLSYGATAPGLSDK--------SRYAYFLRTVPPdSKQADAMLALVRRLGWNKVVLIYsDDEYGE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 179 RGIQEFLDKVSQQG-MDVALQKVENNINKMITtlfdtmriEELNRYRDTL-RRAILVMNPATAKSFITEVVETNLVAFDC 256
Cdd:cd06269   151 FGLEGLEELFQEKGgLITSRQSFDENKDDDLT--------KLLRNLRDTEaRVIILLASPDTARSLMLEAKRLDMTSKDY 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942472 257 HWIIINEEINDVDVQ-ELVRRSIGRLTIIRQTFPVPQNIsQRCFRGNHRiSSTLCDPKDPFAQNMEISNLYIYDTVLL 333
Cdd:cd06269   223 VWFVIDGEASSSDEHgDEARQAAEGAITVTLIFPVVKEF-LKFSMELKL-KSSKRKQGLNEEYELNNFAAFFYDAVLA 298
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
443-804 1.19e-48

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: 172.82  E-value: 1.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMVsenvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGS--PQEDGTWNGLVGELVFKRADIG 520
Cdd:cd13687     4 LKVVTLEEAPFVYV--------KCCYGFCIDLLKKLAEDVNFTYDLYLVTDGKFGTvnKSINGEWNGMIGELVSGRADMA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKtvdmfaclapfdlslwacIAGtvllvgllvyllnwLNPPRLQMGSm 600
Cdd:cd13687    76 VASLTINPERSEVIDFSKPFKYTGITILVKKRNE------------------LSG--------------INDPRLRNPS- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 601 tsttlynsmwfvygsfvqqggeVPYTtlatrmmmgawwlfalivissytanlaafltitriessiqslqdlskqteipYG 680
Cdd:cd13687   123 ----------------------PPFR----------------------------------------------------FG 128
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 681 TVLDSAVYEHVRmkglnpferdSMYSQMWRMINRsngseNNVLESQAGIQKVKYGNY-AFVWDAAVLEYVAINDPDCSFY 759
Cdd:cd13687   129 TVPNSSTERYFR----------RQVELMHRYMEK-----YNYETVEEAIQALKNGKLdAFIWDSAVLEYEASQDEGCKLV 193
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 804
Cdd:cd13687   194 TVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHESGFMEELDKKW 238
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
445-811 1.01e-46

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: 167.92  E-value: 1.01e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 445 VVTVLEEPFVMVSENVLGKP----KKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSP-QEDGTWNGLVGELVFKRADI 519
Cdd:cd13715     6 VTTILEEPYVMMKKNHEGEPlegnERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARdADTGIWNGMVGELVRGEADI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAektvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgs 599
Cdd:cd13715    86 AIAPLTITLVRERVIDFSKPFMSLGISIMIKKP----------------------------------------------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mtsttlynsmwfvygsfvqqggeVPyttlatrmmmgawwlfalivissytanlaafltitriessIQSLQDLSKQTEIPY 679
Cdd:cd13715   119 -----------------------VP----------------------------------------IESAEDLAKQTEIAY 135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 680 GTVLDSAVYEhvrmkglnpFERDS---MYSQMWRMINrSNGSENNVLESQAGIQKVK--YGNYAFVWDAAVLEYVAINDP 754
Cdd:cd13715   136 GTLDSGSTKE---------FFRRSkiaVYDKMWEYMN-SAEPSVFVRTTDEGIARVRksKGKYAYLLESTMNEYINQRKP 205
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942472 755 dCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQC 811
Cdd:cd13715   206 -CDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC 261
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
443-805 2.37e-46

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: 169.42  E-value: 2.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMVSEN--VLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIG 520
Cdd:cd13724     4 LVVTTILENPYLMLKGNhqEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKADLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLR-RAEKTVDMFACLAPFDLSLWACI------AGTVLLVGLLVYLLNWLNPP 593
Cdd:cd13724    84 VAGLTITAEREKVIDFSKPFMTLGISILYRvHMGRKPGYFSFLDPFSPGVWLFMllaylaVSCVLFLVARLTPYEWYSPH 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 594 RLQMGS----MTSTTLYNSMWFVYGSFVQQGgevpyttlatrmmmgawwlfalivissytanlaafltiTRIESSIQSLQ 669
Cdd:cd13724   164 PCAQGRcnllVNQYSLGNSLWFPVGGFMQQG--------------------------------------STIAPPIESVD 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 670 DLSKQTEIPYGTVLDSAVYEhvrmkglnpFERDSMYSQMWRMINRSNGSENNVL--ESQAGIQKVKYGNYAFVWDAAVLE 747
Cdd:cd13724   206 DLADQTAIEYGTIHGGSSMT---------FFQNSRYQTYQRMWNYMYSKQPSVFvkSTEEGIARVLNSNYAFLLESTMNE 276
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622942472 748 YVaiNDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd13724   277 YY--RQRNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWW 332
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
664-807 3.95e-46

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: 161.30  E-value: 3.95e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  664 SIQSLQDLSKQTEIPYGTVLDSAVYEHVRMKGLNPferdsmYSQMWRMINRSngsENNVLESQAGIQKVKYGNYAFVWDA 743
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPE------YSRMWPYMKSP---EVFVKSYAEGVQRVRVSNYAFIMES 71
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622942472  744 AVLEYVAINDpdCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPK 807
Cdd:smart00079  72 PYLDYELSRN--CDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
441-551 8.71e-46

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: 159.61  E-value: 8.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 441 VVLRVVTVLEEPFVMVSENVLGkPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDG-TWNGLVGELVFKRADI 519
Cdd:pfam10613   1 KTLIVTTILEPPFVMLKENLEG-NDRYEGFCIDLLKELAEILGFKYEIRLVPDGKYGSLDPTTgEWNGMIGELIDGKADL 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRR 551
Cdd:pfam10613  80 AVAPLTITSEREKVVDFTKPFMTLGISILMKK 111
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
41-404 3.75e-41

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: 154.85  E-value: 3.75e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  41 DEVFRTAVGDLNQNEEILQTEKITFSVtfVDGNNPFQAVQEAC-ELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLfi 119
Cdd:pfam01094   3 LLAVRLAVEDINADPGLLPGTKLEYII--LDTCCDPSLALAAAlDLLKGEVVAIIGPSCSSVASAVASLANEWKVPLI-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 120 qrSTAGTPRSGCGLTRSnrndDYTLSVRPP-VYLNDVILRVVTEYAWQKFIIFY-DSEYDIRGIQEFLDKVSQQGMDVAL 197
Cdd:pfam01094  79 --SYGSTSPALSDLNRY----PTFLRTTPSdTSQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 198 QKV---ENNINKMITTLfdtmrieeLNRYRDTLRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQELV 274
Cdd:pfam01094 153 KAVippAQDDDEIARKL--------LKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSLVILNPS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 275 -RRSIGRLTIIRQTFPVPQNISQrcFRgNHRISSTLCDPKDPFAQNMeISNLYIYDTVLLLANAFHKKLEDRKWHSmasl 353
Cdd:pfam01094 225 tLEAAGGVLGFRLHPPDSPEFSE--FF-WEKLSDEKELYENLGGLPV-SYGALAYDAVYLLAHALHNLLRDDKPGR---- 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622942472 354 SCIRknSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTN 404
Cdd:pfam01094 297 ACGA--LGPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLN 345
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
443-805 2.78e-38

