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Conserved domains on  [gi|11038637|ref|NP_015566|]
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glutamate receptor ionotropic, NMDA 1 isoform GluN1-1a precursor [Homo sapiens]

Protein Classification

glutamate receptor ionotropic, NMDA 1( domain architecture ID 10157243)

glutamate receptor ionotropic, NMDA 1 is a component of NMDA (N-methyl-D-aspartate) receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
25-383 0e+00

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


:

Pssm-ID: 380602  Cd Length: 364  Bit Score: 590.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  25 KIVNIGAVLSTRKHEQMFREAVNQANK-RHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDhFT 103
Cdd:cd06379   1 KIFNIGAVLSSPKHEEIFREAVNEVNAhSHLPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVIVSHPPTPSD-LS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 104 PTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETL 183
Cdd:cd06379  80 PTSVSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 184 LEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREisgNALRYAP 263
Cdd:cd06379 160 AETKDIKIEKVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIVTEQA---LAASNVP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 264 DGILGLQLINGKNESAHISDAVGVVAQAVHELL-EKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNE 342
Cdd:cd06379 237 DGVLGLQLIHGKNESAHIRDSVSVVAQAIRELFrSSENITDPPVDCRDDTNIWKSGQKFFRVLKSVKLSDGRTGRVEFND 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 11038637 343 DGDRKFANYSIMNLQN-RKLVQVGIYNG------THVIPNDRKIIWPG 383
Cdd:cd06379 317 KGDRIGAEYDIINVQNpRKLVQVGIYVGsqrptkSLLSLNDRKIIWPG 364
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
395-799 0e+00

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: 526.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 395 STRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGdpvkkvictgPNDTSPGspRHTVPQCCYGFCIDLLIKLARTMNFTY 474
Cdd:cd13719   1 STHLKIVTIHEEPFVYVRPTPSDGTCREEFTVNC----------PNFNISG--RPTVPFCCYGYCIDLLIKLARKMNFTY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 475 EVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIprstldsf 554
Cdd:cd13719  69 ELHLVADGQFGTQERVNNSNKKEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEI-------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 555 mqpfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsarilgm 634
Cdd:cd13719     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 635 vwagfamiivasytanlaaflvldrpeeRITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESA 714
Cdd:cd13719 141 ----------------------------RLTGINDPRLRNPSEKFIYATVKGSSVDMYFRRQVELSTMYRHMEKHNYETA 192
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 715 AEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVR 794
Cdd:cd13719 193 EEAIQAVRDGKLHAFIWDSSRLEFEASQDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWIR 272

                ....*
gi 11038637 795 YQECD 799
Cdd:cd13719 273 YQECE 277
CaM_bdg_C0 pfam10562
Calmodulin-binding domain C0 of NMDA receptor NR1 subunit; This is a very short highly ...
835-863 2.37e-09

Calmodulin-binding domain C0 of NMDA receptor NR1 subunit; This is a very short highly conserved domain that is C-terminal to the cytosolic transmembrane region IV of the NMDA-receptor 1. It has been shown to bind Calmodulin-Calcium with high affinity. The ionotropic N-methyl-D-aspartate receptor (NMDAR) is a major source of calcium flux into neurons in the brain and plays a critical role in learning, memory, neural development, and synaptic plasticity. Calmodulin (CaM) regulates NMDARs by binding tightly to the C0 and C1 regions of their NR1 subunit. The conserved tryptophan is considered to be the anchor residue.


:

Pssm-ID: 402271  Cd Length: 29  Bit Score: 53.29  E-value: 2.37e-09
                          10        20
                  ....*....|....*....|....*....
gi 11038637   835 IAYKRHKDARRKQMQLAFAAVNVWRKNLQ 863
Cdd:pfam10562   1 IAYKKHQGRKQKQLELARHAADKWRGNIE 29
 
Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
25-383 0e+00

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


Pssm-ID: 380602  Cd Length: 364  Bit Score: 590.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  25 KIVNIGAVLSTRKHEQMFREAVNQANK-RHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDhFT 103
Cdd:cd06379   1 KIFNIGAVLSSPKHEEIFREAVNEVNAhSHLPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVIVSHPPTPSD-LS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 104 PTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETL 183
Cdd:cd06379  80 PTSVSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 184 LEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREisgNALRYAP 263
Cdd:cd06379 160 AETKDIKIEKVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIVTEQA---LAASNVP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 264 DGILGLQLINGKNESAHISDAVGVVAQAVHELL-EKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNE 342
Cdd:cd06379 237 DGVLGLQLIHGKNESAHIRDSVSVVAQAIRELFrSSENITDPPVDCRDDTNIWKSGQKFFRVLKSVKLSDGRTGRVEFND 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 11038637 343 DGDRKFANYSIMNLQN-RKLVQVGIYNG------THVIPNDRKIIWPG 383
Cdd:cd06379 317 KGDRIGAEYDIINVQNpRKLVQVGIYVGsqrptkSLLSLNDRKIIWPG 364
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
395-799 0e+00

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: 526.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 395 STRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGdpvkkvictgPNDTSPGspRHTVPQCCYGFCIDLLIKLARTMNFTY 474
Cdd:cd13719   1 STHLKIVTIHEEPFVYVRPTPSDGTCREEFTVNC----------PNFNISG--RPTVPFCCYGYCIDLLIKLARKMNFTY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 475 EVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIprstldsf 554
Cdd:cd13719  69 ELHLVADGQFGTQERVNNSNKKEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEI-------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 555 mqpfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsarilgm 634
Cdd:cd13719     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 635 vwagfamiivasytanlaaflvldrpeeRITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESA 714
Cdd:cd13719 141 ----------------------------RLTGINDPRLRNPSEKFIYATVKGSSVDMYFRRQVELSTMYRHMEKHNYETA 192
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 715 AEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVR 794
Cdd:cd13719 193 EEAIQAVRDGKLHAFIWDSSRLEFEASQDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWIR 272

                ....*
gi 11038637 795 YQECD 799
Cdd:cd13719 273 YQECE 277
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
560-823 2.14e-79

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: 258.78  E-value: 2.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   560 STLWLLVGLSVHVVAVMLYLLDRFSPFGRFkvNSEEEEEDALTLSSAMWFSWGVLLNSGiGEGAPRSFSARILGMVWAGF 639
Cdd:pfam00060   2 LEVWLGILVAFLIVGVVLFLLERFSPYEWR--GPLETEENRFTLSNSLWFSFGALVQQG-HRENPRSLSGRIVVGVWWFF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   640 AMIIVASYTANLAAFLVLDRPEERITGINDprLRNpSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQ 719
Cdd:pfam00060  79 ALILLSSYTANLAAFLTVERMQSPIQSLED--LAK-QTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   720 AVRDNKLHAFIWDSAVLEFEAS-----QKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVR 794
Cdd:pfam00060 156 NEEGVALVRNGIYAYALLSENYylfqrECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWP 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 11038637   795 YQ-ECDSRSNAPAT--LTFENMAGVFMLVAGG 823
Cdd:pfam00060 236 KSgECDSKSSASSSsqLGLKSFAGLFLILGIG 267
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
663-795 3.11e-44

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: 156.30  E-value: 3.11e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637    663 RITGINDPRLRnpsDKFIYATVKQSSVDIYFRRQVEL--STMYRHM--EKHNYESAAEAIQAVRDNKlHAFIWDSAVLEF 738
Cdd:smart00079   1 PITSVEDLAKQ---TKIEYGTQDGSSTLAFFKRSGNPeySRMWPYMksPEVFVKSYAEGVQRVRVSN-YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11038637    739 EASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRY 795
Cdd:smart00079  77 ELSRNCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
42-357 2.59e-38

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: 146.38  E-value: 2.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637    42 FREAVNQANKRHG-SWKIQLNATsVTHKPNAIQMALSVCEDLISSQVYAILvshppTPNDHFTPTPVSYTAGFYRIPVLG 120
Cdd:pfam01094   6 VRLAVEDINADPGlLPGTKLEYI-ILDTCCDPSLALAAALDLLKGEVVAII-----GPSCSSVASAVASLANEWKVPLIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   121 LTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPG 200
Cdd:pfam01094  80 YGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPPA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   201 T--KNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGER-----EISGNALRYAPDGILGLQLIN 273
Cdd:pfam01094 160 QddDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGlttslVILNPSTLEAAGGVLGFRLHP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   274 GKNES---------------------------AHISDAVGVVAQAVHELLEKenitDPPRGCVGNTNIWKTGPLFKRVLM 326
Cdd:pfam01094 240 PDSPEfseffweklsdekelyenlgglpvsygALAYDAVYLLAHALHNLLRD----DKPGRACGALGPWNGGQKLLRYLK 315
                         330       340       350
                  ....*....|....*....|....*....|.
gi 11038637   327 SSKYaDGVTGRVEFNEDGDRKFANYSIMNLQ 357
Cdd:pfam01094 316 NVNF-TGLTGNVQFDENGDRINPDYDILNLN 345
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
457-792 1.43e-11

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: 65.00  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVadgkfgtqervnnsnkkEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:COG0834  23 GFDVDLARAIAKRLGLKVEFVPV-----------------PWDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPYYTS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEIPR-STLDSfmqpfqstlwlLVGLSVhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvll 615
Cdd:COG0834  86 GQVLLVRKDNSGiKSLAD-----------LKGKTV--------------------------------------------- 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 616 nsgigegaprsfsarilgmvwagfamiivasytanlaaflvldrpeeritgindprlrnpsdkfiyATVKQSSVDIYFRR 695
Cdd:COG0834 110 ------------------------------------------------------------------GVQAGTTYEEYLKK 123
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 696 qvelstMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQK--CDLVTTGELFFRSGFGIGMRKDSP-WKQNV 772
Cdd:COG0834 124 ------LGPNAEIVEFDSYAEALQALASGRVDAVVTDEPVAAYLLAKNpgDDLKIVGEPLSGEPYGIAVRKGDPeLLEAV 197
                       330       340
                ....*....|....*....|
gi 11038637 773 SLSILKSHENGFMEDLDKTW 792
Cdd:COG0834 198 NKALAALKADGTLDKILEKW 217
CaM_bdg_C0 pfam10562
Calmodulin-binding domain C0 of NMDA receptor NR1 subunit; This is a very short highly ...
835-863 2.37e-09

Calmodulin-binding domain C0 of NMDA receptor NR1 subunit; This is a very short highly conserved domain that is C-terminal to the cytosolic transmembrane region IV of the NMDA-receptor 1. It has been shown to bind Calmodulin-Calcium with high affinity. The ionotropic N-methyl-D-aspartate receptor (NMDAR) is a major source of calcium flux into neurons in the brain and plays a critical role in learning, memory, neural development, and synaptic plasticity. Calmodulin (CaM) regulates NMDARs by binding tightly to the C0 and C1 regions of their NR1 subunit. The conserved tryptophan is considered to be the anchor residue.


Pssm-ID: 402271  Cd Length: 29  Bit Score: 53.29  E-value: 2.37e-09
                          10        20
                  ....*....|....*....|....*....
gi 11038637   835 IAYKRHKDARRKQMQLAFAAVNVWRKNLQ 863
Cdd:pfam10562   1 IAYKKHQGRKQKQLELARHAADKWRGNIE 29
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
114-345 1.10e-08

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: 57.63  E-value: 1.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 114 YRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFE-MMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAE 192
Cdd:COG0683  94 AGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDDYAYGQGLAAAFKAALKAAGGEVV 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 193 KVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGE-REISGNalryAPDGIlglql 271
Cdd:COG0683 174 GEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGLKGPLNKAFVKAyKAKYGR----EPSSY----- 244
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11038637 272 ingkneSAHISDAVGVVAQAVhellEKENITDPPRgcvgntniwktgplFKRVLMSSKYaDGVTGRVEFNEDGD 345
Cdd:COG0683 245 ------AAAGYDAALLLAEAI----EKAGSTDREA--------------VRDALEGLKF-DGVTGPITFDPDGQ 293
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
498-545 3.13e-05

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 46.64  E-value: 3.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 11038637  498 WNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKE 545
Cdd:PRK11260  89 WDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTVSGIQALVKKG 136
 
Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
25-383 0e+00

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


Pssm-ID: 380602  Cd Length: 364  Bit Score: 590.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  25 KIVNIGAVLSTRKHEQMFREAVNQANK-RHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDhFT 103
Cdd:cd06379   1 KIFNIGAVLSSPKHEEIFREAVNEVNAhSHLPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVIVSHPPTPSD-LS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 104 PTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETL 183
Cdd:cd06379  80 PTSVSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 184 LEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREisgNALRYAP 263
Cdd:cd06379 160 AETKDIKIEKVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIVTEQA---LAASNVP 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 264 DGILGLQLINGKNESAHISDAVGVVAQAVHELL-EKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNE 342
Cdd:cd06379 237 DGVLGLQLIHGKNESAHIRDSVSVVAQAIRELFrSSENITDPPVDCRDDTNIWKSGQKFFRVLKSVKLSDGRTGRVEFND 316
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 11038637 343 DGDRKFANYSIMNLQN-RKLVQVGIYNG------THVIPNDRKIIWPG 383
Cdd:cd06379 317 KGDRIGAEYDIINVQNpRKLVQVGIYVGsqrptkSLLSLNDRKIIWPG 364
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
395-799 0e+00

