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Conserved domains on  [gi|30680330|ref|NP_187408|]
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glutamate receptor 1.4 [Arabidopsis thaliana]

Protein Classification

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 ...
47-410 4.46e-158

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: 466.32  E-value: 4.46e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDMGSMEGKLVTTSISMALSDFYHVNNGYRTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNL 126
Cdd:cd19990   1 KIGAILDLNSRVGKEAKVAIEMAVSDFNSDSSSYGTKLVLHVRDSKGDPLQAASAALDLIKNKKVEAIIGPQTSEEASFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 127 AELGEKTKVPVISSFQVPSSLSLAKYNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQNA 206
Cdd:cd19990  81 AELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 207 IHIEYKAEFSVSSNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILTARSMNNFQDTNYLAKE 286
Cdd:cd19990 161 SRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNLLDSLDSSTIS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 287 EMEGVIGFKSYIPLTEELHNFTLRWKRSLRLE---EVVTRMSVCSIWAHDIAWSLARAAEVAKLPGLSVY------DLLE 357
Cdd:cd19990 241 SMQGVIGIKTYIPESSEFQDFKARFRKKFRSEypeEENAEPNIYALRAYDAIWALAHAVEKLNSSGGNISvsdsgkKLLE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 30680330 358 AIpESAKHKGLSGDIKFIDKKFISD-KFEIVNMIGRGERSVGLWNSGSFISNRR 410
Cdd:cd19990 321 EI-LSTKFKGLSGEVQFVDGQLAPPpAFEIVNVIGKGYRELGFWSPGSGFSEVL 373
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
448-778 6.77e-80

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: 257.45  E-value: 6.77e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 448 LRVLVPAGNITPQILEVKTDFKTGVTAATGYCIDVFETSI--LPFNYEVEYIPWPgaiNYKNYNDLVYTLYSQKdkYDAA 525
Cdd:cd13686   3 LRIGVPVKSGFKEFVKVTRDPITNSTSVTGFCIDVFEAAVkrLPYAVPYEFIPFN---DAGSYDDLVYQVYLKK--FDAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 526 VGDITITDNRSLYVDFTLPFTDMGLAVVTAKDKsmwiifkpltlslwltiasffiltgaivwlierhdnadfqgscfqqi 605
Cdd:cd13686  78 VGDITITANRSLYVDFTLPYTESGLVMVVPVKD----------------------------------------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 606 gtllcfgfstlvfahrerlqhnmsrfvvivwifavliltsnytatltsvmtVQQIRGL-KSNENIGFFSASIAANVVNDN 684
Cdd:cd13686 111 ---------------------------------------------------VTDIEELlKSGEYVGYQRGSFVREYLEEV 139
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 685 PtFQGPRYKGLKTADDFTNALRNGTISFIVDEVPYVKLFVAKHPSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKL 764
Cdd:cd13686 140 L-FDESRLKPYGSPEEYAEALSKGSIAAAFDEIPYLKLFLAKYCKKYTMVGPTYKTGGFGFAFPKGSPLVADVSRAILKV 218
                       330
                ....*....|....
gi 30680330 765 RRTEKLKAIENWWF 778
Cdd:cd13686 219 TEGGKLQQIENKWF 232
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
476-657 2.14e-06

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


The actual alignment was detected with superfamily member cd13717:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 360  Bit Score: 50.76  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 476 TGYCIDVFE--TSILPFNYEVEYIP------------WPGAINyknynDLVytlysqKDKYDAAVGDITITDNRSLYVDF 541
Cdd:cd13717  26 EGYCIDLIEeiSEILNFDYEIVEPEdgkfgtmdengeWNGLIG-----DLV------RKEADIALAALSVMAEREEVVDF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 542 TLPFTDM-GLAVVTAKDKSMWIIFKPLTL-------------SLWltiasfFILTgaivwlierhdnadfqgSCFQQIGT 607
Cdd:cd13717  95 TVPYYDLvGITILMKKPERPTSLFKFLTVlelevwreftlkeSLW------FCLT-----------------SLTPQGGG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 30680330 608 llcfgfstlvFAHRerlqhNMS-RFVVIV-WIFAVLILTSnYTATLTSVMTV 657
Cdd:cd13717 152 ----------EAPK-----NLSgRLLVATwWLFVFIIIAS-YTANLAAFLTV 187
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
47-410 4.46e-158