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: 143.62  E-value: 2.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMV--SENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQE-DGTWNGLVGELVFKRADI 519
Cdd:cd13721     4 LIVTTILEEPYVLFkkSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHKADL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 520 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAektvdmfaclapfdlslwaciagtvllvgllvyllnwlNPprlqmgs 599
Cdd:cd13721    84 AVAPLAITYVREKVIDFSKPFMTLGISILYRKG--------------------------------------TP------- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 600 mtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriessIQSLQDLSKQTEIPY 679
Cdd:cd13721   119 -----------------------------------------------------------------IDSADDLAKQTKIEY 133
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 680 GTVLDSAVYEHVRMkglnpfERDSMYSQMWRMINrSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVaiNDPDCSFY 759
Cdd:cd13721   134 GAVEDGATMTFFKK------SKISTYDKMWAFMS-SRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFV--TQRNCNLT 204
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd13721   205 QIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWW 250
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
445-811 1.48e-36

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: 138.62  E-value: 1.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 445 VVTVLEEPFVMVSENV--LGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDG-TWNGLVGELVFKRADIGI 521
Cdd:cd13729     6 VTTILESPYVMLKKNHeqFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETkMWNGMVGELVYGKADVAV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsmt 601
Cdd:cd13729    86 APLTITLVREEVIDFSKPFMSLGISIMIKKPT------------------------------------------------ 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 602 sttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitrieSSIQSLQDLSKQTEIPYGT 681
Cdd:cd13729   118 -------------------------------------------------------------SPIESAEDLAKQTEIAYGT 136
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 682 VLDSAVYEHVRMKGLNPFERdsMYSQMwrminRSNGSENNVLESQAGIQKVKY--GNYAFVWDAAVLEYVAINDPdCSFY 759
Cdd:cd13729   137 LDAGSTKEFFRRSKIAVFEK--MWSYM-----KSADPSVFVKTTDEGVMRVRKskGKYAYLLESTMNEYIEQRKP-CDTM 208
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQC 811
Cdd:cd13729   209 KVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 260
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
443-805 8.10e-36

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: 136.33  E-value: 8.10e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMV--SENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIG 520
Cdd:cd13722     4 LIVTTILEEPYVMYrkSDKPLYGNDRFEGYCLDLLKELSNILGFLYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRADLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRRAektvdmfaclapfdlslwaciagtvllvgllvyllnwlNPprlqmgsm 600
Cdd:cd13722    84 VAPLTITYVREKVIDFSKPFMTLGISILYRKG--------------------------------------TP-------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 601 tsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriessIQSLQDLSKQTEIPYG 680
Cdd:cd13722   118 ----------------------------------------------------------------IDSADDLAKQTKIEYG 133
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 681 TVLDSAVYEHVRMKGLnpferdSMYSQMWR-MINRSNGSEnnVLESQAGIQKVKYGNYAFVWDAAVLEYVAinDPDCSFY 759
Cdd:cd13722   134 AVRDGSTMTFFKKSKI------STYEKMWAfMSSRQQTAL--VKNSDEGIQRVLTTDYALLMESTSIEYVT--QRNCNLT 203
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd13722   204 QIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWW 249
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
445-811 9.89e-35

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: 133.62  E-value: 9.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 445 VVTVLEEPFVMVSEN--VLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDG-TWNGLVGELVFKRADIGI 521
Cdd:cd13727     6 VTTIMESPYVMYKKNheMFEGNDKFEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDPETkIWNGMVGELVYGKAEIAV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsmt 601
Cdd:cd13727    86 APLTITLVREEVIDFSKPFMSLGISIMIKKPQ------------------------------------------------ 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 602 sttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPYGT 681
Cdd:cd13727   118 --------------------------------------------------------------PIESAEDLAKQTEIAYGT 135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 682 VLDSAVYEHVRMKGLnpferdSMYSQMWRMINRSNGS--ENNVLESQAGIQKVKyGNYAFVWDAAVLEYVAINDPdCSFY 759
Cdd:cd13727   136 LDSGSTKEFFRRSKI------AVYEKMWTYMKSAEPSvfTRTTAEGVARVRKSK-GKFAFLLESTMNEYIEQRKP-CDTM 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQC 811
Cdd:cd13727   208 KVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
445-811 1.56e-34

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: 132.84  E-value: 1.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 445 VVTVLEEPFVMVSEN--VLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGS-PQEDGTWNGLVGELVFKRADIGI 521
Cdd:cd13726     6 VTTILESPYVMMKKNheMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGArDADTKIWNGMVGELVYGKADIAI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsmt 601
Cdd:cd13726    86 APLTITLVREEVIDFSKPFMSLGISIMIKKGT------------------------------------------------ 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 602 sttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPYGT 681
Cdd:cd13726   118 --------------------------------------------------------------PIESAEDLSKQTEIAYGT 135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 682 VLDSAVYEHVRMKGLnpferdSMYSQMWRMInRSNGSENNVLESQAGIQKVK--YGNYAFVWDAAVLEYVAINDPdCSFY 759
Cdd:cd13726   136 LDSGSTKEFFRRSKI------AVFDKMWTYM-RSAEPSVFVRTTAEGVARVRksKGKYAYLLESTMNEYIEQRKP-CDTM 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQC 811
Cdd:cd13726   208 KVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
443-804 3.06e-32

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: 127.07  E-value: 3.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMVS--ENVLGKPKK-----------------------YQ---GFSIDVLDALSNYLGFNYEIYVAPDH 494
Cdd:cd13718     4 LKIVTLEEAPFVIVEpvDPLTGTCMRntvpcrkqlnhenstdadenryvKKcckGFCIDILKKLAKDVGFTYDLYLVTNG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 495 KYGSpQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKtvdmfaclapfdlslwacIA 574
Cdd:cd13718    84 KHGK-KINGVWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMVARSNQ------------------VS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 575 GtvllvgllvyllnwLNPPRLQMgsmtsttlynsmwfvygsfvqqggevPYttlatrmmmgawwlfalivissytanlaa 654
Cdd:cd13718   145 G--------------LSDKKFQR--------------------------PH----------------------------- 155
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 655 fltitriessiqslqdlSKQTEIPYGTVLDSAVYEHVRmkglnpferdSMYSQMWRMINRSNgsENNVlesQAGIQKVKY 734
Cdd:cd13718   156 -----------------DQSPPFRFGTVPNGSTERNIR----------NNYPEMHQYMRKYN--QKGV---EDALVSLKT 203
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942472 735 GNY-AFVWDAAVLEYVAINDPDCSFYTIGNTV--ADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 804
Cdd:cd13718   204 GKLdAFIYDAAVLNYMAGQDEGCKLVTIGSGKwfAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLW 276
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
443-805 3.21e-32

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: 125.97  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMVSENV--LGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIG 520
Cdd:cd13725     4 LVVTTILENPYVMRRPNFqaLSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLrraektvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsm 600
Cdd:cd13725    84 VAAFTITAEREKVIDFSKPFMTLGISILY--------------------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 601 tsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitRIESSIQSLQDLSKQTEIPYG 680
Cdd:cd13725   113 -----------------------------------------------------------RVHMPVESADDLADQTNIEYG 133
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 681 TVLDSAVYEhvrmkglnpFERDSMYSQMWRMINRSNGSENNVL--ESQAGIQKVKYGNYAFVWDAAVLEYVaiNDPDCSF 758
Cdd:cd13725   134 TIHAGSTMT---------FFQNSRYQTYQRMWNYMQSKQPSVFvkSTEEGIARVLNSRYAFLLESTMNEYH--RRLNCNL 202
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622942472 759 YTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 805
Cdd:cd13725   203 TQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 249
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
443-804 9.20e-32