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: 526.16  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 395 STRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGdpvkkvictgPNDTSPGspRHTVPQCCYGFCIDLLIKLARTMNFTY 474
Cdd:cd13719   1 STHLKIVTIHEEPFVYVRPTPSDGTCREEFTVNC----------PNFNISG--RPTVPFCCYGYCIDLLIKLARKMNFTY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 475 EVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIprstldsf 554
Cdd:cd13719  69 ELHLVADGQFGTQERVNNSNKKEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEI-------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 555 mqpfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsarilgm 634
Cdd:cd13719     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 635 vwagfamiivasytanlaaflvldrpeeRITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESA 714
Cdd:cd13719 141 ----------------------------RLTGINDPRLRNPSEKFIYATVKGSSVDMYFRRQVELSTMYRHMEKHNYETA 192
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 715 AEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVR 794
Cdd:cd13719 193 EEAIQAVRDGKLHAFIWDSSRLEFEASQDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWIR 272

                ....*
gi 11038637 795 YQECD 799
Cdd:cd13719 273 YQECE 277
PBP1_iGluR_NMDA cd06367
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic ...
25-376 2.62e-154

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


Pssm-ID: 380590 [Multi-domain]  Cd Length: 357  Bit Score: 458.63  E-value: 2.62e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  25 KIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTH-KPNAIQMALSVCEDLISSQVYAILVSHPPTPNDhfT 103
Cdd:cd06367   1 PSVNIGAILGTKKEVAIKDEAEKDDFHHHFTLPVQLRVELVTMpEPDPKSIITRICDLLSDSKVQGVVFSDDTDQEA--I 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 104 PTPVSYTAGFYRIPVLGLTTRMSIY-SDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLET 182
Cdd:cd06367  79 AQILDFIAAQTLTPVLGLHGRSSMImADKSEHSMFLQFGPPIEQQASVMLNIMEEYDWYIVSLVTTYFPGYQDFVNKLRS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 183 LLEERESKAEKVLQFDPGT----KNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREI-SGN 257
Cdd:cd06367 159 TIENSGWELEEVLQLDMSLddgdSKLQAQLKKLQSPEARVILLYCTKEEATYVFEVAASVGLTGYGYTWLVGSLVAgTDT 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 258 ALRYAPDGILGLQLINGKNESAHISDAVGVVAQAVHELL-EKENITDPPRGCVGNTNIWK-TGPLFKRVLMSSKYadgVT 335
Cdd:cd06367 239 VPAEFPTGLISLSYDEWYNLPARIRDGVAIVATAASEMLsEHEQIPDPPSSCVNNQEIRKyTGPMLKRYLINVTF---EG 315
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 11038637 336 GRVEFNEDGDRKFANYSIMNLQN-RKLVQVGIYNGTHVIPND 376
Cdd:cd06367 316 RDLSFSEDGYQMHPKLVIILLNNeRKWERVGKWKDSSLIMND 357
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
395-793 8.63e-118

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: 359.26  E-value: 8.63e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 395 STRLKIVTIHQEPFVYVkptlsdgtckeeftvngdpvkkvictgpndtspgsprhtvpQCCYGFCIDLLIKLARTMNFTY 474
Cdd:cd13687   1 STHLKVVTLEEAPFVYV-----------------------------------------KCCYGFCIDLLKKLAEDVNFTY 39
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 475 EVHLVADGKFGTqerVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEiprstldsf 554
Cdd:cd13687  40 DLYLVTDGKFGT---VNKSINGEWNGMIGELVSGRADMAVASLTINPERSEVIDFSKPFKYTGITILVKKR--------- 107
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 555 mqpfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsarilgm 634
Cdd:cd13687     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 635 vwagfamiivasytanlaaflvldrpeERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELstMYRHMEKHNYESA 714
Cdd:cd13687 108 ---------------------------NELSGINDPRLRNPSPPFRFGTVPNSSTERYFRRQVEL--MHRYMEKYNYETV 158
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 715 AEAIQAVRDNKLHAFIWDSAVLEFEASQK--CDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTW 792
Cdd:cd13687 159 EEAIQALKNGKLDAFIWDSAVLEYEASQDegCKLVTVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHESGFMEELDKKW 238

                .
gi 11038637 793 V 793
Cdd:cd13687 239 L 239
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
560-823 2.14e-79

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: 258.78  E-value: 2.14e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   560 STLWLLVGLSVHVVAVMLYLLDRFSPFGRFkvNSEEEEEDALTLSSAMWFSWGVLLNSGiGEGAPRSFSARILGMVWAGF 639
Cdd:pfam00060   2 LEVWLGILVAFLIVGVVLFLLERFSPYEWR--GPLETEENRFTLSNSLWFSFGALVQQG-HRENPRSLSGRIVVGVWWFF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   640 AMIIVASYTANLAAFLVLDRPEERITGINDprLRNpSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQ 719
Cdd:pfam00060  79 ALILLSSYTANLAAFLTVERMQSPIQSLED--LAK-QTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   720 AVRDNKLHAFIWDSAVLEFEAS-----QKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVR 794
Cdd:pfam00060 156 NEEGVALVRNGIYAYALLSENYylfqrECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWP 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 11038637   795 YQ-ECDSRSNAPAT--LTFENMAGVFMLVAGG 823
Cdd:pfam00060 236 KSgECDSKSSASSSsqLGLKSFAGLFLILGIG 267
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
28-369 1.67e-76

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: 253.49  E-value: 1.67e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  28 NIGAVL-------STRKHEQMFREAVNQANKRH-GSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPN 99
Cdd:cd06269   1 TIGALLpvhdyleSGAKVLPAFELALSDVNSRPdLLPKTTLGLAIRDSECNPTQALLSACDLLAAAKVVAILGPGCSASA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 100 DhftptPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKR 179
Cdd:cd06269  81 A-----PVANLARHWDIPVLSYGATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 180 LETLLEERESKAEKVLQFDPG-TKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREIS--- 255
Cdd:cd06269 156 LEELFQEKGGLITSRQSFDENkDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFVIDGEASssd 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 256 --GNALRYAPDGILGLQLINGKNES-AHISdavgvvaQAVHELLEKENITDPPRGCVGNTNIWktgplfkrvlmsskYAD 332
Cdd:cd06269 236 ehGDEARQAAEGAITVTLIFPVVKEfLKFS-------MELKLKSSKRKQGLNEEYELNNFAAF--------------FYD 294
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 11038637 333 GVTgrvefnedGDRKFaNYSIMNLQN---RKLVQVGIYNG 369
Cdd:cd06269 295 AVL--------ADRPG-QFSIINLQYteaGDYRKVGTWDS 325
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
457-794 6.24e-58

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: 203.38  E-value: 6.24e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQErvnnsNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13723  32 GYCIDLLKELAHILGFSYEIRLVEDGKYGAQD-----DKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKeiPRST---LDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVN----SEEEEEDALTLSSAMWF 609
Cdd:cd13723 107 GVSILYRK--PNGTnpsVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHpcnpGSEVVENNFTLLNSFWF 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 610 SWGVLLNSGiGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNpsdKFIYATVKQSSV 689
Cdd:cd13723 185 GMGSLMQQG-SELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQT---KIEYGAVKDGAT 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 690 DIYFRRQvELST---MYRHME-------KHNYESAAEAIQAVrdnklHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFG 759
Cdd:cd13723 261 MTFFKKS-KISTfekMWAFMSskpsalvKNNEEGIQRALTAD-----YALLMESTTIEYVTQRNCNLTQIGGLIDSKGYG 334
                       330       340       350
                ....*....|....*....|....*....|....*
gi 11038637 760 IGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVR 794
Cdd:cd13723 335 IGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWR 369
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
396-792 2.80e-53

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: 190.20  E-value: 2.80e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 396 TRLKIVTIHQEPFVYVKPTLSDGTckeeftvngdpvkkvictgpndtspgsprhtvpqccYGFCIDLLIKLARTMNFTYE 475
Cdd:cd13717   2 RVYRIGTVESPPFVYRDRDGSPIW------------------------------------EGYCIDLIEEISEILNFDYE 45
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 476 VHLVADGKFGTqeRVNNSNkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKP-FKYQGLTILVKKEIPRSTLDSF 554
Cdd:cd13717  46 IVEPEDGKFGT--MDENGE---WNGLIGDLVRKEADIALAALSVMAEREEVVDFTVPyYDLVGITILMKKPERPTSLFKF 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 555 MQPFQSTLWllvglsvhvvavmlylldRFspfgrfkvnseeeeedaLTLSSAMWFSWGVLLNSGIGEgAPRSFSARILGM 634
Cdd:cd13717 121 LTVLELEVW------------------RE-----------------FTLKESLWFCLTSLTPQGGGE-APKNLSGRLLVA 164
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 635 VWAGFAMIIVASYTANLAAFLVLDRPEERITGINDprLRNPSdKFIYATVKQSSVDIYFRR----------------QVE 698
Cdd:cd13717 165 TWWLFVFIIIASYTANLAAFLTVSRLQTPVESLDD--LARQY-KIQYTVVKNSSTHTYFERmknaedtlyemwkdmsLND 241
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 699 LST--------------------MYRHMEKHNY-ESAAEAIQAVRD--NKLHAFIWDSAVLEFEASQKCDLVTTGELFFR 755
Cdd:cd13717 242 SLSpveraklavwdypvsekytkIYQAMQEAGLvANAEEGVKRVREstSAGFAFIGDATDIKYEILTNCDLQEVGEEFSR 321
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 11038637 756 SGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTW 792
Cdd:cd13717 322 KPYAIAVQQGSPLKDELNYAILELQNDRFLEKLKAKW 358
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
398-792 4.72e-51

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: 181.00  E-value: 4.72e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 398 LKIVTIHQEPFVYVKPTLSD-GTCKEeftvNGDPVKKVIcTGPNDTSPGSPRhTVPQCCYGFCIDLLIKLARTMNFTYEV 476
Cdd:cd13718   4 LKIVTLEEAPFVIVEPVDPLtGTCMR----NTVPCRKQL-NHENSTDADENR-YVKKCCKGFCIDILKKLAKDVGFTYDL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 477 HLVADGKFGTqeRVNNsnkkEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKeipRSTLdsfmq 556
Cdd:cd13718  78 YLVTNGKHGK--KING----VWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMVAR---SNQV----- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 557 pfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsarilgmvw 636
Cdd:cd13718     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 637 agfamiivasytanlaaflvldrpeeriTGINDPRLRNPSDK---FIYATVKQSSVDIYFRRQveLSTMYRHMEKHNYES 713
Cdd:cd13718 144 ----------------------------SGLSDKKFQRPHDQsppFRFGTVPNGSTERNIRNN--YPEMHQYMRKYNQKG 193
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 714 AAEAIQAVRDNKLHAFIWDSAVLEFEASQ--KCDLVTTG--ELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLD 789
Cdd:cd13718 194 VEDALVSLKTGKLDAFIYDAAVLNYMAGQdeGCKLVTIGsgKWFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLE 273

                ...
gi 11038637 790 KTW 792
Cdd:cd13718 274 RLW 276
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
396-792 2.69e-49

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: 175.07  E-value: 2.69e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 396 TRLKIVTIHQEPFVYVKPTLSDGTckEEFtvngdpvkkvictgpndtspgsprhtvpqccYGFCIDLLIKLARTMNFTYE 475
Cdd:cd13685   2 KTLRVTTILEPPFVMKKRDSLSGN--PRF-------------------------------EGYCIDLLEELAKILGFDYE 48
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 476 VHLVADGKFGTQERVNNsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDsfm 555
Cdd:cd13685  49 IYLVPDGKYGSRDENGN-----WNGMIGELVRGEADIAVAPLTITAEREEVVDFTKPFMDTGISILMRKPTPIESLE--- 120
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 556 qpfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsarilgmv 635
Cdd:cd13685     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 636 wagfamiivasytaNLAaflvldrpeeritgindprlrnPSDKFIYATVKQSSVDIYFRRQVELStmYRHMEKHNYE--- 712
Cdd:cd13685 121 --------------DLA----------------------KQSKIEYGTLKGSSTFTFFKNSKNPE--YRRYEYTKIMsam 162
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 713 -------SAAEAIQAVRD-NKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGF 784
Cdd:cd13685 163 spsvlvaSAAEGVQRVREsNGGYAFIGEATSIDYEVLRNCDLTKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGE 242

                ....*...
gi 11038637 785 MEDLDKTW 792
Cdd:cd13685 243 LEKLKEKW 250
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
396-792 1.67e-48

