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Conserved domains on  [gi|330253582|gb|AEC08676|]
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glutamate receptor 3.5 [Arabidopsis thaliana]

Protein Classification

glutamate receptor( domain architecture ID 14448285)

glutamate receptor is a glutamate-gated receptor that probably acts as a non-selective cation channel and may be involved in light-signal transduction and calcium homeostasis via the regulation of calcium influx into cells

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
44-386 4.81e-130

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: 395.06  E-value: 4.81e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  44 LLAPWELMEN-KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRW 122
Cdd:cd19990   53 ASAALDLIKNkKVEAIIGPQTSEEASFVAELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGW 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 123 REVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSL 202
Cdd:cd19990  133 RRVVLIYEDDDYGSGIIPYLSDALQEVGSRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 203 GMMGSGYVWITTDWLLTALDSMeplDPRALDLLQGVVAFRHYTPESDNKRQFKGRWKN-LRFKESLKSDDGFNSYALYAY 281
Cdd:cd19990  213 GMMEKGYVWIVTDGITNLLDSL---DSSTISSMQGVIGIKTYIPESSEFQDFKARFRKkFRSEYPEEENAEPNIYALRAY 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 282 DSVWLVARALDVFFSQGNTVTFSndpslrntndsgiklsklhifNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYD 361
Cdd:cd19990  290 DAIWALAHAVEKLNSSGGNISVS---------------------DSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFE 348
                        330       340
                 ....*....|....*....|....*
gi 330253582 362 ILNIKSTGPLRVGYWSNHTGFSVAP 386
Cdd:cd19990  349 IVNVIGKGYRELGFWSPGSGFSEVL 373
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
427-770 1.09e-71

Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily contains the glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


:

Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 235.88  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 427 KPLKIGVPNRVSYKNYASKDKNPLG----VKGFCIDIFEAAIQLLPYPVPRTYILYGDgkkNPSYDNLISEVAANIFDVA 502
Cdd:cd13686    1 KKLRIGVPVKSGFKEFVKVTRDPITnstsVTGFCIDVFEAAVKRLPYAVPYEFIPFND---AGSYDDLVYQVYLKKFDAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 503 VGDVTIITNRTKFVDFTQPFIESGLVVVAPVKgaksspwsflkpftiemwavtgalflfvgaviwilehrfneefrgppr 582
Cdd:cd13686   78 VGDITITANRSLYVDFTLPYTESGLVMVVPVK------------------------------------------------ 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 583 rqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsRIEGMDTLIASNEPIGVQDG 662
Cdd:cd13686  110 ------------------------------------------------------------DVTDIEELLKSGEYVGYQRG 129
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 663 TFAWKFLVNELNiAPSRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSnSNCKFRT-VGQEFTRTGWGFAFQR 741
Cdd:cd13686  130 SFVREYLEEVLF-DESRLKPYGSPEEYAEALSKGS----IAAAFDEIPYLKLFLA-KYCKKYTmVGPTYKTGGFGFAFPK 203
                        330       340
                 ....*....|....*....|....*....
gi 330253582 742 DSPLAVDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd13686  204 GSPLVADVSRAILKVTEGGKLQQIENKWF 232
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
44-386 4.81e-130

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: 395.06  E-value: 4.81e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  44 LLAPWELMEN-KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRW 122
Cdd:cd19990   53 ASAALDLIKNkKVEAIIGPQTSEEASFVAELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGW 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 123 REVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSL 202
Cdd:cd19990  133 RRVVLIYEDDDYGSGIIPYLSDALQEVGSRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 203 GMMGSGYVWITTDWLLTALDSMeplDPRALDLLQGVVAFRHYTPESDNKRQFKGRWKN-LRFKESLKSDDGFNSYALYAY 281
Cdd:cd19990  213 GMMEKGYVWIVTDGITNLLDSL---DSSTISSMQGVIGIKTYIPESSEFQDFKARFRKkFRSEYPEEENAEPNIYALRAY 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 282 DSVWLVARALDVFFSQGNTVTFSndpslrntndsgiklsklhifNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYD 361
Cdd:cd19990  290 DAIWALAHAVEKLNSSGGNISVS---------------------DSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFE 348
                        330       340
                 ....*....|....*....|....*
gi 330253582 362 ILNIKSTGPLRVGYWSNHTGFSVAP 386
Cdd:cd19990  349 IVNVIGKGYRELGFWSPGSGFSEVL 373
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
49-368 3.26e-87

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: 281.97  E-value: 3.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582   49 ELMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVA 127
Cdd:pfam01094  45 DLLKGEVVAIIGPSCSSVASAVASLANEWKVPLISYGSTSPALSDLNrYPTFLRTTPSDTSQADAIVDILKHFGWKRVAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  128 IFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGS 207
Cdd:pfam01094 125 IYSDDDYGESGLQALEDALRERGIRVAYKAVIPPAQDDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  208 GYVWITTDWLLTALDSMEPLDpraLDLLQGVVAFRHYTPESDNKRQFKGrWKNLRFKESLKSDDGFN-SYALYAYDSVWL 286
Cdd:pfam01094 205 GYVWIATDGLTTSLVILNPST---LEAAGGVLGFRLHPPDSPEFSEFFW-EKLSDEKELYENLGGLPvSYGALAYDAVYL 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  287 VARALDvffsqgntvtfsndpSLRNTNDSGIKLSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIK 366
Cdd:pfam01094 281 LAHALH---------------NLLRDDKPGRACGALGPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLN 345

                  ..
gi 330253582  367 ST 368
Cdd:pfam01094 346 GS 347
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
427-770 1.09e-71

Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily contains the glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 235.88  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 427 KPLKIGVPNRVSYKNYASKDKNPLG----VKGFCIDIFEAAIQLLPYPVPRTYILYGDgkkNPSYDNLISEVAANIFDVA 502
Cdd:cd13686    1 KKLRIGVPVKSGFKEFVKVTRDPITnstsVTGFCIDVFEAAVKRLPYAVPYEFIPFND---AGSYDDLVYQVYLKKFDAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 503 VGDVTIITNRTKFVDFTQPFIESGLVVVAPVKgaksspwsflkpftiemwavtgalflfvgaviwilehrfneefrgppr 582
Cdd:cd13686   78 VGDITITANRSLYVDFTLPYTESGLVMVVPVK------------------------------------------------ 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 583 rqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsRIEGMDTLIASNEPIGVQDG 662
Cdd:cd13686  110 ------------------------------------------------------------DVTDIEELLKSGEYVGYQRG 129
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 663 TFAWKFLVNELNiAPSRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSnSNCKFRT-VGQEFTRTGWGFAFQR 741
Cdd:cd13686  130 SFVREYLEEVLF-DESRLKPYGSPEEYAEALSKGS----IAAAFDEIPYLKLFLA-KYCKKYTmVGPTYKTGGFGFAFPK 203
                        330       340
                 ....*....|....*....|....*....
gi 330253582 742 DSPLAVDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd13686  204 GSPLVADVSRAILKVTEGGKLQQIENKWF 232
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
548-802 1.68e-63

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: 214.86  E-value: 1.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  548 TIEMWAVTGALFLFVGAVIWILEHRFNEEFRGP-----PRRQIITVFWFSFSTMFFS-HRENTVSTLGRFVLLVWLFVVL 621
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPleteeNRFTLSNSLWFSFGALVQQgHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  622 IINSSYTASLTSILTVQQLTSRIEGMDTLiASNEPIGVQDGTFAWKFLVNELNIAPSRIIPLKDEEEYLSALQRGPRGGG 701
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSPIQSLEDL-AKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  702 VAAIVDELPYIKALLSNS------NCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHE 775
Cdd:pfam00060 160 VALVRNGIYAYALLSENYylfqreCCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGE 239
                         250       260
                  ....*....|....*....|....*..
gi 330253582  776 CTMQISDTENYQISVQSFWGLFLICGV 802
Cdd:pfam00060 240 CDSKSSASSSSQLGLKSFAGLFLILGI 266
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
643-772 2.81e-41

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: 147.44  E-value: 2.81e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582   643 RIEGMDTLIAS-NEPIGVQDGTFAWKFLVNELNIAPSRIIPL-KDEEEYLSALQRGPRGGGVA--AIVDELPYIKALLSN 718
Cdd:smart00079   1 PITSVEDLAKQtKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYmKSPEVFVKSYAEGVQRVRVSnyAFIMESPYLDYELSR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 330253582   719 sNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTY 772
Cdd:smart00079  81 -NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
52-373 4.87e-20

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: 91.92  E-value: 4.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSY-FRWREVVAIF 129
Cdd:COG0683   69 QDKVDAIVGPLSSGVALAVAPVAEEAGVPLISPSATAPALTGPEcSPYVFRTAPSDAQQAEALADYLAKkLGAKKVALLY 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 130 VDDEYGRNGISVLGDALAKKRAKISYKAAFPPGAdnSSISDLLAsvNLMESR---IFVVHVNPDSGLnifsVAKSLGMMG 206
Cdd:COG0683  149 DDYAYGQGLAAAFKAALKAAGGEVVGEEYYPPGT--TDFSAQLT--KIKAAGpdaVFLAGYGGDAAL----FIKQAREAG 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 207 sgyvwittdwlltaldsmepldpraldlLQGVVAfrhytpesdnkRQFKGRWKNlrfkeslKSDDGFNSYALYAYDSVWL 286
Cdd:COG0683  221 ----------------------------LKGPLN-----------KAFVKAYKA-------KYGREPSSYAAAGYDAALL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 287 VARALDvffsQGNTVTfsndpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYdILNIK 366
Cdd:COG0683  255 LAEAIE----KAGSTD-------------------------REAVRDALEGLKFDGVTGPITFDPDGQGVQPVY-IVQVK 304

                 ....*..
gi 330253582 367 STGPLRV 373
Cdd:COG0683  305 ADGKFVV 311
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
642-773 1.80e-12

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 67.70  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 642 SRIEGMDTLiaSNEPIGVQDGTFAWKFLVNelNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDELPYIKALLS-NSN 720
Cdd:COG0834   96 SGIKSLADL--KGKTVGVQAGTTYEEYLKK--LGPNAEIVEFDSYAEALQALASG----RVDAVVTDEPVAAYLLAkNPG 167
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330253582 721 CKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKWLTYD 773
Cdd:COG0834  168 DDLKIVGEPLSGEPYGIAVRKGDPeLLEAVNKALAALKADGTLDKILEKWFGED 221
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
44-386 4.81e-130

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: 395.06  E-value: 4.81e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  44 LLAPWELMEN-KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRW 122
Cdd:cd19990   53 ASAALDLIKNkKVEAIIGPQTSEEASFVAELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGW 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 123 REVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSL 202
Cdd:cd19990  133 RRVVLIYEDDDYGSGIIPYLSDALQEVGSRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKL 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 203 GMMGSGYVWITTDWLLTALDSMeplDPRALDLLQGVVAFRHYTPESDNKRQFKGRWKN-LRFKESLKSDDGFNSYALYAY 281
Cdd:cd19990  213 GMMEKGYVWIVTDGITNLLDSL---DSSTISSMQGVIGIKTYIPESSEFQDFKARFRKkFRSEYPEEENAEPNIYALRAY 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 282 DSVWLVARALDVFFSQGNTVTFSndpslrntndsgiklsklhifNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYD 361
Cdd:cd19990  290 DAIWALAHAVEKLNSSGGNISVS---------------------DSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFE 348
                        330       340
                 ....*....|....*....|....*
gi 330253582 362 ILNIKSTGPLRVGYWSNHTGFSVAP 386
Cdd:cd19990  349 IVNVIGKGYRELGFWSPGSGFSEVL 373
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
49-368 3.26e-87

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: 281.97  E-value: 3.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582   49 ELMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVA 127
Cdd:pfam01094  45 DLLKGEVVAIIGPSCSSVASAVASLANEWKVPLISYGSTSPALSDLNrYPTFLRTTPSDTSQADAIVDILKHFGWKRVAL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  128 IFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGS 207
Cdd:pfam01094 125 IYSDDDYGESGLQALEDALRERGIRVAYKAVIPPAQDDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGE 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  208 GYVWITTDWLLTALDSMEPLDpraLDLLQGVVAFRHYTPESDNKRQFKGrWKNLRFKESLKSDDGFN-SYALYAYDSVWL 286
Cdd:pfam01094 205 GYVWIATDGLTTSLVILNPST---LEAAGGVLGFRLHPPDSPEFSEFFW-EKLSDEKELYENLGGLPvSYGALAYDAVYL 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  287 VARALDvffsqgntvtfsndpSLRNTNDSGIKLSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIK 366
Cdd:pfam01094 281 LAHALH---------------NLLRDDKPGRACGALGPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLN 345

                  ..
gi 330253582  367 ST 368
Cdd:pfam01094 346 GS 347
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
427-770 1.09e-71

Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily contains the glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 235.88  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 427 KPLKIGVPNRVSYKNYASKDKNPLG----VKGFCIDIFEAAIQLLPYPVPRTYILYGDgkkNPSYDNLISEVAANIFDVA 502
Cdd:cd13686    1 KKLRIGVPVKSGFKEFVKVTRDPITnstsVTGFCIDVFEAAVKRLPYAVPYEFIPFND---AGSYDDLVYQVYLKKFDAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 503 VGDVTIITNRTKFVDFTQPFIESGLVVVAPVKgaksspwsflkpftiemwavtgalflfvgaviwilehrfneefrgppr 582
Cdd:cd13686   78 VGDITITANRSLYVDFTLPYTESGLVMVVPVK------------------------------------------------ 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 583 rqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsRIEGMDTLIASNEPIGVQDG 662
Cdd:cd13686  110 ------------------------------------------------------------DVTDIEELLKSGEYVGYQRG 129
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 663 TFAWKFLVNELNiAPSRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSnSNCKFRT-VGQEFTRTGWGFAFQR 741
Cdd:cd13686  130 SFVREYLEEVLF-DESRLKPYGSPEEYAEALSKGS----IAAAFDEIPYLKLFLA-KYCKKYTmVGPTYKTGGFGFAFPK 203
                        330       340
                 ....*....|....*....|....*....
gi 330253582 742 DSPLAVDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd13686  204 GSPLVADVSRAILKVTEGGKLQQIENKWF 232
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
548-802 1.68e-63