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: 466.32  E-value: 4.46e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDMGSMEGKLVTTSISMALSDFYHVNNGYRTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNL 126
Cdd:cd19990   1 KIGAILDLNSRVGKEAKVAIEMAVSDFNSDSSSYGTKLVLHVRDSKGDPLQAASAALDLIKNKKVEAIIGPQTSEEASFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 127 AELGEKTKVPVISSFQVPSSLSLAKYNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQNA 206
Cdd:cd19990  81 AELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 207 IHIEYKAEFSVSSNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILTARSMNNFQDTNYLAKE 286
Cdd:cd19990 161 SRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNLLDSLDSSTIS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 287 EMEGVIGFKSYIPLTEELHNFTLRWKRSLRLE---EVVTRMSVCSIWAHDIAWSLARAAEVAKLPGLSVY------DLLE 357
Cdd:cd19990 241 SMQGVIGIKTYIPESSEFQDFKARFRKKFRSEypeEENAEPNIYALRAYDAIWALAHAVEKLNSSGGNISvsdsgkKLLE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 30680330 358 AIpESAKHKGLSGDIKFIDKKFISD-KFEIVNMIGRGERSVGLWNSGSFISNRR 410
Cdd:cd19990 321 EI-LSTKFKGLSGEVQFVDGQLAPPpAFEIVNVIGKGYRELGFWSPGSGFSEVL 373
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
448-778 6.77e-80

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: 257.45  E-value: 6.77e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 448 LRVLVPAGNITPQILEVKTDFKTGVTAATGYCIDVFETSI--LPFNYEVEYIPWPgaiNYKNYNDLVYTLYSQKdkYDAA 525
Cdd:cd13686   3 LRIGVPVKSGFKEFVKVTRDPITNSTSVTGFCIDVFEAAVkrLPYAVPYEFIPFN---DAGSYDDLVYQVYLKK--FDAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 526 VGDITITDNRSLYVDFTLPFTDMGLAVVTAKDKsmwiifkpltlslwltiasffiltgaivwlierhdnadfqgscfqqi 605
Cdd:cd13686  78 VGDITITANRSLYVDFTLPYTESGLVMVVPVKD----------------------------------------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 606 gtllcfgfstlvfahrerlqhnmsrfvvivwifavliltsnytatltsvmtVQQIRGL-KSNENIGFFSASIAANVVNDN 684
Cdd:cd13686 111 ---------------------------------------------------VTDIEELlKSGEYVGYQRGSFVREYLEEV 139
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 685 PtFQGPRYKGLKTADDFTNALRNGTISFIVDEVPYVKLFVAKHPSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKL 764
Cdd:cd13686 140 L-FDESRLKPYGSPEEYAEALSKGSIAAAFDEIPYLKLFLAKYCKKYTMVGPTYKTGGFGFAFPKGSPLVADVSRAILKV 218
                       330
                ....*....|....
gi 30680330 765 RRTEKLKAIENWWF 778
Cdd:cd13686 219 TEGGKLQQIENKWF 232
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
61-391 4.19e-62

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: 213.40  E-value: 4.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330    61 LVTTSISMALSDFYHVNNGYR-TRVSVLSRDSHGDPLQALAAAMDLLQTEqVEALVGGQSLLEAKNLAELGEKTKVPVIS 139
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPgTKLEYIILDTCCDPSLALAAALDLLKGE-VVAIIGPSCSSVASAVASLANEWKVPLIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   140 SFQVPSSLS-LAKYNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQNAIHIEYKAEFSVS 218
Cdd:pfam01094  80 YGSTSPALSdLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPPA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   219 SNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILTARSMNNFQDTNYLAKEEMEGVIGFKSYI 298
Cdd:pfam01094 160 QDDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSLVILNPSTLEAAGGVLGFRLHP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   299 PLTEELHNFTLRWKRSLR-LEEVVTRMSV-CSIWAHDIAWSLARAAEVA--KLPGLSVYDLLEAIPESAK---------H 365
Cdd:pfam01094 240 PDSPEFSEFFWEKLSDEKeLYENLGGLPVsYGALAYDAVYLLAHALHNLlrDDKPGRACGALGPWNGGQKllrylknvnF 319
                         330       340
                  ....*....|....*....|....*..
gi 30680330   366 KGLSGDIKF-IDKKFISDKFEIVNMIG 391
Cdd:pfam01094 320 TGLTGNVQFdENGDRINPDYDILNLNG 346
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
568-808 1.19e-55