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: 125.55  E-value: 9.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMVS------------------ENVLGKPKKYQ---GFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQE 501
Cdd:cd13719     4 LKIVTIHEEPFVYVRptpsdgtcreeftvncpnFNISGRPTVPFccyGYCIDLLIKLARKMNFTYELHLVADGQFGTQER 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 502 DG-----TWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKtvdmfaclapfdlslwacIAGt 576
Cdd:cd13719    84 VNnsnkkEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEIR------------------LTG- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 577 vllvgllvyllnwLNPPRLQmgsmtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytaNLAAFL 656
Cdd:cd13719   145 -------------INDPRLR------------------------------------------------------NPSEKF 157
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 657 TitriessiqslqdlskqteipYGTVLDSAVYEHVRMKglnpFERDSMYSQMwrminrsngSENNVLESQAGIQKVKYGN 736
Cdd:cd13719   158 I---------------------YATVKGSSVDMYFRRQ----VELSTMYRHM---------EKHNYETAEEAIQAVRDGK 203
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942472 737 -YAFVWDAAVLEYVAINdpDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 804
Cdd:cd13719   204 lHAFIWDSSRLEFEASQ--DCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTW 270
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
29-426 4.49e-31

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


Pssm-ID: 380605  Cd Length: 335  Bit Score: 125.03  E-value: 4.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  29 IGAIFDESAKKDDEVFRTAVGDLNqNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSL 108
Cdd:cd06382     2 IGGIFDEDDEDLEIAFKYAVDRIN-RERTLPNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSDIVQSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 109 ADAMHIPHLFIQRStagtprsgcglTRSNRNDDYTLSVRP-PVYLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06382    81 CDALEIPHIETRWD-----------PKESNRDTFTINLYPdPDALSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINkmittlfdtmrieelnrYRDTLRRA--------ILVMNPATAKSFITEVVETNLVAFDCHWI 259
Cdd:cd06382   150 PKPKDIPITVRQLDPGDD-----------------YRPVLKEIkksgetriILDCSPDRLVDVLKQAQQVGMLTEYYHYI 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 260 IINEEINDVDVQElVRRSIGRLTIIR----QTFPVpQNISQRCFRGNHRISSTLCDPkdpfaQNMEISNLYIYDTVLLLA 335
Cdd:cd06382   213 LTNLDLHTLDLEP-FKYSGANITGFRlvdpENPEV-KNVLKDWSKREKEGFNKDIGP-----GQITTETALMYDAVNLFA 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 336 NAFHKkledrkwhsmaslscirknskpwqggrsmletikkggvsGLTGELEFGENGGNPNVHFEILgtnygeELGR-GVR 414
Cdd:cd06382   286 NALKE---------------------------------------GLTGPIKFDEEGQRTDFKLDIL------ELTEgGLV 320
                         410
                  ....*....|..
gi 1622942472 415 KLGCWNPVTGLN 426
Cdd:cd06382   321 KVGTWNPTDGLN 332
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
445-811 3.78e-30

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: 120.18  E-value: 3.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 445 VVTVLEEPFVMVSEN--VLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQ-EDGTWNGLVGELVFKRADIGI 521
Cdd:cd13728     6 VTTILESPYVMYKKNheQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDpETKIWNGMVGELVYGRADIAV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYSVGVLLRRAEktvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsmt 601
Cdd:cd13728    86 APLTITLVREEVIDFSKPFMSLGISIMIKKPQ------------------------------------------------ 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 602 sttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfalivissytanlaafltitriesSIQSLQDLSKQTEIPYGT 681
Cdd:cd13728   118 --------------------------------------------------------------PIESAEDLAKQTEIAYGT 135
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 682 VLDSAVYEHVRMKGLnpferdSMYSQMWRMINRSNGS--ENNVLESQAGIQKVKyGNYAFVWDAAVLEYVAINDPdCSFY 759
Cdd:cd13728   136 LDSGSTKEFFRRSKI------AVYEKMWSYMKSAEPSvfTKTTADGVARVRKSK-GKFAFLLESTMNEYIEQRKP-CDTM 207
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622942472 760 TIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWWPKNGQC 811
Cdd:cd13728   208 KVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
29-425 1.10e-29

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor, a member of the glutamate-receptor ion channels (iGluRs). AMPA receptors are the major mediators of excitatory synaptic transmission in the central nervous system. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. AMPA receptors consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important roles in mediating the rapid excitatory synaptic current.


Pssm-ID: 380603 [Multi-domain]  Cd Length: 390  Bit Score: 122.39  E-value: 1.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  29 IGAIFDESAKKDDEVFRTAVGDLNQNEEilQTEKITFSVTFVD--GNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQ 106
Cdd:cd06380     2 IGAIFDSGEDQVQTAFRYAIDRHNSNNN--NRFRLFPLTERIDitNADSFSVSRAICSQLSRGVFAIFGSSDASSLNTIQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 107 SLADAMHIPhlFIQRSTAGTPRSGcgltrsnrNDDYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLD 186
Cdd:cd06380    80 SYSDTFHMP--YITPSFPKNEPSD--------SNPFELSLRPS--YIEAIVDLIRHYGWKKVVYLYDSDEGLLRLQQLYD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 187 KVSQ-QGMDVALQKVEnNINKMITTLfdtMRIEELNRYRDTlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEI 265
Cdd:cd06380   148 YLKEkSNISVRVRRVR-NVNDAYEFL---RTLRELDREKED-KRIVLDLSSERYQKILEQIVEDGMNRRNYHYLLANLDF 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 266 NDVDVqELVRRS---IGRLTIIRQTFPVPQNISQRcfrgnhriSSTLCDPKDPFAQNMEISN---LyIYDTVLLLANAFH 339
Cdd:cd06380   223 LDLDL-ERFLHGgvnITGFQLVDTNNKTVKDFLQR--------WKKLDPREYPGAGTDTIPYeaaL-AVDAVLVIAEAFQ 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 340 KKLEDR------KWHSMASLS------CIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILgtnyge 407
Cdd:cd06380   293 SLLRQNddifrfTFHGELYNNgskgidCDPNPPLPWEHGKAIMKALKKVRFEGLTGNVQFDDFGQRKNYTLDVI------ 366
                         410       420
                  ....*....|....*....|
gi 1622942472 408 ELG--RGVRKLGCWNPVTGL 425
Cdd:cd06380   367 ELTsnRGLRKIGTWSEGDGF 386
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
442-805 1.29e-28

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: 116.49  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVTVLEEPFVMVSE----------------------------NVLG-----KPKKYQ----GFSIDVLDALSNYLGF 484
Cdd:cd13720     3 HLRVVTLLEHPFVFTREvdeeglcpagqlcldpmtndsstldalfSSLHssndtVPIKFRkccyGYCIDLLEKLAEDLGF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 485 NYEIYVAPDHKYGsPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRraektvdmfaclap 564
Cdd:cd13720    83 DFDLYIVGDGKYG-AWRNGRWTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSLGILVR-------------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 565 fdlslwaciagtvllvgllvyllnwlnpPRLQmgsmtsttlynsmwfvygsfvqqggevpyttlatrmmmgawwlfaliv 644
Cdd:cd13720   148 ----------------------------TRDE------------------------------------------------ 151
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 645 issytanlaafltITRIESSIQSLQDLSKQteipYGTVLDSAVYEHVRMKglNPferdsmysQMWRMINRSNGSenNVLE 724
Cdd:cd13720   152 -------------LSGIHDPKLHHPSQGFR----FGTVRESSAEYYVKKS--FP--------EMHEHMRRYSLP--NTPE 202
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 725 sqaGIQKVKYGNY---AFVWDAAVLEYVAINDPDCSFYTIGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILK 801
Cdd:cd13720   203 ---GVEYLKNDPEkldAFIMDKALLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQNSPLTSNISELISQYKSNGFMDLLH 279