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: 214.86  E-value: 1.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  548 TIEMWAVTGALFLFVGAVIWILEHRFNEEFRGP-----PRRQIITVFWFSFSTMFFS-HRENTVSTLGRFVLLVWLFVVL 621
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPleteeNRFTLSNSLWFSFGALVQQgHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  622 IINSSYTASLTSILTVQQLTSRIEGMDTLiASNEPIGVQDGTFAWKFLVNELNIAPSRIIPLKDEEEYLSALQRGPRGGG 701
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSPIQSLEDL-AKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  702 VAAIVDELPYIKALLSNS------NCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHE 775
Cdd:pfam00060 160 VALVRNGIYAYALLSENYylfqreCCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGE 239
                         250       260
                  ....*....|....*....|....*..
gi 330253582  776 CTMQISDTENYQISVQSFWGLFLICGV 802
Cdd:pfam00060 240 CDSKSSASSSSQLGLKSFAGLFLILGI 266
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
643-772 2.81e-41

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: 147.44  E-value: 2.81e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582   643 RIEGMDTLIAS-NEPIGVQDGTFAWKFLVNELNIAPSRIIPL-KDEEEYLSALQRGPRGGGVA--AIVDELPYIKALLSN 718
Cdd:smart00079   1 PITSVEDLAKQtKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYmKSPEVFVKSYAEGVQRVRVSnyAFIMESPYLDYELSR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 330253582   719 sNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTY 772
Cdd:smart00079  81 -NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
41-286 2.55e-35

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: 137.16  E-value: 2.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  41 AVDLLApwelmENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSY 119
Cdd:cd06269   59 ACDLLA-----AAKVVAILGPGCSASAAPVANLARHWDIPVLSYGATAPGLSDKSrYAYFLRTVPPDSKQADAMLALVRR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 120 FRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNsSISDLLASVNLMESRIFVVHVNPDSGLNIFSVA 199
Cdd:cd06269  134 LGWNKVVLIYSDDEYGEFGLEGLEELFQEKGGLITSRQSFDENKDD-DLTKLLRNLRDTEARVIILLASPDTARSLMLEA 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 200 KSLGMMGSGYVWITTDWLltaLDSMEPLDPRALDLLQGVVAFRHYTPESDNKRQF--KGRWKNLRFKESLKSDDGFNSYA 277
Cdd:cd06269  213 KRLDMTSKDYVWFVIDGE---ASSSDEHGDEARQAAEGAITVTLIFPVVKEFLKFsmELKLKSSKRKQGLNEEYELNNFA 289

                 ....*....
gi 330253582 278 LYAYDSVWL 286
Cdd:cd06269  290 AFFYDAVLA 298
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
427-770 5.36e-35

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: 133.65  E-value: 5.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 427 KPLKIGVPNRVSYKNYASKDKNPLGV---KGFCIDIFEAAIQLLPYPVprTYILYGDGK----KNPSYDNLISEVAANIF 499
Cdd:cd00998    1 KTLKVVVPLEPPFVMFVTGSNAVTGNgrfEGYCIDLLKELSQSLGFTY--EYYLVPDGKfgapVNGSWNGMVGEVVRGEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 500 DVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKsspwsflkpftiemwavtgalflfvgaviwilehrfneefrg 579
Cdd:cd00998   79 DLAVGPITITSERSVVIDFTQPFMTSGIGIMIPIRSID------------------------------------------ 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 580 pprrqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsriegmDTLIASNEPIGV 659
Cdd:cd00998  117 --------------------------------------------------------------------DLKRQTDIEFGT 128
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 660 QDGTFAWKFLVNELNIAP--------SRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSNSNCKFRTVGQEFT 731
Cdd:cd00998  129 VENSFTETFLRSSGIYPFyktwmyseARVVFVNNIAEGIERVRKGK----VYAFIWDRPYLEYYARQDPCKLIKTGGGFG 204
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 330253582 732 RTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd00998  205 SIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
70-411 4.90e-31

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: 125.53  E-value: 4.90e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  70 ISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAK 148
Cdd:cd06379   83 VSYTAGFYRIPVIGISARDSAFSDKNiHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETLAET 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 149 KRAKISYKAAFPPGADNssISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTAldSMEPLD 228
Cdd:cd06379  163 KDIKIEKVIEFEPGEKN--FTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIVTEQALAA--SNVPDG 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 229 PRALDLLQGVVAFRHytpesdnkrqfkgrwknLRfkeslksddgfnsyalyayDSVWLVARALDVFFSQGNTVTFSndPs 308
Cdd:cd06379  239 VLGLQLIHGKNESAH-----------------IR-------------------DSVSVVAQAIRELFRSSENITDP--P- 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 309 lRNTNDSGiklsklHIFNEGERFLQVILEMNYT-GLTGQIEFNSEKNRINPAYDILNIKSTG-PLRVGYWSnhtgfsvap 386
Cdd:cd06379  280 -VDCRDDT------NIWKSGQKFFRVLKSVKLSdGRTGRVEFNDKGDRIGAEYDIINVQNPRkLVQVGIYV--------- 343
                        330       340
                 ....*....|....*....|....*
gi 330253582 387 petlYSKPSNTSAKDQRLNEIIWPG 411
Cdd:cd06379  344 ----GSQRPTKSLLSLNDRKIIWPG 364
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
49-284 4.26e-30

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: 122.40  E-value: 4.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVA 127
Cdd:cd06350   89 NIGPPNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSdKIRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVST 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 128 IFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMES-RIFVVHVNPDSGLNIFSVAKSLGMMg 206
Cdd:cd06350  169 VYSDDDYGRSGIEAFEREAKERGICIAQTIVIPENSTEDEIKRIIDKLKSSPNaKVVVLFLTESDARELLKEAKRRNLT- 247
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253582 207 sGYVWITTD-WlltaLDSMEPLDpRALDLLQGVVAFrhyTPESDNKRQFkgrwknlrfkeslksDDGFNSYALYAYDSV 284
Cdd:cd06350  248 -GFTWIGSDgW----GDSLVILE-GYEDVLGGAIGV---VPRSKEIPGF---------------DDYLKSYAPYVIDAV 302
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
54-411 1.87e-27

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: 115.81  E-value: 1.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  54 KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDD 132
Cdd:cd06366   70 PKVMLLGPGCSSVTEPVAEASKYWNLVQLSYAATSPALSDrKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQND 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 133 EYGRNGISVLGDALAKKRAKISYKAAFPPgadnssiSDLLASV-NLMES--RIFVVHVNPDSGLNIFSVAKSLGMMGSGY 209
Cdd:cd06366  150 EVFSSTAEDLEELLEEANITIVATESFSS-------EDPTDQLeNLKEKdaRIIIGLFYEDAARKVFCEAYKLGMYGPKY 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 210 VWI-----TTDWLLTALDSMEPLDPRALDLLQGVVAFRHYTPESDNKRQFKGR----WKNLRFKESLKSDDGFNSYALYA 280
Cdd:cd06366  223 VWIlpgwyDDNWWDVPDNDVNCTPEQMLEALEGHFSTELLPLNPDNTKTISGLtaqeFLKEYLERLSNSNYTGSPYAPFA 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 281 YDSVWLVARALDvffsqgNTVT--FSNDPSLRNTNDSGIKLSKLhifnegerFLQVILEMNYTGLTGQIEFNSEKNRInP 358
Cdd:cd06366  303 YDAVWAIALALN------KTIEklAEYNKTLEDFTYNDKEMADL--------FLEAMNSTSFEGVSGPVSFDSKGDRL-G 367
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 330253582 359 AYDILNIKSTGPLRVGYWsnhtgfsvappetlysKPSNTSAKDQRLNEIIWPG 411
Cdd:cd06366  368 TVDIEQLQGGSYVKVGLY----------------DPNADSLLLLNESSIVWPG 404
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
54-381 1.13e-23

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: 105.45  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  54 KVVAAIGPQSSGIghiiS-HVANEL---HVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAI 128
Cdd:cd06362  107 DVVGVIGAESSSV----SiQVANLLrlfKIPQISYASTSDELSDkERYPYFLRTVPSDSFQAKAIVDILLHFNWTYVSVV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 129 FVDDEYGRNGISVLgdalaKKRAK-----ISYKAAFPPGADNSS----ISDLLASVNlmeSRIFVVHVNPDSGLNIFSVA 199
Cdd:cd06362  183 YSEGSYGEEGYKAF-----KKLARkagicIAESERISQDSDEKDyddvIQKLLQKKN---ARVVVLFADQEDIRGLLRAA 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 200 KSLGMMGSgYVWITTDWLLTALDSMEPLdpraLDLLQGVVAFRHYTPESdnkRQFKGRWKNLR---------FKES---- 266
Cdd:cd06362  255 KRLGASGR-FIWLGSDGWGTNIDDLKGN----EDVALGALTVQPYSEEV---PRFDDYFKSLTpsnntrnpwFREFwqel 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 267 -------------------LKSDDGFN--SYALYAYDSVWLVARALDVFfsqgntvtfsndpsLRN--TNDSGIKLSKLH 323
Cdd:cd06362  327 fqcsfrpsrenscnddkllINKSEGYKqeSKVSFVIDAVYAFAHALHKM--------------HKDlcPGDTGLCQDLMK 392
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253582 324 IFNeGERFLQVILEMNYTGLTG-QIEFNsEKNRINPAYDILNIKSTGP-----LRVGYWSNHTG 381
Cdd:cd06362  393 CID-GSELLEYLLNVSFTGEAGgEIRFD-ENGDGPGRYDIMNFQRNNDgsyeyVRVGVWDQYTQ 454
PBP1_ABC_ligand_binding-like cd06346
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
53-290 5.96e-22

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: 380569 [Multi-domain]  Cd Length: 314  Bit Score: 97.63  E-value: 5.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  53 NKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVD 131
Cdd:cd06346   66 EGVPAIVGAASSGVTLAVASVAVPNGVVQISPSSTSPALTTLEdKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVN 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 132 DEYGRnGIS-VLGDALAKKRAKISYKAAFPPGAdnssiSDLLASVNlmesRIF------VVHV-NPDSGLNIFSVAKSLG 203
Cdd:cd06346  146 NDYGQ-GLAdAFKKAFEALGGTVTASVPYEPGQ-----TSYRAELA----QAAaggpdaLVLIgYPEDGATILREALELG 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 204 MMGSgyVWITTDWLLtaldSMEPLDPRALDLLQGVVAFRHYTPESDNKRQFKGRWKNlrfkeslKSDDGFNSYALYAYDS 283
Cdd:cd06346  216 LDFT--PWIGTDGLK----SDDLVEAAGAEALEGMLGTAPGSPGSPAYEAFAAAYKA-------EYGDDPGPFAANAYDA 282

                 ....*..
gi 330253582 284 VWLVARA 290
Cdd:cd06346  283 VMLLALA 289
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
41-386 6.99e-21

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: 95.89  E-value: 6.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  41 AVDLLapwelMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSY 119
Cdd:cd06352   61 AADLI-----YKRNVDVFIGPACSAAADAVGRLATYWNIPIITWGAVSASFLDKSrYPTLTRTSPNSLSLAEALLALLKQ 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 120 FRWREVVAIFVDDEygrNGISVLGDALAKKRA-----KISYKaAFPPGADNSSISDLLASVNLmESRIFVVHVNPDSGLN 194
Cdd:cd06352  136 FNWKRAAIIYSDDD---SKCFSIANDLEDALNqednlTISYY-EFVEVNSDSDYSSILQEAKK-RARIIVLCFDSETVRQ 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 195 IFSVAKSLGMMGSGYVWITTDWLLTA-----LDSMEPLDPRALDLLQgvvAFRH---------YTPESDN-KRQFKGRWK 259
Cdd:cd06352  211 FMLAAHDLGMTNGEYVFIFIELFKDGfggnsTDGWERNDGRDEDAKQ---AYESllvislsrpSNPEYDNfSKEVKARAK 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 260 NLRFKESLKSDDGFNSYALYAYDSVWLVARALdvffsqgnTVTFSNDPSLRNtndsGIKLSKlHIFNegerflqvileMN 339
Cdd:cd06352  288 EPPFYCYDASEEEVSPYAAALYDAVYLYALAL--------NETLAEGGNYRN----GTAIAQ-RMWN-----------RT 343
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 330253582 340 YTGLTGQIEFNSEKNRiNPAYDILNI-KSTGPLRVGYWSNHTGFSVAP 386
Cdd:cd06352  344 FQGITGPVTIDSNGDR-DPDYALLDLdPSTGKFVVVLTYDGTSNGLVV 390
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
52-373 4.87e-20

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: 91.92  E-value: 4.87e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSY-FRWREVVAIF 129
Cdd:COG0683   69 QDKVDAIVGPLSSGVALAVAPVAEEAGVPLISPSATAPALTGPEcSPYVFRTAPSDAQQAEALADYLAKkLGAKKVALLY 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 130 VDDEYGRNGISVLGDALAKKRAKISYKAAFPPGAdnSSISDLLAsvNLMESR---IFVVHVNPDSGLnifsVAKSLGMMG 206
Cdd:COG0683  149 DDYAYGQGLAAAFKAALKAAGGEVVGEEYYPPGT--TDFSAQLT--KIKAAGpdaVFLAGYGGDAAL----FIKQAREAG 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 207 sgyvwittdwlltaldsmepldpraldlLQGVVAfrhytpesdnkRQFKGRWKNlrfkeslKSDDGFNSYALYAYDSVWL 286
Cdd:COG0683  221 ----------------------------LKGPLN-----------KAFVKAYKA-------KYGREPSSYAAAGYDAALL 254
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 287 VARALDvffsQGNTVTfsndpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYdILNIK 366
Cdd:COG0683  255 LAEAIE----KAGSTD-------------------------REAVRDALEGLKFDGVTGPITFDPDGQGVQPVY-IVQVK 304