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: 173.88  E-value: 1.67e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 396 TRLKIVTIHQEPFVYVKPTLSDG------TCKEEFTVNGDPVKKVIctGPNDTSPGSPRHTVPQCCYGFCIDLLIKLART 469
Cdd:cd13720   2 PHLRVVTLLEHPFVFTREVDEEGlcpagqLCLDPMTNDSSTLDALF--SSLHSSNDTVPIKFRKCCYGYCIDLLEKLAED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 470 MNFTYEVHLVADGKFGtqervNNSNKKeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVkkeiprs 549
Cdd:cd13720  80 LGFDFDLYIVGDGKYG-----AWRNGR-WTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSLGILV------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 550 tldsfmqpfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsa 629
Cdd:cd13720     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 630 rilgmvwagfamiivasytanlaaflvldRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQveLSTMYRHMEKH 709
Cdd:cd13720 147 -----------------------------RTRDELSGIHDPKLHHPSQGFRFGTVRESSAEYYVKKS--FPEMHEHMRRY 195
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 710 NYESAAEAIQAVRDN--KLHAFIWDSAVLEFEAS--QKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFM 785
Cdd:cd13720 196 SLPNTPEGVEYLKNDpeKLDAFIMDKALLDYEVSidADCKLLTVGKPFAIEGYGIGLPQNSPLTSNISELISQYKSNGFM 275

                ....*..
gi 11038637 786 EDLDKTW 792
Cdd:cd13720 276 DLLHDKW 282
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
663-795 3.11e-44

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: 156.30  E-value: 3.11e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637    663 RITGINDPRLRnpsDKFIYATVKQSSVDIYFRRQVEL--STMYRHM--EKHNYESAAEAIQAVRDNKlHAFIWDSAVLEF 738
Cdd:smart00079   1 PITSVEDLAKQ---TKIEYGTQDGSSTLAFFKRSGNPeySRMWPYMksPEVFVKSYAEGVQRVRVSN-YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11038637    739 EASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRY 795
Cdd:smart00079  77 ELSRNCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
397-792 4.01e-40

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: 148.68  E-value: 4.01e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 397 RLKIVTIHQEPFVYVKPtlsdgtckeeftvngdpvkkvictgpndtspGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEV 476
Cdd:cd00998   2 TLKVVVPLEPPFVMFVT-------------------------------GSNAVTGNGRFEGYCIDLLKELSQSLGFTYEY 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 477 HLVADGKFGtqERVNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVkkeiprstldsfmq 556
Cdd:cd00998  51 YLVPDGKFG--APVNGS----WNGMVGEVVRGEADLAVGPITITSERSVVIDFTQPFMTSGIGIMI-------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 557 pfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvllnsgigegaprsfsarilgmvw 636
Cdd:cd00998     --------------------------------------------------------------------------------
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 637 agfamiivasytanlaaflvldrpeeRITGINDprLRNPSDkFIYATVKQSSVDIYFRRQVELS--TMYRHMEKHN--YE 712
Cdd:cd00998 111 --------------------------PIRSIDD--LKRQTD-IEFGTVENSFTETFLRSSGIYPfyKTWMYSEARVvfVN 161
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 713 SAAEAIQAVRDNKLHAFIWDSAVLEFEASQK-CDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKT 791
Cdd:cd00998 162 NIAEGIERVRKGKVYAFIWDRPYLEYYARQDpCKLIKTGGGFGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNK 241

                .
gi 11038637 792 W 792
Cdd:cd00998 242 W 242
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
42-357 2.59e-38

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: 146.38  E-value: 2.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637    42 FREAVNQANKRHG-SWKIQLNATsVTHKPNAIQMALSVCEDLISSQVYAILvshppTPNDHFTPTPVSYTAGFYRIPVLG 120
Cdd:pfam01094   6 VRLAVEDINADPGlLPGTKLEYI-ILDTCCDPSLALAAALDLLKGEVVAII-----GPSCSSVASAVASLANEWKVPLIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   121 LTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPG 200
Cdd:pfam01094  80 YGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPPA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   201 T--KNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGER-----EISGNALRYAPDGILGLQLIN 273
Cdd:pfam01094 160 QddDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGlttslVILNPSTLEAAGGVLGFRLHP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   274 GKNES---------------------------AHISDAVGVVAQAVHELLEKenitDPPRGCVGNTNIWKTGPLFKRVLM 326
Cdd:pfam01094 240 PDSPEfseffweklsdekelyenlgglpvsygALAYDAVYLLAHALHNLLRD----DKPGRACGALGPWNGGQKLLRYLK 315
                         330       340       350
                  ....*....|....*....|....*....|.
gi 11038637   327 SSKYaDGVTGRVEFNEDGDRKFANYSIMNLQ 357
Cdd:pfam01094 316 NVNF-TGLTGNVQFDENGDRINPDYDILNLN 345
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
396-544 5.13e-38

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: 137.65  E-value: 5.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   396 TRLKIVTIHQEPFVYVKPTLSDgtckeeftvngdpvkkvictgpNDTspgsprhtvpqcCYGFCIDLLIKLARTMNFTYE 475
Cdd:pfam10613   1 KTLIVTTILEPPFVMLKENLEG----------------------NDR------------YEGFCIDLLKELAEILGFKYE 46
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11038637   476 VHLVADGKFGTQervnNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKK 544
Cdd:pfam10613  47 IRLVPDGKYGSL----DPTTGEWNGMIGELIDGKADLAVAPLTITSEREKVVDFTKPFMTLGISILMKK 111
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
457-792 1.63e-37

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: 141.13  E-value: 1.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQervnNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13714  32 GFCIDLLKELAKILGFNYTIRLVPDGKYGSY----DPETGEWNGMVRELIDGRADLAVADLTITYERESVVDFTKPFMNL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEIPrstldsfmqpfqstlwllvglsvhvvavmlylldrfspfgrfkVNSEEEeedaltLSSAMWFSWGVLLn 616
Cdd:cd13714 108 GISILYRKPTP-------------------------------------------IESADD------LAKQTKIKYGTLR- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 617 sgigEGAPRSFsarilgmvwagFamiivasytanlaaflvldrpeeritgindprlrnpsdkfiyatvKQSSVDIYFRrq 696
Cdd:cd13714 138 ----GGSTMTF-----------F---------------------------------------------RDSNISTYQK-- 155
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 697 velstMYRHMEKHN----YESAAEAIQAVRDNKlHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNV 772
Cdd:cd13714 156 -----MWNFMMSAKpsvfVKSNEEGVARVLKGK-YAFLMESTSIEYVTQRNCNLTQIGGLLDSKGYGIATPKGSPYRDKL 229
                       330       340
                ....*....|....*....|.
gi 11038637 773 SLSILKSHENGFMEDL-DKTW 792
Cdd:cd13714 230 SLAILKLQEKGKLEMLkNKWW 250
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
457-792 3.74e-30

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: 122.43  E-value: 3.74e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQErVNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13724  32 GFCVDMLKELAEILRFNYKIRLVGDGVYGVPE-ANGT----WTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEIPRST-LDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEE-----DALTLSSAMWFS 610
Cdd:cd13724 107 GISILYRVHMGRKPgYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSPHPCAQGRcnllvNQYSLGNSLWFP 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 611 WGVLLNSGiGEGAPrsfsarilgmvwagfamiivasytanlaaflvldrPEERITGINDprlrnpSDKFIYATVKQSSVD 690
Cdd:cd13724 187 VGGFMQQG-STIAP-----------------------------------PIESVDDLAD------QTAIEYGTIHGGSSM 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 691 IYFR--RQVELSTMYRHMEKHN----YESAAEAIQAVRDNKlHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRK 764
Cdd:cd13724 225 TFFQnsRYQTYQRMWNYMYSKQpsvfVKSTEEGIARVLNSN-YAFLLESTMNEYYRQRNCNLTQIGGLLDTKGYGIGMPV 303
                       330       340
                ....*....|....*....|....*...
gi 11038637 765 DSPWKQNVSLSILKSHENGFMEDLDKTW 792
Cdd:cd13724 304 GSVFRDEFDLAILQLQENNRLEILKRKW 331
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
105-383 4.54e-28

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: 117.73  E-value: 4.54e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 105 TPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLL 184
Cdd:cd06366  84 EPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLEELL 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 185 EERESK---AEKVLQFDPGTkNVTALlmeaKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVW-LVGE--------- 251
Cdd:cd06366 164 EEANITivaTESFSSEDPTD-QLENL----KEKDARIIIGLFYEDAARKVFCEAYKLGMYGPKYVWiLPGWyddnwwdvp 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 252 -----------REISGN--ALRYAPDGILGLQLINGK--------------NESAHIS-------DAVGVVAQAVHELLE 297
Cdd:cd06366 239 dndvnctpeqmLEALEGhfSTELLPLNPDNTKTISGLtaqeflkeylerlsNSNYTGSpyapfayDAVWAIALALNKTIE 318
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 298 KENITDPPRGCVGNTNIwKTGPLFKRVLMSSKYaDGVTGRVEFNEDGDRKfANYSIMNLQNRKLVQVGIYNGTH---VIP 374
Cdd:cd06366 319 KLAEYNKTLEDFTYNDK-EMADLFLEAMNSTSF-EGVSGPVSFDSKGDRL-GTVDIEQLQGGSYVKVGLYDPNAdslLLL 395

                ....*....
gi 11038637 375 NDRKIIWPG 383
Cdd:cd06366 396 NESSIVWPG 404
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-798 2.70e-27

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: 112.06  E-value: 2.70e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQervnNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13715  34 GYCVDLADEIAKHLGIKYELRIVKDGKYGAR----DADTGIWNGMVGELVRGEADIAIAPLTITLVRERVIDFSKPFMSL 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEIPrstldsfmqpfqstlwllvglsvhvvavmlylldrfspfgrfkVNSEEEeedaltLSSAMWFSWGVLLN 616
Cdd:cd13715 110 GISIMIKKPVP-------------------------------------------IESAED------LAKQTEIAYGTLDS 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 617 sgigegaprsfsarilGMVWAGFamiivasytanlaaflvldrpeeritgindprlrnpsdkfiyatvKQSSVDIYFRrq 696
Cdd:cd13715 141 ----------------GSTKEFF---------------------------------------------RRSKIAVYDK-- 157
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 697 velstMYRHM---EKHNY-ESAAEAIQAVRDNK-LHAFIWDSAVLEF-EASQKCDLVTTGELFFRSGFGIGMRKDSPWKQ 770
Cdd:cd13715 158 -----MWEYMnsaEPSVFvRTTDEGIARVRKSKgKYAYLLESTMNEYiNQRKPCDTMKVGGNLDSKGYGIATPKGSPLRN 232
                       330       340
                ....*....|....*....|....*....
gi 11038637 771 NVSLSILKSHENGFMEDL-DKTWVRYQEC 798
Cdd:cd13715 233 PLNLAVLKLKENGELDKLkNKWWYDKGEC 261
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
27-367 2.97e-25

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


Pssm-ID: 380601  Cd Length: 356  Bit Score: 108.54  E-value: 2.97e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  27 VNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQlNATSVTHKPNAIQMALSVCEDLISSQVYAILVShppTPNDHFTPTP 106
Cdd:cd06378   3 LNIAVILPGTSFEVRIRSRLEPDAFHGLPFEVS-PITVLMNDTNPKSILTQICDLLSGRKVHGIVFE---DDTDQEAVAQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 107 VSY---TAGFYRIPVLGLTTRMSIySDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWnHIILLVSDDHEG-RAAQKRLET 182
Cdd:cd06378  79 ILDfisLQTYLPILGISGGSANVL-LDKEEGSTFLQLGPSIEQQATVMLNILEEYDW-HQFSVVTSLFPGyRDFVDAIRS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 183 LLEERES--KAEKVLQFDPG-TKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREIsGNAL 259
Cdd:cd06378 157 TIDNSFVgwELQDVLTLDMSnDGSDAKTLRQLKKIEAQVILLYCTKEEAQYIFEAAEEAGLTGYGYVWIVPSLVL-GNTD 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 260 rYAPD----GILGLqLINGKNES--AHISDAVGVVAQAVHELLEKEN-ITDPPRGCVG-NTNIWKTGPLFKRVLMSSKYA 331
Cdd:cd06378 236 -PPPAefpvGLISV-HFDTWDYSlrARVRDGVAIIATGAEAMLSEHGfLPEPKSDCYApNETREPANETLHRYLINVTWE 313
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 11038637 332 dgvtGR-VEFNEDGDRKFANYSIMNLQN-RKLVQVGIY 367
Cdd:cd06378 314 ----GRdLSFNEDGYLVNPELVIINLNReRLWEKVGKW 347
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
457-794 1.64e-24