                  ....
gi 1622942472 802 HKWW 805
Cdd:cd13720   280 DKWY 283
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
452-513 6.78e-24

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: 95.39  E-value: 6.78e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622942472  452 PFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELV 513
Cdd:smart00918   1 PYVMLKESPDGGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLPNGSWNGMVGELV 62
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
28-420 6.90e-21

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


Pssm-ID: 380610 [Multi-domain]  Cd Length: 375  Bit Score: 95.86  E-value: 6.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEIlqTEK---ITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGS 104
Cdd:cd06387     1 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNT--TEKpfhLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 105 LQSLADAMHIPhlFIqrsTAGTPrsgcgltrSNRNDDYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEF 184
Cdd:cd06387    79 LTSFCGALHTS--FI---TPSFP--------TDADVQFVIQMRPA--LKGAILSLLAHYKWEKFVYLYDTERGFSILQAI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 185 LDKVSQQGMDVALQKVENninkmITTLFDTMR-IEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINE 263
Cdd:cd06387   144 MEAAVQNNWQVTARSVGN-----IKDVQEFRRiIEEMDRRQE--KRYLIDCEVERINTILEQVVILGKHSRGYHYMLANL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 264 EINDVDVQELVR--RSIGRLTIIRQTFPVPQNISQRCFRGNHRisstlcdpKDPFAQN--MEISNLYIYDTVLLLANAFH 339
Cdd:cd06387   217 GFTDILLERVMHggANITGFQIVNNENPMVQQFLQRWVRLDER--------EFPEAKNapLKYTSALTHDAILVIAEAFR 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 340 KKLEDRKWHSMASLS--CIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILGTNYGeelgrGVRKLG 417
Cdd:cd06387   289 YLRRQRVDVSRRGSAgdCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPS-----GSRKAG 363

                  ...
gi 1622942472 418 CWN 420
Cdd:cd06387   364 YWN 366
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
28-420 7.37e-20

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


Pssm-ID: 380613 [Multi-domain]  Cd Length: 367  Bit Score: 92.31  E-value: 7.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQtekitfSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06390     1 QIGGLFPNQQSQEHAAFRFALSQLTEPPKLLP------QIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLTS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIphlfiqrstagtprsgCGLTRS---NRNDDYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEF 184
Cdd:cd06390    75 FCGALHV----------------CFITPSfpvDTSNQFVLQLRPE--LQDALISVIEHYKWQKFVYIYDADRGLSVLQKV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 185 LDKVSQQGMDValqkveNNINKMITTLFD-TMRIEELNRYRDtlRRAILVMNPATAKSFITEVV--ETNLVAFdcHWIII 261
Cdd:cd06390   137 LDTAAEKNWQV------TAVNILTTTEEGyRMLFQDLDKKKE--RLVVVDCESERLNAILGQIVklEKNGIGY--HYILA 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 262 NEEINDVDVQELvRRSIGRLT---IIRQTFPVPQNISQRcFRGNHRISSTLCDPKDPfaqnmEISNLYIYDTVLLLANAF 338
Cdd:cd06390   207 NLGFMDIDLTKF-KESGANVTgfqLVNYTDTIPARIMQQ-WKNSDSRDLPRVDWKRP-----KYTSALTYDGVKVMAEAF 279
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 339 H---KKLEDRKWHSMASlSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILgtnygeELGR-GVR 414
Cdd:cd06390   280 QslrRQRIDISRRGNAG-DCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVI------EMKHdGIR 352

                  ....*.
gi 1622942472 415 KLGCWN 420
Cdd:cd06390   353 KIGYWN 358
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
442-563 7.29e-18

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: 83.45  E-value: 7.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVTVLE-EPFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIG 520
Cdd:cd13530     1 TLRVGTDADyPPFEYIDKN-----GKLVGFDVDLANAIAKRLGVKVEF------------VDTDFDGLIPALQSGKIDVA 63
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLA 563
Cdd:cd13530    64 ISGMTITPERAKVVDFSDPYYYTGQVLVVKKDSKITKTVADLK 106
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
443-556 8.13e-16

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: 77.33  E-value: 8.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLE-EPFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGI 521
Cdd:COG0834     1 LRVGVDPDyPPFSFRDED-----GKLVGFDVDLARAIAKRLGLKVEFVPVP------------WDRLIPALQSGKVDLII 63
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTV 556
Cdd:COG0834    64 AGMTITPEREKQVDFSDPYYTSGQVLLVRKDNSGI 98
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit ...
28-425 1.80e-15

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


Pssm-ID: 380611 [Multi-domain]  Cd Length: 373  Bit Score: 79.30  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVgdLNQNEEILQTEKITFSVTFVDG---NNPFQAVQEACELMNQGILALVSSIGCTSAGS 104
Cdd:cd06388     1 QIGGLFIRNTDQEYTAFRLAI--FLHNTSPNASEAPFNLVPHVDNietANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 105 LQSLADAMHIPHLfiqrsTAGTPRSGcgltrsnrNDDYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEF 184
Cdd:cd06388    79 LTSFCSALHISLI-----TPSFPTEG--------ESQFVLQLRPS--LRGALLSLLDHYEWNRFVFLYDTDRGYSILQAI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 185 LDKVSQQGMDVALQKVENNINKMITTLfdtmrIEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEE 264
Cdd:cd06388   144 MEKAGQNGWQVSAICVENFNDASYRRL-----LEDLDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 265 INDVDVQELVR--RSIGRLTIIRQTFPVPQNISQRCFRGNHR-ISSTLCDPKdpfaqnmeISNLYIYDTVLLLANAF--- 338
Cdd:cd06388   217 FKDISLERFMHggANVTGFQLVDFNTPMVTKLMQRWKKLDQReYPGSETPPK--------YTSALTYDGVLVMAETFrnl 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 339 -HKKLEDRKWHSMAslSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILgtnygEELGRGVRKLG 417
Cdd:cd06388   289 rRQKIDISRRGNAG--DCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVF-----ELKSTGPRKVG 361

                  ....*...
gi 1622942472 418 CWNPVTGL 425
Cdd:cd06388   362 YWNDMDKL 369
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
452-558 2.58e-15

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: 76.18  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:pfam00497  11 PFEYVDEN-----GKLVGFDVDLAKAIAKRLGVKVEF------------VPVSWDGLIPALQSGKVDLIIAGMTITPERA 73
                          90       100
                  ....*....|....*....|....*..
gi 1622942472 532 NVVDFTTRYMDYSVGVLLRRAEKTVDM 558
Cdd:pfam00497  74 KQVDFSDPYYYSGQVILVRKKDSSKSI 100
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
28-422 4.15e-15