                 ....*..
gi 330253582 367 STGPLRV 373
Cdd:COG0683  305 ADGKFVV 311
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
52-289 1.43e-19

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


Pssm-ID: 380492 [Multi-domain]  Cd Length: 298  Bit Score: 90.08  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSY-FRWREVVAIFV 130
Cdd:cd06268   65 DDKVLAVVGHYSSSVTLAAAPIYQEAGIPLISPGSTAPELTEGGGPYVFRTVPSDAMQAAALADYLAKkLKGKKVAILYD 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNssISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMmgsGYV 210
Cdd:cd06268  145 DYDYGKSLADAFKKALKALGGEIVAEEDFPLGTTD--FSAQLTKIKAAGPDVLFLAGYGADAANALKQARELGL---KLP 219
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253582 211 WITTDWLLTaldsmEPLDPRALDLLQGVVAFRHYTPESDNKRQFKgrwKNLRFKEslKSDDGFNSYALYAYDSVWLVAR 289
Cdd:cd06268  220 ILGGDGLYS-----PELLKLGGEAAEGVVVAVPWHPDSPDPPKQA---FVKAYKK--KYGGPPSWRAATAYDATQALAG 288
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
53-384 1.45e-19

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: 92.71  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  53 NKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVD 131
Cdd:cd06365   99 RKLVAFIGDLSSSTSVAMARILGLYKYPQISYGAFDPLLSDkVQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISD 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 132 DEYGRNGISVLGDALAKKRAKISYKAAFPpgADNSSISDLLASVNLMES--RIFVVHVNPDS-GLNIFSVAKSLgmmGSG 208
Cdd:cd06365  179 DDYGEQFSQDLKKEMEKNGICVAFVEKIP--TNSSLKRIIKYINQIIKSsaNVIIIYGDTDSlLELLFRLWEQL---VTG 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 209 YVWITTdwllTALDSMEPLDPRALDLLQGVVAFRHYTPE---------SDNKRQ--------------FKGRWK------ 259
Cdd:cd06365  254 KVWITT----SQWDISTLPFEFYLNLFNGTLGFSQHSGEipgfkeflqSVHPSKypediflktlwesyFNCKWPdqncks 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 260 --NLRFKESLKS------DDGFNSYALYAYDSVWLVARAL-DVFFSQGNTVTFSNDpslrntNDSGIKLSKLHIFNEGER 330
Cdd:cd06365  330 lqNCCGNESLETldvhsfDMTMSRLSYNVYNAVYAVAHALhEMLLCQPKTGPGNCS------DRRNFQPWQLHHYLKKVQ 403
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330253582 331 FLqvilemnyTGLTGQIEFNsEKNRINPAYDILNIKSTgplrvgywSNHTGFSV 384
Cdd:cd06365  404 FT--------NPAGDEVNFD-EKGDLPTKYDILNWQIF--------PNGTGTKV 440
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
49-384 1.09e-18

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: 88.43  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAIGPQSSGIGHIISHVANELHVPFLSfaatdpTLSSLQYPYFLRTTQN---DYFQMN-AITDFVSYFRWRE 124
Cdd:cd06382   56 ELLEEGVAAIFGPSSPSSSDIVQSICDALEIPHIE------TRWDPKESNRDTFTINlypDPDALSkAYADLVKSLNWKS 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 125 VVAIFVDDEygrnGISVLGDALA---KKRAKISYKaAFPPGADNssiSDLLASVNLMESRIFVVHVNPDSGLNIFSVAKS 201
Cdd:cd06382  130 FTILYEDDE----GLIRLQELLKlpkPKDIPITVR-QLDPGDDY---RPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQ 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 202 LGMMGSGYVWITTDWLLTALDsMEPldpraldLLQGVV---AFRHYTPESDNKRQFKGRWKNlRFKESLKSDDGFNSY-- 276
Cdd:cd06382  202 VGMLTEYYHYILTNLDLHTLD-LEP-------FKYSGAnitGFRLVDPENPEVKNVLKDWSK-REKEGFNKDIGPGQItt 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 277 --ALyAYDSVWLVARALDvffsqgntvtfsndpslrntndsgiklsklhifnegerflqvilemnyTGLTGQIEFNSEKN 354
Cdd:cd06382  273 etAL-MYDAVNLFANALK------------------------------------------------EGLTGPIKFDEEGQ 303
                        330       340       350
                 ....*....|....*....|....*....|
gi 330253582 355 RINPAYDILNIKSTGPLRVGYWSNHTGFSV 384
Cdd:cd06382  304 RTDFKLDILELTEGGLVKVGTWNPTDGLNI 333
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
453-769 1.46e-18

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: 88.59  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 453 KGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGL-V 528
Cdd:cd13723   31 EGYCIDLLKELAHILGFSYEIRLVedgKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVsI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 529 VVAPVKGAKSSPWSFLKPFTIEMWAVTGALFLFVGAVIWILEhRFN--EEFRGPP----------RRQIITVFWFSFSTM 596
Cdd:cd13723  111 LYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIA-RFSpyEWYDAHPcnpgsevvenNFTLLNSFWFGMGSL 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 597 FFSHRENTVSTLG-RFVLLVWLFVVLIINSSYTASLTSILTVQQLTSRIEGMDTLIASN--EPIGVQDG----------- 662
Cdd:cd13723  190 MQQGSELMPKALStRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTkiEYGAVKDGatmtffkkski 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 663 -TFA--WKFLVNElniaPSRIIplKDEEEylsALQRGPRGGgvAAIVDELPYIKaLLSNSNCKFRTVGQEFTRTGWGFAF 739
Cdd:cd13723  270 sTFEkmWAFMSSK----PSALV--KNNEE---GIQRALTAD--YALLMESTTIE-YVTQRNCNLTQIGGLIDSKGYGIGT 337
                        330       340       350
                 ....*....|....*....|....*....|
gi 330253582 740 QRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13723  338 PMGSPYRDKITIAILQLQEEDKLHIMKEKW 367
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
52-218 6.08e-18

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: 87.36  E-value: 6.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSG----IGHIISHVAnelhVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVV 126
Cdd:cd06363  106 QPRVVAVIGPDSSElaltTAKLLGFFL----MPQISYGASSEELSnKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVA 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 127 AIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSS-ISDLLASVNLMESRIFVVHVNPDSGLNIF--SVAKSLg 203
Cdd:cd06363  182 FLGSDDEYGQDGLQLFSEKAANTGICVAYQGLIPTDTDPKPkYQDILKKINQTKVNVVVVFAPKQAAKAFFeeVIRQNL- 260
                        170
                 ....*....|....*.
gi 330253582 204 mmgSGYVWI-TTDWLL 218
Cdd:cd06363  261 ---TGKVWIaSEAWSL 273
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
55-241 1.11e-16

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: 83.85  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  55 VVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDE 133
Cdd:cd06364  101 VAAVIGESGSTLSIAVARTLGLFYIPQVSYFASCACLSDkKQFPSFLRTIPSDYYQSRALAQLVKHFGWTWVGAIASDDD 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 134 YGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVnPDSGL----------NIfsvakslg 203
Cdd:cd06364  181 YGRNGIKAFLEEAEKLGICIAFSETIPRTYSQEKILRIVEVIKKSTAKVIVVFS-SEGDLeplikelvrqNI-------- 251
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 330253582 204 mmgSGYVWITTD-WLLTALdsmePLDPRALDLLQGVVAF 241
Cdd:cd06364  252 ---TGRQWIASEaWITSSL----LATPEYFPVLGGTIGF 283
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
49-382 1.24e-16

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: 83.10  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFA-ATDPTLSSLQYPYFLRTtqnDYFQmnAITDFVSYFRWREVVA 127
Cdd:cd06380   57 SQLSRGVFAIFGSSDASSLNTIQSYSDTFHMPYITPSfPKNEPSDSNPFELSLRP---SYIE--AIVDLIRHYGWKKVVY 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 128 IFVDDEygrnGISVLGDAL--AKKRAKISYKAAFPPGADNSSisDLLASVNLMESRI----FVVHVNPDSGLNIFSVAKS 201
Cdd:cd06380  132 LYDSDE----GLLRLQQLYdyLKEKSNISVRVRRVRNVNDAY--EFLRTLRELDREKedkrIVLDLSSERYQKILEQIVE 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 202 LGMMGSGYvwittDWLLTALDsMEPLDPRALdlLQG---VVAFRHYTPESDNKRQFKGRWKNLRFKESLKSDDGFNSY-- 276
Cdd:cd06380  206 DGMNRRNY-----HYLLANLD-FLDLDLERF--LHGgvnITGFQLVDTNNKTVKDFLQRWKKLDPREYPGAGTDTIPYea 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 277 ALyAYDSVWLVARALDVFFSQGNTVTFSNDPSLRNTNDS-GIKLSKLHI--FNEGERFLQVILEMNYTGLTGQIEFNSEK 353
Cdd:cd06380  278 AL-AVDAVLVIAEAFQSLLRQNDDIFRFTFHGELYNNGSkGIDCDPNPPlpWEHGKAIMKALKKVRFEGLTGNVQFDDFG 356
                        330       340       350
                 ....*....|....*....|....*....|
gi 330253582 354 NRINPAYDILNIKST-GPLRVGYWSNHTGF 382
Cdd:cd06380  357 QRKNYTLDVIELTSNrGLRKIGTWSEGDGF 386
PBP1_ABC_ligand_binding-like cd19984
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
53-288 2.01e-16

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: 380639 [Multi-domain]  Cd Length: 296  Bit Score: 80.73  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  53 NKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLqYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDD 132
Cdd:cd19984   66 DKVKAIIGGVCSSETLAIAPIAEQNKVVLISPGASSPEITKA-GDYIFRNYPSDAYQGKVLAEFAYNKLYKKVAILYENN 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 133 EYGRNGISVLGDALAKKRAKISYKAAFPPGA-DNSSISDLLASVNLMesRIFVVhVNPDSGLNIFSVAKSLGMMG---SG 208
Cdd:cd19984  145 DYGVGLKDVFKKEFEELGGKIVASESFEQGEtDFRTQLTKIKAANPD--AIFLP-GYPKEGGLILKQAKELGIKApilGS 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 209 YVWITTDWLLTALDSMEpldpraldllqGVV-AFRHYTPESDNKRQFKGRwknlRFKEslKSDDGFNSYALYAYDSVWLV 287
Cdd:cd19984  222 DGFEDPELLEIAGEAAE-----------GVIfTYPAFDDSSEKKQKFFFY----RYKE--KYGKEPDIYAALAYDAVMIL 284

                 .
gi 330253582 288 A 288
Cdd:cd19984  285 A 285
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
423-771 1.90e-15

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: 77.76  E-value: 1.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 423 PENGKPLKIGVPNRVSYK--NYASKDKNP---LGVKGFCIDIFEAAIQLLPYpvprTYILY--GDGK----KNPSYDNLI 491
Cdd:cd13718   22 PLTGTCMRNTVPCRKQLNheNSTDADENRyvkKCCKGFCIDILKKLAKDVGF----TYDLYlvTNGKhgkkINGVWNGMI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 492 SEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVApvkgAKSSpwsflkpftiemwAVTGalflfvgaviwILEH 571
Cdd:cd13718   98 GEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMV----ARSN-------------QVSG-----------LSDK 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 572 RFNEEF-RGPPrrqiitvfwFSFSTMFFSHRENTvstlgrfvllvwlfvvliINSSYTAsltsiltvqqltsriegMDTL 650
Cdd:cd13718  150 KFQRPHdQSPP---------FRFGTVPNGSTERN------------------IRNNYPE-----------------MHQY 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 651 IASNEPIGVQDGtfawkflvnelniapsriiplkdeeeyLSALQRGPrgggvaaiVDELPYIKALLS-----NSNCKFRT 725
Cdd:cd13718  186 MRKYNQKGVEDA---------------------------LVSLKTGK--------LDAFIYDAAVLNymagqDEGCKLVT 230
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 330253582 726 VGQE--FTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLT 771
Cdd:cd13718  231 IGSGkwFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLT 278
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
445-769 2.95e-15

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: 78.49  E-value: 2.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 445 KDKNPLGVKGFCIDIFEAAIQLLPYpvprTYILY--GDGK-----KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVD 517
Cdd:cd13717   18 DRDGSPIWEGYCIDLIEEISEILNF----DYEIVepEDGKfgtmdENGEWNGLIGDLVRKEADIALAALSVMAEREEVVD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 518 FTQPFIES-GLVVVAPVKGAKSSPWSFLKPFTIEMWAVtgalflfvgaviwilehrFNeefrgpprrqIITVFWF---SF 593
Cdd:cd13717   94 FTVPYYDLvGITILMKKPERPTSLFKFLTVLELEVWRE------------------FT----------LKESLWFcltSL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 594 STMFFSHRENTVStlGRFVLLVWLFVVLIINSSYTASLTSILTVQQLTSRIEGMDTLIASNEP-IGVQDGTFAWKFLVNE 672
Cdd:cd13717  146 TPQGGGEAPKNLS--GRLLVATWWLFVFIIIASYTANLAAFLTVSRLQTPVESLDDLARQYKIqYTVVKNSSTHTYFERM 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 673 LNI----------------------APSRI--IPLKD---------EEEYLS-----ALQRGPRGGGVA-AIVDELPYIK 713
Cdd:cd13717  224 KNAedtlyemwkdmslndslspverAKLAVwdYPVSEkytkiyqamQEAGLVanaeeGVKRVRESTSAGfAFIGDATDIK 303
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 714 ALLSNsNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13717  304 YEILT-NCDLQEVGEEFSRKPYAIAVQQGSPLKDELNYAILELQNDRFLEKLKAKW 358
PBP1_ABC_HAAT-like cd19988
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-288 1.06e-14