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: 103.56  E-value: 1.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNsnkkEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13721  32 GYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNG----QWNGMVRELIDHKADLAVAPLAITYVREKVIDFSKPFMTL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEIPRSTLDSFMQPFQstlwLLVGlSVHVVAVMLYlldrfspFGRFKVNSEEEeedaltlssaMWfswgVLLN 616
Cdd:cd13721 108 GISILYRKGTPIDSADDLAKQTK----IEYG-AVEDGATMTF-------FKKSKISTYDK----------MW----AFMS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 617 SgigegaprsfsarilgmvwagfamiivasytanlaaflvldrpeeritgindprlrnpsdkfiyatvkqssvdiyfRRQ 696
Cdd:cd13721 162 S----------------------------------------------------------------------------RRQ 165
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 697 velSTMYRHMEkhnyesaaEAIQAVRDNKlHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSI 776
Cdd:cd13721 166 ---SVLVKSNE--------EGIQRVLTSD-YAFLMESTTIEFVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAI 233
                       330
                ....*....|....*...
gi 11038637 777 LKSHENGFMEDLDKTWVR 794
Cdd:cd13721 234 LQLQEEGKLHMMKEKWWR 251
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-798 4.47e-23

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: 99.71  E-value: 4.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQErvnnSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13729  32 GYCVELAAEIAKHVGYSYKLEIVSDGKYGARD----PETKMWNGMVGELVYGKADVAVAPLTITLVREEVIDFSKPFMSL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKeiPRSTLDSfmqpfqstlwllvglsvhvvavmlylldrfspfgrfkvnseeeEEDaltLSSAMWFSWGVLln 616
Cdd:cd13729 108 GISIMIKK--PTSPIES-------------------------------------------AED---LAKQTEIAYGTL-- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 617 sgiGEGAPRSFSARilgmvwagfamiivasytANLAAFlvldrpeERitgindprlrnpsdkfIYATVKQSSVDIYFRrq 696
Cdd:cd13729 138 ---DAGSTKEFFRR------------------SKIAVF-------EK----------------MWSYMKSADPSVFVK-- 171
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 697 velstmyrhmekhnyeSAAEAIQAVRDNK-LHAFIWDSAVLEF-EASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSL 774
Cdd:cd13729 172 ----------------TTDEGVMRVRKSKgKYAYLLESTMNEYiEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNL 235
                       330       340
                ....*....|....*....|....*
gi 11038637 775 SILKSHENGFMEDL-DKTWVRYQEC 798
Cdd:cd13729 236 AVLKLNEQGLLDKLkNKWWYDKGEC 260
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-798 3.46e-21

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: 94.32  E-value: 3.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQErvnnSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13726  32 GYCVDLAAEIAKHCGFKYKLTIVGDGKYGARD----ADTKIWNGMVGELVYGKADIAIAPLTITLVREEVIDFSKPFMSL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEiprstldsfmQPFQSTlwllvglsvhvvavmlylldrfspfgrfkvnseeeeEDaltLSSAMWFSWGVLln 616
Cdd:cd13726 108 GISIMIKKG----------TPIESA------------------------------------ED---LSKQTEIAYGTL-- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 617 sgiGEGAPRSFSARilgmvwagfamiivasytANLAAFlvldrpeeritgindprlrnpsDKfIYATVKQSSVDIYFRrq 696
Cdd:cd13726 137 ---DSGSTKEFFRR------------------SKIAVF----------------------DK-MWTYMRSAEPSVFVR-- 170
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 697 velstmyrhmekhnyeSAAEAIQAVRDNK-LHAFIWDSAVLEF-EASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSL 774
Cdd:cd13726 171 ----------------TTAEGVARVRKSKgKYAYLLESTMNEYiEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNL 234
                       330       340
                ....*....|....*....|....*
gi 11038637 775 SILKSHENGFMEDL-DKTWVRYQEC 798
Cdd:cd13726 235 AVLKLNEQGLLDKLkNKWWYDKGEC 259
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-547 6.92e-21

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: 93.17  E-value: 6.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQErvnnSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13727  32 GYCVDLASEIAKHIGIKYKIAIVPDGKYGARD----PETKIWNGMVGELVYGKAEIAVAPLTITLVREEVIDFSKPFMSL 107
                        90
                ....*....|.
gi 11038637 537 GLTILVKKEIP 547
Cdd:cd13727 108 GISIMIKKPQP 118
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
398-792 7.60e-21

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


Pssm-ID: 270434 [Multi-domain]  Cd Length: 257  Bit Score: 92.98  E-value: 7.60e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 398 LKIVTIHQEPFVYVKPTlsdgtckeeftVNGDPVKKvictgpndtspgsprhtvpqccYGFCIDLLIKLARTMNFTYEVH 477
Cdd:cd13716   4 LRVVTVLEEPFVMVSEN-----------VLGKPKKY----------------------QGFSIDVLDALANYLGFKYEIY 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 478 LVADGKFGTQERvNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPrstldsfMQP 557
Cdd:cd13716  51 VAPDHKYGSQQE-DGT----WNGLIGELVFKRADIGISALTITPERENVVDFTTRYMDYSVGVLLRKAES-------IQS 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 558 FQStlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltLSSAMWFSWGVLLNSGIGEgaprsfSARILGMvwa 637
Cdd:cd13716 119 LQD------------------------------------------LSKQTDIPYGTVLDSAVYE------YVRSKGT--- 147
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 638 gfamiivasytanlaaflvldrpeeritgindprlrNPsdkfiyatvkqssvdiyFRRQVELSTMYRHMEK-----HNYE 712
Cdd:cd13716 148 ------------------------------------NP-----------------FERDSMYSQMWRMINRsngseNNVS 174
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 713 SAAEAIQAVRDNKlHAFIWDSAVLEFEA--SQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDK 790
Cdd:cd13716 175 ESSEGIRKVKYGN-YAFVWDAAVLEYVAinDDDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKH 253

                ..
gi 11038637 791 TW 792
Cdd:cd13716 254 KW 255
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
457-556 7.93e-21

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: 92.81  E-value: 7.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQervnnSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13722  32 GYCLDLLKELSNILGFLYDVKLVPDGKYGAQ-----NDKGEWNGMVKELIDHRADLAVAPLTITYVREKVIDFSKPFMTL 106
                        90       100
                ....*....|....*....|
gi 11038637 537 GLTILVKKEIPRSTLDSFMQ 556
Cdd:cd13722 107 GISILYRKGTPIDSADDLAK 126
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
398-792 1.34e-20

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: 92.33  E-value: 1.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 398 LKIVTIHQEPFVYVKPTLSdgtckeeftvngdpvkkvictgpndtspGSPRHTvpqccYGFCIDLLIKLARTMNFTYEVH 477
Cdd:cd13730   4 LKVVTVLEEPFVMVAENIL----------------------------GQPKRY-----KGFSIDVLDALAKALGFKYEIY 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 478 LVADGKFGTQERvNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTldsfmqp 557
Cdd:cd13730  51 QAPDGKYGHQLH-NTS----WNGMIGELISKRADLAISAITITPERESVVDFSKRYMDYSVGILIKKPEPIRT------- 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 558 FQStlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltLSSAMWFSWGvllnsgigegaprsfsarilgmvwa 637
Cdd:cd13730 119 FQD------------------------------------------LSKQVEMSYG------------------------- 131
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 638 gfamiivasytanlaaflvldrpeeritgindprlrnpsdkfiyaTVKQSSVDIYFR--------RQVELSTMYRHMEKH 709
Cdd:cd13730 132 ---------------------------------------------TVRDSAVYEYFRakgtnpleQDSTFAELWRTISKN 166
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 710 N-----YESAAEAIQAVRDNKlHAFIWDSAVLEFEA--SQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHEN 782
Cdd:cd13730 167 GgadncVSSPSEGIRKAKKGN-YAFLWDVAVVEYAAltDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDT 245
                       410
                ....*....|
gi 11038637 783 GFMEDLDKTW 792
Cdd:cd13730 246 GDLDVLKQKW 255
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
457-792 2.28e-19

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: 88.61  E-value: 2.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQERvNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13725  32 GFCVDMLRELAELLRFRYRLRLVEDGLYGAPEP-NGS----WTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEIPRSTLDSFMQpfQSTLWLlvgLSVHVVAVMLYLLD-RFSPFGRfkvnseeeeedaltlssaMWFswgvll 615
Cdd:cd13725 107 GISILYRVHMPVESADDLAD--QTNIEY---GTIHAGSTMTFFQNsRYQTYQR------------------MWN------ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 616 nsgigegaprsfsarilgmvwagfamiivasytanlaaflvldrpeeritgindprlrnpsdkfiYATVKQSSVDIyfrr 695
Cdd:cd13725 158 -----------------------------------------------------------------YMQSKQPSVFV---- 168
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 696 qvelstmyrhmekhnyESAAEAIQAVRDNKlHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLS 775
Cdd:cd13725 169 ----------------KSTEEGIARVLNSR-YAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLA 231
                       330
                ....*....|....*..
gi 11038637 776 ILKSHENGFMEDLDKTW 792
Cdd:cd13725 232 ILQLQENNRLEILKRKW 248
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
457-547 9.31e-19

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: 87.05  E-value: 9.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADGKFGTQErvnnSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13728  32 GYCVDLAYEIAKHVRIKYKLSIVGDGKYGARD----PETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSL 107
                        90
                ....*....|.
gi 11038637 537 GLTILVKKEIP 547
Cdd:cd13728 108 GISIMIKKPQP 118
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
398-792 1.90e-17

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: 83.16  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 398 LKIVTIHQEPFVYVKPTlsdgtckeeftVNGDPVKKvictgpndtspgsprhtvpqccYGFCIDLLIKLARTMNFTYEVH 477
Cdd:cd13731   4 LRVVTVLEEPFVMVSEN-----------VLGKPKKY----------------------QGFSIDVLDALSNYLGFNYEIY 50
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 478 LVADGKFGTQERvnnsnKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEiprstldSFMQP 557
Cdd:cd13731  51 VAPDHKYGSPQE-----DGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRA-------ESIQS 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 558 FQStlwllvglsvhvvavmlylldrfspfgrfkvnseeeeedaltLSSAMWFSWGVLLNSGIGEgaprsfSARILGMvwa 637
Cdd:cd13731 119 LQD------------------------------------------LSKQTDIPYGTVLDSAVYE------HVRMKGL--- 147
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 638 gfamiivasytanlaaflvldrpeeritgindprlrNPsdkfiyatvkqssvdiyFRRQVELSTMYRHMEK-----HNYE 712
Cdd:cd13731 148 ------------------------------------NP-----------------FERDSMYSQMWRMINRsngseNNVL 174
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 713 SAAEAIQAVRDNKlHAFIWDSAVLEFEA--SQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDK 790
Cdd:cd13731 175 ESQAGIQKVKYGN-YAFVWDAAVLEYVAinDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKH 253

                ..
gi 11038637 791 TW 792
Cdd:cd13731 254 KW 255
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
450-506 4.98e-17

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: 75.75  E-value: 4.98e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 11038637    450 TVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERvnnsnKKEWNGMMGELL 506
Cdd:smart00918  11 GGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLP-----NGSWNGMVGELV 62
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
105-370 3.60e-16

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: 81.63  E-value: 3.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 105 TPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEG-RAAQKRLETL 183
Cdd:cd06352  83 DAVGRLATYWNIPIITWGAVSASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDDSKcFSIANDLEDA 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 184 LEERESK--AEKVLQFDPGTKNVTALLMEAKElEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGE---REISGNA 258
Cdd:cd06352 163 LNQEDNLtiSYYEFVEVNSDSDYSSILQEAKK-RARIIVLCFDSETVRQFMLAAHDLGMTNGEYVFIFIElfkDGFGGNS 241
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 259 L-------------RYAPDGILGLQLINGKNE-------------------------------SAHISDAVGVVAQAVHE 294
Cdd:cd06352 242 TdgwerndgrdedaKQAYESLLVISLSRPSNPeydnfskevkarakeppfycydaseeevspyAAALYDAVYLYALALNE 321
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11038637 295 LLEK-ENITDpprgcvgNTNIWKtgplfkrvLMSSKYADGVTGRVEFNEDGDRKFaNYSIMNLQ--NRKLVQVGIYNGT 370
Cdd:cd06352 322 TLAEgGNYRN-------GTAIAQ--------RMWNRTFQGITGPVTIDSNGDRDP-DYALLDLDpsTGKFVVVLTYDGT 384
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
106-376 2.42e-15