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


Pssm-ID: 380612 [Multi-domain]  Cd Length: 372  Bit Score: 78.13  E-value: 4.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEVFRTAVGDLNQNEEilqteKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 107
Cdd:cd06389     1 QIGGLFPRGADQEYSAFRVGMVQFSTSEF-----RLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 108 LADAMHIPhlFIqrsTAGTPRSGcgltrsnrNDDYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDK 187
Cdd:cd06389    76 FCGTLHVS--FI---TPSFPTDG--------THPFVIQMRPD--LKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDS 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 188 VSQQGMDVALQKVENNINKMITTLFDTMrIEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIND 267
Cdd:cd06389   141 AAEKKWQVTAINVGNINNDKKDETYRSL-FQDLELKKE--RRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTD 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 268 VDVQELVR--RSIGRLTIIRQTFPVPQNISQRCfrgnhrisSTLCDPKDPFAQNMEI--SNLYIYDTVLLLANAF---HK 340
Cdd:cd06389   218 GDLLKIQFggANVSGFQIVDYDDSLVSKFIERW--------STLEEKEYPGAHTTTIkyTSALTYDAVQVMTEAFrnlRK 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 341 KLEDRKWHSMASlSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFGENGGNPNVHFEILgtnygEELGRGVRKLGCWN 420
Cdd:cd06389   290 QRIEISRRGNAG-DCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIM-----ELKTNGPRKIGYWS 363

                  ..
gi 1622942472 421 PV 422
Cdd:cd06389   364 EV 365
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
442-556 1.06e-12

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: 68.29  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVTVLE-EPFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIG 520
Cdd:cd13624     1 TLVVGTDATfPPFEFVDEN-----GKIVGFDIDLIKAIAKEAGFEVEF------------KNMAFDGLIPALQSGKIDII 63
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTV 556
Cdd:cd13624    64 ISGMTITEERKKSVDFSDPYYEAGQAIVVRKDSTII 99
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
466-556 2.21e-12

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: 67.30  E-value: 2.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 466 KYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSV 545
Cdd:cd00994    20 KYVGFDIDLWEAIAKEAGFKYEL------------QPMDFKGIIPALQTGRIDIAIAGITITEERKKVVDFSDPYYDSGL 87
                          90
                  ....*....|.
gi 1622942472 546 GVLLRRAEKTV 556
Cdd:cd00994    88 AVMVKADNNSI 98
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
28-425 5.23e-12

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: 68.41  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  28 HIGAIFDESAKKDDEV---FRTAVGDLNQNEEILQTEkitFSVTFVD-GNNPFQAVQEACELMN----QGILALVSSIGc 99
Cdd:cd19990     1 KIGAILDLNSRVGKEAkvaIEMAVSDFNSDSSSYGTK---LVLHVRDsKGDPLQAASAALDLIKnkkvEAIIGPQTSEE- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 100 tsAGSLQSLADAMHIPHLfiqrSTAGTPrsgcgLTRSnrnddytlSVRPPvYL-----ND-----VILRVVTEYAWQKFI 169
Cdd:cd19990    77 --ASFVAELGNKAQVPII----SFSATS-----PTLS--------SLRWP-FFirmthNDssqmkAIAAIVQSYGWRRVV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 170 IFY-DSEYDIRGIQEFLDkvsqqgmdvALQKVENNI-NKMITTLF--DTMRIEELNRYRDTLRRAILV-MNPATAKSFIT 244
Cdd:cd19990   137 LIYeDDDYGSGIIPYLSD---------ALQEVGSRIeYRVALPPSspEDSIEEELIKLKSMQSRVFVVhMSSLLASRLFQ 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 245 EVVETNLVAFDCHWIIINE-----EINDVDVQELVRRSIGrltiIRQTFPVP---QNISQRcFRGNHRIsstlcDPKDPF 316
Cdd:cd19990   208 EAKKLGMMEKGYVWIVTDGitnllDSLDSSTISSMQGVIG----IKTYIPESsefQDFKAR-FRKKFRS-----EYPEEE 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 317 AQNMEISNLYIYDTVLLLANAFHKKLEDRKwhsmaslscirkNSKPWQGGRSMLETIKKGGVSGLTGELEFgENGGNPNV 396
Cdd:cd19990   278 NAEPNIYALRAYDAIWALAHAVEKLNSSGG------------NISVSDSGKKLLEEILSTKFKGLSGEVQF-VDGQLAPP 344
                         410       420       430
                  ....*....|....*....|....*....|
gi 1622942472 397 H-FEILGTNygeelGRGVRKLGCWNPVTGL 425
Cdd:cd19990   345 PaFEIVNVI-----GKGYRELGFWSPGSGF 369
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
443-804 5.39e-11

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: 63.12  E-value: 5.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPFVMVSENVLgkpkkyQGFSIDVLDALSNYLGFNYEiYVAPDhkygspqedgTWNGLVGELVFKRADIGIS 522
Cdd:cd00997     5 LTVATVPRPPFVFYNDGEL------TGFSIDLWRAIAERLGWETE-YVRVD----------SVSALLAAVAEGEADIAIA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 523 ALTITPDRENVVDFTTRYMDYSVGVLLRraektvdmfaclapfdlslwaciagtvllvgllvyllnwlnpprlqmgsmtS 602
Cdd:cd00997    68 AISITAEREAEFDFSQPIFESGLQILVP---------------------------------------------------N 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 603 TTLYNSMWFVYGSFVqqgGEVPYTTLATrmmmgawWLfalivissyTANLAAFLTITRIESSIQSLQDlsKQTEipygtv 682
Cdd:cd00997    97 TPLINSVNDLYGKRV---ATVAGSTAAD-------YL---------RRHDIDVVEVPNLEAAYTALQD--KDAD------ 149
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 683 ldsavyehvrmkglnpferdsmysqmwrminrsngsennvlesqagiqkvkygnyAFVWDAAVLEYVAINDPDCSFYTIG 762
Cdd:cd00997   150 -------------------------------------------------------AVVFDAPVLRYYAAHDGNGKAEVTG 174
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1622942472 763 NTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 804
Cdd:cd00997   175 SVFLEENYGIVFPTGSPLRKPINQALLNLREDGTYDELYEKW 216
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
452-556 1.99e-10

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: 61.45  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlGKPkkyQGFSIDVLDALSNYLGFNYEIYVapdhkygspqedGTWNGLVGELVFKRADIgISALTITPDRE 531
Cdd:cd13704    14 PYEFLDEN--GNP---TGFNVDLLRAIAEEMGLKVEIRL------------GPWSEVLQALENGEIDV-LIGMAYSEERA 75
                          90       100
                  ....*....|....*....|....*
gi 1622942472 532 NVVDFTTRYMDYSVGVLLRRAEKTV 556
Cdd:cd13704    76 KLFDFSDPYLEVSVSIFVRKGSSII 100
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
462-540 1.03e-09

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: 59.40  E-value: 1.03e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942472 462 GKPKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRY 540
Cdd:cd13628    18 GDRGKIVGFDIELAKTIAKKLGLKLQI------------QEYDFNGLIPALASGQADLALAGITPTPERKKVVDFSEPY 84
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
452-551 1.07e-09

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 59.26  E-value: 1.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVApdhkygspqedgTWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:smart00062  12 PFSFADED-----GELTGFDVDLAKAIAKELGLKVEFVEV------------SFDSLLTALKSGKIDVVAAGMTITPERA 74
                           90       100
                   ....*....|....*....|
gi 1622942472  532 NVVDFTTRYMDYSVGVLLRR 551
Cdd:smart00062  75 KQVDFSDPYYRSGQVILVRK 94
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
465-548 5.53e-09

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: 57.64  E-value: 5.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 465 KKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTrYMDYS 544
Cdd:cd01004    22 GKLIGFDVDLAKAIAKRLGLKVEI------------VNVSFDGLIPALQSGRYDIIMSGITDTPERAKQVDFVD-YMKDG 88

                  ....
gi 1622942472 545 VGVL 548
Cdd:cd01004    89 LGVL 92
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
452-558 5.21e-08

