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Conserved domains on  [gi|755532823|ref|XP_011241425|]
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glutamate receptor ionotropic, kainate 2 isoform X2 [Mus musculus]

Protein Classification

glutamate receptor ionotropic, kainate( domain architecture ID 10157259)

glutamate receptor ionotropic, kainate is a non-NMDA (N-methyl-D-aspartate) ionotropic receptor that responds to the neurotransmitter glutamate, which acts as an excitatory neurotransmitter at many synapses in the central nervous system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
430-835 0e+00

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


The actual alignment was detected with superfamily member cd13723:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 369  Bit Score: 687.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHK 509
Cdd:cd13723    1 NRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDD-KGQWNGMVKELIDHK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARqskfsw 589
Cdd:cd13723   80 ADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIAR------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTR 669
Cdd:cd13723  154 -----------------------------FSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTR 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 IVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSrRQ 749
Cdd:cd13723  205 IIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSS-KP 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 829
Cdd:cd13723  284 SALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIM 363

                 ....*.
gi 755532823 830 KEKWWR 835
Cdd:cd13723  364 KEKWWR 369
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
37-414 2.44e-157

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: 465.16  E-value: 2.44e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  37 RFGGIFEYVESgpmgAEELAFRFAVNTINRNRTLlPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSAN 116
Cdd:cd06382    1 RIGGIFDEDDE----DLEIAFKYAVDRINRERTL-PNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 117 AVQSICNALGVPHIQTRWKHQvSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYN 196
Cdd:cd06382   76 IVQSICDALEIPHIETRWDPK-ESNRDTFTINLYPDPDALSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPKD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 197 LRLKIRQLPaDTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNM 276
Cdd:cd06382  155 IPITVRQLD-PGDDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 277 TGFRILNTENTQVSSIIEKWSMERLQAPPKPdsgLLDGFMTTDAALMYDAVHVVSVAVQqfpqmtvsslqcnrhkpwrfg 356
Cdd:cd06382  234 TGFRLVDPENPEVKNVLKDWSKREKEGFNKD---IGPGQITTETALMYDAVNLFANALK--------------------- 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755532823 357 trfmslikeahwEGLTGRITFNKtNGLRTDFDLDVISLKEEGLEKIGTWDPSSGLNMT 414
Cdd:cd06382  290 ------------EGLTGPIKFDE-EGQRTDFKLDILELTEGGLVKVGTWNPTDGLNIT 334
 
Name Accession Description Interval E-value
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
430-835 0e+00

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: 687.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHK 509
Cdd:cd13723    1 NRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDD-KGQWNGMVKELIDHK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARqskfsw 589
Cdd:cd13723   80 ADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIAR------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTR 669
Cdd:cd13723  154 -----------------------------FSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTR 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 IVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSrRQ 749
Cdd:cd13723  205 IIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSS-KP 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 829
Cdd:cd13723  284 SALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIM 363

                 ....*.
gi 755532823 830 KEKWWR 835
Cdd:cd13723  364 KEKWWR 369
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
37-414 2.44e-157

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: 465.16  E-value: 2.44e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  37 RFGGIFEYVESgpmgAEELAFRFAVNTINRNRTLlPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSAN 116
Cdd:cd06382    1 RIGGIFDEDDE----DLEIAFKYAVDRINRERTL-PNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 117 AVQSICNALGVPHIQTRWKHQvSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYN 196
Cdd:cd06382   76 IVQSICDALEIPHIETRWDPK-ESNRDTFTINLYPDPDALSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPKD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 197 LRLKIRQLPaDTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNM 276
Cdd:cd06382  155 IPITVRQLD-PGDDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 277 TGFRILNTENTQVSSIIEKWSMERLQAPPKPdsgLLDGFMTTDAALMYDAVHVVSVAVQqfpqmtvsslqcnrhkpwrfg 356
Cdd:cd06382  234 TGFRLVDPENPEVKNVLKDWSKREKEGFNKD---IGPGQITTETALMYDAVNLFANALK--------------------- 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755532823 357 trfmslikeahwEGLTGRITFNKtNGLRTDFDLDVISLKEEGLEKIGTWDPSSGLNMT 414
Cdd:cd06382  290 ------------EGLTGPIKFDE-EGQRTDFKLDILELTEGGLVKVGTWNPTDGLNIT 334
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
560-865 3.60e-106

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: 329.65  E-value: 3.60e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  560 SPDIWMYILLAYLGVSCVLFVIARqskfswfkypncshyhhsqrclctqhlesymelclFSPYEWYNPHPcnpdsdVVEN 639
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLER-----------------------------------FSPYEWRGPLE------TEEN 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  640 NFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGA 719
Cdd:pfam00060  40 RFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVGVWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  720 VEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGY 799
Cdd:pfam00060 120 VRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEGVALVRNGIYAYALLSENYYLFQRECCDTMIVGETFATGGY 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532823  800 GVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNG-CPEEESKEASA-LGVQNIGGIFIVLAAG 865
Cdd:pfam00060 200 GIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGeCDSKSSASSSSqLGLKSFAGLFLILGIG 267
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
52-395 2.02e-78

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: 258.85  E-value: 2.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823   52 AEELAFRFAVNTINRNRTLLPNTTLTYdtQKINLYDSFEASKKACDQLSLG-VAAIFGPSHSSSANAVQSICNALGVPHI 130
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPGTKLEY--IILDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  131 QTRWKHQVSDNKDSF--YVSLYPDFSSLSRAILDLVQFFKWKTVTVVY-DDSTGLIRLQELIKAPSRYNLRLKIRQLPA- 206
Cdd:pfam01094  79 SYGSTSPALSDLNRYptFLRTTPSDTSQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVIPp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  207 ---DTKDAKPLLKEMKRgKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTT--LDLFALDVEPYRYSGVNMTGFRI 281
Cdd:pfam01094 159 aqdDDEIARKLLKEVKS-RARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDglTTSLVILNPSTLEAAGGVLGFRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  282 LNTENTQVSSIIEkWSMERLQAPPKPDSGLLDGFMttdaALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMS 361
Cdd:pfam01094 238 HPPDSPEFSEFFW-EKLSDEKELYENLGGLPVSYG----ALAYDAVYLLAHALHNLLRDDKPGRACGALGPWNGGQKLLR 312
                         330       340       350
                  ....*....|....*....|....*....|....
gi 755532823  362 LIKEAHWEGLTGRITFNKtNGLRTDFDLDVISLK 395
Cdd:pfam01094 313 YLKNVNFTGLTGNVQFDE-NGDRINPDYDILNLN 345
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
702-836 6.97e-56

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: 189.04  E-value: 6.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823   702 PIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRqsVLVKSNEEGIQRVLTSDYAFLMESTTIEFVT 781
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKSPE--VFVKSYAEGVQRVRVSNYAFIMESPYLDYEL 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755532823   782 QRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRG 836
Cdd:smart00079  79 SRNCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
456-544 2.05e-12

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: 67.70  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 456 NDRFEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMT 535
Cdd:COG0834   18 DGKLVGFDVDLARAIAKRLGLKVEFVPVP-------------WDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPYYT 84

                 ....*....
gi 755532823 536 LGISILYRK 544
Cdd:COG0834   85 SGQVLLVRK 93
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
47-247 7.21e-11

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


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 64.57  E-value: 7.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  47 SGPMGA----EELAFRFAVNTINRNRTLLPNT--TLTYDTQkinlYDSFEASKKAcDQL--SLGVAAIFGPSHSSSANAV 118
Cdd:COG0683   13 TGPYAAlgqpIKNGAELAVEEINAAGGVLGRKieLVVEDDA----SDPDTAVAAA-RKLidQDKVDAIVGPLSSGVALAV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHIQTRW-KHQVSDNKDSFYV-SLYPDFSSLSRAILD-LVQFFKWKTVTVVYDDST-GLIRLQELIKAPSR 194
Cdd:COG0683   88 APVAEEAGVPLISPSAtAPALTGPECSPYVfRTAPSDAQQAEALADyLAKKLGAKKVALLYDDYAyGQGLAAAFKAALKA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755532823 195 YNLRL-KIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGM 247
Cdd:COG0683  168 AGGEVvGEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGL 221
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
446-546 2.25e-04

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 43.96  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 446 FKKSDKplygndrFEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREK 525
Cdd:PRK09495  40 FKQGDK-------YVGFDIDLWAAIAKELKLDYTLKPMD-------------FSGIIPALQTKNVDLALAGITITDERKK 99
                         90       100
                 ....*....|....*....|.
gi 755532823 526 VIDFSKPFMTLGISILYRKPN 546
Cdd:PRK09495 100 AIDFSDGYYKSGLLVMVKANN 120
 
Name Accession Description Interval E-value
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
430-835 0e+00

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: 687.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHK 509
Cdd:cd13723    1 NRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDD-KGQWNGMVKELIDHK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARqskfsw 589
Cdd:cd13723   80 ADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIAR------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTR 669
Cdd:cd13723  154 -----------------------------FSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTR 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 IVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSrRQ 749
Cdd:cd13723  205 IIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSS-KP 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 829
Cdd:cd13723  284 SALVKNNEEGIQRALTADYALLMESTTIEYVTQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIM 363

                 ....*.
gi 755532823 830 KEKWWR 835
Cdd:cd13723  364 KEKWWR 369
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
430-835 1.20e-164

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: 480.67  E-value: 1.20e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 509
Cdd:cd13721    1 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNgtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13721   81 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKGT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13721      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermesPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13721  118 --------------------------------PIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 165
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 829
Cdd:cd13721  166 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 245

                 ....*.
gi 755532823 830 KEKWWR 835
Cdd:cd13721  246 KEKWWR 251
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
37-414 2.44e-157

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: 465.16  E-value: 2.44e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  37 RFGGIFEYVESgpmgAEELAFRFAVNTINRNRTLlPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSAN 116
Cdd:cd06382    1 RIGGIFDEDDE----DLEIAFKYAVDRINRERTL-PNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 117 AVQSICNALGVPHIQTRWKHQvSDNKDSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYN 196
Cdd:cd06382   76 IVQSICDALEIPHIETRWDPK-ESNRDTFTINLYPDPDALSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPKD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 197 LRLKIRQLPaDTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNM 276
Cdd:cd06382  155 IPITVRQLD-PGDDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 277 TGFRILNTENTQVSSIIEKWSMERLQAPPKPdsgLLDGFMTTDAALMYDAVHVVSVAVQqfpqmtvsslqcnrhkpwrfg 356
Cdd:cd06382  234 TGFRLVDPENPEVKNVLKDWSKREKEGFNKD---IGPGQITTETALMYDAVNLFANALK--------------------- 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755532823 357 trfmslikeahwEGLTGRITFNKtNGLRTDFDLDVISLKEEGLEKIGTWDPSSGLNMT 414
Cdd:cd06382  290 ------------EGLTGPIKFDE-EGQRTDFKLDILELTEGGLVKVGTWNPTDGLNIT 334
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
430-835 4.40e-152

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: 448.14  E-value: 4.40e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 509
Cdd:cd13714    1 NKTLIVTTILEEPYVMLKESAKPLTGNDRFEGFCIDLLKELAKILGFNYTIRLVPDGKYGSYDPETGEWNGMVRELIDGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNgtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13714   81 ADLAVADLTITYERESVVDFTKPFMNLGISILYRKPT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13714      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermesPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13714  118 --------------------------------PIESADDLAKQTKIKYGTLRGGSTMTFFRDSNISTYQKMWNFMMSAKP 165
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 829
Cdd:cd13714  166 SVFVKSNEEGVARVLKGKYAFLMESTSIEYVTQRNCNLTQIGGLLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEML 245

                 ....*.
gi 755532823 830 KEKWWR 835
Cdd:cd13714  246 KNKWWK 251
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
430-835 1.05e-137

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: 410.98  E-value: 1.05e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHK 509
Cdd:cd13722    1 NRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFLYDVKLVPDGKYGAQND-KGEWNGMVKELIDHR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNgtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13722   80 ADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKGT------------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13722      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermesPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13722  117 --------------------------------PIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQ 164
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 829
Cdd:cd13722  165 TALVKNSDEGIQRVLTTDYALLMESTSIEYVTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMM 244

                 ....*.
gi 755532823 830 KEKWWR 835
Cdd:cd13722  245 KEKWWR 250
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
430-834 3.88e-132