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


Pssm-ID: 380643 [Multi-domain]  Cd Length: 302  Bit Score: 75.78  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDF-VSYFRWREVVAIFV 130
Cdd:cd19988   65 QDKVWAIIGSINSSCTLAAIRVALKAGVPQINPGSSAPTITESGNPWVFRCTPDDRQQAYALVDYaFEKLKVTKIAVLYV 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNssISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMgsgyv 210
Cdd:cd19988  145 NDDYGRGGIDAFKDAAKKYGIEVVVEESYNRGDKD--FSPQLEKIKDSGAQAIVMWGQYTEGALIAKQARELGLK----- 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 211 wittdwlLTALDSMEPLDPRALDL----LQGVVAFRHYTPESDNKR--QFKGRWKNlRFKESLksddgfNSYALYAYDSV 284
Cdd:cd19988  218 -------QPLFGSDGLVTPKFIELagdaAEGAIATTPFLPDSDDPKvsAFVEKYKK-RYGEEP------DVFAAQAYDAM 283

                 ....
gi 330253582 285 WLVA 288
Cdd:cd19988  284 NILA 287
Peripla_BP_6 pfam13458
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ...
52-370 1.22e-14

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


Pssm-ID: 433225 [Multi-domain]  Cd Length: 342  Bit Score: 76.16  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582   52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSlqyPYFLRTTQNDYFQMNAITDF-VSYFRWREVVAIFV 130
Cdd:pfam13458  67 QDGVDAIVGGVSSAVALAVAEVLAKKGVPVIGPAALTGEKCS---PYVFSLGPTYSAQATALGRYlAKELGGKKVALIGA 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNssISDLLAsvNLMESR--IFVVHVNPDSGLNIFSVAKSLGMMGSG 208
Cdd:pfam13458 144 DYAFGRALAAAAKAAAKAAGGEVVGEVRYPLGTTD--FSSQVL--QIKASGadAVLLANAGADTVNLLKQAREAGLDAKG 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  209 yvwITTDWLLTALDSMEPLDPRAldlLQGVVAFRHYTPESDNK--RQFKGRWKNlRFKEslksdDGFNSYALYAYDSVWL 286
Cdd:pfam13458 220 ---IKLVGLGGDEPDLKALGGDA---AEGVYATVPFFPDLDNPatRAFVAAFAA-KYGE-----APPTQFAAGGYIAADL 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  287 VARALDvffsQGNTVTfsndpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIK 366
Cdd:pfam13458 288 LLAALE----AAGSPT-------------------------REAVIAALRALPYDGPFGPVGFRAEDHQAVHCMYLVQVK 338

                  ....
gi 330253582  367 STGP 370
Cdd:pfam13458 339 ADGK 342
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
53-362 2.78e-14

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: 74.87  E-value: 2.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  53 NKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVsyFRWREV--VAIfV 130
Cdd:cd06342   65 DGVVAVIGHYNSGAAIAAAPIYAEAGIPMISPSATNPKLTEQGYKNFFRVVGTDDQQGPAAADYA--AKTLKAkrVAV-I 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DD--EYGRNGISVLGDALAKKRAKISYKAAFPPGADNssISDLLASVnlMESR---IFVVHVNPDSGLnIFSVAKSLGM- 204
Cdd:cd06342  142 HDgtAYGKGLADAFKKALKALGGTVVGREGITPGTTD--FSALLTKI--KAANpdaVYFGGYYPEAGL-LLRQLREAGLk 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 205 ---MGSGyvwittdwlltALDSMEPLDpRALDLLQGVVAFRHYTPESDNKrqfkgRWKNL--RFKESLKSDDGfnSYALY 279
Cdd:cd06342  217 apfMGGD-----------GIVSPDFIK-AAGDAAEGVYATTPGAPPEKLP-----AAKAFlkAYKAKFGEPPG--AYAAY 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 280 AYDSVWLVARALDvffsQGNTVTfsndpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPA 359
Cdd:cd06342  278 AYDAAQVLLAAIE----KAGSTD-------------------------RAAVAAALRATDFDGVTGTISFDAKGDLTGPA 328

                 ...
gi 330253582 360 YDI 362
Cdd:cd06342  329 FTV 331
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
47-215 1.72e-13

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: 72.34  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  47 PWELMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREV 125
Cdd:cd04509   93 PVFVKPEGIKGVIGHLCSSVTIPVSNILELFGIPQITYAATAPELSDDRgYQLFLRVVPLDSDQAPAMADIVKEKVWQYV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 126 VAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLASV-NLMESRIFVVHVNPDSGLNIFSVAKSLGM 204
Cdd:cd04509  173 SIVHDEGQYGEGGARAFQDGLKKGGLCIAFSDGITAGEKTKDFDRLVARLkKENNIRFVVYFGYHPEMGQILRAARRAGL 252
                        170
                 ....*....|.
gi 330253582 205 MGSgYVWITTD 215
Cdd:cd04509  253 VGK-FQFMGSD 262
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
54-225 1.79e-13

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: 73.17  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  54 KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDD 132
Cdd:cd06361  101 PVKAVIGASYSEISIAVARLLNLQLIPQISYESSAPILSdKLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDD 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 133 EYGRNGISVLGDALAKKRAKISYKAAFPPGAD----NSSISDLLASVNlMESRIFVVHV--NPDSGLNIFsvaKSLGMMG 206
Cdd:cd06361  181 DYGRSALESFIIQAEAENVCIAFKEVLPAYLSdptmNVRINDTIQTIQ-SSSQVNVVVLflKPSLVKKLF---KEVIERN 256
                        170       180
                 ....*....|....*....|....
gi 330253582 207 SGYVWITTD-----WLLTALDSME 225
Cdd:cd06361  257 ISKIWIASDnwstaREILKMPNIN 280
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
50-384 3.23e-13

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: 72.01  E-value: 3.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  50 LMENKVVAAIGPQSSGIGHIISHVANELHVPFLSfaATDPTLSSLQYPYFLRTTQNDYFQmnAITDFVSYFRWREVVAIF 129
Cdd:cd06368   59 LLEKGVVAIVGPSSSDSNNALQSICDALDVPHIT--VHDDPRLSKSQYSLSLYPRNQLSQ--AVSDLLKYWRWKRFVLVY 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 130 VDDEygrnGISVLGDALakKRAKISYKAAFPPGADNSSISD----LLASV-NLMESRIfVVHVNPDSGLNIFSVAKSLGM 204
Cdd:cd06368  135 DDDD----RLRRLQELL--EAARFSKRFVSVRKVDLDYKTLdetpLLKRKdCSLFSRI-LIDLSPEKAYTFLLQALEMGM 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 205 MGSGYVWITTDWLLTALDSMEPLdpRALDL-LQGVVAFRHYTPESDNKRqfkgRW--KNLRFKESLKSD---DGFNSYAL 278
Cdd:cd06368  208 TIELYHYFLTTMDLSLLLDLELF--RYNHAnITGFQLVDNNSMYKEDIN----RLafNWSRFRQHIKIEsnlRGPPYEAA 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 279 YAYDSVWLVARAldvffsqgntvtfsndpslrntndsgiklsklhiFNEgerflqvilemnytglTGQIEFNSEKNRINP 358
Cdd:cd06368  282 LMFDAVLLLADA----------------------------------FRR----------------TGDLRFNGTGLRSNF 311
                        330       340
                 ....*....|....*....|....*.
gi 330253582 359 AYDILNIKSTGPLRVGYWSNHTGFSV 384
Cdd:cd06368  312 TLRILELGYGGLRKIGFWDSNTRLAM 337
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
429-769 8.10e-13

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


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 68.43  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 429 LKIGVpnRVSYKNYASKDKNpLGVKGFCIDIFEAAIQLLpypvprtyilygdGKK----NPSYDNLISEVAANIFDVAVG 504
Cdd:cd13530    2 LRVGT--DADYPPFEYIDKN-GKLVGFDVDLANAIAKRL-------------GVKvefvDTDFDGLIPALQSGKIDVAIS 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 505 DVTIITNRTKFVDFTQPFIESGLVVVAPvkgaKSSPwsflkpftiemwavtgalflfvgaviwilehrfneefrgpprrq 584
Cdd:cd13530   66 GMTITPERAKVVDFSDPYYYTGQVLVVK----KDSK-------------------------------------------- 97
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 585 iitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltSILTVQQLTSRIegmdtliasnepIGVQDGTF 664
Cdd:cd13530   98 ------------------------------------------------ITKTVADLKGKK------------VGVQAGTT 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 665 AWKFLVNelNIAPSRIIPLKDEEEYLSALqrgpRGGGVAAIVDELPYIKALLSNSNCKFRTVGQEFTRTGWGFAF-QRDS 743
Cdd:cd13530  118 GEDYAKK--NLPNAEVVTYDNYPEALQAL----KAGRIDAVITDAPVAKYYVKKNGPDLKVVGEPLTPEPYGIAVrKGNP 191
                        330       340
                 ....*....|....*....|....*.
gi 330253582 744 PLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13530  192 ELLDAINKALAELKADGTLDKLLEKW 217
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-292 8.44e-13

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: 70.71  E-value: 8.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDF-VSYFRWREVVAIFV 130
Cdd:cd19980   65 DDKVPAIIGAWCSSVTLAVMPVAERAKVPLVVEISSAPKITEGGNPYVFRLNPTNSMLAKAFAKYlADKGKPKKVAFLAE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGAdnSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGM----MG 206
Cdd:cd19980  145 NDDYGRGAAEAFKKALKAKGVKVVATEYFDQGQ--TDFTTQLTKLKAANPDAIFVVAETEDGALILKQARELGLkqqlVG 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 207 SGyVWITTDWLLTALDSMEpldpraldllqGVVAFRHYTPESDNKRQFKgrwKNLRFKESLKSDDGFNSYAlyAYDSVWL 286
Cdd:cd19980  223 TG-GTTSPDLIKLAGDAAE-----------GVYGASIYAPTADNPANKA---FVAAYKKKYGEPPDKFAAL--GYDAVMV 285

                 ....*.
gi 330253582 287 VARALD 292
Cdd:cd19980  286 IAEAIK 291
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
642-773 1.80e-12

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 67.70  E-value: 1.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 642 SRIEGMDTLiaSNEPIGVQDGTFAWKFLVNelNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDELPYIKALLS-NSN 720
Cdd:COG0834   96 SGIKSLADL--KGKTVGVQAGTTYEEYLKK--LGPNAEIVEFDSYAEALQALASG----RVDAVVTDEPVAAYLLAkNPG 167
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330253582 721 CKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKWLTYD 773
Cdd:COG0834  168 DDLKIVGEPLSGEPYGIAVRKGDPeLLEAVNKALAALKADGTLDKILEKWFGED 221
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
453-770 4.38e-12

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: 66.89  E-value: 4.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 453 KGFCIDIFEAaiqlLPYPVPRTYILY--GDGK---KNPSYDN----LISEVAANIFDVAVGDVTIITNRTKFVDFTQPFI 523
Cdd:cd13687   21 YGFCIDLLKK----LAEDVNFTYDLYlvTDGKfgtVNKSINGewngMIGELVSGRADMAVASLTINPERSEVIDFSKPFK 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 524 ESGLVVVApvkgAKSSpwsflkpftiemwAVTGalflfvgaviwILEHRFneefrgppRRQIITvfwFSFSTMFFSHREN 603
Cdd:cd13687   97 YTGITILV----KKRN-------------ELSG-----------INDPRL--------RNPSPP---FRFGTVPNSSTER 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 604 TvstlgrfvllvwlfvvliINSSYTASLTSILTVQQLTSriegmdtliasnepigvqdgtfawkflvnelniapsriipl 683
Cdd:cd13687  138 Y------------------FRRQVELMHRYMEKYNYETV----------------------------------------- 158
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 684 kdeEEYLSALQRGPrgggvaaiVDELPYIKALL-----SNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAE 758
Cdd:cd13687  159 ---EEAIQALKNGK--------LDAFIWDSAVLeyeasQDEGCKLVTVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHE 227
                        330
                 ....*....|..
gi 330253582 759 EGKLEKIRKKWL 770
Cdd:cd13687  228 SGFMEELDKKWL 239
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-360 5.51e-12

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


Pssm-ID: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 67.95  E-value: 5.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSlQYPYFLRTTQNDYFQMNAITDFV-SYFRWREVVAIF- 129
Cdd:cd06347   65 EDKVVAIIGPVTSSIALAAAPIAQKAKIPMITPSATNPLVTK-GGDYIFRACFTDPFQGAALAKFAyEELGAKKAAVLYd 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 130 VDDEYGRnGIS-VLGDALAKKRAKISYKAAFPPGadNSSISDLLAsvNLMESR---IFVVHVNPDSGLnIFSVAKSLG-- 203
Cdd:cd06347  144 VSSDYSK-GLAkAFKEAFEKLGGEIVAEETYTSG--DTDFSAQLT--KIKAANpdvIFLPGYYEEAAL-IIKQARELGit 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 204 --MMGsGYVWITTDWLLTALDSMEpldpraldllqGVVAFRHYTPESDNK--RQFKGRWKNlRFKESLksddgfNSYALY 279
Cdd:cd06347  218 apILG-GDGWDSPELLELGGDAVE-----------GVYFTTHFSPDDPSPevQEFVKAYKA-KYGEPP------NAFAAL 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 280 AYDSVWLVARALdvffsqgNTVTFSNDPSLRNtndsgiKLSKLhifnegerflqvileMNYTGLTGQIEFNSEKNRINPA 359
Cdd:cd06347  279 GYDAVMLLADAI-------KRAGSTDPEAIRD------ALAKT---------------KDFEGVTGTITFDPNGNPIKPA 330

                 .
gi 330253582 360 Y 360
Cdd:cd06347  331 V 331
PBP1_ABC_ligand_binding-like cd06335
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
49-291 4.19e-11