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: 54.61  E-value: 5.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFvmvseNVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:cd01001    14 PF-----NFLDADGKLVGFDIDLANALCKRMKVKCEIVTQP------------WDGLIPALKAGKYDAIIASMSITDKRR 76
                          90       100
                  ....*....|....*....|....*..
gi 1622942472 532 NVVDFTTRYMDYSVGVLLRRAEKTVDM 558
Cdd:cd01001    77 QQIDFTDPYYRTPSRFVARKDSPITDT 103
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
442-551 9.17e-08

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: 53.69  E-value: 9.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVTVLE-EPFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVAPDhkygspqedgtWNGLVGELVFKRADIg 520
Cdd:cd01007     3 VIRVGVDPDwPPFEFIDEG-----GEPQGIAADYLKLIAKKLGLKFEYVPGDS-----------WSELLEALKAGEIDL- 65
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRR 551
Cdd:cd01007    66 LSSVSKTPEREKYLLFTKPYLSSPLVIVTRK 96
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
462-554 9.66e-07

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: 50.80  E-value: 9.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 462 GKpKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYM 541
Cdd:cd13620    25 GK-NQVVGADIDIAKAIAKELGVKLEI------------KSMDFDNLLASLQSGKVDMAISGMTPTPERKKSVDFSDVYY 91
                          90
                  ....*....|...
gi 1622942472 542 DYSVGVLLRRAEK 554
Cdd:cd13620    92 EAKQSLLVKKADL 104
PBP2_YxeM cd13709
Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein ...
442-557 1.92e-06

Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein fold; This group contains cystine-binding domain (YxeM) of a periplasmic receptor-dependent ATP-binding cassette transporter and its closely related proteins. 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: 270427 [Multi-domain]  Cd Length: 227  Bit Score: 50.04  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRV-VTVLEEPFVMVSENVLgkpkkyQGFSIDVLDALSNYLGFNYEIYVApdhkygspqedgTWNGLVGELVFKRADIG 520
Cdd:cd13709     2 VIKVgSSGSSYPFTFKENGKL------KGFEVDVWNAIGKRTGYKVEFVTA------------DFSGLFGMLDSGKVDTI 63
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622942472 521 ISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVD 557
Cdd:cd13709    64 ANQITITPERQEKYDFSEPYVYDGAQIVVKKDNNSIK 100
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
469-541 2.99e-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: 49.20  E-value: 2.99e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622942472 469 GFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYM 541
Cdd:cd13713    24 GFDVDVAKAIAKRLGVKVEPVTTA------------WDGIIAGLWAGRYDIIIGSMTITEERLKVVDFSNPYY 84
PBP2_GlnP cd13619
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ...
465-556 4.17e-06

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: 48.85  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 465 KKYQGFSIDVLDALSNYLGFNYEIyvapdhkygSPQEdgtWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYS 544
Cdd:cd13619    20 GKYVGIDVDLLNAIAKDQGFKVEL---------KPMG---FDAAIQAVQSGQADGVIAGMSITDERKKTFDFSDPYYDSG 87
                          90
                  ....*....|..
gi 1622942472 545 VGVLLRRAEKTV 556
Cdd:cd13619    88 LVIAVKKDNTSI 99
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
442-540 4.88e-06

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: 48.72  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVTVLE-EPFVMVSENvlGKPkkyQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIG 520
Cdd:cd13629     1 VLRVGMEAGyPPFEMTDKK--GEL---IGFDVDLAKALAKDLGVKVEF------------VNTAWDGLIPALQTGKFDLI 63
                          90       100
                  ....*....|....*....|
gi 1622942472 521 ISALTITPDRENVVDFTTRY 540
Cdd:cd13629    64 ISGMTITPERNLKVNFSNPY 83
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
452-553 9.74e-06

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 48.18  E-value: 9.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:PRK11260   53 PFSFQGED-----GKLTGFEVEFAEALAKHLGVKASLKPTK------------WDGMLASLDSKRIDVVINQVTISDERK 115
                          90       100
                  ....*....|....*....|..
gi 1622942472 532 NVVDFTTRYMDYSVGVLLRRAE 553
Cdd:PRK11260  116 KKYDFSTPYTVSGIQALVKKGN 137
PBP2_mlr5654_like cd13702
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
466-540 1.08e-05

Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the type 2 periplasmic-binding protein fold; This group includes uncharacterized periplasmic substrate-binding protein similar to HisJ and LAO proteins which serve as initial receptors in the ABC transport of histidine-, arginine, and lysine-arginine-ornithine amino acids. 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 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: 270420 [Multi-domain]  Cd Length: 223  Bit Score: 47.70  E-value: 1.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622942472 466 KYQGFSIDVLDALSNYLGFNYEIyVAPDhkygspqedgtWNGLVGELVFKRADIGISALTITPDRENVVDFTTRY 540
Cdd:cd13702    23 KLGGFDVDIANALCAEMKAKCEI-VAQD-----------WDGIIPALQAKKFDAIIASMSITPERKKQVDFTDPY 85
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
452-540 1.22e-05

Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein fold; Cystine-binding domain of periplasmic receptor-dependent 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. Also, 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: 270344 [Multi-domain]  Cd Length: 219  Bit Score: 47.31  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:cd13626    12 PFTFKDED-----GKLTGFDVEVGREIAKRLGLKVEF------------KATEWDGLLPGLNSGKFDVIANQVTITPERE 74

                  ....*....
gi 1622942472 532 NVVDFTTRY 540
Cdd:cd13626    75 EKYLFSDPY 83
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
466-553 1.47e-05

The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They 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: 270230 [Multi-domain]  Cd Length: 223  Bit Score: 47.21  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 466 KYQGFSIDVLDALSNYLGFNYEIYVAPDhkygspqedgtWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMdYSV 545
Cdd:cd01009    20 GPRGFEYELAKAFADYLGVELEIVPADN-----------LEELLEALEEGKGDLAAAGLTITPERKKKVDFSFPYY-YVV 87

                  ....*...
gi 1622942472 546 GVLLRRAE 553
Cdd:cd01009    88 QVLVYRKG 95
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
466-556 2.02e-05

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 47.05  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 466 KYQGFSIDVLDALSNYLGFNYEIyvapdhkygSPQEdgtWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSV 545
Cdd:PRK09495   45 KYVGFDIDLWAAIAKELKLDYTL---------KPMD---FSGIIPALQTKNVDLALAGITITDERKKAIDFSDGYYKSGL 112
                          90
                  ....*....|.
gi 1622942472 546 GVLLRRAEKTV 556
Cdd:PRK09495  113 LVMVKANNNDI 123
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
453-548 2.50e-05

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: 46.74  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 453 FVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEiyvapdHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDREN 532
Cdd:cd13686    16 FVKVTRDPITNSTSVTGFCIDVFEAAVKRLPYAVP------YEFIPFNDAGSYDDLVYQVYLKKFDAAVGDITITANRSL 89
                          90
                  ....*....|....*.
gi 1622942472 533 VVDFTTRYMDYSVGVL 548
Cdd:cd13686    90 YVDFTLPYTESGLVMV 105
PBP2_Arg_STM4351 cd13700
Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding ...
452-551 2.80e-05

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: 46.28  E-value: 2.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygSPQedgTWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:cd13700    14 PFESIGAK-----GEIVGFDIDLANALCKQMQAECTF---------TNQ---AFDSLIPSLKFKKFDAVISGMDITPERE 76
                          90       100
                  ....*....|....*....|
gi 1622942472 532 NVVDFTTRYMDYSVGVLLRR 551
Cdd:cd13700    77 KQVSFSTPYYENSAVVIAKK 96
PBP2_AA_binding_like_1 cd13625
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
466-563 2.95e-05