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: 400.16  E-value: 3.88e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDdVNGQWNGMVRELIDHK 509
Cdd:cd13724    1 NTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPE-ANGTWTGMVGELIARK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARqskfsw 589
Cdd:cd13724   80 ADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVAR------ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclFSPYEWYNPHPCNPDS-DVVENNFTLLNSFWFGVGALMQQGSELMPkalst 668
Cdd:cd13724  154 -----------------------------LTPYEWYSPHPCAQGRcNLLVNQYSLGNSLWFPVGGFMQQGSTIAP----- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 669 rivggiwwfftliiissytanlaafltvermesPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRR 748
Cdd:cd13724  200 ---------------------------------PIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQ 246
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 749 QSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHM 828
Cdd:cd13724  247 PSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRNCNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEI 326

                 ....*.
gi 755532823 829 MKEKWW 834
Cdd:cd13724  327 LKRKWW 332
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
37-415 2.15e-131

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: 398.28  E-value: 2.15e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  37 RFGGIFEYVEsgpMGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSAN 116
Cdd:cd06368    1 KIGAIFNEVN---DAHERAAFRYAVERLNTNIVKLAYFRITYSIEAIDSNSHFDATDKACDLLEKGVVAIVGPSSSDSNN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 117 AVQSICNALGVPHIQTRWKHQVSdnKDSFYVSLYPDfSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYN 196
Cdd:cd06368   78 ALQSICDALDVPHITVHDDPRLS--KSQYSLSLYPR-NQLSQAVSDLLKYWRWKRFVLVYDDDDRLRRLQELLEAARFSK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 197 LRLKIRQLPAD--TKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFAL-DVEPYRYSG 273
Cdd:cd06368  155 RFVSVRKVDLDykTLDETPLLKRKDCSLFSRILIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDLSLLlDLELFRYNH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 274 VNMTGFRILNTeNTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAVQQfpqmtvsslqcnrhkpw 353
Cdd:cd06368  235 ANITGFQLVDN-NSMYKEDINRLAFNWSRFRQHIKIESNLRGPPYEAALMFDAVLLLADAFRR----------------- 296
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532823 354 rfgtrfmslikeahweglTGRITFNKTnGLRTDFDLDVISLKEEGLEKIGTWDPSSGLNMTE 415
Cdd:cd06368  297 ------------------TGDLRFNGT-GLRSNFTLRILELGYGGLRKIGFWDSNTRLAMNL 339
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
430-834 5.73e-107

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: 331.07  E-value: 5.73e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLfkKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHK 509
Cdd:cd13685    1 NKTLRVTTILEPPFVM--KKRDSLSGNPRFEGYCIDLLEELAKILGFDYEIYLVPDGKYGSRDE-NGNWNGMIGELVRGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13685   78 ADIAVAPLTITAEREEVVDFTKPFMDTGISILMRKP-------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13685      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermeSPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKM--WAFMSSR 747
Cdd:cd13685  114 -------------------------------TPIESLEDLAKQSKIEYGTLKGSSTFTFFKNSKNPEYRRYeyTKIMSAM 162
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 748 RQSVLVKSNEEGIQRVLTS--DYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGK 825
Cdd:cd13685  163 SPSVLVASAAEGVQRVRESngGYAFIGEATSIDYEVLRNCDLTKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGE 242

                 ....*....
gi 755532823 826 LHMMKEKWW 834
Cdd:cd13685  243 LEKLKEKWW 251
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
560-865 3.60e-106

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: 329.65  E-value: 3.60e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  560 SPDIWMYILLAYLGVSCVLFVIARqskfswfkypncshyhhsqrclctqhlesymelclFSPYEWYNPHPcnpdsdVVEN 639
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLER-----------------------------------FSPYEWRGPLE------TEEN 39
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  640 NFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGA 719
Cdd:pfam00060  40 RFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVGVWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  720 VEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGY 799
Cdd:pfam00060 120 VRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEGVALVRNGIYAYALLSENYYLFQRECCDTMIVGETFATGGY 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532823  800 GVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNG-CPEEESKEASA-LGVQNIGGIFIVLAAG 865
Cdd:pfam00060 200 GIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGeCDSKSSASSSSqLGLKSFAGLFLILGIG 267
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
430-838 1.44e-104

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: 325.08  E-value: 1.44e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKS--DKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELID 507
Cdd:cd13715    1 NRTYIVTTILEEPYVMMKKNheGEPLEGNERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARDADTGIWNGMVGELVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 508 HKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskf 587
Cdd:cd13715   81 GEADIAIAPLTITLVRERVIDFSKPFMSLGISIMIKKP------------------------------------------ 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 588 swfkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkals 667
Cdd:cd13715      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 668 trivggiwwfftliiissytanlaafltvermeSPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSR 747
Cdd:cd13715  119 ---------------------------------VPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYDKMWEYMNSA 165
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 748 RQSVLVKSNEEGIQRVLTSD--YAFLMESTTIEFVTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEG 824
Cdd:cd13715  166 EPSVFVRTTDEGIARVRKSKgkYAYLLESTMNEYINQRKpCDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENG 245
                        410
                 ....*....|....
gi 755532823 825 KLHMMKEKWWRGNG 838
Cdd:cd13715  246 ELDKLKNKWWYDKG 259
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
435-834 4.21e-94

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: 301.14  E-value: 4.21e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 435 VTTILEEPYVLFKKSdkplyGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHKADLAV 514
Cdd:cd13717    6 IGTVESPPFVYRDRD-----GSPIWEGYCIDLIEEISEILNFDYEIVEPEDGKFGTMDE-NGEWNGLIGDLVRKEADIAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 515 APLAITYVREKVIDFSKPFMTL-GISILYRKPNgTNPGVFSFLNPLSPDIWmyillaylgvscvlfviaRQskfswfkyp 593
Cdd:cd13717   80 AALSVMAEREEVVDFTVPYYDLvGITILMKKPE-RPTSLFKFLTVLELEVW------------------RE--------- 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 594 ncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennFTLLNSFWFGVGALMQQGSELMPKALSTRIVGG 673
Cdd:cd13717  132 -----------------------------------------------FTLKESLWFCLTSLTPQGGGEAPKNLSGRLLVA 164
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 674 IWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVEDGATMTFFKK---------------------- 731
Cdd:cd13717  165 TWWLFVFIIIASYTANLAAFLTVSRLQTPVESLDDLARQYKIQYTVVKNSSTHTYFERmknaedtlyemwkdmslndsls 244
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 732 ----SKISTYD--------KMWAFMSSrrqSVLVKSNEEGIQRV---LTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDS 796
Cdd:cd13717  245 pverAKLAVWDypvsekytKIYQAMQE---AGLVANAEEGVKRVresTSAGFAFIGDATDIKYEILTNCDLQEVGEEFSR 321
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 755532823 797 KGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWW 834
Cdd:cd13717  322 KPYAIAVQQGSPLKDELNYAILELQNDRFLEKLKAKWW 359
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
430-838 1.20e-85

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: 274.98  E-value: 1.20e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 509
Cdd:cd13729    1 NRTYIVTTILESPYVMLKKNHEQFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETKMWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13729   81 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKP-------------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13729      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13729  117 ------------------------------TSPIESAEDLAKQTEIAYGTLDAGSTKEFFRRSKIAVFEKMWSYMKSADP 166
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTS--DYAFLMESTTIEFVTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKL 826
Cdd:cd13729  167 SVFVKTTDEGVMRVRKSkgKYAYLLESTMNEYIEQRKpCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLL 246
                        410
                 ....*....|..
gi 755532823 827 HMMKEKWWRGNG 838
Cdd:cd13729  247 DKLKNKWWYDKG 258
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
430-834 2.60e-85

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: 273.89  E-value: 2.60e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHK 509
Cdd:cd13725    1 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEP-NGSWTGMVGELINRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRkpngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13725   80 ADLAVAAFTITAEREKVIDFSKPFMTLGISILYR---------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13725      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltverMESPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13725  114 -----------------------------VHMPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQP 164
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMM 829
Cdd:cd13725  165 SVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEIL 244

                 ....*
gi 755532823 830 KEKWW 834
Cdd:cd13725  245 KRKWW 249
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
38-411 8.28e-79

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: 261.44  E-value: 8.28e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  38 FGGIFeyvesgPMGAEEL--AFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSA 115
Cdd:cd06380    2 IGAIF------DSGEDQVqtAFRYAIDRHNSNNNNRFRLFPLTERIDITNADSFSVSRAICSQLSRGVFAIFGSSDASSL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 116 NAVQSICNALGVPHIQTR-WKHQVSDNKDsFYVSLYPdfsSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELI---KA 191
Cdd:cd06380   76 NTIQSYSDTFHMPYITPSfPKNEPSDSNP-FELSLRP---SYIEAIVDLIRHYGWKKVVYLYDSDEGLLRLQQLYdylKE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 192 PSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEF-HVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYR 270
Cdd:cd06380  152 KSNISVRVRRVRNVNDAYEFLRTLRELDREKEDkRIVLDLSSERYQKILEQIVEDGMNRRNYHYLLANLDFLDLDLERFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 271 YSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSglldGFMTTDAALMYDAVHVVSVAVQQ-FPQMT-------- 341
Cdd:cd06380  232 HGGVNITGFQLVDTNNKTVKDFLQRWKKLDPREYPGAGT----DTIPYEAALAVDAVLVIAEAFQSlLRQNDdifrftfh 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 342 -------VSSLQCNRH--KPWRFGTRFMSLIKEAHWEGLTGRITFNKtNGLRTDFDLDVISLK-EEGLEKIGTWDPSSGL 411
Cdd:cd06380  308 gelynngSKGIDCDPNppLPWEHGKAIMKALKKVRFEGLTGNVQFDD-FGQRKNYTLDVIELTsNRGLRKIGTWSEGDGF 386
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
52-395 2.02e-78

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: 258.85  E-value: 2.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823   52 AEELAFRFAVNTINRNRTLLPNTTLTYdtQKINLYDSFEASKKACDQLSLG-VAAIFGPSHSSSANAVQSICNALGVPHI 130
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPGTKLEY--IILDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  131 QTRWKHQVSDNKDSF--YVSLYPDFSSLSRAILDLVQFFKWKTVTVVY-DDSTGLIRLQELIKAPSRYNLRLKIRQLPA- 206
Cdd:pfam01094  79 SYGSTSPALSDLNRYptFLRTTPSDTSQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVIPp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  207 ---DTKDAKPLLKEMKRgKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTT--LDLFALDVEPYRYSGVNMTGFRI 281
Cdd:pfam01094 159 aqdDDEIARKLLKEVKS-RARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDglTTSLVILNPSTLEAAGGVLGFRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  282 LNTENTQVSSIIEkWSMERLQAPPKPDSGLLDGFMttdaALMYDAVHVVSVAVQQFPQMTVSSLQCNRHKPWRFGTRFMS 361
Cdd:pfam01094 238 HPPDSPEFSEFFW-EKLSDEKELYENLGGLPVSYG----ALAYDAVYLLAHALHNLLRDDKPGRACGALGPWNGGQKLLR 312
                         330       340       350
                  ....*....|....*....|....*....|....
gi 755532823  362 LIKEAHWEGLTGRITFNKtNGLRTDFDLDVISLK 395
Cdd:pfam01094 313 YLKNVNFTGLTGNVQFDE-NGDRINPDYDILNLN 345
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
430-838 3.16e-78

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: 255.34  E-value: 3.16e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 509
Cdd:cd13727    1 NRTVVVTTIMESPYVMYKKNHEMFEGNDKFEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDPETKIWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13727   81 AEIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKP-------------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13727      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermeSPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13727  117 -------------------------------QPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMKSAEP 165
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTS--DYAFLMESTTIEFVTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKL 826
Cdd:cd13727  166 SVFTRTTAEGVARVRKSkgKFAFLLESTMNEYIEQRKpCDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLL 245
                        410
                 ....*....|..
gi 755532823 827 HMMKEKWWRGNG 838
Cdd:cd13727  246 DKLKNKWWYDKG 257
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
430-838 6.02e-77

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: 251.87  E-value: 6.02e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 509
Cdd:cd13726    1 NKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13726   81 ADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKG-------------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13726      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermeSPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13726  117 -------------------------------TPIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEP 165
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTS--DYAFLMESTTIEFVTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKL 826
Cdd:cd13726  166 SVFVRTTAEGVARVRKSkgKYAYLLESTMNEYIEQRKpCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLL 245
                        410
                 ....*....|..
gi 755532823 827 HMMKEKWWRGNG 838
Cdd:cd13726  246 DKLKNKWWYDKG 257
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
430-838 1.63e-69