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: 65.32  E-value: 4.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMEN-KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSL---QYPYFLRTTQNDYFQMNAITDFVSYFRWRE 124
Cdd:cd06335   61 ELIDKeKVVAIIGPTNSGVALATIPILQEAKIPLIIPVATGTAITKPpakPRNYIFRVAASDTLQADFLVDYAVKKGFKK 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 125 vVAIFVDDE-YGRNGISVLGDALAKKRAKISYKAAFPPGADnssisDLLASVNLMESR----IFVVHVNPDSGLnifsVA 199
Cdd:cd06335  141 -IAILHDTTgYGQGGLKDVEAALKKRGITPVATESFKIGDT-----DMTPQLLKAKDAgadvILVYGLGPDLAQ----IL 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 200 KSLGMMGsGYVWITTDWLLtaldSMEPLDPRALDLLQGVVAFRHYTPESDNKRQfkgrWK-NLRFKESLKSDDGFNSY-A 277
Cdd:cd06335  211 KAMEKLG-WKVPLVGSWGL----SMPNFIELAGPLAEGTIMTQTFIEDYLTPRA----KKfIDAYKKKYGTDRIPSPVsA 281
                        250
                 ....*....|....
gi 330253582 278 LYAYDSVWLVARAL 291
Cdd:cd06335  282 AQGYDAVYLLAAAI 295
PBP1_ABC_HAAT-like cd19986
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-288 5.64e-11

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


Pssm-ID: 380641 [Multi-domain]  Cd Length: 297  Bit Score: 64.57  E-value: 5.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLsFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVS-YFRWREVVAIFV 130
Cdd:cd19986   65 DDKVVAVIGPHYSTQVLAVSPLVKEAKIPVI-TGGTSPKLTEQGNPYMFRIRPSDSVSAKALAKYAVeELGAKKIAILYD 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPG-ADNSSIsdLLASVNLMESRIFVVHVNPDSGLnIFSVAKSLGM----M 205
Cdd:cd19986  144 NDDFGTGGADVVTAALKALGLEPVAVESYNTGdKDFTAQ--LLKLKNSGADVIIAWGHDAEAAL-IARQIRQLGLdvpvI 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 206 GSGyVWITTDWLLTALDSMEpldpraldllqGVVAFRHYTPESDNKRQfKGRWKnlRFKESLKSDDGFNSyALYaYDSVW 285
Cdd:cd19986  221 GSS-SFATPTVLLLAGEALE-----------GIYSVTDFVPSDPDPKV-QAFVK--KYKAKYGEDPDLYS-AWY-YDAMY 283

                 ...
gi 330253582 286 LVA 288
Cdd:cd19986  284 LLA 286
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
49-292 9.08e-11

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: 64.96  E-value: 9.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAIGPQSS-GIGHIISHVANelhVPFLSFAATDPTLS-SLQYPYFLRTtqndYFQMNAITDFVS----YFRW 122
Cdd:cd06370   65 ELWKRGVSAFIGPGCTcATEARLAAAFN---LPMISYKCADPEVSdKSLYPTFART----IPPDSQISKSVIallkHFNW 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 123 REVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGA-----DNSSISDLLASVnLMESRIFVVHVNPDSGLNIFS 197
Cdd:cd06370  138 NKVSIVYENETKWSKIADTIKELLELNNIEINHEEYFPDPYpyttsHGNPFDKIVEET-KEKTRIYVFLGDYSLLREFMY 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 198 VAKSLGMMGSG-YVWITTDW------------LLTALDSMEPLDPRALDLLQGVVAFrhyTPESDNKRQFKGRWKNLRfk 264
Cdd:cd06370  217 YAEDLGLLDNGdYVVIGVELdqydvddpakypNFLSGDYTKNDTKEALEAFRSVLIV---TPSPPTNPEYEKFTKKVK-- 291
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 330253582 265 ESLKsDDGFNS--------------YALYAYDSVWLVARALD 292
Cdd:cd06370  292 EYNK-LPPFNFpnpegiektkevpiYAAYLYDAVMLYARALN 332
PBP1_mGluR_groupIII cd06376
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
54-379 1.45e-10

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: 64.44  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  54 KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDD 132
Cdd:cd06376  107 KVVGVIGASASSVSIMVANILRLFQIPQISYASTAPELSdDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEG 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 133 EYGRNGISVL-------GDALAKKRAKISYKAAfpPGADNSSISDLLASVNlmeSRIFVVHVNPDSGLNIFSVAKSLGMM 205
Cdd:cd06376  187 NYGEKGVESFvqisreaGGVCIAQSEKIPRERR--TGDFDKIIKRLLETPN---ARAVVIFADEDDIRRVLAAAKRANKT 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 206 GSgYVWITTD-W--LLTALDSMEPLDPRALDLL---QGVVAFRHY----TPEsDNKRQ--FKGRWK---NLRF------- 263
Cdd:cd06376  262 GH-FLWVGSDsWgaKISPVLQQEDVAEGAITILpkrASIEGFDAYftsrTLE-NNRRNvwFAEFWEenfNCKLtssgskk 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 264 ---------KESLKSDDGFNSYAL--YAYDSVWLVARALDvffsqgntvtfsndpSLRNT---NDSGIKLSKLHIfnEGE 329
Cdd:cd06376  340 edtlrkctgQERIGRDSGYEQEGKvqFVVDAVYAMAHALH---------------NMNKDlcpGYRGLCPEMEPA--GGK 402
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 330253582 330 RFLQVILEMNYTGLTGQ-IEFNseKNRINPA-YDIL-----NIKSTGPLRVGYWSNH 379
Cdd:cd06376  403 KLLKYIRNVNFNGSAGTpVMFN--KNGDAPGrYDIFqyqttNGSNYGYRLIGQWTDE 457
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
453-769 1.97e-10

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: 62.20  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 453 KGFCIDIFEAAIQLLP-----YPVPRTyiLYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGL 527
Cdd:cd13685   29 EGYCIDLLEELAKILGfdyeiYLVPDG--KYGSRDENGNWNGMIGELVRGEADIAVAPLTITAEREEVVDFTKPFMDTGI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 528 VVVapvkgaksspwsFLKPFTIEmwavtgalflfvgaviwilehrfneEFRGPPRRQII--TVFWFSfSTM-FFSHRENT 604
Cdd:cd13685  107 SIL------------MRKPTPIE-------------------------SLEDLAKQSKIeyGTLKGS-STFtFFKNSKNP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 605 VSTLGRFvllvwlfvvliinssytasltsiltvqqltsriegmdtliasnepigvqdgtfaWKFLVNElniapSRIIPLK 684
Cdd:cd13685  149 EYRRYEY------------------------------------------------------TKIMSAM-----SPSVLVA 169
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 685 DEEEylsALQRGPRGGGVAAIVDELPYIKaLLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEK 764
Cdd:cd13685  170 SAAE---GVQRVRESNGGYAFIGEATSID-YEVLRNCDLTKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGELEK 245

                 ....*
gi 330253582 765 IRKKW 769
Cdd:cd13685  246 LKEKW 250
PBP1_ABC_RPA1789-like cd06333
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ...
52-291 2.00e-10

type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, RPA1791-1793), involved in active transport of lignin-derived aromatic substrates, and its close homologs; This group includes RPA1789 (CouP) from Rhodopseudomonas palustris and its close homologs in other bacteria. RPA1789 (CouP) is the periplasmic binding-protein component of an ABC system (CouPSTU; RPA1789, RPA1791-1793) that is involved in the active transport of lignin-derived aromatic substrates. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).


Pssm-ID: 380556 [Multi-domain]  Cd Length: 342  Bit Score: 63.34  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSlQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVD 131
Cdd:cd06333   65 EDKVDAIIGPSTTGESLAVAPIAEEAKVPLISLAGAAAIVEP-VRKWVFKTPQSDSLVAEAILDYMKKKGIKKVALLGDS 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 132 DEYGRNGISVLGDALAKKRAKISYKAAFPPGAdnSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGM-----MG 206
Cdd:cd06333  144 DAYGQSGRAALKKLAPEYGIEIVADERFARTD--TDMTAQLTKIRAAKPDAVLVWASGPPAALVAKNLRQLGYkgpiyQS 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 207 SGYVwiTTDWLLTALDSME--------PLDPRALdllqgvvafrhytPESDNKR----QFKGRWKNlRFKEslksddGFN 274
Cdd:cd06333  222 HGAA--NQDFIKLAGKAAEgvilpagkLLVADQL-------------PDSDPQKkvllEFVKAYEA-KYGE------GPS 279
                        250
                 ....*....|....*..
gi 330253582 275 SYALYAYDSVWLVARAL 291
Cdd:cd06333  280 TFAGHAYDALLLLVEAI 296
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
55-375 5.70e-10

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: 62.75  E-value: 5.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  55 VVAAIGPQSSgigHIISHVANEL---HVPFLSFAATDPTLSSL-QYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFV 130
Cdd:cd06374  119 IVGVIGPGSS---SVTIQVQNLLqlfHIPQIGYSATSIDLSDKsLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHT 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSSISDLLAsvNLME----SRIFVVHVNPDSGLNIFSVAKSLGMMG 206
Cdd:cd06374  196 EGNYGESGIEAFKELAAEEGICIAHSDKIYSNAGEEEFDRLLR--KLMNtpnkARVVVCFCEGETVRGLLKAMRRLNATG 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 207 sGYVWITTDWLLTALDSMEPLDPRAldllQG----------VVAF-RHYT---PESdNKRQ--FKGRWKNlRFKESLKSD 270
Cdd:cd06374  274 -HFLLIGSDGWADRKDVVEGYEDEA----AGgitikihspeVESFdEYYFnlkPET-NSRNpwFREFWQH-RFDCRLPGH 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 271 DGFNSYalyaYDSVWLVARALDVFFSQGNTVTFSNDP-------------SLRNTNDSGIKLSKLHIfnEGERFLQVILE 337
Cdd:cd06374  347 PDENPY----FKKCCTGEESLLGNYVQDSKLGFVINAiyamahalhrmqeDLCGGYSVGLCPAMLPI--NGSLLLDYLLN 420
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 330253582 338 MNYTGLTGQ-IEFNseKNRINPA-YDILNIKSTGPLRVGY 375
Cdd:cd06374  421 VSFVGVSGDtIMFD--ENGDPPGrYDIMNFQKTGEGSYDY 458
PBP1_ABC_HAAT-like cd06344
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
44-291 1.07e-09

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


Pssm-ID: 380567 [Multi-domain]  Cd Length: 332  Bit Score: 61.09  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  44 LLAPWELMENK-VVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRW 122
Cdd:cd06344   54 LAIAQRFADNPdVVAVIGHRSSYVAIPASIIYERAGLLMLSPGATAPKLTQHGFKYIFRNIPSDEDIARQLARYAARQGY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 123 REVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFppGADNSSISDLLASVNLMESR--IFVVHVNPDSGLNIfsvaK 200
Cdd:cd06344  134 KRIVIYYDDDSYGKGLANAFEEEARELGITIVDRRSY--SSDEEDFRRLLSKWKALDFFdaIFLAGSMPEGAEFI----K 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 201 SLGMMGSGYVWITTDwlltALDSMEPLDpraldlLQGVVAFRHYTPES-DNKRQfkgRWKNLRFKESLKSDDGF--NSYA 277
Cdd:cd06344  208 QARELGIKVPIIGGD----GLDSPELIE------IAGKAAEGVVVATVfDPDDP---RPEVRAFVEAFRKKYGRepDVWA 274
                        250
                 ....*....|....
gi 330253582 278 LYAYDSVWLVARAL 291
Cdd:cd06344  275 AQGYDAVKLLAEAI 288
PBP1_SBP-like cd19989
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
52-296 1.13e-09

periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.


Pssm-ID: 380644 [Multi-domain]  Cd Length: 299  Bit Score: 60.75  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFL-SFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFV 130
Cdd:cd19989   65 QDGVDFLTGAVSSAVALAVAPKAAELKVPYLvTVAADDELTGENCNRYTFRVNTSDRMIARALAPWLAENGGKKWYIVYA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGADN--SSISdllasvNLMESR---IFVVHVNPDSgLNIFSVAKSLGMM 205
Cdd:cd19989  145 DYAWGQSSAEAFKEAIEELGGEVVGTLFAPLGTTDfsSYIT------QISDSGadgLLLALAGSDA-VNFLKQAGQFGLG 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 206 GSgYVWITTDWLLTALDSmEPLDPRALDLLQGVvaFRHYTPESDNKRQFKGRWKNlrfkeslKSDDGFNSYALYAYDSV- 284
Cdd:cd19989  218 KK-YKIVGGILSIEPLAL-PALGDAAEGVYGGV--RYPPTLDTPANRAFVEAYEK-------EYGEAPDNFAGEAYEAMq 286
                        250
                 ....*....|...
gi 330253582 285 WLVARAL-DVFFS 296
Cdd:cd19989  287 ALAHQAVqPGYIG 299
PBP1_iGluR_NMDA cd06367
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic ...
49-376 1.46e-09

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: 60.72  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAI----GPQSSGIGHIISHVANELHVPFL------SFAATDPTLSSLqypyFLRTTQNDYFQMNAITDFVS 118
Cdd:cd06367   57 DLLSDSKVQGVvfsdDTDQEAIAQILDFIAAQTLTPVLglhgrsSMIMADKSEHSM----FLQFGPPIEQQASVMLNIME 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 119 YFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADN--SSISDLLASVNLMESRIFVVHVNPDSGLNIF 196
Cdd:cd06367  133 EYDWYIVSLVTTYFPGYQDFVNKLRSTIENSGWELEEVLQLDMSLDDgdSKLQAQLKKLQSPEARVILLYCTKEEATYVF 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 197 SVAKSLGMMGSGYVWIttdwlltaLDSMEPLDPRALDLL-QGVVafrhytpesdnkrqfkgrwknlrfkeSLKSDDGFNS 275
Cdd:cd06367  213 EVAASVGLTGYGYTWL--------VGSLVAGTDTVPAEFpTGLI--------------------------SLSYDEWYNL 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 276 YAlYAYDSVWLVARALDVFFSQGNTVTfsnDPSLRNTNDSGIKLSKLHIFNegeRFLqvileMNYTGLTGQIEFNSEKNR 355
Cdd:cd06367  259 PA-RIRDGVAIVATAASEMLSEHEQIP---DPPSSCVNNQEIRKYTGPMLK---RYL-----INVTFEGRDLSFSEDGYQ 326
                        330       340
                 ....*....|....*....|..
gi 330253582 356 INPAYDILNIKSTGPL-RVGYW 376
Cdd:cd06367  327 MHPKLVIILLNNERKWeRVGKW 348
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
429-770 8.15e-09