Substrate-binding domain of putative amino acid-binding protein; the type 2 periplasmic-binding protein fold; This putative amino acid-binding protein 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: 270343 [Multi-domain]  Cd Length: 230  Bit Score: 46.21  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 466 KYQGFSIDVLDALSNYLGFNYEiyvapdhkygspQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSV 545
Cdd:cd13625    25 KIVGFDRDLLDEMAKKLGVKVE------------QQDLPWSGILPGLLAGKFDMVATSVTITKERAKRFAFTLPIAEATA 92
                          90
                  ....*....|....*...
gi 1622942472 546 GVLLRRAEKTVDMFACLA 563
Cdd:cd13625    93 ALLKRAGDDSIKTIEDLA 110
PBP2_HisJ_LAO cd13703
Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; ...
451-540 3.07e-05

Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; the type 2 periplasmic-binding protein fold; This subgroup includes the periplasmic-binding proteins, HisJ and LAO, that serve as initial receptors in the ABC transport of histidine and lysine-arginine-ornithine amino acids. They are 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: 270421 [Multi-domain]  Cd Length: 229  Bit Score: 46.47  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 451 EPFVMVSENvlGKPkkyQGFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDR 530
Cdd:cd13703    13 PPFESKDAD--GEL---TGFDIDLGNALCAEMKVKCTWVEQD------------FDGLIPGLLARKFDAIISSMSITEER 75
                          90
                  ....*....|
gi 1622942472 531 ENVVDFTTRY 540
Cdd:cd13703    76 KKVVDFTDKY 85
PBP2_OccT_like cd13699
Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding ...
469-540 3.30e-05

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: 45.83  E-value: 3.30e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622942472 469 GFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDRENVVDFTTRY 540
Cdd:cd13699    26 GFEIDLANVLCERMKVKCTFVVQD------------WDGMIPALNAGKFDVIMDAMSITAERKKVIDFSTPY 85
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
452-555 3.59e-05

Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic binding protein fold; This group contains cystine binding domain FliY and its related proteins. 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: 270430 [Multi-domain]  Cd Length: 219  Bit Score: 45.84  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFvmvseNVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:cd13712    12 PF-----NFKDETGQLTGFEVDVAKALAAKLGVKPEFVTTE------------WSGILAGLQAGKYDVIINQVGITPERQ 74
                          90       100
                  ....*....|....*....|....
gi 1622942472 532 NVVDFTTRYMdYSVGVLLRRAEKT 555
Cdd:cd13712    75 KKFDFSQPYT-YSGIQLIVRKNDT 97
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
25-401 4.33e-05

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: 46.95  E-value: 4.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  25 SIIHIGAIFdeSAKKDDEVFRTAVGDLNQNEEIlqTEKITFSVTFVD-GNNPFQAVQEACE-LMNQGILALVSSIGCTSa 102
Cdd:cd06379     1 KIFNIGAVL--SSPKHEEIFREAVNEVNAHSHL--PRKITLNATSITlDPNPIRTALSVCEdLIASQVYAVIVSHPPTP- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 103 GSLQSLADAM-----HIPHLFIQ-RSTAgtprsgcgltRSNRNDdYTLSVRP-PVYLN--DVILRVVTEYAWQKFIIFYD 173
Cdd:cd06379    76 SDLSPTSVSYtagfyRIPVIGISaRDSA----------FSDKNI-HVSFLRTvPPYSHqaDVWAEMLRHFEWKQVIVIHS 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 174 SEYDIRGIQEFLDKVSQQGMDVALQKVENNIN-KMITTLFDTMRIEELNRYrdtlrraILVMNPATAKSFITEVVETNLV 252
Cdd:cd06379   145 DDQDGRALLGRLETLAETKDIKIEKVIEFEPGeKNFTSLLEEMKELQSRVI-------LLYASEDDAEIIFRDAAMLNMT 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 253 AFDCHWIiineeindVDVQELVRRSigrltiirqtfpVPQNIsqrcfrgnhrISSTLCDPKDPFAQnmeisnlyIYDTVL 332
Cdd:cd06379   218 GAGYVWI--------VTEQALAASN------------VPDGV----------LGLQLIHGKNESAH--------IRDSVS 259
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 333 LLANAFHKKLEDRKWHSMASLSCiRKNSKPWQGGRSMLETIKKGGVS-GLTGELEFGENGGNPNVHFEIL 401
Cdd:cd06379   260 VVAQAIRELFRSSENITDPPVDC-RDDTNIWKSGQKFFRVLKSVKLSdGRTGRVEFNDKGDRIGAEYDII 328
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
452-558 6.95e-05

Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein fold; This subfamily comprises of the periplasmic-binding protein component of ABC transporter specific for cysteine and its closely related proteins. The cysteine-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: 270412 [Multi-domain]  Cd Length: 229  Bit Score: 45.04  E-value: 6.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYL-GFNYEI-YVAPDHKYGSPQedgtwnglvgeLVFKRADIGISALTITPD 529
Cdd:cd13694    20 PFGYVDEN-----GKFQGFDIDLAKQIAKDLfGSGVKVeFVLVEAANRVPY-----------LTSGKVDLILANFTVTPE 83
                          90       100
                  ....*....|....*....|....*....
gi 1622942472 530 RENVVDFTTRYMDYSVGVLLRRAEKTVDM 558
Cdd:cd13694    84 RAEVVDFANPYMKVALGVVSPKDSNITSV 112
PBP2_ml15202_like cd13701
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
452-540 8.95e-05

Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the type 2 periplasmic-binding protein fold; This group includes uncharacterized periplasmic substrate-binding protein similar to HisJ and LAO proteins which are involved in the ABC transport of histidine-, arginine, and lysine-arginine-ornithine amino acids. 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 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: 270419 [Multi-domain]  Cd Length: 227  Bit Score: 44.76  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRE 531
Cdd:cd13701    15 PFTSKDAS-----GKWSGWEIDLIDALCARLDARCEI------------TPVAWDGIIPALQSGKIDMIWNSMSITDERK 77

                  ....*....
gi 1622942472 532 NVVDFTTRY 540
Cdd:cd13701    78 KVIDFSDPY 86
PBP2_SMa0082_like cd01072
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ...
439-547 1.24e-04

The substrate-binding domain of putatuve 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 Sinorhizobium meliloti and its related proteins. The putative SMa0082-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: 270233 [Multi-domain]  Cd Length: 238  Bit Score: 44.56  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 439 RGVVLRVVTVLEEPFVMVSENvlGKPkkyQGFSIDVLDALSNYLGFNYEIY-VAPDHKYGSPQEDgtwnglvgelvfkRA 517
Cdd:cd01072    12 RGKLKVGVLVDAPPFGFVDAS--MQP---QGYDVDVAKLLAKDLGVKLELVpVTGANRIPYLQTG-------------KV 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622942472 518 DIGISALTITPDRENVVDFTTRYMDYSVGV 547
Cdd:cd01072    74 DMLIASLGITPERAKVVDFSQPYAAFYLGV 103
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
442-551 1.42e-04

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 45.44  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVTVLEEPFVMVSENvlgkpkKYQGFSIDVLDALSNYLGFNYEIYVAPDHkygspqedgtwNGLVGELVFKRADIGI 521
Cdd:COG4623    23 VLRVLTRNSPTTYFIYRG------GPMGFEYELAKAFADYLGVKLEIIVPDNL-----------DELLPALNAGEGDIAA 85
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622942472 522 SALTITPDRENVVDFTTRYMDYSVGVLLRR 551
Cdd:COG4623    86 AGLTITPERKKQVRFSPPYYSVSQVLVYRK 115
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
466-555 2.07e-04

Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes cyclohexadienyl dehydratase PheC. These proteins catalyze the decarboxylation of prephenate to phenylpyruvate in the alternative phenylalanine biosynthesis pathway in some proteobacteria and archaea. The PheC 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. Since they the PheC proteins are so similar to periplasmic binding proteins, (PBP), it is evolutionarily plausible that several pre-existing PBP proteins might have been recruited to perform the enzymatic function.