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: 192.91  E-value: 1.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   568 TLSLWLTIASFFILTGAIVWLIERHDNADFQG-----SCFQQIGTLLCFGFSTLVFA-HRERLQHNMSRFVVIVWIFAVL 641
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGpleteENRFTLSNSLWFSFGALVQQgHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   642 ILTSNYTATLTSVMTVQQIRG-------LKSNENIGFFsASIAANVVNDNPTFQGPRYKGLKTADDFTNALRNGTISFIV 714
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSpiqsledLAKQTKIEYG-TVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   715 DEVPYVKLFVAK-----------HPSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKLRRTEKLKAIENWWFQRQTT 783
Cdd:pfam00060 160 VALVRNGIYAYAllsenyylfqrECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGE 239
                         250       260
                  ....*....|....*....|....*..
gi 30680330   784 --SATSEDTFHPLTVYTFRGLFMITGV 808
Cdd:pfam00060 240 cdSKSSASSSSQLGLKSFAGLFLILGI 266
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
696-778 3.36e-14

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: 70.01  E-value: 3.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330    696 KTADDFTNALRNGTISFIvDEVPYVKLFVAKHpSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKLRRTEKLKAIEN 775
Cdd:smart00079  51 KSYAEGVQRVRVSNYAFI-MESPYLDYELSRN-CDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRN 128

                   ...
gi 30680330    776 WWF 778
Cdd:smart00079 129 KWW 131
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
44-189 8.18e-13

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: 70.35  E-value: 8.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  44 EDVRIGLVVDM-GSME--GKLVTTSISMALSDfyhVN-----NGYRtrVSVLSRDSHGDPLQALAAAMDLLQTEQVEALV 115
Cdd:COG0683   2 DPIKIGVLLPLtGPYAalGQPIKNGAELAVEE---INaaggvLGRK--IELVVEDDASDPDTAVAAARKLIDQDKVDAIV 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680330 116 GGQSLLEAKNLAELGEKTKVPVISSFQVPSSLS-LAKYNYFIQATHDTSSEAKGIA-ALFSNFDWRTAVLIYEDDD 189
Cdd:COG0683  77 GPLSSGVALAVAPVAEEAGVPLISPSATAPALTgPECSPYVFRTAPSDAQQAEALAdYLAKKLGAKKVALLYDDYA 152
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
476-783 3.77e-10

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: 60.76  E-value: 3.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 476 TGYCIDVFE--TSILPFNYEVEYIPWPGAINYknyndlvytLysQKDKYDAAVGDITITDNRSLYVDFTLPFTDMGLAVV 553
Cdd:COG0834  22 VGFDVDLARaiAKRLGLKVEFVPVPWDRLIPA---------L--QSGKVDLIIAGMTITPEREKQVDFSDPYYTSGQVLL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 554 TAKDKSmwiifkpltlslwltiasffiltgaivwlierhdnadfqgscfqqigtllcfgfstlvfahrerlqhnmsrfvv 633
Cdd:COG0834  91 VRKDNS-------------------------------------------------------------------------- 96
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 634 ivwifavliltsnytatltSVMTVQQIRGLKsnenIGFFSASIAANVVNDNptFQGPRYKGLKTADDFTNALRNGTISFI 713
Cdd:COG0834  97 -------------------GIKSLADLKGKT----VGVQAGTTYEEYLKKL--GPNAEIVEFDSYAEALQALASGRVDAV 151
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30680330 714 VDEVPYVKLFVAKHPS-EFVIVETESVTNGFGFAFQKGSP-LVQKVSREIEKLRRTEKLKAIENWWFQRQTT 783
Cdd:COG0834 152 VTDEPVAAYLLAKNPGdDLKIVGEPLSGEPYGIAVRKGDPeLLEAVNKALAALKADGTLDKILEKWFGEDVP 223
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
476-657 2.14e-06