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: 231.50  E-value: 1.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 430 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 509
Cdd:cd13728    1 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfsw 589
Cdd:cd13728   81 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKP-------------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13728      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermeSPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQ 749
Cdd:cd13728  117 -------------------------------QPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEP 165
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 SVLVKSNEEGIQRVLTS--DYAFLMESTTIEFVTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKL 826
Cdd:cd13728  166 SVFTKTTADGVARVRKSkgKFAFLLESTMNEYIEQRKpCDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLL 245
                        410
                 ....*....|..
gi 755532823 827 HMMKEKWWRGNG 838
Cdd:cd13728  246 DKLKNKWWYDKG 257
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
431-834 1.29e-60

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: 206.46  E-value: 1.29e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 431 RSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQddVNGQWNGMVRELIDHKA 510
Cdd:cd00998    1 KTLKVVVPLEPPFVMFVTGSNAVTGNGRFEGYCIDLLKELSQSLGFTYEYYLVPDGKFGAP--VNGSWNGMVGEVVRGEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 511 DLAVAPLAITYVREKVIDFSKPFMTLGISILYrkpngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfswf 590
Cdd:cd00998   79 DLAVGPITITSERSVVIDFTQPFMTSGIGIMI------------------------------------------------ 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 591 kypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstri 670
Cdd:cd00998      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 671 vggiwwfftliiissytanlaafltvermesPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRqs 750
Cdd:cd00998  111 -------------------------------PIRSIDDLKRQTDIEFGTVENSFTETFLRSSGIYPFYKTWMYSEARV-- 157
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 751 VLVKSNEEGIQRVLTS-DYAFLMESTTIEFVTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHM 828
Cdd:cd00998  158 VFVNNIAEGIERVRKGkVYAFIWDRPYLEYYARQDpCKLIKTGGGFGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQK 237

                 ....*.
gi 755532823 829 MKEKWW 834
Cdd:cd00998  238 LKNKWL 243
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
431-544 2.34e-59

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: 197.74  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  431 RSLIVTTILEEPYVLFKKSdkpLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHKA 510
Cdd:pfam10613   1 KTLIVTTILEPPFVMLKEN---LEGNDRYEGFCIDLLKELAEILGFKYEIRLVPDGKYGSLDPTTGEWNGMIGELIDGKA 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 755532823  511 DLAVAPLAITYVREKVIDFSKPFMTLGISILYRK 544
Cdd:pfam10613  78 DLAVAPLTITSEREKVVDFTKPFMTLGISILMKK 111
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
702-836 6.97e-56

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: 189.04  E-value: 6.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823   702 PIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRqsVLVKSNEEGIQRVLTSDYAFLMESTTIEFVT 781
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKSPE--VFVKSYAEGVQRVRVSNYAFIMESPYLDYEL 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 755532823   782 QRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRG 836
Cdd:smart00079  79 SRNCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
39-406 4.13e-50

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: 181.29  E-value: 4.13e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEYVESgpmgAEELAFRFAVNTINRNRTLLPNTTLtydtqkINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAV 118
Cdd:cd06390    3 GGLFPNQQS----QEHAAFRFALSQLTEPPKLLPQIDI------VNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNML 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHIQTRWKhqvSDNKDSFYVSLYPDfssLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLR 198
Cdd:cd06390   73 TSFCGALHVCFITPSFP---VDTSNQFVLQLRPE---LQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 199 LKIRQLPADTKDA-KPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMT 277
Cdd:cd06390  147 VTAVNILTTTEEGyRMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVT 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 278 GFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLdgfmTTDAALMYDAVHVVSVAVQQFPQMTV------SSLQC--NR 349
Cdd:cd06390  227 GFQLVNYTDTIPARIMQQWKNSDSRDLPRVDWKRP----KYTSALTYDGVKVMAEAFQSLRRQRIdisrrgNAGDClaNP 302
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755532823 350 HKPWRFGTRFMSLIKEAHWEGLTGRITFNKtNGLRTDFDLDVISLKEEGLEKIGTWD 406
Cdd:cd06390  303 AVPWGQGIDIQRALQQVRFEGLTGNVQFNE-KGRRTNYTLHVIEMKHDGIRKIGYWN 358
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
53-413 2.48e-46

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


Pssm-ID: 380616  Cd Length: 379  Bit Score: 170.86  E-value: 2.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  53 EELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHS-SSANAVQSICNALGVPHIQ 131
Cdd:cd06394   18 ERLALALAREQINSIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSpASASTVSHICGEKEIPHIK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 132 TRWKHQVSDNKDSF-YVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLPaDTKD 210
Cdd:cd06394   98 VGPEETPRLQYLRFaSVSLYPSNEDISLAVSRILKSFNYPSASLICAKAECLLRLEELVRQFLISKETLSVRMLD-DSRD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 211 AKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVS 290
Cdd:cd06394  177 PTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQSNILGFSMFNTSHPFYL 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 291 SIIEKWSM---ERLQAPPKPDSGLldgfmttDAALMYDAVHVVSVAVQQF---PQMTVSSLQCNRHKPWRFGTRFMSLIK 364
Cdd:cd06394  257 EFVRSLNMswrENCDASTYPGPAL-------SSALMFDAVHVVVSAVRELnrsQEIGVKPLSCTSAQIWQHGTSLMNYLR 329
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755532823 365 EAHWEGLTGRITFNkTNGLRTDFDLDVISLKEEGLEKIGTWDPSSGLNM 413
Cdd:cd06394  330 MVEYDGLTGRVEFN-SKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAM 377
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
53-406 6.39e-44

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: 163.66  E-value: 6.39e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  53 EELAFRFAVNTINRNRtllpNTT-----LTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALGV 127
Cdd:cd06387   13 EHSAFRFAVQLYNTNQ----NTTekpfhLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 128 PHIQTRWKhqvSDNKDSFYVSLYPdfsSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLP-- 205
Cdd:cd06387   89 SFITPSFP---TDADVQFVIQMRP---ALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGni 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 206 ADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTE 285
Cdd:cd06387  163 KDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNE 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 286 NTQVSSIIEKWsmERLQAPPKPDSGllDGFMTTDAALMYDAVHVVSVAVQQFPQMTV------SSLQC--NRHKPWRFGT 357
Cdd:cd06387  243 NPMVQQFLQRW--VRLDEREFPEAK--NAPLKYTSALTHDAILVIAEAFRYLRRQRVdvsrrgSAGDClaNPAVPWSQGI 318
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755532823 358 RFMSLIKEAHWEGLTGRITFNkTNGLRTDFDLDVISLKEEGLEKIGTWD 406
Cdd:cd06387  319 DIERALKMVQVQGMTGNIQFD-TYGRRTNYTIDVYEMKPSGSRKAGYWN 366
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
432-834 1.34e-43

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: 158.97  E-value: 1.34e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 432 SLIVTTILEEPYVLFkkSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHKAD 511
Cdd:cd13730    3 TLKVVTVLEEPFVMV--AENILGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGKYGHQLH-NTSWNGMIGELISKRAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 512 LAVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfswfk 591
Cdd:cd13730   80 LAISAITITPERESVVDFSKRYMDYSVGILIKKP---------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 592 ypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstriv 671
Cdd:cd13730      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 672 ggiwwfftliiissytanlaafltvermeSPIDSADDLAKQTKIEYGAVEDGATMTFFKKS------KISTYDKMWAFMS 745
Cdd:cd13730  114 -----------------------------EPIRTFQDLSKQVEMSYGTVRDSAVYEYFRAKgtnpleQDSTFAELWRTIS 164
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 746 -SRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEF--VTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQE 822
Cdd:cd13730  165 kNGGADNCVSSPSEGIRKAKKGNYAFLWDVAVVEYaaLTDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQD 244
                        410
                 ....*....|..
gi 755532823 823 EGKLHMMKEKWW 834
Cdd:cd13730  245 TGDLDVLKQKWW 256
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
433-834 1.62e-41

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: 153.07  E-value: 1.62e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 433 LIVTTILEEPYVLFkkSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHKADL 512
Cdd:cd13716    4 LRVVTVLEEPFVMV--SENVLGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHKYGSQQE-DGTWNGLIGELVFKRADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 513 AVAPLAITYVREKVIDFSKPFMTLGISILYRKPngtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfswfky 592
Cdd:cd13716   81 GISALTITPERENVVDFTTRYMDYSVGVLLRKA----------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 593 pncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstrivg 672
Cdd:cd13716      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 673 giwwfftliiissytanlaafltvermeSPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKI------STYDKMWAFMSS 746
Cdd:cd13716  114 ----------------------------ESIQSLQDLSKQTDIPYGTVLDSAVYEYVRSKGTnpferdSMYSQMWRMINR 165
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 747 RRQSV-LVKSNEEGIQRVLTSDYAFLMESTTIEFV--TQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEE 823
Cdd:cd13716  166 SNGSEnNVSESSEGIRKVKYGNYAFVWDAAVLEYVaiNDDDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQN 245
                        410
                 ....*....|.
gi 755532823 824 GKLHMMKEKWW 834
Cdd:cd13716  246 GDMDILKHKWW 256
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
37-415 1.86e-41

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: 156.33  E-value: 1.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  37 RFGGIFeyvesgPMGAEELAFRFAVNTINRNRTllpNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSAN 116
Cdd:cd06389    1 QIGGLF------PRGADQEYSAFRVGMVQFSTS---EFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 117 AVQSICNALGVPHIQTRWKhqvSDNKDSFYVSLYPDfssLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYN 196
Cdd:cd06389   72 TITSFCGTLHVSFITPSFP---TDGTHPFVIQMRPD---LKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 197 LR---LKIRQLPADTKDA--KPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRY 271
Cdd:cd06389  146 WQvtaINVGNINNDKKDEtyRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQF 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 272 SGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLdgfmTTDAALMYDAVHVVSVAVQQFPQMTV------SSL 345
Cdd:cd06389  226 GGANVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTI----KYTSALTYDAVQVMTEAFRNLRKQRIeisrrgNAG 301
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532823 346 QC--NRHKPWRFGTRFMSLIKEAHWEGLTGRITFNKtNGLRTDFDLDVISLKEEGLEKIGTWDPSSGLNMTE 415
Cdd:cd06389  302 DClaNPAVPWGQGVEIERALKQVQVEGLSGNIKFDQ-NGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTL 372
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
431-833 1.01e-34

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: 132.76  E-value: 1.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 431 RSLIVTTILEEPYVlFKKSDKplygndrfeGYCIDLLRELSTILGFTYEIRLVEDGKYGAQD-DVNGQWNGMVRELIDHK 509
Cdd:cd13687    2 THLKVVTLEEAPFV-YVKCCY---------GFCIDLLKKLAEDVNFTYDLYLVTDGKFGTVNkSINGEWNGMIGELVSGR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 510 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGtnpgvFSFLNplspdiwmyillaylgvscvlfviarQSKFSw 589
Cdd:cd13687   72 ADMAVASLTINPERSEVIDFSKPFKYTGITILVKKRNE-----LSGIN--------------------------DPRLR- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 590 fkypncshyhhsqrclctqhlesymelclfspyewyNPHPcnpdsdvvenNFTllnsfwfgvgalmqqgselmpkalstr 669
Cdd:cd13687  120 ------------------------------------NPSP----------PFR--------------------------- 126
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 670 ivggiwwfftliiissytanlaafltvermespidsaddlakqtkieYGAVEDGATMTFFKKSKISTYDKMWAFMssrrq 749
Cdd:cd13687  127 -----------------------------------------------FGTVPNSSTERYFRRQVELMHRYMEKYN----- 154
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 750 svlVKSNEEGIQRVLTSDY-AFLMESTTIEFVTQRN--CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKL 826
Cdd:cd13687  155 ---YETVEEAIQALKNGKLdAFIWDSAVLEYEASQDegCKLVTVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHESGFM 231

                 ....*..
gi 755532823 827 HMMKEKW 833
Cdd:cd13687  232 EELDKKW 238
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
433-834 4.40e-32

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: 125.91  E-value: 4.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 433 LIVTTILEEPYVLFkkSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELIDHKADL 512
Cdd:cd13731    4 LRVVTVLEEPFVMV--SENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQE-DGTWNGLVGELVFKRADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 513 AVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGtnpgvfsflnplspdiwmyillaylgvscvlfviarqskfswfky 592
Cdd:cd13731   81 GISALTITPDRENVVDFTTRYMDYSVGVLLRRAES--------------------------------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 593 pncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsfwfgvgalmqqgselmpkalstrivg 672
Cdd:cd13731      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 673 giwwfftliiissytanlaafltvermespIDSADDLAKQTKIEYGAVEDGAT--------MTFFKKSkiSTYDKMWAFM 744
Cdd:cd13731  116 ------------------------------IQSLQDLSKQTDIPYGTVLDSAVyehvrmkgLNPFERD--SMYSQMWRMI 163
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 745 SSRRQSV-LVKSNEEGIQRVLTSDYAFLMESTTIEFV--TQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQ 821
Cdd:cd13731  164 NRSNGSEnNVLESQAGIQKVKYGNYAFVWDAAVLEYVaiNDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQ 243
                        410
                 ....*....|...
gi 755532823 822 EEGKLHMMKEKWW 834
Cdd:cd13731  244 QNGDMDILKHKWW 256
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
431-840 1.35e-30