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: 78.49  E-value: 2.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 106 PVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLE 185
Cdd:cd06350 109 AVANLLGLFKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVSTVYSDDDYGRSGIEAFEREAK 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 186 ERESKAEKVLQFDPGTknvTALLMEA--KELE----ARVIILSASEDDAATVYRAAAMLNMTgsGYVWLvgereisgnal 259
Cdd:cd06350 189 ERGICIAQTIVIPENS---TEDEIKRiiDKLKsspnAKVVVLFLTESDARELLKEAKRRNLT--GFTWI----------- 252
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 260 ryAPDGiLGLQLINGKNESAHISDAVGVVaqavhelLEKENITDpprgcvgntniwktgplFKRVLMSSKYA--DGVTGR 337
Cdd:cd06350 253 --GSDG-WGDSLVILEGYEDVLGGAIGVV-------PRSKEIPG-----------------FDDYLKSYAPYviDAVYAT 305
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 11038637 338 VEFNEDGDRkFANYSIMNLQNR-----KLVQVGIY--NGTHVIPND 376
Cdd:cd06350 306 VKFDENGDG-NGGYDIVNLQRTgtgnyEYVEVGTWdsNSGGLSLNS 350
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
28-365 6.57e-15

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: 77.65  E-value: 6.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  28 NIGAVL---STRKHEQM--FREAVNQANKRHGSWKIQLnatsVTH----KPNAIQmALSVCEDLISS-QVYAILVshppt 97
Cdd:cd19990   1 KIGAILdlnSRVGKEAKvaIEMAVSDFNSDSSSYGTKL----VLHvrdsKGDPLQ-AASAALDLIKNkKVEAIIG----- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  98 PNDHFTPTPVSYTAGFYRIPVLGLT-TRMSIYSDKSIHlsFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAA 176
Cdd:cd19990  71 PQTSEEASFVAELGNKAQVPIISFSaTSPTLSSLRWPF--FIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 177 QKRLETLLEERESKAEKVLQFDPGT--KNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGERei 254
Cdd:cd19990 149 IPYLSDALQEVGSRIEYRVALPPSSpeDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDG-- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 255 SGNALRYAPD-------GILGL---------------------QLINGKNESAHIS-------DAVGVVAQAVHELLEKE 299
Cdd:cd19990 227 ITNLLDSLDSstissmqGVIGIktyipessefqdfkarfrkkfRSEYPEEENAEPNiyalrayDAIWALAHAVEKLNSSG 306
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11038637 300 nitdpprgcvGNTNIWKTGPLFKRVLMSSKYaDGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVG 365
Cdd:cd19990 307 ----------GNISVSDSGKKLLEEILSTKF-KGLSGEVQFVDGQLAPPPAFEIVNVIGKGYRELG 361
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
112-367 5.52e-14

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: 75.41  E-value: 5.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 112 GFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERE--- 188
Cdd:cd06362 128 RLFKIPQISYASTSDELSDKERYPYFLRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGSYGEEGYKAFKKLARKAGici 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 189 SKAEKVLQfDPGTKNVTALLME-AKELEARVIILSASEDDAATVYRAAAMLNMTGSgYVWL----VGEREISGNALRYAP 263
Cdd:cd06362 208 AESERISQ-DSDEKDYDDVIQKlLQKKNARVVVLFADQEDIRGLLRAAKRLGASGR-FIWLgsdgWGTNIDDLKGNEDVA 285
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 264 DGILGLQLI--------------------------------------------------------NGKNESAHIS--DAV 285
Cdd:cd06362 286 LGALTVQPYseevprfddyfksltpsnntrnpwfrefwqelfqcsfrpsrenscnddkllinkseGYKQESKVSFviDAV 365
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 286 GVVAQAVHELLeKENITDPPRGCVGNTNIWKtGPLFKRVLMSSKYADGVTGRVEFNEDGDRKfANYSIMNLQNR-----K 360
Cdd:cd06362 366 YAFAHALHKMH-KDLCPGDTGLCQDLMKCID-GSELLEYLLNVSFTGEAGGEIRFDENGDGP-GRYDIMNFQRNndgsyE 442

                ....*..
gi 11038637 361 LVQVGIY 367
Cdd:cd06362 443 YVRVGVW 449
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
457-554 2.34e-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: 67.32  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   457 GFCIDLLIKLARTMNFTYEVHLVadgkfgtqervnnsnkkEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:pfam00497  23 GFDVDLAKAIAKRLGVKVEFVPV-----------------SWDGLIPALQSGKVDLIIAGMTITPERAKQVDFSDPYYYS 85
                          90
                  ....*....|....*...
gi 11038637   537 GLTILVKKEIPRSTLDSF 554
Cdd:pfam00497  86 GQVILVRKKDSSKSIKSL 103
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
28-368 4.98e-12

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: 68.40  E-value: 4.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  28 NIGAVLSTR--KHEQMFREAVNQANKRHGSWKIQLNATSV-THKPNAIQMALSVCeDLISSQVYAILVSHPPTPNDHftp 104
Cdd:cd06382   1 RIGGIFDEDdeDLEIAFKYAVDRINRERTLPNTKLVPDIErVPRDDSFEASKKVC-ELLEEGVAAIFGPSSPSSSDI--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 105 tpVSYTAGFYRIPVLglTTRMSIYSDKSIHLSFlrTVPPYSHQ-SSVWFEMMRVYSWNHIILLVSDDhEGRAaqkRLETL 183
Cdd:cd06382  77 --VQSICDALEIPHI--ETRWDPKESNRDTFTI--NLYPDPDAlSKAYADLVKSLNWKSFTILYEDD-EGLI---RLQEL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 184 LEERESKAEKVL--QFDPGtKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVgereisGN---- 257
Cdd:cd06382 147 LKLPKPKDIPITvrQLDPG-DDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYIL------TNldlh 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 258 -----ALRYAPDGILGLQLINGKNESahisdavgvVAQAVHELLEKENITDPPRgcvGNTNIWKTGP--------LFKRV 324
Cdd:cd06382 220 tldlePFKYSGANITGFRLVDPENPE---------VKNVLKDWSKREKEGFNKD---IGPGQITTETalmydavnLFANA 287
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 11038637 325 LmsskyADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYN 368
Cdd:cd06382 288 L-----KEGLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGTWN 326
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
107-345 1.22e-11

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


Pssm-ID: 380584 [Multi-domain]  Cd Length: 401  Bit Score: 67.78  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 107 VSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAqkrLETLLEE 186
Cdd:cd06361 117 VARLLNLQLIPQISYESSAPILSDKLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDDDYGRSA---LESFIIQ 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 187 RESKA-----EKVL--QFDPGTKNV--TALLME-AKELEARVIILSASEDDAATVYRAAAMLNMTgsgYVWLVGE----- 251
Cdd:cd06361 194 AEAENvciafKEVLpaYLSDPTMNVriNDTIQTiQSSSQVNVVVLFLKPSLVKKLFKEVIERNIS---KIWIASDnwsta 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 252 REIS--------GNalryapdgILGLQLINGKNESAH----------ISDAVGVVAQAVHELLEKenitdppRGCVGNTN 313
Cdd:cd06361 271 REILkmpninkvGK--------ILGFTFKSGNISSFHnylknlliysIQLAVTAIANALRKLCCE-------RGCQDPTA 335
                       250       260       270
                ....*....|....*....|....*....|....*
gi 11038637 314 I--WKtgpLFKrVLMSSKYADGvtGR-VEFNEDGD 345
Cdd:cd06361 336 FqpWE---LLK-ELKKVTFTDD--GEtYHFDANGD 364
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
457-792 1.43e-11

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: 65.00  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVadgkfgtqervnnsnkkEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:COG0834  23 GFDVDLARAIAKRLGLKVEFVPV-----------------PWDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPYYTS 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 537 GLTILVKKEIPR-STLDSfmqpfqstlwlLVGLSVhvvavmlylldrfspfgrfkvnseeeeedaltlssamwfswgvll 615
Cdd:COG0834  86 GQVLLVRKDNSGiKSLAD-----------LKGKTV--------------------------------------------- 109
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 616 nsgigegaprsfsarilgmvwagfamiivasytanlaaflvldrpeeritgindprlrnpsdkfiyATVKQSSVDIYFRR 695
Cdd:COG0834 110 ------------------------------------------------------------------GVQAGTTYEEYLKK 123
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 696 qvelstMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQK--CDLVTTGELFFRSGFGIGMRKDSP-WKQNV 772
Cdd:COG0834 124 ------LGPNAEIVEFDSYAEALQALASGRVDAVVTDEPVAAYLLAKNpgDDLKIVGEPLSGEPYGIAVRKGDPeLLEAV 197
                       330       340
                ....*....|....*....|
gi 11038637 773 SLSILKSHENGFMEDLDKTW 792
Cdd:COG0834 198 NKALAALKADGTLDKILEKW 217
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
112-389 4.19e-11

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: 66.18  E-value: 4.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 112 GFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERE--S 189
Cdd:cd06363 129 GFFLMPQISYGASSEELSNKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAANTGicV 208
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 190 KAEKVLQFD-PGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSgyVWLVGER-----------EIS-- 255
Cdd:cd06363 209 AYQGLIPTDtDPKPKYQDILKKINQTKVNVVVVFAPKQAAKAFFEEVIRQNLTGK--VWIASEAwslndtvtslpGIQsi 286
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 256 ----GNALRYAPdgILGLQ-LINGKNESAHisDAVGVVAQAVHELLE------KENITDPPrgcvgntniWKtgpLFKRV 324
Cdd:cd06363 287 gtvlGFAIQTGT--LPGFQeFIYAFAFSVY--AAVYAVAHALHNLLGcnsgacPKGRVVYP---------WQ---LLEEL 350
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 11038637 325 LMSSKYADGVTgrVEFNEDGDRKFAnYSIMNLQNR----KLVQVGIYNG--THVIPNDRKIIWPGGETEKP 389
Cdd:cd06363 351 KKVNFTLLNQT--IRFDENGDPNFG-YDIVQWIWNnsswTFEVVGSYSTypIQLTINESKIKWHTKDSPVP 418
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
457-553 3.17e-10

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 61.11  E-value: 3.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVhlvadgkfgtqerVNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13530  24 GFDVDLANAIAKRLGVKVEF-------------VDTD----FDGLIPALQSGKIDVAISGMTITPERAKVVDFSDPYYYT 86
                        90
                ....*....|....*..
gi 11038637 537 GLTILVKKEIPRSTLDS 553
Cdd:cd13530  87 GQVLVVKKDSKITKTVA 103
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
457-545 6.61e-10

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: 60.02  E-value: 6.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNftYEVHLVAdgkfgtqervnnsnkKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13626  24 GFDVEVGREIAKRLG--LKVEFKA---------------TEWDGLLPGLNSGKFDVIANQVTITPEREEKYLFSDPYLVS 86

                ....*....
gi 11038637 537 GLTILVKKE 545
Cdd:cd13626  87 GAQIIVKKD 95
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
457-545 9.48e-10

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: 59.43  E-value: 9.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVhlvadgkfgtqerVNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13624  24 GFDIDLIKAIAKEAGFEVEF-------------KNMA----FDGLIPALQSGKIDIIISGMTITEERKKSVDFSDPYYEA 86

                ....*....
gi 11038637 537 GLTILVKKE 545
Cdd:cd13624  87 GQAIVVRKD 95
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
105-370 1.83e-09

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


Pssm-ID: 380596 [Multi-domain]  Cd Length: 394  Bit Score: 60.75  E-value: 1.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 105 TPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSdDHEGRAAQKR----- 179
Cdd:cd06373  81 APVARYAGHWNVPVLTAGGLAAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVALLYH-DNLRRKAGNSncyft 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 180 ----LETLLEERESKAEKVLQFDPGTKNVTALLMEAKeLEARVIILSASEDdaaTVYR---AAAMLNMTGSGYV------ 246
Cdd:cd06373 160 legiFNALTGERDSIHKSFDEFDETKDDFEILLKRVS-NSARIVILCASPD---TVREimlAAHELGMINGEYVffnidl 235
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 247 ----------WLV-----GEREISGNALR-------YAPDG-----------ILGLQ---LINGKNE--SAHIS---DAV 285
Cdd:cd06373 236 fsssskgarpWYRendtdERNEKARKAYRalltvtlRRPDSpeyrnfseevkERAKEkynYFTYGDEevNSFVGafhDAV 315
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 286 GVVAQAVHELLEKEniTDPPRGcvgnTNIWKtgplfkrvLMSSKYADGVTGRVEFNEDGDRkFANYSI--MNLQNRKLVQ 363
Cdd:cd06373 316 LLYALALNETLAEG--GSPRNG----TEITE--------RMWNRTFEGITGNVSIDANGDR-NADYSLldMNPVTGKFEV 380

                ....*..
gi 11038637 364 VGIYNGT 370
Cdd:cd06373 381 VANYFGN 387
CaM_bdg_C0 pfam10562
Calmodulin-binding domain C0 of NMDA receptor NR1 subunit; This is a very short highly ...
835-863 2.37e-09

Calmodulin-binding domain C0 of NMDA receptor NR1 subunit; This is a very short highly conserved domain that is C-terminal to the cytosolic transmembrane region IV of the NMDA-receptor 1. It has been shown to bind Calmodulin-Calcium with high affinity. The ionotropic N-methyl-D-aspartate receptor (NMDAR) is a major source of calcium flux into neurons in the brain and plays a critical role in learning, memory, neural development, and synaptic plasticity. Calmodulin (CaM) regulates NMDARs by binding tightly to the C0 and C1 regions of their NR1 subunit. The conserved tryptophan is considered to be the anchor residue.