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: 50.76  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 476 TGYCIDVFE--TSILPFNYEVEYIP------------WPGAINyknynDLVytlysqKDKYDAAVGDITITDNRSLYVDF 541
Cdd:cd13717  26 EGYCIDLIEeiSEILNFDYEIVEPEdgkfgtmdengeWNGLIG-----DLV------RKEADIALAALSVMAEREEVVDF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 542 TLPFTDM-GLAVVTAKDKSMWIIFKPLTL-------------SLWltiasfFILTgaivwlierhdnadfqgSCFQQIGT 607
Cdd:cd13717  95 TVPYYDLvGITILMKKPERPTSLFKFLTVlelevwreftlkeSLW------FCLT-----------------SLTPQGGG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 30680330 608 llcfgfstlvFAHRerlqhNMS-RFVVIV-WIFAVLILTSnYTATLTSVMTV 657
Cdd:cd13717 152 ----------EAPK-----NLSgRLLVATwWLFVFIIIAS-YTANLAAFLTV 187
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
47-410 4.46e-158

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: 466.32  E-value: 4.46e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDMGSMEGKLVTTSISMALSDFYHVNNGYRTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNL 126
Cdd:cd19990   1 KIGAILDLNSRVGKEAKVAIEMAVSDFNSDSSSYGTKLVLHVRDSKGDPLQAASAALDLIKNKKVEAIIGPQTSEEASFV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 127 AELGEKTKVPVISSFQVPSSLSLAKYNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQNA 206
Cdd:cd19990  81 AELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 207 IHIEYKAEFSVSSNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILTARSMNNFQDTNYLAKE 286
Cdd:cd19990 161 SRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNLLDSLDSSTIS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 287 EMEGVIGFKSYIPLTEELHNFTLRWKRSLRLE---EVVTRMSVCSIWAHDIAWSLARAAEVAKLPGLSVY------DLLE 357
Cdd:cd19990 241 SMQGVIGIKTYIPESSEFQDFKARFRKKFRSEypeEENAEPNIYALRAYDAIWALAHAVEKLNSSGGNISvsdsgkKLLE 320
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 30680330 358 AIpESAKHKGLSGDIKFIDKKFISD-KFEIVNMIGRGERSVGLWNSGSFISNRR 410
Cdd:cd19990 321 EI-LSTKFKGLSGEVQFVDGQLAPPpAFEIVNVIGKGYRELGFWSPGSGFSEVL 373
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
448-778 6.77e-80

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: 257.45  E-value: 6.77e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 448 LRVLVPAGNITPQILEVKTDFKTGVTAATGYCIDVFETSI--LPFNYEVEYIPWPgaiNYKNYNDLVYTLYSQKdkYDAA 525
Cdd:cd13686   3 LRIGVPVKSGFKEFVKVTRDPITNSTSVTGFCIDVFEAAVkrLPYAVPYEFIPFN---DAGSYDDLVYQVYLKK--FDAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 526 VGDITITDNRSLYVDFTLPFTDMGLAVVTAKDKsmwiifkpltlslwltiasffiltgaivwlierhdnadfqgscfqqi 605
Cdd:cd13686  78 VGDITITANRSLYVDFTLPYTESGLVMVVPVKD----------------------------------------------- 110
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 606 gtllcfgfstlvfahrerlqhnmsrfvvivwifavliltsnytatltsvmtVQQIRGL-KSNENIGFFSASIAANVVNDN 684
Cdd:cd13686 111 ---------------------------------------------------VTDIEELlKSGEYVGYQRGSFVREYLEEV 139
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 685 PtFQGPRYKGLKTADDFTNALRNGTISFIVDEVPYVKLFVAKHPSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKL 764
Cdd:cd13686 140 L-FDESRLKPYGSPEEYAEALSKGSIAAAFDEIPYLKLFLAKYCKKYTMVGPTYKTGGFGFAFPKGSPLVADVSRAILKV 218
                       330
                ....*....|....
gi 30680330 765 RRTEKLKAIENWWF 778
Cdd:cd13686 219 TEGGKLQQIENKWF 232
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
61-391 4.19e-62