Pssm-ID: 270231 [Multi-domain]  Cd Length: 232  Bit Score: 43.87  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 466 KYQGFSIDVLDALSNYLGFnyEIYVAPDhkygspqedgTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSV 545
Cdd:cd01069    31 QYEGYDIDMAEALAKSLGV--KVEFVPT----------SWPTLMDDLAADKFDIAMGGISITLERQRQAFFSAPYLRFGK 98
                          90
                  ....*....|
gi 1622942472 546 GVLLRRAEKT 555
Cdd:cd01069    99 TPLVRCADVD 108
PBP2_Arg_3 cd13622
Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding ...
452-541 4.82e-04

Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding fold; This subgroup is similar to the HisJ-like family that 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: 270340 [Multi-domain]  Cd Length: 222  Bit Score: 42.67  E-value: 4.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 452 PFVMVSENvlgkpKKYQGFSIDVLDALSNYL--GFNYEIYvapdhkygspqedgTWNGLVGELVFKRADIGISALTITPD 529
Cdd:cd13622    14 PFEMQGTN-----NELFGFDIDLMNEICKRIqrTCQYKPM--------------RFDDLLAALNNGKVDVAISSISITPE 74
                          90
                  ....*....|..
gi 1622942472 530 RENVVDFTTRYM 541
Cdd:cd13622    75 RSKNFIFSLPYL 86
PRK11917 PRK11917
bifunctional adhesin/ABC transporter aspartate/glutamate-binding protein; Reviewed
463-560 5.45e-04

bifunctional adhesin/ABC transporter aspartate/glutamate-binding protein; Reviewed


Pssm-ID: 183381 [Multi-domain]  Cd Length: 259  Bit Score: 42.60  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 463 KPKKYQGFSIDVLDALSNY-LGFNYEI-YVAPDHKYGSPQEDgtwNGLVgelvfkraDIGISALTITPDRENVVDFTTRY 540
Cdd:PRK11917   57 ATGEIKGFEIDVAKLLAKSiLGDDKKIkLVAVNAKTRGPLLD---NGSV--------DAVIATFTITPERKRIYNFSEPY 125
                          90       100
                  ....*....|....*....|
gi 1622942472 541 MDYSVGVLLRRaEKTVDMFA 560
Cdd:PRK11917  126 YQDAIGLLVLK-EKNYKSLA 144
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
442-554 6.02e-04

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS 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: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 42.21  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 442 VLRVVtVLEE--PFVMVSENvlgkpKKYQGFSIDVLDALSNYLGFNYEIYVAPdhkygSPQEdgtwngLVGELVFKRADI 519
Cdd:cd13707     3 VVRVV-VNPDlaPLSFFDSN-----GQFRGISADLLELISLRTGLRFEVVRAS-----SPAE------MIEALRSGEADM 65
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622942472 520 gISALTITPDRENVVDFTTRYMDYSVGVLLRRAEK 554
Cdd:cd13707    66 -IAALTPSPEREDFLLFTRPYLTSPFVLVTRKDAA 99
PBP2_ArtJ cd00999
The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold ...
466-542 1.13e-03

The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold protein superfamily; An arginine-binding protein found in Chlamydiae trachomatis (CT-ArtJ) and pneumoniae (CPn-ArtJ) and its closely related proteins. CT- and CPn-ArtJ are shown to have different immunogenic properties despite a high sequence similarity. The ArtJ proteins display the type 2 periplasmic binding fold organized in two alpha-beta domains with arginine-binding region at their interface.


Pssm-ID: 270220 [Multi-domain]  Cd Length: 223  Bit Score: 41.54  E-value: 1.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622942472 466 KYQGFSIDVLDALSNYLGFNYEIyvapdhkygspqEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMD 542
Cdd:cd00999    25 ELVGFDIDLAEAISEKLGKKLEW------------RDMAFDALIPNLLTGKIDAIAAGMSATPERAKRVAFSPPYGE 89
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
464-540 2.13e-03

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: 40.68  E-value: 2.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622942472 464 PKKYQ--GFSIDVLDALSNYLGfnyeiyVAPDHKYGSPQedgtwnGLVGELVFKRADIGISALTITPDRENVVDFTTRY 540
Cdd:cd13689    26 PKTREivGFDVDLCKAIAKKLG------VKLELKPVNPA------ARIPELQNGRVDLVAANLTYTPERAEQIDFSDPY 92
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
443-552 2.46e-03

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: 40.44  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 443 LRVVTVLEEPfVMVSENVLGKPkkyQGFSIDVLDALSNYLGFNYEIYVAPdhkygSPQEdgtwnglVGELVFKRADIGIS 522
Cdd:cd13696    10 LRCGVCLDFP-PFGFRDAAGNP---VGYDVDYAKDLAKALGVKPEIVETP-----SPNR-------IPALVSGRVDVVVA 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1622942472 523 ALTITPDRENVVDFTTRYMDYSVGVLLRRA 552
Cdd:cd13696    74 NTTRTLERAKTVAFSIPYVVAGMVVLTRKD 103
PBP2_Ngo0372_TcyA cd13711
Substrate binding domain of ABC transporters involved in cystine import; the type 2 ...
469-555 4.49e-03

Substrate binding domain of ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This subgroup includes cystine-binding domain of periplasmic receptor-dependent ATP-binding cassette transporters from Neisseria gonorrhoeae and Bacillus subtilis and their related proteins. 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: 270429 [Multi-domain]  Cd Length: 222  Bit Score: 39.59  E-value: 4.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472 469 GFSIDVLDALSNYLGFNYEIYVAPdhkygspqedgtWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMdYSVGVL 548
Cdd:cd13711    25 GFDVEVARAVAKKLGVKVEFVETQ------------WDSMIAGLDAGRFDVVANQVGITDERKKKYDFSTPYI-YSRAVL 91

                  ....*..
gi 1622942472 549 LRRAEKT 555
Cdd:cd13711    92 IVRKDNS 98
PBP1_ABC_ligand_binding-like cd19978
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ...
62-172 7.94e-03

periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in the uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally, however.


Pssm-ID: 380633 [Multi-domain]  Cd Length: 341  Bit Score: 39.48  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622942472  62 KITFsVTFVDGNNPFQAVQEACELMNQ-GILALVSSIGCTSAGSLQSLADAMHIPHLFiqrstagtPRSGCGLTRsNRND 140
Cdd:cd19978    41 KIKL-IALDDGYEPDRTVKNTKKLIEEdKVFALIGYVGTPTALAALPLANEKKIPLFG--------PFTGAEFLR-TPFL 110
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1622942472 141 DYTLSVRPPvYLNDV---ILRVVTEYAWQKFIIFY 172
Cdd:cd19978   111 PYVFNLRAS-YADETealVDYLVKTLGPKRIAIFY 144
 
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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