Pssm-ID: 402271  Cd Length: 29  Bit Score: 53.29  E-value: 2.37e-09
                          10        20
                  ....*....|....*....|....*....
gi 11038637   835 IAYKRHKDARRKQMQLAFAAVNVWRKNLQ 863
Cdd:pfam10562   1 IAYKKHQGRKQKQLELARHAADKWRGNIE 29
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
179-357 7.19e-09

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: 58.77  E-value: 7.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 179 RLETLLEE----RESKAEKVLQfdpGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREI 254
Cdd:cd06394 151 RLEELVRQflisKETLSVRMLD---DSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDF 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 255 SGNALRYAPD---GILGLQLINGKN----------------------------ESAHISDAVGVVAQAVHELLEKENITD 303
Cdd:cd06394 228 PLLHLDGIVDdqsNILGFSMFNTSHpfylefvrslnmswrencdastypgpalSSALMFDAVHVVVSAVRELNRSQEIGV 307
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 11038637 304 PPRGCvGNTNIWKTGPLFKRVLMSSKYaDGVTGRVEFNEDGDRkfANYSIMNLQ 357
Cdd:cd06394 308 KPLSC-TSAQIWQHGTSLMNYLRMVEY-DGLTGRVEFNSKGQR--TNYTLRILE 357
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
114-345 1.10e-08

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: 57.63  E-value: 1.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 114 YRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFE-MMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAE 192
Cdd:COG0683  94 AGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDDYAYGQGLAAAFKAALKAAGGEVV 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 193 KVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGE-REISGNalryAPDGIlglql 271
Cdd:COG0683 174 GEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYGGDAALFIKQAREAGLKGPLNKAFVKAyKAKYGR----EPSSY----- 244
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11038637 272 ingkneSAHISDAVGVVAQAVhellEKENITDPPRgcvgntniwktgplFKRVLMSSKYaDGVTGRVEFNEDGD 345
Cdd:COG0683 245 ------AAAGYDAALLLAEAI----EKAGSTDREA--------------VRDALEGLKF-DGVTGPITFDPDGQ 293
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
107-381 1.79e-08

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: 58.04  E-value: 1.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 107 VSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAqkrLETLLEE 186
Cdd:cd06364 116 VARTLGLFYIPQVSYFASCACLSDKKQFPSFLRTIPSDYYQSRALAQLVKHFGWTWVGAIASDDDYGRNG---IKAFLEE 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 187 RESK------AEKVLQFDPGTKNVTALLMeAKELEARVIILSASEDDAATVYRAAAMLNMTgsGYVWLVGEREISGNAL- 259
Cdd:cd06364 193 AEKLgiciafSETIPRTYSQEKILRIVEV-IKKSTAKVIVVFSSEGDLEPLIKELVRQNIT--GRQWIASEAWITSSLLa 269
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 260 --RYAP--DGILGLQLINGK-----------------------------------NESAHISD----------------- 283
Cdd:cd06364 270 tpEYFPvlGGTIGFAIRRGEipglkefllrvhpskspsnpfvkefweetfncslsSSSKSNSSsssrppctgsenlenvq 349
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 284 -----------------AVGVVAQAVHELLEKENITDP-PRGCVGN-TNI--WKTGPLFKRVLMSSKYADgvtgRVEFNE 342
Cdd:cd06364 350 npytdvsqlrisynvykAVYAIAHALHDLLQCEPGKGPfSNGSCADiKKVepWQLLYYLKHVNFTTKFGE----EVYFDE 425
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 11038637 343 DGDRKfANYSIMNLQ-----NRKLVQVGIYNGT-----HVIPNDRKIIW 381
Cdd:cd06364 426 NGDPV-ASYDIINWQlsddgTIQFVTVGYYDASapsgeELVINESKILW 473
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
112-381 4.02e-08

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: 56.88  E-value: 4.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 112 GFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGraaQKRLETLLEERESK- 190
Cdd:cd06365 121 GLYKYPQISYGAFDPLLSDKVQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDDDYG---EQFSQDLKKEMEKNg 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 191 -----AEKVLQFDPGTKNVTALLMEAKELeARVIILSASEDDaaTVYRAAAMLNMTGSGYVWLV---------------- 249
Cdd:cd06365 198 icvafVEKIPTNSSLKRIIKYINQIIKSS-ANVIIIYGDTDS--LLELLFRLWEQLVTGKVWITtsqwdistlpfefyln 274
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 250 ---G-------EREISG--------NALRYaPDGIL-------------------GLQLINGKNE--------------- 277
Cdd:cd06365 275 lfnGtlgfsqhSGEIPGfkeflqsvHPSKY-PEDIFlktlwesyfnckwpdqnckSLQNCCGNESletldvhsfdmtmsr 353
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 278 -SAHISDAVGVVAQAVHELLEKEnITDPPRGCVGNTNI--WKTGPLFKRVlmssKYADGVTGRVEFNEDGDRKfANYSIM 354
Cdd:cd06365 354 lSYNVYNAVYAVAHALHEMLLCQ-PKTGPGNCSDRRNFqpWQLHHYLKKV----QFTNPAGDEVNFDEKGDLP-TKYDIL 427
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 11038637 355 NLQNR-----KLVQVGIY-----NGTHVIPNDRKIIW 381
Cdd:cd06365 428 NWQIFpngtgTKVKVGTFdpsapSGQQLIINDSMIEW 464
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
457-552 4.85e-08

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 54.64  E-value: 4.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637    457 GFCIDLLIKLARTMNFTYEVHLVAdgkfgtqervnnsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:smart00062  24 GFDVDLAKAIAKELGLKVEFVEVS-----------------FDSLLTALKSGKIDVVAAGMTITPERAKQVDFSDPYYRS 86
                           90
                   ....*....|....*.
gi 11038637    537 GLTILVKKEIPRSTLD 552
Cdd:smart00062  87 GQVILVRKDSPIKSLE 102
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
457-544 9.81e-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: 9.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVhlvadgkfgtqervnnsNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd00994  23 GFDIDLWEAIAKEAGFKYEL-----------------QPMDFKGIIPALQTGRIDIAIAGITITEERKKVVDFSDPYYDS 85

                ....*...
gi 11038637 537 GLTILVKK 544
Cdd:cd00994  86 GLAVMVKA 93
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
457-557 5.22e-07

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: 51.42  E-value: 5.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVAdgkfgtqervnnsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13629  24 GFDVDLAKALAKDLGVKVEFVNTA-----------------WDGLIPALQTGKFDLIISGMTITPERNLKVNFSNPYLVS 86
                        90       100
                ....*....|....*....|...
gi 11038637 537 GLTILVKKE--IPRSTLDSFMQP 557
Cdd:cd13629  87 GQTLLVNKKsaAGIKSLEDLNKP 109
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
158-368 5.86e-07

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: 52.64  E-value: 5.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 158 YSWNHIILLVSDDHEGRAAQKRLETLLEeresKAEKVLQFDPGTKNVTALLMEAKELEA---RVIILSASEDDAATVYRA 234
Cdd:cd06390 115 YKWQKFVYIYDADRGLSVLQKVLDTAAE----KNWQVTAVNILTTTEEGYRMLFQDLDKkkeRLVVVDCESERLNAILGQ 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 235 AAMLNMTGSGYVWLV---GEREISGNALRYAPDGILGLQLIN----------------------------GKNESAHISD 283
Cdd:cd06390 191 IVKLEKNGIGYHYILanlGFMDIDLTKFKESGANVTGFQLVNytdtiparimqqwknsdsrdlprvdwkrPKYTSALTYD 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 284 AVGVVAQAVHELlEKENITDPPRG----CVGNTNI-WKTGPLFKRVLMSSKYaDGVTGRVEFNEDGDRKFANYSIMNLQN 358
Cdd:cd06390 271 GVKVMAEAFQSL-RRQRIDISRRGnagdCLANPAVpWGQGIDIQRALQQVRF-EGLTGNVQFNEKGRRTNYTLHVIEMKH 348
                       250
                ....*....|
gi 11038637 359 RKLVQVGIYN 368
Cdd:cd06390 349 DGIRKIGYWN 358
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
29-353 7.03e-07

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: 52.37  E-value: 7.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  29 IGAVLS---TRKHEQMFREAV---NQANKRHGSWKIQLNaTSVTHKPNAIQMALSVCeDLISSQVYAILVSHPPTPNDHf 102
Cdd:cd06368   2 IGAIFNevnDAHERAAFRYAVerlNTNIVKLAYFRITYS-IEAIDSNSHFDATDKAC-DLLEKGVVAIVGPSSSDSNNA- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 103 tptpVSYTAGFYRIP----VLGLTTRMSIYSdksIHLSflrtvpPYSHQSSVWFEMMRVYSWNHIILLVSDDhegrAAQK 178
Cdd:cd06368  79 ----LQSICDALDVPhitvHDDPRLSKSQYS---LSLY------PRNQLSQAVSDLLKYWRWKRFVLVYDDD----DRLR 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 179 RLETLLEERESKAE----KVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREI 254
Cdd:cd06368 142 RLQELLEAARFSKRfvsvRKVDLDYKTLDETPLLKRKDCSLFSRILIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 255 SG----NALRYAPDGILGLQLINGKN-ESAHISDAVGVVAQAVHELLEKENITDPPRgcvgntniwKTGPLFKRVLMssk 329
Cdd:cd06368 222 SLlldlELFRYNHANITGFQLVDNNSmYKEDINRLAFNWSRFRQHIKIESNLRGPPY---------EAALMFDAVLL--- 289
                       330       340
                ....*....|....*....|....*.
gi 11038637 330 YADGV--TGRVEFNEDGDRkfANYSI 353
Cdd:cd06368 290 LADAFrrTGDLRFNGTGLR--SNFTL 313
PBP2_AA_binding_like_2 cd13627
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
495-544 8.30e-07

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


Pssm-ID: 270345 [Multi-domain]  Cd Length: 243  Bit Score: 51.25  E-value: 8.30e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 11038637 495 KKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKK 544
Cdd:cd13627  58 KIEWNGLIPALNSGDIDLIIAGMSKTPEREKTIDFSDPYYISNIVMVVKK 107
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
497-549 1.14e-06

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: 50.46  E-value: 1.14e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 11038637 497 EWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRS 549
Cdd:cd13712  47 EWSGILAGLQAGKYDVIINQVGITPERQKKFDFSQPYTYSGIQLIVRKNDTRT 99
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
457-554 1.22e-06

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


Pssm-ID: 270407 [Multi-domain]  Cd Length: 229  Bit Score: 50.69  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVhlvadgkfgtqERVNNSNKkewngmMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13689  33 GFDVDLCKAIAKKLGVKLEL-----------KPVNPAAR------IPELQNGRVDLVAANLTYTPERAEQIDFSDPYFVT 95
                        90
                ....*....|....*...
gi 11038637 537 GLTILVKKEIPRSTLDSF 554
Cdd:cd13689  96 GQKLLVKKGSGIKSLKDL 113
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
442-572 1.40e-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: 50.16  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 442 TSPGSP----RHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVAdgkfgtqervnnsnkkeWNGMMGELLSGQADMIVAPL 517
Cdd:cd13628   6 TSPDYPpfefKIGDRGKIVGFDIELAKTIAKKLGLKLQIQEYD-----------------FNGLIPALASGQADLALAGI 68
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 11038637 518 TINNERAQYIEFSKPFkYQGLTILVkkeiprSTLDSFMQPFQStlwlLVGLSVHV 572
Cdd:cd13628  69 TPTPERKKVVDFSEPY-YEASDTIV------S*KDRKIKQLQD----LNGKSLGV 112
PBP2_mlr5654_like cd13702
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
497-545 2.16e-06

Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the type 2 periplasmic-binding protein fold; This group includes uncharacterized periplasmic substrate-binding protein similar to HisJ and LAO proteins which serve as initial receptors in the ABC transport of histidine-, arginine, and lysine-arginine-ornithine amino acids. This group belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270420 [Multi-domain]  Cd Length: 223  Bit Score: 49.63  E-value: 2.16e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 11038637 497 EWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKE 545
Cdd:cd13702  49 DWDGIIPALQAKKFDAIIASMSITPERKKQVDFTDPYYTNPLVFVAPKD 97
PBP1_mGluR_groupIII cd06376
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
114-248 6.05e-06

ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain of the group III metabotropic glutamate receptor, a family which contains mGlu4R, mGluR6R, mGluR7, and mGluR8; 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: 380599 [Multi-domain]  Cd Length: 467  Bit Score: 49.80  E-value: 6.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 114 YRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSddhEGRAAQKRLETLLE-ERE---- 188
Cdd:cd06376 130 FQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLAS---EGNYGEKGVESFVQiSREaggv 206
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11038637 189 --SKAEKVLQF-DPGT-KNVTALLMEAKelEARVIILSASEDDAATVYRAAAMLNMTGSgYVWL 248
Cdd:cd06376 207 ciAQSEKIPRErRTGDfDKIIKRLLETP--NARAVVIFADEDDIRRVLAAAKRANKTGH-FLWV 267
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
114-376 6.29e-06