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: 213.40  E-value: 4.19e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330    61 LVTTSISMALSDFYHVNNGYR-TRVSVLSRDSHGDPLQALAAAMDLLQTEqVEALVGGQSLLEAKNLAELGEKTKVPVIS 139
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPgTKLEYIILDTCCDPSLALAAALDLLKGE-VVAIIGPSCSSVASAVASLANEWKVPLIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   140 SFQVPSSLS-LAKYNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQNAIHIEYKAEFSVS 218
Cdd:pfam01094  80 YGSTSPALSdLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPPA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   219 SNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILTARSMNNFQDTNYLAKEEMEGVIGFKSYI 298
Cdd:pfam01094 160 QDDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSLVILNPSTLEAAGGVLGFRLHP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   299 PLTEELHNFTLRWKRSLR-LEEVVTRMSV-CSIWAHDIAWSLARAAEVA--KLPGLSVYDLLEAIPESAK---------H 365
Cdd:pfam01094 240 PDSPEFSEFFWEKLSDEKeLYENLGGLPVsYGALAYDAVYLLAHALHNLlrDDKPGRACGALGPWNGGQKllrylknvnF 319
                         330       340
                  ....*....|....*....|....*..
gi 30680330   366 KGLSGDIKF-IDKKFISDKFEIVNMIG 391
Cdd:pfam01094 320 TGLTGNVQFdENGDRINPDYDILNLNG 346
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
568-808 1.19e-55

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: 192.91  E-value: 1.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   568 TLSLWLTIASFFILTGAIVWLIERHDNADFQG-----SCFQQIGTLLCFGFSTLVFA-HRERLQHNMSRFVVIVWIFAVL 641
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGpleteENRFTLSNSLWFSFGALVQQgHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   642 ILTSNYTATLTSVMTVQQIRG-------LKSNENIGFFsASIAANVVNDNPTFQGPRYKGLKTADDFTNALRNGTISFIV 714
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSpiqsledLAKQTKIEYG-TVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   715 DEVPYVKLFVAK-----------HPSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKLRRTEKLKAIENWWFQRQTT 783
Cdd:pfam00060 160 VALVRNGIYAYAllsenyylfqrECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGE 239
                         250       260
                  ....*....|....*....|....*..
gi 30680330   784 --SATSEDTFHPLTVYTFRGLFMITGV 808
Cdd:pfam00060 240 cdSKSSASSSSQLGLKSFAGLFLILGI 266
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
59-336 3.68e-30

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: 122.14  E-value: 3.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  59 GKLVTTSISMALSDFYHVNNGYR-TRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPV 137
Cdd:cd06269  15 GAKVLPAFELALSDVNSRPDLLPkTTLGLAIRDSECNPTQALLSACDLLAAAKVVAILGPGCSASAAPVANLARHWDIPV 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 138 ISsFQVPSSLSLAK--YNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQNAIHIEYKAEF 215
Cdd:cd06269  95 LS-YGATAPGLSDKsrYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEELFQEKGGLITSRQSF 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 216 SvSSNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILTARSMNNFQDTNYLAKEEMEGVIGFK 295
Cdd:cd06269 174 D-ENKDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFVIDGEASSSDEHGDEARQAAEGAITVT 252
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 30680330 296 SYIPLTEELHNFTLRWKRSL------RLEEVVTRMSVCsiWAHDIAW 336
Cdd:cd06269 253 LIFPVVKEFLKFSMELKLKSskrkqgLNEEYELNNFAA--FFYDAVL 297
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
448-778 9.27e-21