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


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 56.92  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  429 LKIGVpnRVSYKNYASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYIlygdgkkNPSYDNLISEVAANIFDVAVGDVTI 508
Cdd:pfam00497   1 LRVGT--DGDYPPFEYVDENG-KLVGFDVDLAKAIAKRLGVKV--EFV-------PVSWDGLIPALQSGKVDLIIAGMTI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  509 ITNRTKFVDFTQPFIESGLVVVAPVKGAKSSpwsflkpftiemwavtgalflfvgaviwilehrfneefrgpprrqiitv 588
Cdd:pfam00497  69 TPERAKQVDFSDPYYYSGQVILVRKKDSSKS------------------------------------------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  589 fwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsILTVQQLTSRIegmdtliasnepIGVQDGTFAWKF 668
Cdd:pfam00497 100 ---------------------------------------------IKSLADLKGKT------------VGVQKGSTAEEL 122
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  669 LVNeLNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDELPYIKALLSNSNCKFRTV-GQEFTRTGWGFAFQRDSP-LA 746
Cdd:pfam00497 123 LKN-LKLPGAEIVEYDDDAEALQALANG----RVDAVVADSPVAAYLIKKNPGLNLVVvGEPLSPEPYGIAVRKGDPeLL 197
                         330       340
                  ....*....|....*....|....
gi 330253582  747 VDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:pfam00497 198 AAVNKALAELKADGTLAKIYEKWF 221
PBP1_ABC_ligand_binding-like cd06340
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
52-292 1.16e-08

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


Pssm-ID: 380563 [Multi-domain]  Cd Length: 352  Bit Score: 57.95  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNaitDFVSYFRW--------- 122
Cdd:cd06340   68 QEGVVAIIGAYSSSVTLAASQVAERYGVPFVTASAVADEITERGFKYVFRTAPTASQFAE---DAVDFLKElakkkgkki 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 123 REVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGAdnssiSDLLASVN-LMESR---IFVVHVNPDSGLnIFSV 198
Cdd:cd06340  145 KKVAIIYEDSAFGTSVAKGLKKAAKKAGLEVVLDEPYPAGA-----TDLSSEVLkLKAAKpdvVFATSYTNDAIL-LLRT 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 199 AKSLG-----MMGSGYVWITTDWLltaldsmepldpRAL-DLLQGVVAFRHYTPESDNKRQfkgRWKNL--RFKESLKSD 270
Cdd:cd06340  219 MKELGfkpkaIIGVGGGYSDPEFL------------KALgKDAEGVFSVVPWSPDLAKKKP---GAKEVneRYKKKYGED 283
                        250       260
                 ....*....|....*....|..
gi 330253582 271 dgFNSYALYAYDSVWLVARALD 292
Cdd:cd06340  284 --MTGHAARAYTAAWVLADALE 303
PBP1_ABC_ligand_binding-like cd06343
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
36-291 1.85e-08

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: 380566 [Multi-domain]  Cd Length: 355  Bit Score: 57.19  E-value: 1.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  36 SRTLIAVDllapwELME-NKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFlRTTQNDY-FQMNAI 113
Cdd:cd06343   60 ARAVAAVR-----KLVEqDKVFAIVGGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKPYT-FGVQPSYeDEGRIL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 114 TDF-VSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGAdnssiSDLLASV-NLMESR--IFVVHVNP 189
Cdd:cd06343  134 ADYiVETLPAAKVAVLYQNDDFGKDGLEGLKEALKAYGLEVVAEETYEPGD-----TDFSSQVlKLKAAGadVVVLGTLP 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 190 DSGLNIFSVAKSLGMmgsgyvwiTTDWLLTA----LDSMEPLDPRALDLLQGVVAFRHYTPESDNKRQfkgrwknlRFKE 265
Cdd:cd06343  209 KEAAAALKEAAKLGW--------KPTFLGSSvsadPTTLAKAGGDAAEGVYSASYLKDPTDADDPAVK--------EFRE 272
                        250       260
                 ....*....|....*....|....*....
gi 330253582 266 SLK---SDDGFNSYALYAYDSVWLVARAL 291
Cdd:cd06343  273 AYKkyfPDDPPNAYALYGYAAAQVFVEAL 301
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
453-580 2.51e-08

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: 56.94  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 453 KGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVV 529
Cdd:cd13724   31 EGFCVDMLKELAEILRFNYKIRLVgdgVYGVPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISI 110
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 330253582 530 VAPVK-GAKSSPWSFLKPFTIEMWAVTGALFLFVGAVIWILEHRFNEEFRGP 580
Cdd:cd13724  111 LYRVHmGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSP 162
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
454-526 4.36e-08

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: 52.14  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  454 GFCIDIFEAAIQLLPYpvprTYILY--GDGK------KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIES 525
Cdd:pfam10613  28 GFCIDLLKELAEILGF----KYEIRlvPDGKygsldpTTGEWNGMIGELIDGKADLAVAPLTITSEREKVVDFTKPFMTL 103

                  .
gi 330253582  526 G 526
Cdd:pfam10613 104 G 104
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
73-216 4.66e-08

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: 56.37  E-value: 4.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  73 VANEL---HVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGD---- 144
Cdd:cd06375  126 VANLLrlfQIPQISYASTSAKLSdKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQearl 205
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 330253582 145 -----ALAKKRAKISYKAAFppgadNSSISDLLASVNlmeSRIFVVHVNPDSGLNIFSVAKSLGMmgsGYVWITTD-W 216
Cdd:cd06375  206 rniciATAEKVGRSADRKSF-----DGVIRELLQKPN---ARVVVLFTRSDDARELLAAAKRLNA---SFTWVASDgW 272
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
70-377 1.13e-07

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: 55.02  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  70 ISHVANELHVPFLSfaATDPTLSSLQYPYFLRTTQNdyfqmNAITDFVSYFRWREVVAIFvDDEYGRNGISVLGDALAKK 149
Cdd:cd06389   73 ITSFCGTLHVSFIT--PSFPTDGTHPFVIQMRPDLK-----GALLSLIEYYQWDKFAYLY-DSDRGLSTLQAVLDSAAEK 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 150 RAKISykaAFPPGADNSSISD-----LLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTaldsm 224
Cdd:cd06389  145 KWQVT---AINVGNINNDKKDetyrsLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFT----- 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 225 eplDPRALDLLQG---VVAFRHYTPESDNKRQFKGRWKNLRFKESLKSDDGFNSY-ALYAYDSVWLVARALDVFFSQGNT 300
Cdd:cd06389  217 ---DGDLLKIQFGganVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYtSALTYDAVQVMTEAFRNLRKQRIE 293
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253582 301 VTfsndpslRNTNDSGIKLSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWS 377
Cdd:cd06389  294 IS-------RRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWS 363
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit ...
68-378 1.40e-07

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


Pssm-ID: 380611 [Multi-domain]  Cd Length: 373  Bit Score: 54.64  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  68 HIISHVANELHVPFLSfaATDPTLSSLQYPYFLRTTQNdyfqmNAITDFVSYFRWREVVAIFVDDEygrnGISVLgDALA 147
Cdd:cd06388   77 HTLTSFCSALHISLIT--PSFPTEGESQFVLQLRPSLR-----GALLSLLDHYEWNRFVFLYDTDR----GYSIL-QAIM 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 148 KKRAKISYK--AAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALdSME 225
Cdd:cd06388  145 EKAGQNGWQvsAICVENFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDI-SLE 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 226 pldpRALDLLQGVVAFRHYTPESDNKRQFKGRWKNLRFKESLKSDDGFNSYALYAYDSVWLVARALDVFFSQGNTVTfsn 305
Cdd:cd06388  224 ----RFMHGGANVTGFQLVDFNTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDIS--- 296
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 330253582 306 dpslRNTNDSGIKLSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSN 378
Cdd:cd06388  297 ----RRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWND 365
PBP1_As_SBP-like cd06330
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
49-174 1.41e-07

periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea that is predicted to be involved in the efflux of toxic compounds. Members of this subgroup include proteins from Herminiimonas arsenicoxydans, which is resistant to arsenic (As) and various heavy metals such as cadmium and zinc. Moreover, they show significant sequence similarity to the cluster of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa.


Pssm-ID: 380553 [Multi-domain]  Cd Length: 342  Bit Score: 54.49  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMEN-KVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVS--YFRWRE 124
Cdd:cd06330   61 ELVLQeGVDFLIGTISSGVALAVAPVAEELKVLFIATDAATDRLTeENFNPYVFRTSPNTYMDAVAAALYAAkkPPDVKR 140
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330253582 125 VVAIFVDDEYGRNGISVLGDALAKKR--AKISYKAAFPPGA-D-NSSISDLLAS 174
Cdd:cd06330  141 WAGIGPDYEYGRDSWAAFKAALKKLKpdVEVVGELWPKLGAtDyTAYITALLAA 194
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
438-557 2.54e-07

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: 52.79  E-value: 2.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 438 SYKNYASKDKnplgVKGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTK 514
Cdd:cd13725   20 NFQALSGNER----FEGFCVDMLRELAELLRFRYRLRLVedgLYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREK 95
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 330253582 515 FVDFTQPFIESGLVVVAPVKGAKSSPWSFLKPFTIEMWAVTGA 557
Cdd:cd13725   96 VIDFSKPFMTLGISILYRVHMPVESADDLADQTNIEYGTIHAG 138
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
77-386 8.02e-07

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


Pssm-ID: 380610 [Multi-domain]  Cd Length: 375  Bit Score: 52.33  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  77 LHVPFLSfaATDPTLSSLQYPYFLRTTQNdyfqmNAITDFVSYFRWREVVAIFvDDEYGRNGISVLGDALAKKRAKISYK 156
Cdd:cd06387   86 LHTSFIT--PSFPTDADVQFVIQMRPALK-----GAILSLLAHYKWEKFVYLY-DTERGFSILQAIMEAAVQNNWQVTAR 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 157 AAfppG--ADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALdSMEPLDPRALDl 234
Cdd:cd06387  158 SV---GniKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDI-LLERVMHGGAN- 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 235 lqgVVAFRHYTPESDNKRQFKGRWKNL---RFKESLKSDDGFNSyALyAYDSVWLVARALDVFFSQgntvtfSNDPSLRN 311
Cdd:cd06387  233 ---ITGFQIVNNENPMVQQFLQRWVRLderEFPEAKNAPLKYTS-AL-THDAILVIAEAFRYLRRQ------RVDVSRRG 301
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330253582 312 TndSGIKLSKLHI-FNEG---ERFLQVIlemNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSNHTGFSVAP 386
Cdd:cd06387  302 S--AGDCLANPAVpWSQGidiERALKMV---QVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEYERFVPFS 375
PBP1_ABC_ligand_binding-like cd06345
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-353 1.55e-06

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


Pssm-ID: 380568 [Multi-domain]  Cd Length: 356  Bit Score: 51.11  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSL------QYPYFLRTTQNDYFQMNAITDFVSYFRWREV 125
Cdd:cd06345   62 EDKVDAIVGGFRSEVVLAAMEVAAEYKVPFIVTGAASPAITKKvkkdyeKYKYVFRVGPNNSYLGATVAEFLKDLLVEKL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 126 ----VAIFVDD-EYGRNGISVLGDALAKKRAKISYKAAFPPGAdnssiSDLLASVNLMESRifvvhvNPDSGLNIFSvak 200
Cdd:cd06345  142 gfkkVAILAEDaAWGRGIAEALKKLLPEAGLEVVGVERFPTGT-----TDFTPILSKIKAS------GADVIVTIFS--- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 201 slgmMGSGYVwITTDW------LLTALDSMEPLDPRALDLL----QGVVAFRHYTPES---DNKRQFKGrwknlRFKEsl 267
Cdd:cd06345  208 ----GPGGIL-LVKQWaelgvpAPLVGINVPAQDPEFWENTggagEYEITLAFAAPKAkvtPKTKPFVD-----AYKK-- 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 268 KSDDGFNSYALYAYDSVWLVARALDvffsqgNTVTFSNDpslrntndsgiKLSKlhifnegerflqVILEMNYTGLTGQI 347
Cdd:cd06345  276 KYGEAPNYTAYTAYDAIYILAEAIE------RAGSTDPD-----------ALVK------------ALEKTDYEGVRGRI 326

                 ....*.
gi 330253582 348 EFNSEK 353
Cdd:cd06345  327 KFDKKD 332
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
719-776 1.78e-06

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: 50.44  E-value: 1.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 330253582 719 SNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYdHEC 776
Cdd:cd13719  220 QDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWIRY-QEC 276
PBP1_ABC_ligand_binding-like cd06336
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
52-291 3.34e-06

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 group 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 (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.