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


Pssm-ID: 380597 [Multi-domain]  Cd Length: 474  Bit Score: 49.65  E-value: 6.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 114 YRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEER---ESK 190
Cdd:cd06374 141 FHIPQIGYSATSIDLSDKSLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEEgicIAH 220
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 191 AEKVLQfDPGTKNVTALLMEAKEL--EARVIILSASEDDAATVYRAAAMLNMTGsGYVWL-------------VGEREIS 255
Cdd:cd06374 221 SDKIYS-NAGEEEFDRLLRKLMNTpnKARVVVCFCEGETVRGLLKAMRRLNATG-HFLLIgsdgwadrkdvveGYEDEAA 298
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 256 GN-----------------------------------------ALRYAPDGILGLQLINGKNESAHIS-----------D 283
Cdd:cd06374 299 GGitikihspevesfdeyyfnlkpetnsrnpwfrefwqhrfdcRLPGHPDENPYFKKCCTGEESLLGNyvqdsklgfviN 378
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 284 AVGVVAQAVHELLEKENITDPPRGCVGNTNIwkTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKfANYSIMNLQNRK--- 360
Cdd:cd06374 379 AIYAMAHALHRMQEDLCGGYSVGLCPAMLPI--NGSLLLDYLLNVSFVGVSGDTIMFDENGDPP-GRYDIMNFQKTGegs 455
                       330
                ....*....|....*...
gi 11038637 361 --LVQVGIYNGTHVIPND 376
Cdd:cd06374 456 ydYVQVGSWKNGSLKMDD 473
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
29-368 6.32e-06

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: 49.58  E-value: 6.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  29 IGAVLSTRKHE--QMFREAVNQANKRHGSwKIQLNATSV---THKPNAIQMALSVCeDLISSQVYAILVSHPPTPNDhft 103
Cdd:cd06380   2 IGAIFDSGEDQvqTAFRYAIDRHNSNNNN-RFRLFPLTEridITNADSFSVSRAIC-SQLSRGVFAIFGSSDASSLN--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 104 pTPVSYTAGFyRIPVlglttrmsiysdksIHLSFLRTVP--PYSHQSSVW-------FEMMRVYSWNHIILLVsDDHEGR 174
Cdd:cd06380  77 -TIQSYSDTF-HMPY--------------ITPSFPKNEPsdSNPFELSLRpsyieaiVDLIRHYGWKKVVYLY-DSDEGL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 175 AaqkRLETLLE---ERES---KAEKVLQFDPGtKNVTALLMEA-KELEARVIILSASEDDAATVYRAAAMLNMTGSGYVW 247
Cdd:cd06380 140 L---RLQQLYDylkEKSNisvRVRRVRNVNDA-YEFLRTLRELdREKEDKRIVLDLSSERYQKILEQIVEDGMNRRNYHY 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 248 LVGE---REISGNALRYAPDGILGLQLINGKN----------------------------ESAHISDAVGVVAQAVHELL 296
Cdd:cd06380 216 LLANldfLDLDLERFLHGGVNITGFQLVDTNNktvkdflqrwkkldpreypgagtdtipyEAALAVDAVLVIAEAFQSLL 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 297 eKENIT--------------DPPRGC-VGNTNIWKTGPLFKRVLMSSKYaDGVTGRVEFNEDGDRKfaNYS--IMNLQ-N 358
Cdd:cd06380 296 -RQNDDifrftfhgelynngSKGIDCdPNPPLPWEHGKAIMKALKKVRF-EGLTGNVQFDDFGQRK--NYTldVIELTsN 371
                       410
                ....*....|
gi 11038637 359 RKLVQVGIYN 368
Cdd:cd06380 372 RGLRKIGTWS 381
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
456-596 6.89e-06

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


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 47.96  E-value: 6.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 456 YGFCIDLLIKLARTMNFTYEVHLvadgkfgtqervnnsnkKEWNGMMGELLSGQADMIvAPLTINNERAQYIEFSKPFKY 535
Cdd:cd13704  25 TGFNVDLLRAIAEEMGLKVEIRL-----------------GPWSEVLQALENGEIDVL-IGMAYSEERAKLFDFSDPYLE 86
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11038637 536 QGLTILVKKEiprstldsfmQPFQSTLWLLVGLSVHVVA--VM-LYLLDRFSPFGRFKVNSEEE 596
Cdd:cd13704  87 VSVSIFVRKG----------SSIINSLEDLKGKKVAVQRgdIMhEYLKERGLGINLVLVDSPEE 140
PBP2_YxeM cd13709
Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein ...
497-554 7.33e-06

Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein fold; This group contains cystine-binding domain (YxeM) of a periplasmic receptor-dependent ATP-binding cassette transporter and its closely related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270427 [Multi-domain]  Cd Length: 227  Bit Score: 48.11  E-value: 7.33e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 11038637 497 EWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEipRSTLDSF 554
Cdd:cd13709  47 DFSGLFGMLDSGKVDTIANQITITPERQEKYDFSEPYVYDGAQIVVKKD--NNSIKSL 102
PBP1_GC_G-like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
111-249 8.81e-06

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


Pssm-ID: 380595 [Multi-domain]  Cd Length: 390  Bit Score: 49.03  E-value: 8.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 111 AGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILL---VSDDHEGRAAQ--KRLETLLE 185
Cdd:cd06372  88 ASEWNIPMFGFVGQSPKLDDRDVYDTYVKLVPPLQRIGEVLVKTLQFFGWTHVAMFggsSATSTWDKVDElwKSVENQLK 167
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11038637 186 ERESKAEKVlQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLV 249
Cdd:cd06372 168 FNFNVTAKV-KYDTSNPDLLQENLRYISSVARVIVLICSSEDARSILLEAEKLGLMDGEYVFFL 230
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
505-552 1.08e-05

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


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 47.69  E-value: 1.08e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 11038637 505 LLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLD 552
Cdd:cd01000  66 LQSGKVDLIIATMTITPERAKEVDFSVPYYADGQGLLVRKDSKIKSLE 113
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
656-792 1.19e-05

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: 47.33  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 656 VLDRPEERITGINDprLRNPSdkfiYATVKQSSVDIYFRRqvelstmyRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAV 735
Cdd:cd00997  92 ILVPNTPLINSVND--LYGKR----VATVAGSTAADYLRR--------HDIDVVEVPNLEAAYTALQDKDADAVVFDAPV 157
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 11038637 736 LEFEASQ--KCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTW 792
Cdd:cd00997 158 LRYYAAHdgNGKAEVTGSVFLEENYGIVFPTGSPLRKPINQALLNLREDGTYDELYEKW 216
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
102-247 1.25e-05

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


Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 48.71  E-value: 1.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 102 FTPTPVSYTAGFYRIPVL-------GLTTRMSIYSdksiHLSflRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGR 174
Cdd:cd06386  83 YAAAPVARLASHWNLPMLsagalaaGFSHKDSEYS----HLT--RVAPAYAKMGEMFLALFRHHHWSRAFLVYSDDKLER 156
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11038637 175 AAQKRLETLLE--ERESKAEKVLQFDPgTKNVTA----LLMEAKEleaRVIILSASEDDAATVYRAAAMLNMTGSGYVW 247
Cdd:cd06386 157 NCYFTLEGVHEvfQEEGLHTSIYSFDE-TKDLDLeeivRNIQASE---RVVIMCASSDTIRSIMLVAHRHGMTNGDYAF 231
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
114-248 2.30e-05

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: 47.89  E-value: 2.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 114 YRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERE---SK 190
Cdd:cd06375 133 FQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNiciAT 212
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 11038637 191 AEKVlqfdpGTKN--------VTALLmeaKELEARVIILSASEDDAATVYRAAAMLNMTgsgYVWL 248
Cdd:cd06375 213 AEKV-----GRSAdrksfdgvIRELL---QKPNARVVVLFTRSDDARELLAAAKRLNAS---FTWV 267
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
497-552 2.38e-05

Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270431 [Multi-domain]  Cd Length: 218  Bit Score: 46.51  E-value: 2.38e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 11038637 497 EWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLD 552
Cdd:cd13713  47 AWDGIIAGLWAGRYDIIIGSMTITEERLKVVDFSNPYYYSGAQIFVRKDSTITSLA 102
PBP2_GlnP cd13619
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ...
457-544 2.85e-05

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: 46.15  E-value: 2.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVhlvadgkfgtqervnnsNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13619  24 GIDVDLLNAIAKDQGFKVEL-----------------KPMGFDAAIQAVQSGQADGVIAGMSITDERKKTFDFSDPYYDS 86

                ....*...
gi 11038637 537 GLTILVKK 544
Cdd:cd13619  87 GLVIAVKK 94
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
498-545 3.13e-05

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 46.64  E-value: 3.13e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 11038637  498 WNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKE 545
Cdd:PRK11260  89 WDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTVSGIQALVKKG 136
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
164-242 5.37e-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: 5.37e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11038637 164 ILLVSDDHeGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTG 242
Cdd:cd19980 141 FLAENDDY-GRGAAEAFKKALKAKGVKVVATEYFDQGQTDFTTQLTKLKAANPDAIFVVAETEDGALILKQARELGLKQ 218
PBP2_Arg_3 cd13622
Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding ...
456-534 5.64e-05

Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding fold; This subgroup is similar to the HisJ-like family that comprises the periplasmic substrate-binding proteins, including the lysine-, arginine-, ornithine-binding protein (LAO) and the histidine-binding protein (HisJ), which serve as initial receptors for active transport. HisJ and LAO proteins belong to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270340 [Multi-domain]  Cd Length: 222  Bit Score: 45.37  E-value: 5.64e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11038637 456 YGFCIDLLIKLARTMNFTYEVHLVadgkfgtqervnnsnkkEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFK 534
Cdd:cd13622  25 FGFDIDLMNEICKRIQRTCQYKPM-----------------RFDDLLAALNNGKVDVAISSISITPERSKNFIFSLPYL 86
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
457-542 6.36e-05

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: 45.41  E-value: 6.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVhlvadgkfgtqERVNNsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd00997  25 GFSIDLWRAIAERLGWETEY-----------VRVDS-----VSALLAAVAEGEADIAIAAISITAEREAEFDFSQPIFES 88

                ....*.
gi 11038637 537 GLTILV 542
Cdd:cd00997  89 GLQILV 94
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
129-368 1.15e-04

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: 45.70  E-value: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 129 SDKSIHLSFLRTVPPYSHQS-SVWfEMMRVYSWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPG------- 200
Cdd:cd06370 106 SDKSLYPTFARTIPPDSQISkSVI-ALLKHFNWNKVSIVYENETKWSKIADTIKELLELNNIEINHEEYFPDPypyttsh 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 201 TKNVTALLMEAKElEARVIILSASEDDAATVYRAAAMLNMTGSG---YVWLVGEREISGNALRYAPDGILGL-------- 269
Cdd:cd06370 185 GNPFDKIVEETKE-KTRIYVFLGDYSLLREFMYYAEDLGLLDNGdyvVIGVELDQYDVDDPAKYPNFLSGDYtkndtkea 263
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 270 ------------------------QLINGKN---------------------ESAHISDAVGVVAQAVHELLEKEniTDP 304
Cdd:cd06370 264 leafrsvlivtpspptnpeyekftKKVKEYNklppfnfpnpegiektkevpiYAAYLYDAVMLYARALNETLAEG--GDP 341
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11038637 305 PRGcvgnTNIWKTgpLFKRVLMSskyadgVTG-RVEFNEDGDRKFaNYSIMNLQNRKLVQVGIYN 368
Cdd:cd06370 342 RDG----TAIISK--IRNRTYES------IQGfDVYIDENGDAEG-NYTLLALKPNKGTNDGSYG 393
PBP2_Peb1a_like cd13691
Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 ...
456-545 1.17e-04

Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 periplasmic-binding protein fold; This group includes periplasmic aspartate/glutamate binding domain Peb1a and its closely related protein. The Peb1a is an important virulence factor in the food-borne human pathogen Campylobacter jejuni, which has a major role in adherence and host colonization. The Peb1a 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: 270409 [Multi-domain]  Cd Length: 228  Bit Score: 44.75  E-value: 1.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 456 YGFCIDLLIKLArtmnftyEVHLVADGKFGTqerVNNSNKkewngmmGELL-SGQADMIVAPLTINNERAQYIEFSKPFK 534
Cdd:cd13691  32 EGMEVDLARKLA-------KKGDGVKVEFTP---VTAKTR-------GPLLdNGDVDAVIATFTITPERKKSYDFSTPYY 94
                        90
                ....*....|.
gi 11038637 535 YQGLTILVKKE 545
Cdd:cd13691  95 TDAIGVLVEKS 105
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
711-792 1.53e-04