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: 92.44  E-value: 9.27e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 448 LRVLVPAGNiTPQILEVKTDFKTGVTAATGYCIDVFE--TSILPFNYEVEYIP---WPGAINyKNYNDLVYTLYsqKDKY 522
Cdd:cd00998   3 LKVVVPLEP-PFVMFVTGSNAVTGNGRFEGYCIDLLKelSQSLGFTYEYYLVPdgkFGAPVN-GSWNGMVGEVV--RGEA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 523 DAAVGDITITDNRSLYVDFTLPFTDMGLAVVTAkdksmwiifkpltlslwltiasffiltgaivwlierhdnadfqgscF 602
Cdd:cd00998  79 DLAVGPITITSERSVVIDFTQPFMTSGIGIMIP----------------------------------------------I 112
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 603 QQIGTLLcfgfstlvfahrerLQHNMSRFVVIV-WIFAVLILTSNYTAtltsVMTVQQIRGLKSNENigffsasiaanvv 681
Cdd:cd00998 113 RSIDDLK--------------RQTDIEFGTVENsFTETFLRSSGIYPF----YKTWMYSEARVVFVN------------- 161
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 682 ndnptfqgprykGLKTADDFtnaLRNGTISFIVDEVPYVKLFVAKHPSEFVIVETESVTNGFGFAFQKGSPLVQKVSREI 761
Cdd:cd00998 162 ------------NIAEGIER---VRKGKVYAFIWDRPYLEYYARQDPCKLIKTGGGFGSIGYGFALPKNSPLTNDLSTAI 226
                       330
                ....*....|....*..
gi 30680330 762 EKLRRTEKLKAIENWWF 778
Cdd:cd00998 227 LKLVESGVLQKLKNKWL 243
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
696-778 3.36e-14

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: 70.01  E-value: 3.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330    696 KTADDFTNALRNGTISFIvDEVPYVKLFVAKHpSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKLRRTEKLKAIEN 775
Cdd:smart00079  51 KSYAEGVQRVRVSNYAFI-MESPYLDYELSRN-CDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRN 128

                   ...
gi 30680330    776 WWF 778
Cdd:smart00079 129 KWW 131
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
48-426 1.85e-13

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: 73.05  E-value: 1.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  48 IGLVVDMGSMEGKLVTTSI----SMALSdfyHVNN------GYRTRVsvLSRDSHGDPLQALAAAMDLLQTE-QVEALVG 116
Cdd:cd06366   2 IGGLFPLSGSKGWWGGAGIlpaaEMALE---HINNrsdilpGYNLEL--IWNDTQCDPGLGLKALYDLLYTPpPKVMLLG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 117 GQSLLEAKNLAELGEKTKVPVIS--SfqvpSSLSLA---KYNYFIQaTHDTSSEAK-GIAALFSNFDWRTAVLIYEDDDD 190
Cdd:cd06366  77 PGCSSVTEPVAEASKYWNLVQLSyaA----TSPALSdrkRYPYFFR-TVPSDTAFNpARIALLKHFGWKRVATIYQNDEV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 191 WRESIQPLVGHFQQNAIHIEYKAEFSvssNEEcIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILt 270
Cdd:cd06366 152 FSSTAEDLEELLEEANITIVATESFS---SED-PTDQLENLKEKDARIIIGLFYEDAARKVFCEAYKLGMYGPKYVWIL- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 271 arsMNNFQDTNYLA--------KEEM----EGVIGFKS--YIPLTEELHN--FTLRWKRSL--RLEEVVTRMSVCSIWAH 332
Cdd:cd06366 227 ---PGWYDDNWWDVpdndvnctPEQMlealEGHFSTELlpLNPDNTKTISglTAQEFLKEYleRLSNSNYTGSPYAPFAY 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 333 DIAWSLA----RAAEVAKLPGLSVYD-----------LLEAIpESAKHKGLSGDIKFiDKKfiSD---KFEIVNMIGRGE 394
Cdd:cd06366 304 DAVWAIAlalnKTIEKLAEYNKTLEDftyndkemadlFLEAM-NSTSFEGVSGPVSF-DSK--GDrlgTVDIEQLQGGSY 379
                       410       420       430
                ....*....|....*....|....*....|..
gi 30680330 395 RSVGLWNSgsfiSNRRRRLSSTKaleTIIWPG 426
Cdd:cd06366 380 VKVGLYDP----NADSLLLLNES---SIVWPG 404
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
44-189 8.18e-13

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: 70.35  E-value: 8.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  44 EDVRIGLVVDM-GSME--GKLVTTSISMALSDfyhVN-----NGYRtrVSVLSRDSHGDPLQALAAAMDLLQTEQVEALV 115
Cdd:COG0683   2 DPIKIGVLLPLtGPYAalGQPIKNGAELAVEE---INaaggvLGRK--IELVVEDDASDPDTAVAAARKLIDQDKVDAIV 76
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680330 116 GGQSLLEAKNLAELGEKTKVPVISSFQVPSSLS-LAKYNYFIQATHDTSSEAKGIA-ALFSNFDWRTAVLIYEDDD 189
Cdd:COG0683  77 GPLSSGVALAVAPVAEEAGVPLISPSATAPALTgPECSPYVFRTAPSDAQQAEALAdYLAKKLGAKKVALLYDDYA 152
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
477-777 1.08e-12