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: 122.08  E-value: 1.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 431 RSLIVTTILEEPYVLFKK-----SDKPLY-----------GNDRF---EGYCIDLLRELSTILGFTYEIRLVEDGKYGAQ 491
Cdd:cd13719    2 THLKIVTIHEEPFVYVRPtpsdgTCREEFtvncpnfnisgRPTVPfccYGYCIDLLIKLARKMNFTYELHLVADGQFGTQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 492 DDVNG----QWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGtnpgvfsflnplspdiwmyi 567
Cdd:cd13719   82 ERVNNsnkkEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEIR-------------------- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 568 llaylgvscvlfviarqskfswfkypncshyhhsqrclctqhlesymelclfspyewynphpcnpdsdvvennftllnsf 647
Cdd:cd13719      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 648 wfgvgalmqqgselmpkalstriVGGIwwfftliiissytanlaaflTVERMESPIDsaddlakqtKIEYGAVEDGATMT 727
Cdd:cd13719  142 -----------------------LTGI--------------------NDPRLRNPSE---------KFIYATVKGSSVDM 169
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 728 FFKKS-KISTydkMWAFMSSRRqsvlVKSNEEGIQRVLTSD-YAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPM 805
Cdd:cd13719  170 YFRRQvELST---MYRHMEKHN----YETAEEAIQAVRDGKlHAFIWDSSRLEFEASQDCDLVTAGELFGRSGYGIGLQK 242
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 755532823 806 GSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCP 840
Cdd:cd13719  243 NSPWTDNVSLAILKMHESGFMEDLDKTWIRYQECE 277
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit ...
53-406 3.34e-30

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: 123.59  E-value: 3.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  53 EELAFRFAVNTINRNrtllPNTT-----LTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAVQSICNALgv 127
Cdd:cd06388   13 EYTAFRLAIFLHNTS----PNASeapfnLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSAL-- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 128 pHIQTRWKHQVSDNKDSFYVSLYPdfsSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNLRLKIRQLpAD 207
Cdd:cd06388   87 -HISLITPSFPTEGESQFVLQLRP---SLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICV-EN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 208 TKDA--KPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTE 285
Cdd:cd06388  162 FNDAsyRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDFN 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 286 NTQVSSIIEKWSM--ER----LQAPPKPDSglldgfmttdaALMYDAVHVVSVAVQQFPQMTV------SSLQC--NRHK 351
Cdd:cd06388  242 TPMVTKLMQRWKKldQReypgSETPPKYTS-----------ALTYDGVLVMAETFRNLRRQKIdisrrgNAGDClaNPAA 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755532823 352 PWRFGTRFMSLIKEAHWEGLTGRITFNKTnGLRTDFDLDVISLKEEGLEKIGTWD 406
Cdd:cd06388  311 PWGQGIDMERTLKQVRIQGLTGNVQFDHY-GRRVNYTMDVFELKSTGPRKVGYWN 364
PBP1_iGluR_N_LIVBP-like cd06351
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
39-412 7.43e-30

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: 121.69  E-value: 7.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEyVESGPmgaEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAV 118
Cdd:cd06351    3 GFIFE-VNNEP---AAKAFEVAVTYLKKNINTRYGLSVQYDSIEANKSNAFVLLEAICNKYATGTPALILDTTKSSINSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHI-----QTRWKHQVSDNKDSFYVSLYPDfSSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPS 193
Cdd:cd06351   79 TSALGAPHISASygqqgDLRQWRDLDEAKQKYLLQVRPP-EALRSIVLHLNITNAWIKFVDSYDMEHYKSLLQNIQTRAV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 194 RYNLRLKIR---------QLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFAL 264
Cdd:cd06351  158 QNNVIVAIAkvgkrereeQLDINNFFILGTLQSIRMVLEVRPAYFERNFAWHAITQNEVEISSQSDNAHIMFMNPMAYDI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 265 DVEPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDgfmtTDAALMYDAVHVVSVAVQQfpqmtvss 344
Cdd:cd06351  238 LLETVYRDRLGLTRTTYNLNENPMVQQFIQRWVRLDEREFPEAKNAELQ----LSSAFYFDLALRSALAFKE-------- 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532823 345 lqcnrhkpwrfgtrfmslikeahweglTGRITFNkTNGLRTDFDLDVISLK-EEGLEKIGTWDPSSGLN 412
Cdd:cd06351  306 ---------------------------TGYGTFD-LQSTQPFNGHSFMKFEmDINVRKIRGWSEYESVN 346
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
442-506 1.16e-27

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: 106.18  E-value: 1.16e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755532823   442 PYVLFKKSdkPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvNGQWNGMVRELI 506
Cdd:smart00918   1 PYVMLKES--PDGGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLP-NGSWNGMVGELV 62
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
386-546 1.13e-26

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: 110.89  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 386 DFDLDVISLKEEGLEKIGTWDPSSGlnmTESQKGKPANITDSLSNrslivTTILEEPyVLFKKSDKplygndrfeGYCID 465
Cdd:cd13718    1 KFHLKIVTLEEAPFVIVEPVDPLTG---TCMRNTVPCRKQLNHEN-----STDADEN-RYVKKCCK---------GFCID 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 466 LLRELSTILGFTYEIRLVEDGKYGAQddVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKP 545
Cdd:cd13718   63 ILKKLAKDVGFTYDLYLVTNGKHGKK--INGVWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMVARS 140

                 .
gi 755532823 546 N 546
Cdd:cd13718  141 N 141
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
39-412 1.01e-23

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: 104.69  E-value: 1.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEyvESGpmGAEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAV 118
Cdd:cd06381    3 GAIFE--ENA--AKDDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHI----------QTRWKHQVSDNKDSFYVSLYPDFsSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQEL 188
Cdd:cd06381   79 QSLTDAMHIPHLfvqrnpggspRTACHLNPSPDGEAYTLASRPPV-RLNDVMLRLVTELRWQKFVMFYDSEYDIRGLQSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 189 IKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFH--------VIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLD 260
Cdd:cd06381  158 LDQASRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNryrdtlrrAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 261 LFALDVEPYRYSGVN-MTGFR-ILNTENTQVSSIIEKWSMERLQAPPKpdsgllDGF---MTTDAALMYDAVHVVSVAVQ 335
Cdd:cd06381  238 ISDPEILDLVHSALGrMTVVRqIFPSAKDNQKCFRNNHRISSLLCDPQ------EGYlqmLQISNLYLYDSVLMLANAFH 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 336 QFPQ----MTVSSLQCNRH--KPWRFGTRFMSLIKEAHWEGLTGRITFNKTNG-LRTDFDLDVISLKEE---GLEKIGTW 405
Cdd:cd06381  312 RKLEdrkwHSMASLNCIRKstKPWNGGRSMLDTIKKGHITGLTGVMEFREDSSnPYVQFEILGTTYSETfgkDMRKLATW 391

                 ....*..
gi 755532823 406 DPSSGLN 412
Cdd:cd06381  392 DSEKGLN 398
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
39-327 6.57e-22

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: 97.87  E-value: 6.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEYVESGPMGAEEL-AFRFAVNTINRNRTLLPNTTLTYdTQKINLYDSFEASKKACDQL-SLGVAAIFGPSHSSSAN 116
Cdd:cd06269    3 GALLPVHDYLESGAKVLpAFELALSDVNSRPDLLPKTTLGL-AIRDSECNPTQALLSACDLLaAAKVVAILGPGCSASAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 117 AVQSICNALGVPHIQTRWKHQVSDNKD--SFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVY-DDSTGLIRLQELIKAPS 193
Cdd:cd06269   82 PVANLARHWDIPVLSYGATAPGLSDKSryAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYsDDEYGEFGLEGLEELFQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 194 RYNLRLKIRQ--LPADTKDAKPLLKEMKRgKEFHVIFDCSHEMAA-GILKQALAMGMMTEYYHYIFTtlDLFALD----V 266
Cdd:cd06269  162 EKGGLITSRQsfDENKDDDLTKLLRNLRD-TEARVIILLASPDTArSLMLEAKRLDMTSKDYVWFVI--DGEASSsdehG 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755532823 267 EPYRYSGVNMTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSG-LLDGFMttdaALMYDAV 327
Cdd:cd06269  239 DEARQAAEGAITVTLIFPVVKEFLKFSMELKLKSSKRKQGLNEEyELNNFA----AFFYDAV 296
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
426-543 1.53e-21

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: 95.69  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 426 DSLSNRSLIVTTILEEPYvlFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAqdDVNGQWNGMVREL 505
Cdd:cd13720   34 DPMTNDSSTLDALFSSLH--SSNDTVPIKFRKCCYGYCIDLLEKLAEDLGFDFDLYIVGDGKYGA--WRNGRWTGLVGDL 109
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755532823 506 IDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYR 543
Cdd:cd13720  110 LSGRAHMAVTSFSINSARSQVIDFTSPFFSTSLGILVR 147
PBP1_iGluR_delta_1 cd06392
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 ...
39-412 5.04e-20

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: 93.53  E-value: 5.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEYVESGpmgaEELAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAV 118
Cdd:cd06392    3 GAIFEENAAK----DDRVFQLAVSDLSLNDDILQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHI----------QTRWKHQVSDNKDSFYVSLYPDFsSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQEL 188
Cdd:cd06392   79 QSLTDAMHIPHLfvqrnsggspRTACHLNPSPEGEEYTLAARPPV-RLNDVMLKLVTELRWQKFIVFYDSEYDIRGLQSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 189 IKAPSRYNLRLKIRQLPAD-TKDAKPLLKEMK-------RGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLD 260
Cdd:cd06392  158 LDQASRLGLDVSLQKVDRNiSRVFTNLFTTMKteelnryRDTLRRAILLLSPRGAQSFINEAVETNLASKDSHWVFVNEE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 261 LFALDVEPYRYSGVN-MTGFRILNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALmYDAVHVVSVA----VQ 335
Cdd:cd06392  238 ISDPEILELVHSALGrMTVIRQIFPLSKDNNQRCMRNNHRISSLLCDPQEGYLQMLQVSNLYL-YDSVLMLANAfhrkLE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 336 QFPQMTVSSLQCNRH--KPWRFGTRFMSLIKEAHWEGLTGRITFnKTNGLRTDFDLDVI--SLKE---EGLEKIGTWDPS 408
Cdd:cd06392  317 DRKWHSMASLNCIRKstKPWNGGRSMLDTIKKGHITGLTGVMEF-REDGANPYVQFEILgtSYSEtfgKDVRRLATWDSE 395

                 ....
gi 755532823 409 SGLN 412
Cdd:cd06392  396 KGLN 399
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
39-414 1.30e-18

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: 89.33  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEyvESGPMGAEelAFRFAVNTINRNRTLLPNTTLTYDTQKINLYDSFEASKKACDQLSLGVAAIFGPSHSSSANAV 118
Cdd:cd06391    3 GAIFD--ESAKKDDE--VFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHI----------QTRWKHQVSDNKDSFYVSLYPDFsSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQEL 188
Cdd:cd06391   79 QSLADAMHIPHLfiqrstagtpRSGCGLTRSNRNDDYTLSVRPPV-YLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 189 IKAPSRYNLRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDcSHEMAAGILKQALAMGMMTEYY---------HYIFTTL 259
Cdd:cd06391  158 LDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRD-TLRRAILVMNPATAKSFITEVVetnlvafdcHWIIINE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 260 DLFALDV-EPYRYSGVNMTGFRilntentQVSSIIEKWSMERLQAPPKPDSGLLD------GFMTTDAALMYDAVHVVSV 332
Cdd:cd06391  237 EINDVDVqELVRRSIGRLTIIR-------QTFPVPQNISQRCFRGNHRISSSLCDpkdpfaQNMEISNLYIYDTVLLLAN 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 333 AVQQFPQ----MTVSSLQCNRH--KPWRFGTRFMSLIKEAHWEGLTGRITFNKtNGLRTDFDLDVISLK--EE---GLEK 401
Cdd:cd06391  310 AFHKKLEdrkwHSMASLSCIRKnsKPWQGGRSMLETIKKGGVSGLTGLLEFGE-NGGNPNVHFEILGTNygEElgrGVRK 388
                        410
                 ....*....|...
gi 755532823 402 IGTWDPSSGLNMT 414
Cdd:cd06391  389 LGCWNPVTGLNGS 401
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
37-411 1.00e-16