Pssm-ID: 380559 [Multi-domain]  Cd Length: 345  Bit Score: 50.31  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVpFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFV-SYFRWREVVAIFV 130
Cdd:cd06336   69 QDGVKFIFGPGGSAIAAAVQPVTERNKV-LLLTAAFSDPILGPDNPLLFRIPPTPYEYAPPFIKWLkKNGPIKTVALIAP 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNSS--ISDLLASvnlmesrifvvhvNPD-----------SGLnIFS 197
Cdd:cd06336  148 NDATGKDWAAAFVAAWKAAGGEVVAEEFYDRGTTDFYpvLTKILAL-------------KPDaldlggsspgpAGL-IIK 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 198 VAKSLGMMGsgyVWITTDWlltalDSMEPLDPRA-LDLLQGVVAFRHYTPE---SDNKRQFKGRWKNlRFKESLksddgf 273
Cdd:cd06336  214 QARELGFKG---PFVSEGG-----AKADEILKEVgGEAAEGFIGVLPADDDpiaSPGAKAFVERYKK-KYGEPP------ 278
                        250
                 ....*....|....*...
gi 330253582 274 NSYALYAYDSVWLVARAL 291
Cdd:cd06336  279 NSESALFYDAAYILVKAM 296
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
635-770 3.71e-06

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: 48.85  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 635 LTVQQLTSRIEGMDTLiaSNEPIGVQDGTfAWKFLVNELNIaPSRIIPLKDEEEYLSALQRGpRGGgvAAIVDELpYIKA 714
Cdd:cd13626   90 IIVKKDNTIIKSLEDL--KGKVVGVSLGS-NYEEVARDLAN-GAEVKAYGGANDALQDLANG-RAD--ATLNDRL-AALY 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 330253582 715 LLSNSNCKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd13626  162 ALKNSNLPLKIVGDIVSTAKVGFAFRKDNPeLRKKVNKALAEMKADGTLKKLSEKWF 218
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
49-383 3.75e-06

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


Pssm-ID: 380604 [Multi-domain]  Cd Length: 401  Bit Score: 50.37  E-value: 3.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAIGPQSSGIGHIISHVANELHVPFLsFAATDPTLSSLQYPYFLRTTQNDYFQM---------NAITDFVSY 119
Cdd:cd06381   57 DLMTQGILALVTSTGCASANALQSLTDAMHIPHL-FVQRNPGGSPRTACHLNPSPDGEAYTLasrppvrlnDVMLRLVTE 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 120 FRWREVVaIFVDDEYGRNGI-------SVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVhvNPDSG 192
Cdd:cd06381  136 LRWQKFV-MFYDSEYDIRGLqsfldqaSRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNRYRDTLRRAILLL--SPQGA 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 193 LNIFSVAKSLGMMGSGYVWITTDwlltaldsMEPLDPRALDLLQG-----VVAFRHYTPESDNKRQFKGrwkNLRFKESL 267
Cdd:cd06381  213 HSFINEAVETNLASKDSHWVFVN--------EEISDPEILDLVHSalgrmTVVRQIFPSAKDNQKCFRN---NHRISSLL 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 268 -KSDDGFNSYA----LYAYDSVWLVARALDVFFSQGNTVTFSNDPSLRNTNDSgiklsklhiFNEGERFLQVILEMNYTG 342
Cdd:cd06381  282 cDPQEGYLQMLqisnLYLYDSVLMLANAFHRKLEDRKWHSMASLNCIRKSTKP---------WNGGRSMLDTIKKGHITG 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 330253582 343 LTGQIEFNSEKNRINPAYDILNIK-----STGPLRVGYWSNHTGFS 383
Cdd:cd06381  353 LTGVMEFREDSSNPYVQFEILGTTysetfGKDMRKLATWDSEKGLN 398
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
657-769 4.18e-06

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: 48.81  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 657 IGVQDGTFAWKFLVNELNIAPSRIIPlKDEEEYLSAlqrgpRGGGVAAIVDELP----YIKallSNSNCKFRTVGQEFTR 732
Cdd:cd00994  109 VAVKTGTTSVDYLKENFPDAQLVEFP-NIDNAYMEL-----ETGRADAVVHDTPnvlyYAK---TAGKGKVKVVGEPLTG 179
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 330253582 733 TGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd00994  180 EQYGIAFPKGSELREKVNAALKTLKADGTYDEIYKKW 216
PBP1_ABC_ligand_binding-like cd19982
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
52-163 1.32e-05

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


Pssm-ID: 380637 [Multi-domain]  Cd Length: 302  Bit Score: 48.05  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVD 131
Cdd:cd19982   65 QDKVPLIVGGYSSGITLPVAAVAERQKIPLLVPTAADDDITKPGYKYVFRLNPPASIYAKALFDFFKELVKPKTIAILYE 144
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 330253582 132 DeyGRNGISVL--GDALAKKRA-KISYKAAFPPGA 163
Cdd:cd19982  145 N--TAFGTSVAkaARRFAKKRGiEVVADESYDKGA 177
PBP1_ABC_HAAT-like cd06349
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
52-366 1.60e-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 or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.


Pssm-ID: 380572 [Multi-domain]  Cd Length: 338  Bit Score: 47.95  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLqYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIF-V 130
Cdd:cd06349   65 DDKVVAVIGDFSSSCSMAAAPIYEEAGLVQISPTASHPDFTKG-GDYVFRNSPTQAVEAPFLADYAVKKLGAKKIAIIyL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 131 DDEYGRNGISVLGDALAKKRAKISYKAAFPPGAD--NSSISdllasvNLMESR---IFVVHVNPDSGLnIFSVAKSLG-- 203
Cdd:cd06349  144 NTDWGVSAADAFKKAAKALGGEIVATEAYLPGTKdfSAQIT------KIKNANpdaIYLAAYYNDAAL-IAKQARQLGwd 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 204 --MMGSGYVwITTDWLLTALDSMEpldpraldllqGVVAFRHYTPESDNKrqfkgRWKNlrFKESLKSDDGF--NSYALY 279
Cdd:cd06349  217 vqIFGSSSL-YSPEFIELAGDAAE-----------GVYLSSPFFPESPDP-----EVKE--FVKAYKAKYGEdpDDFAAR 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 280 AYDSVWLVARAldvffsqgntvtfsndpsLRNTNDSGiklsklhifnEGERflQVILEM-NYTGLTGQIEFNSEKNRINp 358
Cdd:cd06349  278 AYDAVNILAEA------------------IEKAGTDR----------EAIR--DALANIkDFSGLTGTITFDENGDVLK- 326

                 ....*...
gi 330253582 359 AYDILNIK 366
Cdd:cd06349  327 SLTILVVK 334
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
657-770 2.63e-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: 46.18  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 657 IGVQDGTFAWKFLvNELNIAPSRIIPLkdeEEYLSALQRGprggGVAAIVDELP----YIKallSNSNCKFRTVGQEFTR 732
Cdd:cd00997  111 VATVAGSTAADYL-RRHDIDVVEVPNL---EAAYTALQDK----DADAVVFDAPvlryYAA---HDGNGKAEVTGSVFLE 179
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 330253582 733 TGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd00997  180 ENYGIVFPTGSPLRKPINQALLNLREDGTYDELYEKWF 217
PBP2_Arg_3 cd13622
Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding ...
426-545 4.13e-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: 45.76  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 426 GKPLKIGVPnrvSYKN-YASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYILYgdgkknpSYDNLISEVAANIFDVAVG 504
Cdd:cd13622    1 SKPLIVGVG---KFNPpFEMQGTNN-ELFGFDIDLMNEICKRIQRTC--QYKPM-------RFDDLLAALNNGKVDVAIS 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 330253582 505 DVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKSSPWSFLK 545
Cdd:cd13622   68 SISITPERSKNFIFSLPYLLSYSQFLTNKDNNISSFLEDLK 108
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
483-530 4.46e-05

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


Pssm-ID: 270342 [Multi-domain]  Cd Length: 219  Bit Score: 45.56  E-value: 4.46e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 330253582 483 KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVV 530
Cdd:cd13624   44 KNMAFDGLIPALQSGKIDIIISGMTITEERKKSVDFSDPYYEAGQAIV 91
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
429-532 4.73e-05

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 45.40  E-value: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582   429 LKIGVpnRVSYKNYASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYILYgdgkknpSYDNLISEVAANIFDVAVGDVTI 508
Cdd:smart00062   2 LRVGT--NGDYPPFSFADEDG-ELTGFDVDLAKAIAKELGLKV--EFVEV-------SFDSLLTALKSGKIDVVAAGMTI 69
                           90       100
                   ....*....|....*....|....
gi 330253582   509 ITNRTKFVDFTQPFIESGLVVVAP 532
Cdd:smart00062  70 TPERAKQVDFSDPYYRSGQVILVR 93
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
77-377 5.10e-05

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: 46.47  E-value: 5.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  77 LHVPFL--SFaatdPTLSSLQYPYFLRTTQNDyfqmnAITDFVSYFRWREVVAIFVDDeygrNGISVLG---DALAKKRA 151
Cdd:cd06390   79 LHVCFItpSF----PVDTSNQFVLQLRPELQD-----ALISVIEHYKWQKFVYIYDAD----RGLSVLQkvlDTAAEKNW 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 152 KIS-------YKAAFppgadnssisdLLASVNLMESRIFVVHVNPDSG-LN-IFSVAKSLGMMGSGYVWITTDWLLTALD 222
Cdd:cd06390  146 QVTavnilttTEEGY-----------RMLFQDLDKKKERLVVVDCESErLNaILGQIVKLEKNGIGYHYILANLGFMDID 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 223 SMEPLDPRAldllqGVVAFR--HYTP-----------ESDNKRQFKGRWKNLRFKESLksddgfnsyalyAYDSVWLVAR 289
Cdd:cd06390  215 LTKFKESGA-----NVTGFQlvNYTDtiparimqqwkNSDSRDLPRVDWKRPKYTSAL------------TYDGVKVMAE 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 290 ALDVFFSQ-------GNTVTFSNDPSLrnTNDSGIKLsklhifnegERFLQvilEMNYTGLTGQIEFNSEKNRINPAYDI 362
Cdd:cd06390  278 AFQSLRRQridisrrGNAGDCLANPAV--PWGQGIDI---------QRALQ---QVRFEGLTGNVQFNEKGRRTNYTLHV 343
                        330
                 ....*....|....*
gi 330253582 363 LNIKSTGPLRVGYWS 377
Cdd:cd06390  344 IEMKHDGIRKIGYWN 358
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
454-532 5.56e-05

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: 46.00  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 454 GFCIDIFEAAIQLLPYpvprTYILY--GDGK----KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGL 527
Cdd:cd13720   67 GYCIDLLEKLAEDLGF----DFDLYivGDGKygawRNGRWTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSL 142

                 ....*.
gi 330253582 528 -VVVAP 532
Cdd:cd13720  143 gILVRT 148
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
49-380 8.89e-05

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: 45.67  E-value: 8.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAIGPQSS-GIGHIISHVANELHVPFLSFAATD-PTLSSLQYPYFLRTTQNDYFQMnAITDFVSYFRWREVV 126
Cdd:cd06394   62 QILPKGVVSVLGPSSSpASASTVSHICGEKEIPHIKVGPEEtPRLQYLRFASVSLYPSNEDISL-AVSRILKSFNYPSAS 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 127 AIFVDDEYGRNGISVLGDALAKKRAkISYKAAfppgADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMG 206
Cdd:cd06394  141 LICAKAECLLRLEELVRQFLISKET-LSVRML----DDSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTS 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 207 SGYVWITT--DWLLTALDSMepldpraLDLLQGVVAFRHYTPESDNKRQFKgRWKNLRFKESLKSDDgFNSYALYA---Y 281
Cdd:cd06394  216 AFYKYILTtmDFPLLHLDGI-------VDDQSNILGFSMFNTSHPFYLEFV-RSLNMSWRENCDAST-YPGPALSSalmF 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 282 DSVWLVARALDvffsqgntvtfsndpSLRNTNDSGIK---LSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINP 358
Cdd:cd06394  287 DAVHVVVSAVR---------------ELNRSQEIGVKplsCTSAQIWQHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNY 351
                        330       340
                 ....*....|....*....|...
gi 330253582 359 AYDILNIKSTGPLRVGYW-SNHT 380
Cdd:cd06394  352 TLRILEKSRQGHREIGVWySNRT 374
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
720-769 9.39e-05

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: 44.84  E-value: 9.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 330253582 720 NCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13714  200 NCNLTQIGGLLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKW 249
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
485-540 1.18e-04

Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate receptor domain GluR0. These domains are found in the GluR0 proteins that have been shown to function as prokaryotic L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. The GluR0 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 44.25  E-value: 1.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 485 PSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKSSP 540
Cdd:cd00997   48 DSVSALLAAVAEGEADIAIAAISITAEREAEFDFSQPIFESGLQILVPNTPLINSV 103
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
721-776 1.30e-04

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: 44.63  E-value: 1.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 721 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 776
Cdd:cd13726  204 CDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
632-770 2.12e-04

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


Pssm-ID: 270406 [Multi-domain]  Cd Length: 238  Bit Score: 43.78  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 632 TSILTVQQltSRIEGMDTLiaSNEPIGVQDGTFAWKFL--VNELNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDE- 708
Cdd:cd13688  103 TRLLVRKD--SGLNSLEDL--AGKTVGVTAGTTTEDALrtVNPLAGLQASVVPVKDHAEGFAALETG----KADAFAGDd 174
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 330253582 709 --LPYIKALLSNSNcKFRTVGQEFTRTGWGFAFQRDSP---LAVDmsTAILQLAEEGKLEKIRKKWL 770
Cdd:cd13688  175 ilLAGLAARSKNPD-DLALIPRPLSYEPYGLMLRKDDPdfrLLVD--RALAQLYQSGEIEKLYDKWF 238
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
483-542 2.13e-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: 43.71  E-value: 2.13e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 483 KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKSSPWS 542
Cdd:cd13629   44 VNTAWDGLIPALQTGKFDLIISGMTITPERNLKVNFSNPYLVSGQTLLVNKKSAAGIKSL 103
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
49-383 2.70e-04

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 receptor of an orphan glutamate receptor family. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 are closer related to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq and tumor necrosis factor family that is secreted from cerebellar granule cells.