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: 44.10  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 711 YESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCD-LVTTGELFFRSGFGIGMRK-DSPWKQNVSLSILKSHENGFMEDL 788
Cdd:cd13629 137 FDDEAAAVLEVVNGKADAFIYDQPTPARFAKKNDPtLVALLEPFTYEPLGFAIRKgDPDLLNWLNNFLKQIKGDGTLDEL 216

                ....
gi 11038637 789 DKTW 792
Cdd:cd13629 217 YDKW 220
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
8-286 2.06e-04

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: 44.60  E-value: 2.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637   8 TLALLFSCSvARAACDPKIVNIGAVLSTRKHEQMFrEAVNQAN-KRHGSWKIQLNAT---SVTHKPNAIQMALSVCEDLI 83
Cdd:cd04509   1 KVGVLFAVH-GKGPSGVPCGDIVAQYGIQRFEAME-QALDDINaDPNLLPNNTLGIViydDCCDPKQALEQSNKFVNDLI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637  84 SSQVYAILVSHPpTPNDHFTPTPVSYTAG---------------FYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQS 148
Cdd:cd04509  79 QKDTSDVRCTNG-EPPVFVKPEGIKGVIGhlcssvtipvsnileLFGIPQITYAATAPELSDDRGYQLFLRVVPLDSDQA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 149 SVWFEMMRVYSWNHIILLVSddhEGRAAQKRLETLLEERESKAEKVLQFD-----PGTKNVTALLME-AKELEARVIILS 222
Cdd:cd04509 158 PAMADIVKEKVWQYVSIVHD---EGQYGEGGARAFQDGLKKGGLCIAFSDgitagEKTKDFDRLVARlKKENNIRFVVYF 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11038637 223 ASEDDAATVYRAAAMLNMTGSgYVWL----VGEREISGNALRYAPDGILGLQLINGKNESAHISDAVG 286
Cdd:cd04509 235 GYHPEMGQILRAARRAGLVGK-FQFMgsdgWANVSLSLNIAEESAEGLITIKPKVWFVIAALYADAPG 301
PBP2_ml15202_like cd13701
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
457-542 2.59e-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: 43.60  E-value: 2.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVAdgkfgtqervnnsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFkYQ 536
Cdd:cd13701  27 GWEIDLIDALCARLDARCEITPVA-----------------WDGIIPALQSGKIDMIWNSMSITDERKKVIDFSDPY-YE 88

                ....*.
gi 11038637 537 GLTILV 542
Cdd:cd13701  89 TPTAIV 94
PBP2_AatB_like cd00996
Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong ...
497-553 3.33e-04

Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong to the type 2 periplasmic binding fold protein superfamily; This subfamily includes periplasmic binding domain of ATP-binding cassette transporter-like systems that serve as initial receptors in the ABC transport of amino acids and their derivatives in eubacteria. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The Abp proteins belong to the PBPI 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: 270217 [Multi-domain]  Cd Length: 227  Bit Score: 43.34  E-value: 3.33e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 11038637 497 EWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDS 553
Cdd:cd00996  51 DWDMKETELNSGNIDLIWNGLTITDERKKKVAFSKPYLENRQIIVVKKDSPINSKAD 107
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
457-533 5.31e-04

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: 42.67  E-value: 5.31e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11038637 457 GFCIDLLIKLARTMNFTYEVhlvadgkfgtqerVNNSnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPF 533
Cdd:cd01001  26 GFDIDLANALCKRMKVKCEI-------------VTQP----WDGLIPALKAGKYDAIIASMSITDKRRQQIDFTDPY 85
PBP2_Mlr3796_like cd13695
The substrate-binding domain of putative amino aicd transporter; the type 2 periplasmic ...
478-552 6.03e-04

The substrate-binding domain of putative amino aicd transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Mesorhizobium loti and its related proteins. The putative Mlr3796-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270413 [Multi-domain]  Cd Length: 232  Bit Score: 42.55  E-value: 6.03e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 11038637 478 LVADGKFGTQER---VNNSNKKEWNGmmgeLLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLD 552
Cdd:cd13695  40 IIAKALFGDPQKvefVNQSSDARIPN----LTTDKVDITCQFMTVTAERAQQVAFTIPYYREGVALLTKADSKYKDYD 113
PBP2_SMa0082_like cd01072
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ...
505-573 6.94e-04

The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Sinorhizobium meliloti and its related proteins. The putative SMa0082-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270233 [Multi-domain]  Cd Length: 238  Bit Score: 42.25  E-value: 6.94e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 11038637 505 LLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSfmqpfqstlwlLVGLSVHVV 573
Cdd:cd01072  68 LQTGKVDMLIASLGITPERAKVVDFSQPYAAFYLGVYGPKDAKVKSPAD-----------LKGKTVGVT 125
PBP2_Ngo0372_TcyA cd13711
Substrate binding domain of ABC transporters involved in cystine import; the type 2 ...
497-554 8.10e-04

Substrate binding domain of ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold; This subgroup includes cystine-binding domain of periplasmic receptor-dependent ATP-binding cassette transporters from Neisseria gonorrhoeae and Bacillus subtilis and their related proteins. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270429 [Multi-domain]  Cd Length: 222  Bit Score: 41.90  E-value: 8.10e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 11038637 497 EWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEipRSTLDSF 554
Cdd:cd13711  48 QWDSMIAGLDAGRFDVVANQVGITDERKKKYDFSTPYIYSRAVLIVRKD--NSDIKSF 103
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
496-545 8.11e-04

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


Pssm-ID: 270338 [Multi-domain]  Cd Length: 227  Bit Score: 41.94  E-value: 8.11e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 11038637 496 KEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKE 545
Cdd:cd13620  53 MDFDNLLASLQSGKVDMAISGMTPTPERKKSVDFSDVYYEAKQSLLVKKA 102
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
505-545 8.40e-04

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


Pssm-ID: 270408 [Multi-domain]  Cd Length: 231  Bit Score: 41.87  E-value: 8.40e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 11038637 505 LLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKE 545
Cdd:cd13690  67 LQNGTVDLVVATYSITPERRKQVDFAGPYYTAGQRLLVRAG 107
PBP1_ABC_ligand_binding-like cd06335
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
173-305 1.23e-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: 42.21  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 173 GRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMtgsgYVWLVGE- 251
Cdd:cd06335 151 GQGGLKDVEAALKKRGITPVATESFKIGDTDMTPQLLKAKDAGADVILVYGLGPDLAQILKAMEKLGW----KVPLVGSw 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 252 -------REISGNALryapDGILGLQLIN----------------GKNESAHIS---------DAVGVVAQAVhellEKE 299
Cdd:cd06335 227 glsmpnfIELAGPLA----EGTIMTQTFIedyltprakkfidaykKKYGTDRIPspvsaaqgyDAVYLLAAAI----KQA 298

                ....*.
gi 11038637 300 NITDPP 305
Cdd:cd06335 299 GSTDGK 304
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
457-544 1.31e-03

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


Pssm-ID: 270225 [Multi-domain]  Cd Length: 230  Bit Score: 41.46  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVAdgkfgtqervnnsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSkPFKYQ 536
Cdd:cd01004  26 GFDVDLAKAIAKRLGLKVEIVNVS-----------------FDGLIPALQSGRYDIIMSGITDTPERAKQVDFV-DYMKD 87

                ....*...
gi 11038637 537 GLTILVKK 544
Cdd:cd01004  88 GLGVLVAK 95
PBP2_Ehub_like cd01002
Substrate binding domain of ectoine/hydroxyectoine specific ABC transport system; the type 2 ...
497-554 1.47e-03

Substrate binding domain of ectoine/hydroxyectoine specific ABC transport system; the type 2 periplasmic binding protein fold; This family represents the periplasmic substrate-binding component of ABC transport systems that involved in uptake of osmoprotectants (also termed compatible solutes) such as ectoine and hydroxyectoine. To counteract the efflux of water, bacteria and archaea accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain 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.


Pssm-ID: 270223 [Multi-domain]  Cd Length: 242  Bit Score: 41.50  E-value: 1.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 11038637 497 EWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRStLDSF 554
Cdd:cd01002  57 EFGSLIPGLQAGRFDVIAAGMFITPERCEQVAFSEPTYQVGEAFLVPKGNPKG-LHSY 113
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
505-555 1.77e-03

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: 41.08  E-value: 1.77e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 11038637 505 LLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFM 555
Cdd:cd13688  70 LTSGTIDLECGATTNTLERRKLVDFSIPIFVAGTRLLVRKDSGLNSLEDLA 120
PBP2_AA_binding_like_1 cd13625
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
498-532 2.56e-03

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


Pssm-ID: 270343 [Multi-domain]  Cd Length: 230  Bit Score: 40.44  E-value: 2.56e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 11038637 498 WNGMMGELLSGQADMIVAPLTINNERAQYIEFSKP 532
Cdd:cd13625  52 WSGILPGLLAGKFDMVATSVTITKERAKRFAFTLP 86
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
457-574 2.63e-03

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: 40.27  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADgkfgtqervnnsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFkYQ 536
Cdd:cd01009  23 GFEYELAKAFADYLGVELEIVPADN----------------LEELLEALEEGKGDLAAAGLTITPERKKKVDFSFPY-YY 85
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 11038637 537 GLTILV-KKEIPRSTldsfmqpfqsTLWLLVGLSVHVVA 574
Cdd:cd01009  86 VVQVLVyRKGSPRPR----------SLEDLSGKTIAVRK 114
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
457-574 3.02e-03

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 41.20  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFTYEVHLVADgkfgtqervnnsnkkeWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:COG4623  44 GFEYELAKAFADYLGVKLEIIVPDN----------------LDELLPALNAGEGDIAAAGLTITPERKKQVRFSPPYYSV 107
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 11038637 537 GLTILVKKEIPRSTldsfmqpfqsTLWLLVGLSVHVVA 574
Cdd:COG4623 108 SQVLVYRKGSPRPK----------SLEDLAGKTVHVRA 135
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
197-354 3.65e-03

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


Pssm-ID: 380565 [Multi-domain]  Cd Length: 334  Bit Score: 40.59  E-value: 3.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 197 FDPGTKNVTALLMEAKELEARVIILSASEDDAATVYRAAAMLNMTGSgyvwLVGereisgnalryaPDGILGLQLIN--G 274
Cdd:cd06342 172 ITPGTTDFSALLTKIKAANPDAVYFGGYYPEAGLLLRQLREAGLKAP----FMG------------GDGIVSPDFIKaaG 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 275 KN--------------------------ESAHIS----------DAVGVVAQAVhellEKENITDPprgcvgntniwktg 318
Cdd:cd06342 236 DAaegvyattpgappeklpaakaflkayKAKFGEppgayaayayDAAQVLLAAI----EKAGSTDR-------------- 297
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 11038637 319 plfKRV---LMSSKYaDGVTGRVEFNEDGDRKFANYSIM 354
Cdd:cd06342 298 ---AAVaaaLRATDF-DGVTGTISFDAKGDLTGPAFTVY 332
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
275-368 3.81e-03

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: 40.77  E-value: 3.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 275 KNESAHISDAVGVVAQAVHELlEKENITDPPRG----CVGNTNI-WKTGPLFKRVLMSSKyADGVTGRVEFNEDGDRKFA 349
Cdd:cd06389 267 KYTSALTYDAVQVMTEAFRNL-RKQRIEISRRGnagdCLANPAVpWGQGVEIERALKQVQ-VEGLSGNIKFDQNGKRINY 344
                        90
                ....*....|....*....
gi 11038637 350 NYSIMNLQNRKLVQVGIYN 368
Cdd:cd06389 345 TINIMELKTNGPRKIGYWS 363
PBP2_OccT_like cd13699
Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding ...
457-542 4.35e-03

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


Pssm-ID: 270417 [Multi-domain]  Cd Length: 211  Bit Score: 39.66  E-value: 4.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11038637 457 GFCIDLLIKLARTMNFtyEVHLVAdgkfgtqervnnsnkKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQ 536
Cdd:cd13699  26 GFEIDLANVLCERMKV--KCTFVV---------------QDWDGMIPALNAGKFDVIMDAMSITAERKKVIDFSTPYAAT 88

                ....*.
gi 11038637 537 GLTILV 542
Cdd:cd13699  89 PNSFAV 94
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
505-552 4.80e-03

The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270414 [Multi-domain]  Cd Length: 227  Bit Score: 39.67  E-value: 4.80e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 11038637 505 LLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLD 552
Cdd:cd13696  63 LVSGRVDVVVANTTRTLERAKTVAFSIPYVVAGMVVLTRKDSGIKSFD 110
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
505-545 5.47e-03

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: 39.64  E-value: 5.47e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 11038637 505 LLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKE 545
Cdd:cd13694  66 LTSGKVDLILANFTVTPERAEVVDFANPYMKVALGVVSPKD 106
 
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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