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: 83.05  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  37 RFGGIFEYveSGPMGAEEL-AFRFAVNTINrNRTLLPNTTLTYDTQKINlYDSFEASKKACDQLS-LGVAAIFGPSHSSS 114
Cdd:cd19990    1 KIGAILDL--NSRVGKEAKvAIEMAVSDFN-SDSSSYGTKLVLHVRDSK-GDPLQAASAALDLIKnKKVEAIIGPQTSEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 115 ANAVQSICNALGVPHI----------QTRWkhqvsdnkdSFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDD---STG 181
Cdd:cd19990   77 ASFVAELGNKAQVPIIsfsatsptlsSLRW---------PFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDddyGSG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 182 LIrlQELIKAPSRYNLRLKIR-QLPADTKDA---KPLLKEMKRGKEFHVIFDCShEMAAGILKQALAMGMMTEYYHYIFT 257
Cdd:cd19990  148 II--PYLSDALQEVGSRIEYRvALPPSSPEDsieEELIKLKSMQSRVFVVHMSS-LLASRLFQEAKKLGMMEKGYVWIVT 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 258 TLDLFALDVEPYRYSGvNMTG---FRILNTENTQVSSIIEKW-SMERLQAPPKPDSGLldgfmTTDAALMYDAVHVVSVA 333
Cdd:cd19990  225 DGITNLLDSLDSSTIS-SMQGvigIKTYIPESSEFQDFKARFrKKFRSEYPEEENAEP-----NIYALRAYDAIWALAHA 298
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755532823 334 VQQFpqmtvsSLQCNRHKPWRFGTRFMSLIKEAHWEGLTGRITF-NKTNGLRTDFdlDVISLKEEGLEKIGTWDPSSGL 411
Cdd:cd19990  299 VEKL------NSSGGNISVSDSGKKLLEEILSTKFKGLSGEVQFvDGQLAPPPAF--EIVNVIGKGYRELGFWSPGSGF 369
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
56-406 3.87e-15

Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model.


Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 78.44  E-value: 3.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  56 AFRFAVNTINRNRTLLPNTTLTY---DTQKinlyDSFEASKKACDQLSLGVAAIFGP--SHSSSANAVQsicnALGVPHI 130
Cdd:cd06370   25 AITLAVDDVNNDPNLLPGHTLSFvwnDTRC----DELLSIRAMTELWKRGVSAFIGPgcTCATEARLAA----AFNLPMI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 131 QTRWKHQVSDNKdsfyvSLYPDF-------SSLSRAILDLVQFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNlRLKIRQ 203
Cdd:cd06370   97 SYKCADPEVSDK-----SLYPTFartippdSQISKSVIALLKHFNWNKVSIVYENETKWSKIADTIKELLELN-NIEINH 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 204 L-------PADTKDAKP---LLKEMKRGKEFHVIFDcSHEMAAGILKQALAMGMMT--EyyhYIFTTLDLFALDVEPYRY 271
Cdd:cd06370  171 EeyfpdpyPYTTSHGNPfdkIVEETKEKTRIYVFLG-DYSLLREFMYYAEDLGLLDngD---YVVIGVELDQYDVDDPAK 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 272 SgvNMTGFRILNTENTQ--------VSSII------EKWSM------ERLQAPP----KPDSGLLDGFMTTDAALMYDAV 327
Cdd:cd06370  247 Y--PNFLSGDYTKNDTKealeafrsVLIVTpspptnPEYEKftkkvkEYNKLPPfnfpNPEGIEKTKEVPIYAAYLYDAV 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 328 HVVSVAVQQfpqmTVSSLQCNRHkpwrfGTRFMSLIKEAHWEGLTG-RITFNKtNGlRTDFDLDVISLKEEGLEKIGTWD 406
Cdd:cd06370  325 MLYARALNE----TLAEGGDPRD-----GTAIISKIRNRTYESIQGfDVYIDE-NG-DAEGNYTLLALKPNKGTNDGSYG 393
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
55-220 2.36e-14

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


Pssm-ID: 380573  Cd Length: 350  Bit Score: 75.41  E-value: 2.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  55 LAFRFAVNTINRNRTLLPNTTLTY---DT------------QKINLYDSFEASKKACDQLSLG-VAAIFGPSHSSSANAV 118
Cdd:cd06350   31 EAMIYAIEEINNDSSLLPNVTLGYdirDTcssssvalesslEFLLDNGIKLLANSNGQNIGPPnIVAVIGAASSSVSIAV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPhiqtrwkhQVS--------DNKdsfyvSLYPDF-------SSLSRAILDLVQFFKWKTVTVVY-DDSTGL 182
Cdd:cd06350  111 ANLLGLFKIP--------QISyastspelSDK-----IRYPYFlrtvpsdTLQAKAIADLLKHFNWNYVSTVYsDDDYGR 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755532823 183 --------------------IRLQELIKAPSRYNLRLKIRQLP--------ADTKDAKPLLKEMKR 220
Cdd:cd06350  178 sgieafereakergiciaqtIVIPENSTEDEIKRIIDKLKSSPnakvvvlfLTESDARELLKEAKR 243
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
433-552 2.29e-13

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: 70.36  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 433 LIVTTILE-EPYVLFKKSDKPlygndrfEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKAD 511
Cdd:cd13530    2 LRVGTDADyPPFEYIDKNGKL-------VGFDVDLANAIAKRLGVKVEFVDTD-------------FDGLIPALQSGKID 61
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 755532823 512 LAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGV 552
Cdd:cd13530   62 VAISGMTITPERAKVVDFSDPYYYTGQVLVVKKDSKITKTV 102
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
456-544 2.05e-12

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: 67.70  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 456 NDRFEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMT 535
Cdd:COG0834   18 DGKLVGFDVDLARAIAKRLGLKVEFVPVP-------------WDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPYYT 84

                 ....*....
gi 755532823 536 LGISILYRK 544
Cdd:COG0834   85 SGQVLLVRK 93
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
456-544 8.42e-12

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: 65.78  E-value: 8.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  456 NDRFEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMT 535
Cdd:pfam00497  18 NGKLVGFDVDLAKAIAKRLGVKVEFVPVS-------------WDGLIPALQSGKVDLIIAGMTITPERAKQVDFSDPYYY 84

                  ....*....
gi 755532823  536 LGISILYRK 544
Cdd:pfam00497  85 SGQVILVRK 93
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
432-549 1.27e-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: 65.05  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 432 SLIVTTILEEPYVLfkksdkplYGNDRFEGYCIDLLRELSTILGFTYEirlvedgkYGAQDDVNGqwngMVRELIDHKAD 511
Cdd:cd00997    4 TLTVATVPRPPFVF--------YNDGELTGFSIDLWRAIAERLGWETE--------YVRVDSVSA----LLAAVAEGEAD 63
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 755532823 512 LAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTN 549
Cdd:cd00997   64 IAIAAISITAEREAEFDFSQPIFESGLQILVPNTPLIN 101
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
47-247 7.21e-11

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


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 64.57  E-value: 7.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  47 SGPMGA----EELAFRFAVNTINRNRTLLPNT--TLTYDTQkinlYDSFEASKKAcDQL--SLGVAAIFGPSHSSSANAV 118
Cdd:COG0683   13 TGPYAAlgqpIKNGAELAVEEINAAGGVLGRKieLVVEDDA----SDPDTAVAAA-RKLidQDKVDAIVGPLSSGVALAV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHIQTRW-KHQVSDNKDSFYV-SLYPDFSSLSRAILD-LVQFFKWKTVTVVYDDST-GLIRLQELIKAPSR 194
Cdd:COG0683   88 APVAEEAGVPLISPSAtAPALTGPECSPYVfRTAPSDAQQAEALADyLAKKLGAKKVALLYDDYAyGQGLAAAFKAALKA 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755532823 195 YNLRL-KIRQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGM 247
Cdd:COG0683  168 AGGEVvGEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGL 221
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
60-414 1.40e-10

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


Pssm-ID: 380575 [Multi-domain]  Cd Length: 391  Bit Score: 64.30  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  60 AVNTINRNRTLLPNTTLTYDTQKINLyDSFEASKKACDQL-SLGVAAIFGPSHSSSANAVQSICNALGVPHIQtrWKHQV 138
Cdd:cd06352   27 AIERINSEGLLLPGFNFEFTYRDSCC-DESEAVGAAADLIyKRNVDVFIGPACSAAADAVGRLATYWNIPIIT--WGAVS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 139 SDNKDSFY----VSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDSTG-----LIRLQELIKAPSRYNLRLKIRQLPADTK 209
Cdd:cd06352  104 ASFLDKSRyptlTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDDSkcfsiANDLEDALNQEDNLTISYYEFVEVNSDS 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 210 DAKPLLKEMKrgKEFHVIFDCSHEMAA-GILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNM-------TGFRI 281
Cdd:cd06352  184 DYSSILQEAK--KRARIIVLCFDSETVrQFMLAAHDLGMTNGEYVFIFIELFKDGFGGNSTDGWERNDgrdedakQAYES 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 282 -----LNTENTQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVSVAV----QQFPQMTvsslqcNrhkp 352
Cdd:cd06352  262 llvisLSRPSNPEYDNFSKEVKARAKEPPFYCYDASEEEVSPYAAALYDAVYLYALALnetlAEGGNYR------N---- 331
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755532823 353 wrfGTRFMSLIKEAHWEGLTGRITFNKtNGLR-TDFDLDVISLKEEGLEKIGTWDPSSGLNMT 414
Cdd:cd06352  332 ---GTAIAQRMWNRTFQGITGPVTIDS-NGDRdPDYALLDLDPSTGKFVVVLTYDGTSNGLVV 390
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
57-404 4.23e-10

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: 62.74  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  57 FRFAVNTINRNRTLLPNTTLTYDTQKINLyDSFEASKKACDQLSLGVAAIFGPSHSSSAN-----AVQSICNALGVP--H 129
Cdd:cd06379   18 FREAVNEVNAHSHLPRKITLNATSITLDP-NPIRTALSVCEDLIASQVYAVIVSHPPTPSdlsptSVSYTAGFYRIPviG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 130 IQTRwkhQVSDNKDSFYVSLY---PDFSSLSRAILDLVQFFKWKTVTVVY-DDSTG---LIRLQELikAPSRYNLRLKIR 202
Cdd:cd06379   97 ISAR---DSAFSDKNIHVSFLrtvPPYSHQADVWAEMLRHFEWKQVIVIHsDDQDGralLGRLETL--AETKDIKIEKVI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 203 QLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGMMTEYYHYIFTTLDLFAldvepyRYSGVNMTGFRIL 282
Cdd:cd06379  172 EFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIVTEQALAA------SNVPDGVLGLQLI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 283 NteNTQVSSIIEkwsmerlqappkpdsglldgfmttdaalmyDAVHVVSVAVQQF----PQMTVSSLQCNRHKP-WRFGT 357
Cdd:cd06379  246 H--GKNESAHIR------------------------------DSVSVVAQAIRELfrssENITDPPVDCRDDTNiWKSGQ 293
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 755532823 358 RFMSLIKEAHWE-GLTGRITFNKtNGLRTDFDLDVISLKEEG-LEKIGT 404
Cdd:cd06379  294 KFFRVLKSVKLSdGRTGRVEFND-KGDRIGAEYDIINVQNPRkLVQVGI 341
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
34-246 9.56e-10

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


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 61.93  E-value: 9.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  34 HVLRFGGIfEYVEsgpmgaeelAFRFAVNTINRNRTLLPNTTL---TYDT-------------------QKINLYDSFEA 91
Cdd:cd06362   23 EIREERGI-QRLE---------AMLFAIDEINSRPDLLPNITLgfvILDDcssdttaleqalhfirdslLSQESAGFCQC 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  92 SKKACDQLSLG----VAAIFGPSHSSSANAVQSICNALGVPhiqtrwkhQVSdnkdsfYVS---------LYPDFS---- 154
Cdd:cd06362   93 SDDPPNLDESFqfydVVGVIGAESSSVSIQVANLLRLFKIP--------QIS------YAStsdelsdkeRYPYFLrtvp 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 155 --SLS-RAILDLVQFFKWKTVTVVY-DDSTGLIRLQELIKAPSRYNL----RLKIRQLPaDTKDAKPLLKEMKRGKEFHV 226
Cdd:cd06362  159 sdSFQaKAIVDILLHFNWTYVSVVYsEGSYGEEGYKAFKKLARKAGIciaeSERISQDS-DEKDYDDVIQKLLQKKNARV 237
                        250       260
                 ....*....|....*....|..
gi 755532823 227 I--FdCSHEMAAGILKQALAMG 246
Cdd:cd06362  238 VvlF-ADQEDIRGLLRAAKRLG 258
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
39-410 1.84e-09