Pssm-ID: 380614 [Multi-domain]  Cd Length: 402  Bit Score: 44.26  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKV---VAAIGPQSSGIghiISHVANELHVPFLsFAATDPTLSSLQYPYFLRTTQNDYFQM---------NAITDF 116
Cdd:cd06391   57 ELMNQGIlalVSSIGCTSAGS---LQSLADAMHIPHL-FIQRSTAGTPRSGCGLTRSNRNDDYTLsvrppvylnDVILRV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 117 VSYFRWREVVaIFVDDEYGRNGISVLGDALAKKRAKISYKAAfpPGADNSSISDLLASVNLMES-------RIFVVHVNP 189
Cdd:cd06391  133 VTEYAWQKFI-IFYDSEYDIRGIQEFLDKVSQQGMDVALQKV--ENNINKMITTLFDTMRIEELnryrdtlRRAILVMNP 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 190 DSGLNIFSVAKSLGMMGSGYVWITTDWLLTALDSMEpLDPRALDLLQgVVAFRHYTPESDNKRQFKGrwkNLRFKESL-K 268
Cdd:cd06391  210 ATAKSFITEVVETNLVAFDCHWIIINEEINDVDVQE-LVRRSIGRLT-IIRQTFPVPQNISQRCFRG---NHRISSSLcD 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 269 SDDGFNSYA----LYAYDSVWLVARALDVFFSQGNTVTFSNDPSLRNTNDSgiklsklhiFNEGERFLQVILEMNYTGLT 344
Cdd:cd06391  285 PKDPFAQNMeisnLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKP---------WQGGRSMLETIKKGGVSGLT 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 330253582 345 GQIEFNSEKNRINPAYDILNI-----KSTGPLRVGYWSNHTGFS 383
Cdd:cd06391  356 GLLEFGENGGNPNVHFEILGTnygeeLGRGVRKLGCWNPVTGLN 399
PBP1_ABC_HAAT-like cd19983
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
49-288 3.26e-04

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


Pssm-ID: 380638 [Multi-domain]  Cd Length: 303  Bit Score: 43.73  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  49 ELMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQyPYFLRTTQNDYFQMNAITDFVSYFRWREVVAI 128
Cdd:cd19983   61 ELIAGGVVAIIGHMTSAMTVAVLPVINEAKVLMISPTVSTPELSGKD-DYFFRVTPTTRESAQALARYAYNRGGLRRVAV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 129 FVD---DEYGRNGISVLGDALAKKRAKISYKAAFPPGADnSSISDLLASvnLMESR---IFVVHVNPDSGLnifsVAKSL 202
Cdd:cd19983  140 IYDlsnRAYSESWLDNFRSEFEALGGRIVAEIPFSSGAD-VDFSDLARR--LLASKpdgLLLVASAVDTAM----LAQQI 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 203 GMMGSGYVWITTDWLLTaldsmepldpraLDLLQ-------GVVAFRHYTPESDNKR--QFKGRWKNlRFKEslksDDGF 273
Cdd:cd19983  213 RKLGSKIPLFSSAWAAT------------EELLElggkaveGMLFSQAYDRNSSNPRylAFKEAYEE-RFGR----EPSF 275
                        250
                 ....*....|....*
gi 330253582 274 nsYALYAYDSVWLVA 288
Cdd:cd19983  276 --AAAYAYEAAMVLA 288
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
700-770 3.75e-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: 42.94  E-value: 3.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 330253582 700 GGVAAIVDELPYIKALLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVD-MSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd13629  150 GKADAFIYDQPTPARFAKKNDPTLVALLEPFTYEPLGFAIRKGDPDLLNwLNNFLKQIKGDGTLDELYDKWF 221
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
454-529 4.08e-04

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: 42.65  E-value: 4.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 454 GFCIDIFEAAIQLLPYPVPRTYIlygdgkknpSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVV 529
Cdd:cd00994   23 GFDIDLWEAIAKEAGFKYELQPM---------DFKGIIPALQTGRIDIAIAGITITEERKKVVDFSDPYYDSGLAV 89
PBP1_GC_G-like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
55-332 5.04e-04

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: 43.25  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  55 VVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSlqypyflRTTQNDYFQM--------NAITDFVSYFRWrEVV 126
Cdd:cd06372   69 ISALFGPACPEAAEVTGLLASEWNIPMFGFVGQSPKLDD-------RDVYDTYVKLvpplqrigEVLVKTLQFFGW-THV 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 127 AIF-----------VDDEYGrngisVLGDALaKKRAKISYKAAFppgadNSSISDLLaSVNLME----SRIFVVHVNPDS 191
Cdd:cd06372  141 AMFggssatstwdkVDELWK-----SVENQL-KFNFNVTAKVKY-----DTSNPDLL-QENLRYissvARVIVLICSSED 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 192 GLNIFSVAKSLGMMGSGYVWITTD------WLLTALDSMEPLDPRALD--LLQGVVAFRHYTpESDNKRQFKGRWKNLRF 263
Cdd:cd06372  209 ARSILLEAEKLGLMDGEYVFFLLQqfedsfWKEVLNDEKNQVFLKAYEmvFLIAQSSYGTYG-YSDFRKQVHQKLRRAPF 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 264 KESLKSDDGFNSYALYAYDSVWLVARALDVFFSQGntvtfsNDP--------SLRNTNDS---GIKLSkLHIFNEGERFL 332
Cdd:cd06372  288 YSSISSEDQVSPYSAYLHDAVLLYAMGLKEMLKDG------KDPrdgrallqTLRGYNQTtfyGITGL-VYLDVQGERHM 360
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
438-530 5.20e-04

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: 42.27  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 438 SYKNyaskDKNPLgvKGFCIDIFEA-AIQLLPYPVPRTyilygdgkknPSYDNLISEVAANIFDVAVGDVTIITNRTKFV 516
Cdd:cd13713   14 NFLD----EDNQL--VGFDVDVAKAiAKRLGVKVEPVT----------TAWDGIIAGLWAGRYDIIIGSMTITEERLKVV 77
                         90
                 ....*....|....
gi 330253582 517 DFTQPFIESGLVVV 530
Cdd:cd13713   78 DFSNPYYYSGAQIF 91
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
715-769 5.73e-04

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: 42.70  E-value: 5.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 330253582 715 LLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13721  195 FVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKW 249
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
721-776 6.41e-04

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: 42.71  E-value: 6.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 721 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 776
Cdd:cd13729  205 CDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 260
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
714-769 6.61e-04

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: 42.64  E-value: 6.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 714 ALLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13730  200 AALTDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKW 255
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
721-776 8.00e-04

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: 42.33  E-value: 8.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 721 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 776
Cdd:cd13727  204 CDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
449-524 1.26e-03

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: 41.48  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 449 PLGVKGFCIDIFEAAIQLLP-----YPVPRTYilYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFI 523
Cdd:cd13730   25 PKRYKGFSIDVLDALAKALGfkyeiYQAPDGK--YGHQLHNTSWNGMIGELISKRADLAISAITITPERESVVDFSKRYM 102

                 .
gi 330253582 524 E 524
Cdd:cd13730  103 D 103
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
427-526 1.32e-03

Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes cyclohexadienyl dehydratase PheC. These proteins catalyze the decarboxylation of prephenate to phenylpyruvate in the alternative phenylalanine biosynthesis pathway in some proteobacteria and archaea. The PheC proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Since they the PheC proteins are so similar to periplasmic binding proteins, (PBP), it is evolutionarily plausible that several pre-existing PBP proteins might have been recruited to perform the enzymatic function.


Pssm-ID: 270231 [Multi-domain]  Cd Length: 232  Bit Score: 41.17  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 427 KPLKIGVPNrvSYKNYASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYIlygdgkkNPSYDNLISEVAANIFDVAVGDV 506
Cdd:cd01069   10 GVLRVGTTG--DYKPFTYRDNQG-QYEGYDIDMAEALAKSLGVKV--EFV-------PTSWPTLMDDLAADKFDIAMGGI 77
                         90       100
                 ....*....|....*....|
gi 330253582 507 TIITNRTKFVDFTQPFIESG 526
Cdd:cd01069   78 SITLERQRQAFFSAPYLRFG 97
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
709-769 1.34e-03

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: 41.55  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 330253582 709 LPYIKalLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13731  197 LEYVA--INDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 255
PBP2_Arg_STM4351 cd13700
Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding ...
484-538 1.38e-03

Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding protein fold; This group includes domains similar to Escherichia coli arginine third transport system. STM4351 is the high arginine specific periplasmic-binding protein of ABC transport system. STM4351 belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270418 [Multi-domain]  Cd Length: 222  Bit Score: 41.28  E-value: 1.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 330253582 484 NPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKS 538
Cdd:cd13700   47 NQAFDSLIPSLKFKKFDAVISGMDITPEREKQVSFSTPYYENSAVVIAKKDTYKT 101
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
714-769 1.39e-03

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: 41.37  E-value: 1.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 714 ALLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13716  200 VAINDDDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 255
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
721-776 1.85e-03

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: 41.19  E-value: 1.85e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 721 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 776
Cdd:cd13715  206 CDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC 261
PBP1_ABC_ligand_binding-like cd06338
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
52-291 1.89e-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. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT); however, their ligand specificity has not been determined experimentally.


Pssm-ID: 380561 [Multi-domain]  Cd Length: 347  Bit Score: 41.41  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  52 ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPYflrttqndYFQMNAITD--FVSYFR-WREV--- 125
Cdd:cd06338   69 EDKVDLLLGPYSSGLTLAAAPVAEKYGIPMIAGGAASDSIFERGYKY--------VFGVLPPASdyAKGLLDlLAELgpk 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 126 ---VAIF-VDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNssISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKS 201
Cdd:cd06338  141 pktVAIVyEDDPFGKEVAEGAREAAKKAGLEVVYDESYPPGTTD--FSPLLTKVKAANPDILLVGGYPPDAITLVRQMKE 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 202 LG----MMGSGYVWITTDWlltaldsmepldPRAL-DLLQGVVAFRHYTPESDNKrqFKGRWKNL--RFKESLKSDDGFn 274
Cdd:cd06338  219 LGynpkAFFLTVGPAFPAF------------REALgKDAEGVLGPSQWEPSLPYK--VFPGAKEFvkAYKEKFGEEPSY- 283
                        250
                 ....*....|....*..
gi 330253582 275 sYALYAYDSVWLVARAL 291
Cdd:cd06338  284 -HAAAAYAAGQVLQQAI 299
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
716-769 2.11e-03

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: 40.80  E-value: 2.11e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330253582 716 LSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13722  195 VTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKW 248
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
627-769 3.56e-03

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: 40.06  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 627 YTASLTSILTVQQLTSRIEGMDTLiaSNEPIGVQDGTFAWKFLVNELNIAPSRIIPlkDEEEYLSALQRGPRGggvAAIV 706
Cdd:cd13712   83 YTYSGIQLIVRKNDTRTFKSLADL--KGKKVGVGLGTNYEQWLKSNVPGIDVRTYP--GDPEKLQDLAAGRID---AALN 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 330253582 707 DELpyIKALLSNSNCKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKW 769
Cdd:cd13712  156 DRL--AANYLVKTSLELPPTGGAFARQKSGIPFRKGNPkLKAAINKAIEDLRADGTLAKLSEKW 217
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
439-531 3.58e-03

Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 periplasmic binding protein; This periplasmic substrate component serves as an initial receptor in the ABC transport of glutamine in eubacteria and archaea. After binding the alanine with high affinity, this domain Interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. This alanine specific domain belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 39.76  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 439 YKNYASKDKNPLGVKGFCIDIFEAAIQLLPYPVPRTYIlygdgkknpSYDNLISEVAANIFDVAVGDVTIITNRTKFVDF 518
Cdd:cd13628   10 YPPFEFKIGDRGKIVGFDIELAKTIAKKLGLKLQIQEY---------DFNGLIPALASGQADLALAGITPTPERKKVVDF 80
                         90
                 ....*....|...
gi 330253582 519 TQPFIESGLVVVA 531
Cdd:cd13628   81 SEPYYEASDTIVS 93
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
439-530 4.43e-03

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: 40.03  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 439 YKNYASKDKNPLG---VKGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNR 512
Cdd:cd13722   14 YVMYRKSDKPLYGndrFEGYCLDLLKELSNILGFLYDVKLVpdgKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVR 93
                         90
                 ....*....|....*...
gi 330253582 513 TKFVDFTQPFIESGLVVV 530
Cdd:cd13722   94 EKVIDFSKPFMTLGISIL 111
PBP1_ABC_ligand_binding-like cd06326
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ...
50-165 5.83e-03

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


Pssm-ID: 380549 [Multi-domain]  Cd Length: 339  Bit Score: 39.83  E-value: 5.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582  50 LMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTLSSLQYPY--FLRTTQNDyfQMNAITDFVSYFRWREVVA 127
Cdd:cd06326   64 IEQDKVVALFGYVGTANVEAVLPLLEEAGVPLVGPLTGADSLREPGNPYvfHVRASYAD--EVEKIVRHLATLGLKRIAV 141
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 330253582 128 IFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADN 165
Cdd:cd06326  142 VYQDDPFGKEGLAAAEAALAARGLEPVATAAVARNAAD 179
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
167-214 6.10e-03

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: 39.97  E-value: 6.10e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 330253582 167 SISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITT 214
Cdd:cd06378  180 SDAKTLRQLKKIEAQVILLYCTKEEAQYIFEAAEEAGLTGYGYVWIVP 227
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
692-770 8.99e-03

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: 38.80  E-value: 8.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330253582 692 ALQRGPRGGGVAAIVDELPYIKALLSNsNCKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKWL 770
Cdd:cd13713  139 ALQDLALGRLDAVITDRVTGLNAIKEG-GLPIKIVGKPLYYEPMAIAIRKGDPeLRAAVNKALAEMKADGTLEKISKKWF 217
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
721-776 9.44e-03

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: 38.90  E-value: 9.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 330253582 721 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 776
Cdd:cd13728  204 CDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
 
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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