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


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 60.72  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEYVESGP---MGAEELAFRFAVNTINRNRTLLPNTTL---TYDTQ-------KInLYDSFEASKKacdqlslgVAA 105
Cdd:cd06366    3 GGLFPLSGSKGwwgGAGILPAAEMALEHINNRSDILPGYNLeliWNDTQcdpglglKA-LYDLLYTPPP--------KVM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 106 IFGPSHSSSANAVqsicnALGVPHiqtrWKH-QVS--------DNKDS---FYVSLYPDfSSLSRAILDLVQFFKWKTVT 173
Cdd:cd06366   74 LLGPGCSSVTEPV-----AEASKY----WNLvQLSyaatspalSDRKRypyFFRTVPSD-TAFNPARIALLKHFGWKRVA 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 174 VVY-DDSTGLIRLQELIKAPSRYNLRLKIRQLPADTkDAKPLLKEMKRgKEFHVIF-DCSHEMAAGILKQALAMGM---- 247
Cdd:cd06366  144 TIYqNDEVFSSTAEDLEELLEEANITIVATESFSSE-DPTDQLENLKE-KDARIIIgLFYEDAARKVFCEAYKLGMygpk 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 248 -----MTEYYHYIFTTLD----------LFALDvepyrysGVNMTGFRILNTENTQ-VSSI-IEKWsMERLQAPPKPDSG 310
Cdd:cd06366  222 yvwilPGWYDDNWWDVPDndvnctpeqmLEALE-------GHFSTELLPLNPDNTKtISGLtAQEF-LKEYLERLSNSNY 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 311 LLDGFmttdAALMYDAVHVVSVAVQQfpqmTVSSLQCNRHKPWRF-------GTRFMSLIKEAHWEGLTGRITFNKTNGL 383
Cdd:cd06366  294 TGSPY----APFAYDAVWAIALALNK----TIEKLAEYNKTLEDFtyndkemADLFLEAMNSTSFEGVSGPVSFDSKGDR 365
                        410       420
                 ....*....|....*....|....*..
gi 755532823 384 RTDFDLDVISLKEEglEKIGTWDPSSG 410
Cdd:cd06366  366 LGTVDIEQLQGGSY--VKVGLYDPNAD 390
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
455-547 1.31e-08

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: 56.44  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 455 GNDRFEGYCIDLLRELSTILGFTYEIRLvedgkygaqddvnGQWNGMVRELIDHKADLaVAPLAITYVREKVIDFSKPFM 534
Cdd:cd13704   20 ENGNPTGFNVDLLRAIAEEMGLKVEIRL-------------GPWSEVLQALENGEIDV-LIGMAYSEERAKLFDFSDPYL 85
                         90
                 ....*....|...
gi 755532823 535 TLGISILYRKPNG 547
Cdd:cd13704   86 EVSVSIFVRKGSS 98
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
455-546 2.36e-08

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: 55.58  E-value: 2.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 455 GNDRFEGYCIDLLRELSTILGFTYEIrlvedgkygaqddVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFM 534
Cdd:cd13624   18 ENGKIVGFDIDLIKAIAKEAGFEVEF-------------KNMAFDGLIPALQSGKIDIIISGMTITEERKKSVDFSDPYY 84
                         90
                 ....*....|..
gi 755532823 535 TLGISILYRKPN 546
Cdd:cd13624   85 EAGQAIVVRKDS 96
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
454-544 6.70e-08

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 54.26  E-value: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823   454 YGNDRFEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPF 533
Cdd:smart00062  17 DEDGELTGFDVDLAKAIAKELGLKVEFVEVS-------------FDSLLTALKSGKIDVVAAGMTITPERAKQVDFSDPY 83
                           90
                   ....*....|.
gi 755532823   534 MTLGISILYRK 544
Cdd:smart00062  84 YRSGQVILVRK 94
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
456-546 9.33e-08

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: 53.82  E-value: 9.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 456 NDRFEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMT 535
Cdd:cd00994   18 DGKYVGFDIDLWEAIAKEAGFKYELQPMD-------------FKGIIPALQTGRIDIAIAGITITEERKKVVDFSDPYYD 84
                         90
                 ....*....|.
gi 755532823 536 LGISILYRKPN 546
Cdd:cd00994   85 SGLAVMVKADN 95
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
55-188 1.09e-07

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


Pssm-ID: 380588 [Multi-domain]  Cd Length: 464  Bit Score: 55.34  E-value: 1.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  55 LAFRFAVNTINRNRTLLPNTTLTYDtqkinLYDSFEASKKA-------------------CDQLSLGVAAIFGPSHSSSA 115
Cdd:cd06365   40 LAFLFAIEEINKNPDLLPNITLGFH-----IYDSCSSERLAlesslsilsgnsepipnysCREQRKLVAFIGDLSSSTSV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 116 navqSICNALGVPHIQtrwkhQVS--------DNKD---SFYVSLYPDfSSLSRAILDLVQFFKWKTV-TVVYDDSTGLI 183
Cdd:cd06365  115 ----AMARILGLYKYP-----QISygafdpllSDKVqfpSFYRTVPSD-TSQSLAIVQLLKHFGWTWVgLIISDDDYGEQ 184

                 ....*
gi 755532823 184 RLQEL 188
Cdd:cd06365  185 FSQDL 189
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
39-220 5.42e-07

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


Pssm-ID: 380587 [Multi-domain]  Cd Length: 473  Bit Score: 53.03  E-value: 5.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  39 GGIFEY------------VESGPMGAEELAFR---------FAVNTINRNRTLLPNTTLTYdtqKInlYDS-------FE 90
Cdd:cd06364    3 GGLFPIhfrpvspdpdftTEPHSPECEGFNFRgfrwaqtmiFAIEEINNSPDLLPNITLGY---RI--YDScatiskaLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  91 ASkkacdqLSL-----------------GVAAIFGPSHSSSANAVQSIcnaLGVPHIQtrwkhQV---------SDNKD- 143
Cdd:cd06364   78 AA------LALvngqeetnldercsggpPVAAVIGESGSTLSIAVART---LGLFYIP-----QVsyfascaclSDKKQf 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 144 -SFYVSLYPDFSSlSRAILDLVQFFKWKTV-TVVYDDSTGL----------------IRLQELIkapSRYNLRLKIRQLP 205
Cdd:cd06364  144 pSFLRTIPSDYYQ-SRALAQLVKHFGWTWVgAIASDDDYGRngikafleeaeklgicIAFSETI---PRTYSQEKILRIV 219
                        250       260
                 ....*....|....*....|....*....
gi 755532823 206 --------------ADTKDAKPLLKEMKR 220
Cdd:cd06364  220 evikkstakvivvfSSEGDLEPLIKELVR 248
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
455-552 2.43e-06

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: 49.52  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 455 GNDRFEGYCIDLLRELSTILGFTYEIRLVEDgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFM 534
Cdd:cd01009   17 DRGGPRGFEYELAKAFADYLGVELEIVPADN------------LEELLEALEEGKGDLAAAGLTITPERKKKVDFSFPYY 84
                         90
                 ....*....|....*...
gi 755532823 535 TLGISILYRKPNGTNPGV 552
Cdd:cd01009   85 YVVQVLVYRKGSPRPRSL 102
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
442-546 4.35e-06

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: 48.88  E-value: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 442 PYVLFKKSDkplyGNDRFEGYCIDLLRELSTILGFTYEIrlvedgkygaqddVNGQWNGMVRELIDHKADLAVAPLAITY 521
Cdd:cd13620   16 PFEFQKMKD----GKNQVVGADIDIAKAIAKELGVKLEI-------------KSMDFDNLLASLQSGKVDMAISGMTPTP 78
                         90       100
                 ....*....|....*....|....*
gi 755532823 522 VREKVIDFSKPFMTLGISILYRKPN 546
Cdd:cd13620   79 ERKKSVDFSDVYYEAKQSLLVKKAD 103
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
37-380 5.29e-06

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


Pssm-ID: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 49.46  E-value: 5.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  37 RFGGIFEyvESGPMG----AEELAFRFAVNTINRNRTLLPNT--TLTYDTQKinlyDSFEAS---KKACDQLslGVAAIF 107
Cdd:cd06347    1 KIGVIGP--LTGEAAaygqPALNGAELAVDEINAAGGILGKKieLIVYDNKS----DPTEAAnaaQKLIDED--KVVAII 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 108 GPSHSSSANAVQSICNALGVPHIqTRW--KHQVSDNKDSFYVSLYPD---------FsslsrAILDLvqffKWKTVTVVY 176
Cdd:cd06347   73 GPVTSSIALAAAPIAQKAKIPMI-TPSatNPLVTKGGDYIFRACFTDpfqgaalakF-----AYEEL----GAKKAAVLY 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 177 D----DSTGLIRL--QELIKAPSRynlRLKIRQLPADTKDAKPLLKEMKRgKEFHVIFDCSH-EMAAGILKQALAMGMMT 249
Cdd:cd06347  143 DvssdYSKGLAKAfkEAFEKLGGE---IVAEETYTSGDTDFSAQLTKIKA-ANPDVIFLPGYyEEAALIIKQARELGITA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 250 eyyhYIFTTLDLFALDVEPYRYSGVN----MTGFRILNTeNTQVSSIIEKWsMERLQAPPkpdsglldgfmTTDAALMYD 325
Cdd:cd06347  219 ----PILGGDGWDSPELLELGGDAVEgvyfTTHFSPDDP-SPEVQEFVKAY-KAKYGEPP-----------NAFAALGYD 281
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 326 AVHVVSVAVQqfpqmtvsslqcnrhkpwRFGTRFMSLIKEA-----HWEGLTGRITFNKT 380
Cdd:cd06347  282 AVMLLADAIK------------------RAGSTDPEAIRDAlaktkDFEGVTGTITFDPN 323
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
432-535 5.38e-06

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: 48.62  E-value: 5.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 432 SLIVTTILEEPYVLFKKSDKP-LYGNDrfegycIDLLRELSTILGFTYEIrlvedgkygaQDdvnGQWNGMVRELIDHKA 510
Cdd:cd13628    1 TLNMGTSPDYPPFEFKIGDRGkIVGFD------IELAKTIAKKLGLKLQI----------QE---YDFNGLIPALASGQA 61
                         90       100
                 ....*....|....*....|....*
gi 755532823 511 DLAVAPLAITYVREKVIDFSKPFMT 535
Cdd:cd13628   62 DLALAGITPTPERKKVVDFSEPYYE 86
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
456-533 8.56e-06

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: 48.06  E-value: 8.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532823 456 NDRFEGYCIDLLRELSTILGFTYEIrlvedgkygaqddVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPF 533
Cdd:cd01001   21 DGKLVGFDIDLANALCKRMKVKCEI-------------VTQPWDGLIPALKAGKYDAIIASMSITDKRRQQIDFTDPY 85
PBP2_GlnP cd13619
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ...
446-548 9.07e-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: 47.70  E-value: 9.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 446 FKKSDKPLYGNDrfegycIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREK 525
Cdd:cd13619   15 FQNDDGKYVGID------VDLLNAIAKDQGFKVELKPMG-------------FDAAIQAVQSGQADGVIAGMSITDERKK 75
                         90       100
                 ....*....|....*....|...
gi 755532823 526 VIDFSKPFMTLGISILYRKPNGT 548
Cdd:cd13619   76 TFDFSDPYYDSGLVIAVKKDNTS 98
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
455-544 9.28e-06

Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 periplasmic-bindig protein fold; This group includes periplasmic glutamine-binding domain GlnP from Bacillus subtilis and its related proteins. The GlnP domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270407 [Multi-domain]  Cd Length: 229  Bit Score: 48.00  E-value: 9.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 455 GNDRFEGYCIDLLRELSTILGFTYEIRLVEDgkygaqddvngqwNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFM 534
Cdd:cd13689   27 KTREIVGFDVDLCKAIAKKLGVKLELKPVNP-------------AARIPELQNGRVDLVAANLTYTPERAEQIDFSDPYF 93
                         90
                 ....*....|
gi 755532823 535 TLGISILYRK 544
Cdd:cd13689   94 VTGQKLLVKK 103
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
91-247 1.15e-05

periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.


Pssm-ID: 380492 [Multi-domain]  Cd Length: 298  Bit Score: 48.09  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  91 ASKKACDQlslGVAAIFGPSHSSSANAVQSICNALGVPHIQT-----RWKHQVSDNKdsFYVSlyPDFSSLSRAILD-LV 164
Cdd:cd06268   59 ARKLVDDD---KVLAVVGHYSSSVTLAAAPIYQEAGIPLISPgstapELTEGGGPYV--FRTV--PSDAMQAAALADyLA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 165 QFFKWKTVTVVYDD---STGLIR-LQELIKApsrynLRLKI---RQLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAG 237
Cdd:cd06268  132 KKLKGKKVAILYDDydyGKSLADaFKKALKA-----LGGEIvaeEDFPLGTTDFSAQLTKIKAAGPDVLFLAGYGADAAN 206
                        170
                 ....*....|
gi 755532823 238 ILKQALAMGM 247
Cdd:cd06268  207 ALKQARELGL 216
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
455-546 1.26e-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: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 455 GNDRFEGYCIDLLRELSTILGFTYEIrlvedgkygaqddVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFM 534
Cdd:cd13626   18 EDGKLTGFDVEVGREIAKRLGLKVEF-------------KATEWDGLLPGLNSGKFDVIANQVTITPEREEKYLFSDPYL 84
                         90
                 ....*....|..
gi 755532823 535 TLGISILYRKPN 546
Cdd:cd13626   85 VSGAQIIVKKDN 96
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
56-251 1.58e-05

Family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems; This CD includes members of the family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. The family C GPCR includes glutamate/glycine-gated ion channels such as the NMDA receptor, G-protein-coupled receptors, metabotropic glutamate, GABA-B, calcium sensing, pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. The glutamate receptors that form cation-selective ion channels, iGluR, can be classified into three different subgroups according to their binding-affinity for the agonists NMDA (N-methyl-D-asparate), AMPA (alpha-amino-3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid), and kainate. L-glutamate is a major neurotransmitter in the brain of vertebrates and acts through either mGluRs or iGluRs. mGluRs subunits possess seven transmembrane segments and a large N-terminal extracellular domain. ABC-type leucine-isoleucine-valine binding protein (LIVBP) is a bacterial periplasmic binding protein that has homology with the amino-terminal domain of the glutamate-receptor ion channels (iGluRs). The extracellular regions of iGluRs are made of two PBP-like domains in tandem, a LIVBP-like domain that constitutes the N terminus (included in this model) followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type 2 periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are also included in this family.


Pssm-ID: 380490  Cd Length: 306  Bit Score: 48.07  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  56 AFRFAVNTINRNRTLLPNTTLtydtqKINLYDSFEASKKACDQ---------------------------LSLGVAAIFG 108
Cdd:cd04509   32 AMEQALDDINADPNLLPNNTL-----GIVIYDDCCDPKQALEQsnkfvndliqkdtsdvrctngeppvfvKPEGIKGVIG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 109 PSHSSSANAVQSICNALGVPHIQ-TRWKHQVSDNKD-SFYVSLYPDFSSLSRAILDLVQFFKWKTVTVVYDDST---GLI 183
Cdd:cd04509  107 HLCSSVTIPVSNILELFGIPQITyAATAPELSDDRGyQLFLRVVPLDSDQAPAMADIVKEKVWQYVSIVHDEGQygeGGA 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755532823 184 R-LQELIKapsRYNLRL----KIRQlPADTKDAKPLLKEMKR--GKEFHVIFdCSHEMAAGILKQALAMGMMTEY 251
Cdd:cd04509  187 RaFQDGLK---KGGLCIafsdGITA-GEKTKDFDRLVARLKKenNIRFVVYF-GYHPEMGQILRAARRAGLVGKF 256
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
456-544 1.93e-05

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: 46.76  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 456 NDRFEGYCIDLLRELSTILGFTYEIrlvedgkygaqddVNGQ-WNGMVRELIDHKADLaVAPLAITYVREKVIDFSKPFM 534
Cdd:cd01007   21 GGEPQGIAADYLKLIAKKLGLKFEY-------------VPGDsWSELLEALKAGEIDL-LSSVSKTPEREKYLLFTKPYL 86
                         90
                 ....*....|
gi 755532823 535 TLGISILYRK 544
Cdd:cd01007   87 SSPLVIVTRK 96
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
459-550 2.94e-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: 46.22  E-value: 2.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 459 FEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGI 538
Cdd:cd13712   22 LTGFEVDVAKALAAKLGVKPEFVTTE-------------WSGILAGLQAGKYDVIINQVGITPERQKKFDFSQPYTYSGI 88
                         90
                 ....*....|..
gi 755532823 539 SILYRKPNGTNP 550
Cdd:cd13712   89 QLIVRKNDTRTF 100
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
461-557 3.57e-05

Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily includes the periplasmic binding protein type II (BPBII). This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBPII proteins share the same architecture as periplasmic binding proteins type I (PBPI), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBPII proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 46.03  E-value: 3.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 461 GYCIDLLRELSTILGFTYEIrlvedgkygaqddVNGQWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTLGISI 540
Cdd:cd13629   24 GFDVDLAKALAKDLGVKVEF-------------VNTAWDGLIPALQTGKFDLIISGMTITPERNLKVNFSNPYLVSGQTL 90
                         90
                 ....*....|....*..
gi 755532823 541 LYRKPNGTNPGVFSFLN 557
Cdd:cd13629   91 LVNKKSAAGIKSLEDLN 107
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
452-541 4.42e-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: 45.97  E-value: 4.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 452 PLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDvngqwngMVRELIDHKADLAVAPLAITYVREKVIDFSK 531
Cdd:cd13686   23 PITNSTSVTGFCIDVFEAAVKRLPYAVPYEFIPFNDAGSYDD-------LVYQVYLKKFDAAVGDITITANRSLYVDFTL 95
                         90
                 ....*....|
gi 755532823 532 PFMTLGISIL 541
Cdd:cd13686   96 PYTESGLVMV 105
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
448-544 4.66e-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: 45.81  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 448 KSDKPLYG----NDRFEGYCIDLLRELS-TILGFTYEIRLVEdgkygaqddVNGqwNGMVRELIDHKADLAVAPLAITYV 522
Cdd:cd13694   15 FGDKPPFGyvdeNGKFQGFDIDLAKQIAkDLFGSGVKVEFVL---------VEA--ANRVPYLTSGKVDLILANFTVTPE 83
                         90       100
                 ....*....|....*....|..
gi 755532823 523 REKVIDFSKPFMTLGISILYRK 544
Cdd:cd13694   84 RAEVVDFANPYMKVALGVVSPK 105
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
102-379 5.54e-05

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


Pssm-ID: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 46.45  E-value: 5.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 102 GVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKH---QVSDNKDSFYVSlyPDFSSLSRAILD-LVQFFKWKTVTVVYD 177
Cdd:cd19980   67 KVPAIIGAWCSSVTLAVMPVAERAKVPLVVEISSApkiTEGGNPYVFRLN--PTNSMLAKAFAKyLADKGKPKKVAFLAE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 178 DS----TGLIRLQELIKAP------SRYnlrlkirqLPADTKDAKPLLKEMKRGKEFHVIFDCSHEMAAGILKQALAMGM 247
Cdd:cd19980  145 NDdygrGAAEAFKKALKAKgvkvvaTEY--------FDQGQTDFTTQLTKLKAANPDAIFVVAETEDGALILKQARELGL 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 248 MTEYYHYI-FTTLDLFALDVEPYRYS-GVNMTGFRILNTENTQVssiiEKWSMERLQAPPkpdsglldgfmTTDAALMYD 325
Cdd:cd19980  217 KQQLVGTGgTTSPDLIKLAGDAAEGVyGASIYAPTADNPANKAF----VAAYKKKYGEPP-----------DKFAALGYD 281
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755532823 326 AVHVVSVAVQqfpqmtvsslqcnRHKPWRFGTRFMSLIKEAHWEGLTGRITFNK 379
Cdd:cd19980  282 AVMVIAEAIK-------------KAGSTDPEKIRAAALKKVDYKGPGGTIKFDE 322
PBP1_ABC_ligand_binding-like cd06338
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
102-255 1.21e-04

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


Pssm-ID: 380561 [Multi-domain]  Cd Length: 347  Bit Score: 45.27  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 102 GVAAIFGPSHSSSANAVQSICNALGVPHIQTrwkhqvSDNKDSFYVSLYPD-FSSLSRAILDLVQFFKW--------KTV 172
Cdd:cd06338   71 KVDLLLGPYSSGLTLAAAPVAEKYGIPMIAG------GAASDSIFERGYKYvFGVLPPASDYAKGLLDLlaelgpkpKTV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 173 TVVY-DDSTGLIRLQELIKAPSRYNLRLKIRQ-LPADTKDAKPLLKEMKRGK-EfhVIFDCSH-EMAAGILKQALAMGMM 248
Cdd:cd06338  145 AIVYeDDPFGKEVAEGAREAAKKAGLEVVYDEsYPPGTTDFSPLLTKVKAANpD--ILLVGGYpPDAITLVRQMKELGYN 222

                 ....*..
gi 755532823 249 TEYYHYI 255
Cdd:cd06338  223 PKAFFLT 229
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
779-833 1.45e-04

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: 44.25  E-value: 1.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755532823 779 FVTQR-NCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKW 833
Cdd:cd00997  161 YAAHDgNGKAEVTGSVFLEENYGIVFPTGSPLRKPINQALLNLREDGTYDELYEKW 216
PBP2_ml15202_like cd13701
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
434-533 1.58e-04

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: 43.99  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 434 IVTTILEEPYVLFKKSDkplyGNDRFEGYCIDLLRELSTILGFTYEIRLVedgkygaqddvngQWNGMVRELIDHKADLA 513
Cdd:cd13701    4 LKIGISAEPYPPFTSKD----ASGKWSGWEIDLIDALCARLDARCEITPV-------------AWDGIIPALQSGKIDMI 66
                         90       100
                 ....*....|....*....|
gi 755532823 514 VAPLAITYVREKVIDFSKPF 533
Cdd:cd13701   67 WNSMSITDERKKVIDFSDPY 86
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
54-188 2.02e-04

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


Pssm-ID: 380597 [Multi-domain]  Cd Length: 474  Bit Score: 45.03  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  54 ELAFRfAVNTINRNRTLLPNTTLTYDT------------QKIN-LYDSF------EASKKACDQLSLGV-------AAIF 107
Cdd:cd06374   45 EAMFR-TLDKINKDPNLLPNITLGIEIrdscwyspvaleQSIEfIRDSVasvedeKDTQNTPDPTPLSPpenrkpiVGVI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 108 GPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNKDSFYVSL--YPDFSSLSRAILDLVQFFKWKTVTVVYDD----STG 181
Cdd:cd06374  124 GPGSSSVTIQVQNLLQLFHIPQIGYSATSIDLSDKSLYKYFLrvVPSDYLQARAMLDIVKRYNWTYVSTVHTEgnygESG 203

                 ....*..
gi 755532823 182 LIRLQEL 188
Cdd:cd06374  204 IEAFKEL 210
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
446-546 2.25e-04

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 43.96  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 446 FKKSDKplygndrFEGYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREK 525
Cdd:PRK09495  40 FKQGDK-------YVGFDIDLWAAIAKELKLDYTLKPMD-------------FSGIIPALQTKNVDLALAGITITDERKK 99
                         90       100
                 ....*....|....*....|.
gi 755532823 526 VIDFSKPFMTLGISILYRKPN 546
Cdd:PRK09495 100 AIDFSDGYYKSGLLVMVKANN 120
PBP2_OccT_like cd13699
Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding ...
461-538 2.88e-04

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: 43.13  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 461 GYCIDLLRELSTILGFtyEIRLVedgkygAQDdvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPF------- 533
Cdd:cd13699   26 GFEIDLANVLCERMKV--KCTFV------VQD-----WDGMIPALNAGKFDVIMDAMSITAERKKVIDFSTPYaatpnsf 92

                 ....*..
gi 755532823 534 --MTLGI 538
Cdd:cd13699   93 avVTIGV 99
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
455-550 2.92e-04

Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic binding protein fold; This subfamily represents the periplasmic-binding protein component of ABC transporter specific for carboxylic amino acids, including GtlI from Escherichia coli. The aspartate-glutamate binding domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270406 [Multi-domain]  Cd Length: 238  Bit Score: 43.40  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 455 GNDRFEGYCIDLLREL-----STILGFTYEIRLVEdgkygaqddVNGQwnGMVRELIDHKADLAVAPLAITYVREKVIDF 529
Cdd:cd13688   26 DNGKPVGYSVDLCNAIadalkKKLALPDLKVRYVP---------VTPQ--DRIPALTSGTIDLECGATTNTLERRKLVDF 94
                         90       100
                 ....*....|....*....|.
gi 755532823 530 SKPFMTLGISILYRKPNGTNP 550
Cdd:cd13688   95 SIPIFVAGTRLLVRKDSGLNS 115
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
55-191 3.03e-04

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


Pssm-ID: 380586 [Multi-domain]  Cd Length: 418  Bit Score: 44.22  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  55 LAFRFAVNTINRNRTLLPNTTLTYD-----TQKINLYDSFEA-SKKACDQLSL---------GVAAIFGPsHSSsaNAVQ 119
Cdd:cd06363   46 QAMRFAVEEINNSSDLLPGVTLGYEifdtcSDAVNFRPTLSFlSQNGSHDIEVqcnytnyqpRVVAVIGP-DSS--ELAL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 120 SICNALG---VPhiqtrwkhQVSDNKDSFYVS---LYPDF-------SSLSRAILDLVQFFKWKTVTVVYDDST----GL 182
Cdd:cd06363  123 TTAKLLGfflMP--------QISYGASSEELSnklLYPSFlrtvpsdKYQVEAMVQLLQEFGWNWVAFLGSDDEygqdGL 194

                 ....*....
gi 755532823 183 IRLQELIKA 191
Cdd:cd06363  195 QLFSEKAAN 203
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
455-546 3.55e-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: 43.90  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 455 GNDRFEGYCIDLLRELSTILGFTYEIRLVEDgkygaqddvngqWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFM 534
Cdd:COG4623   38 YRGGPMGFEYELAKAFADYLGVKLEIIVPDN------------LDELLPALNAGEGDIAAAGLTITPERKKQVRFSPPYY 105
                         90
                 ....*....|..
gi 755532823 535 TLGISILYRKPN 546
Cdd:COG4623  106 SVSQVLVYRKGS 117
PBP1_ABC_ligand_binding-like cd06345
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
102-246 1.11e-03

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


Pssm-ID: 380568 [Multi-domain]  Cd Length: 356  Bit Score: 42.25  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 102 GVAAIFGPSHSSSANAVQSICNALGVPHIQTR------WKHQVSDNKDSFYV-SLYPDFSSLSRAILD-----LVQFFKW 169
Cdd:cd06345   64 KVDAIVGGFRSEVVLAAMEVAAEYKVPFIVTGaaspaiTKKVKKDYEKYKYVfRVGPNNSYLGATVAEflkdlLVEKLGF 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 170 KTVTVVYDDS---TGLI-RLQELIKApSRYNLRLKIRqLPADTKDAKPLLKEMKRGKEfHVIFDC-SHEMAAGILKQALA 244
Cdd:cd06345  144 KKVAILAEDAawgRGIAeALKKLLPE-AGLEVVGVER-FPTGTTDFTPILSKIKASGA-DVIVTIfSGPGGILLVKQWAE 220

                 ..
gi 755532823 245 MG 246
Cdd:cd06345  221 LG 222
Peripla_BP_6 pfam13458
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ...
36-382 1.51e-03

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


Pssm-ID: 433225 [Multi-domain]  Cd Length: 342  Bit Score: 41.88  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823   36 LRFGGIfeYVESGPMGA----EELAFRFAVNTINRNRTLL--PNTTLTYDTQkinlYD---SFEASKKACDQLslGVAAI 106
Cdd:pfam13458   2 IKIGVL--TPLSGPYASsgksSRAGARAAIEEINAAGGVNgrKIELVVADDQ----GDpdvAAAAARRLVDQD--GVDAI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  107 FGPSHSSSANAVQSICNALGVPHIQTRwkhQVSDNKDSFYV-SLYPDFSSLSRAILD-LVQFFKWKTVTVVYDDS-TGli 183
Cdd:pfam13458  74 VGGVSSAVALAVAEVLAKKGVPVIGPA---ALTGEKCSPYVfSLGPTYSAQATALGRyLAKELGGKKVALIGADYaFG-- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  184 rlQELIKAPSRY--NLRLKI---RQLPADTKDAKPLLKEMKRGK-EfhVIFDCSH-EMAAGILKQALAMGMMTEYYH-YI 255
Cdd:pfam13458 149 --RALAAAAKAAakAAGGEVvgeVRYPLGTTDFSSQVLQIKASGaD--AVLLANAgADTVNLLKQAREAGLDAKGIKlVG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  256 FTTLDLFALDVEPYRYSGVNMTGFRILNTENTQVSSIIEKWsmeRLQAPPKPDsglldgfmTTDAALMYDAVHVVSVAVQ 335
Cdd:pfam13458 225 LGGDEPDLKALGGDAAEGVYATVPFFPDLDNPATRAFVAAF---AAKYGEAPP--------TQFAAGGYIAADLLLAALE 293
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 755532823  336 QFPQMTVSSlqcnrhkpwrfgtrFMSLIKEAHWEGLTGRITFNKTNG 382
Cdd:pfam13458 294 AAGSPTREA--------------VIAALRALPYDGPFGPVGFRAEDH 326
PBP1_ABC_ligand_binding-like cd06335
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
47-336 2.12e-03

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


Pssm-ID: 380558 [Multi-domain]  Cd Length: 348  Bit Score: 41.44  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  47 SGPMG-AEELAFRFAVNTINRN-----RTLlpnTTLTYDTQKINlydsfEASKKACDQL--SLGVAAIFGPSHSSSANAV 118
Cdd:cd06335   12 SAELGeSARRGVELAVEEINAAggilgRKI---ELVERDDEANP-----TKAVQNAQELidKEKVVAIIGPTNSGVALAT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 119 QSICNALGVPHIQ--------TRWKHQvsDNKDSFYVSLYPDFSslSRAILDLVQFFKWKTVTVVYDDS----TGLIRLQ 186
Cdd:cd06335   84 IPILQEAKIPLIIpvatgtaiTKPPAK--PRNYIFRVAASDTLQ--ADFLVDYAVKKGFKKIAILHDTTgygqGGLKDVE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 187 ELIKApsrYNLRL-KIRQLPADTKDAKPLLKEMKR-GKEFhVIFDCSHEMAAGILKQALAMGMMTEYYHYifttldlFAL 264
Cdd:cd06335  160 AALKK---RGITPvATESFKIGDTDMTPQLLKAKDaGADV-ILVYGLGPDLAQILKAMEKLGWKVPLVGS-------WGL 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755532823 265 DVEPYR------YSGVNMTGFRILNTENTQVSSIIEKWsMERLQAPPKPdsglldgfMTTDAALMYDAVHVVSVAVQQ 336
Cdd:cd06335  229 SMPNFIelagplAEGTIMTQTFIEDYLTPRAKKFIDAY-KKKYGTDRIP--------SPVSAAQGYDAVYLLAAAIKQ 297
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
448-544 3.36e-03

Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 periplasmic-binding protein fold; This family comprises of the periplasmic-binding protein component of ABC transporters specific for cysteine and carboxylic amino acids, as well as their closely related proteins. The cysteine and aspartate-glutamate binding domains belong to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 39.98  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 448 KSDKPLYG----NDRFEGYCIDLLRELS-TILGFTYEIRLVEdgkygaqddVNGQwnGMVRELIDHKADLAVAPLAITYV 522
Cdd:cd01000   15 KPDLPPFGardaNGKIQGFDVDVAKALAkDLLGDPVKVKFVP---------VTSA--NRIPALQSGKVDLIIATMTITPE 83
                         90       100
                 ....*....|....*....|..
gi 755532823 523 REKVIDFSKPFMTLGISILYRK 544
Cdd:cd01000   84 RAKEVDFSVPYYADGQGLLVRK 105
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
451-558 3.54e-03

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: 40.02  E-value: 3.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 451 KPLYGNDR---FEGYCIDLLRELSTILGFTYEIrlvedgkygaqddVNGQWNGMVRELIDHKADLAVAPLAITYVREKVI 527
Cdd:cd01069   21 KPFTYRDNqgqYEGYDIDMAEALAKSLGVKVEF-------------VPTSWPTLMDDLAADKFDIAMGGISITLERQRQA 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 755532823 528 DFSKPFMTLGISILYRKPNGT---------NPGVFSFLNP 558
Cdd:cd01069   88 FFSAPYLRFGKTPLVRCADVDrfqtleainRPGVRVIVNP 127
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
456-535 3.90e-03

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: 39.90  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 456 NDRFEGYCIDLLRELSTILGFTYEIRLVEDgkygaqddvngqWNGMVRELIDHKADLAvAPLAITYVREKVIDFSKPFMT 535
Cdd:cd13707   21 NGQFRGISADLLELISLRTGLRFEVVRASS------------PAEMIEALRSGEADMI-AALTPSPEREDFLLFTRPYLT 87
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
36-175 4.06e-03

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


Pssm-ID: 380598 [Multi-domain]  Cd Length: 462  Bit Score: 40.58  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  36 LRFGGIFEYVESGpMGAEEL-------------AFRFAVNTINRNRTLLPNTTL--------TYDTQKINLYDSF----- 89
Cdd:cd06375    7 LVLGGLFPVHEKG-EGMEECgrinedrgiqrleAMLFAIDRINRDPHLLPGVRLgvhildtcSRDTYALEQSLEFvrasl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  90 ----EASKKACDQLS--------LGVAAIFGPSHSSSANAVQSICNALGVPHIQTRWKHQVSDNK---DSFYVSLYPDFS 154
Cdd:cd06375   86 tkvdDSEYMCPDDGSyaiqedspLPIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKsryDYFARTVPPDFY 165
                        170       180
                 ....*....|....*....|.
gi 755532823 155 SlSRAILDLVQFFKWKTVTVV 175
Cdd:cd06375  166 Q-AKAMAEILRFFNWTYVSTV 185
PBP1_ABC_HAAT-like cd19986
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
103-247 4.98e-03

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


Pssm-ID: 380641 [Multi-domain]  Cd Length: 297  Bit Score: 39.92  E-value: 4.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 103 VAAIFGPSHSSSANAVQSICNALGVPHI--QTRWKhqVSDNKDSFYVSLYPDFSSLSRAILD-LVQFFKWKTVTVVYD-D 178
Cdd:cd19986   68 VVAVIGPHYSTQVLAVSPLVKEAKIPVItgGTSPK--LTEQGNPYMFRIRPSDSVSAKALAKyAVEELGAKKIAILYDnD 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755532823 179 STGLIRLQELIKAPSRYNLR-LKIRQLPADTKDAKPLLKEMKRgKEFHVIFDCSHEMAAG-ILKQALAMGM 247
Cdd:cd19986  146 DFGTGGADVVTAALKALGLEpVAVESYNTGDKDFTAQLLKLKN-SGADVIIAWGHDAEAAlIARQIRQLGL 215
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
686-833 7.94e-03

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: 38.81  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823  686 YTANLAAFLTVERMESPIDSADDLAKQTkIeygAVEDGatmtffkkskiSTYDKMWAFMSSRR-QSVLVKSNEEGIQRVL 764
Cdd:pfam00497  83 YYSGQVILVRKKDSSKSIKSLADLKGKT-V---GVQKG-----------STAEELLKNLKLPGaEIVEYDDDAEALQALA 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755532823  765 T--SDyAFLMESTTIEFVTQRN--CNLTQIGGLIDSKGYGVGTPMGSP-YRDKITIAILQLQEEGKLHMMKEKW 833
Cdd:pfam00497 148 NgrVD-AVVADSPVAAYLIKKNpgLNLVVVGEPLSPEPYGIAVRKGDPeLLAAVNKALAELKADGTLAKIYEKW 220
PBP2_HisK_like_1 cd13706
Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This ...
461-544 9.13e-03

Putative sensor domain similar to HisK; the type 2 periplasmic binding fold protein; This group includes 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: 270424 [Multi-domain]  Cd Length: 219  Bit Score: 38.70  E-value: 9.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755532823 461 GYCIDLLRELSTILGFTYEIRLVEdgkygaqddvngqWNGMVRELIDHKADlAVAPLAITYVREKVIDFSKPFMTLGISI 540
Cdd:cd13706   26 GILVDLWRLWSEKTGIPVEFVLLD-------------WNESLEAVRQGEAD-VHDGLFKSPEREKYLDFSQPIATIDTYL 91

                 ....
gi 755532823 541 LYRK 544
Cdd:cd13706   92 YFHK 95
 
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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