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: 70.49  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 477 GYCIDVFE--TSILPFNYEVEYI---PWPGAINYKNYNDLVYTLYSQKDkyDAAVGDITITDNRSLYVDFTLPFTDMGLA 551
Cdd:cd13723  32 GYCIDLLKelAHILGFSYEIRLVedgKYGAQDDKGQWNGMVKELIDHKA--DLAVAPLTITHVREKAIDFSKPFMTLGVS 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 552 VVTAK----DKSMWIIFKPLTLSLWLTIASFFILTGAIVWLIERHDNADFQGS--------CFQQIGTLL---CFGFSTL 616
Cdd:cd13723 110 ILYRKpngtNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAhpcnpgseVVENNFTLLnsfWFGMGSL 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 617 VFAHRERLQHNMS-RFVVIVWIFAVLILTSNYTATLTSVMTVQQIRGLKSNENIGFFSASIAANVVNDNPTFQGPRYKGL 695
Cdd:cd13723 190 MQQGSELMPKALStRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKI 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 696 KTADDFTNALRNGTISFIVDEVPYVK--------LFVAKHPSEFVIVETESVTN--------GFGFAFQKGSPLVQKVSR 759
Cdd:cd13723 270 STFEKMWAFMSSKPSALVKNNEEGIQraltadyaLLMESTTIEYVTQRNCNLTQigglidskGYGIGTPMGSPYRDKITI 349
                       330
                ....*....|....*....
gi 30680330 760 EIEKLRRTEKLKAI-ENWW 777
Cdd:cd13723 350 AILQLQEEDKLHIMkEKWW 368
Peripla_BP_6 pfam13458
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ...
46-235 2.51e-12

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


Pssm-ID: 433225 [Multi-domain]  Cd Length: 342  Bit Score: 69.22  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330    46 VRIGLVVDM---GSMEGKLVTTSISMAlsdFYHVNNG---YRTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQS 119
Cdd:pfam13458   2 IKIGVLTPLsgpYASSGKSSRAGARAA---IEEINAAggvNGRKIELVVADDQGDPDVAAAAARRLVDQDGVDAIVGGVS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   120 LLEAKNLAELGEKTKVPVISsfqvPSSLSLAKYN-YFIQATHDTSSEAKGIA-ALFSNFDWRTAVLIYEDDDDWRESIQP 197
Cdd:pfam13458  79 SAVALAVAEVLAKKGVPVIG----PAALTGEKCSpYVFSLGPTYSAQATALGrYLAKELGGKKVALIGADYAFGRALAAA 154
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 30680330   198 LVGHFQqnAIHIEYKAEFSVSSNEECIMKQLRKFKASG 235
Cdd:pfam13458 155 AKAAAK--AAGGEVVGEVRYPLGTTDFSSQVLQIKASG 190
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
468-777 7.76e-12

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: 65.73  E-value: 7.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 468 FKTGVTAATGYCIDVFEtSI---LPFNYEVEYIPWPGAINyknynDLvytlysQKDKYDAAVGDITITDNRSLYVDFTLP 544
Cdd:cd13530  15 YIDKNGKLVGFDVDLAN-AIakrLGVKVEFVDTDFDGLIP-----AL------QSGKIDVAISGMTITPERAKVVDFSDP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 545 FTDMGLAVVTAKDKsmWIIFKPltlslwltiasffiltgaivwlierhdnADFQGscfQQIGtllcfgfstlvfahrerl 624
Cdd:cd13530  83 YYYTGQVLVVKKDS--KITKTV----------------------------ADLKG---KKVG------------------ 111
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 625 qhnmsrfvvivwifavliltsnytatltsvmtVQQirglksnenigffsASIAANVVNDNPTFQgpRYKGLKTADDFTNA 704
Cdd:cd13530 112 --------------------------------VQA--------------GTTGEDYAKKNLPNA--EVVTYDNYPEALQA 143
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30680330 705 LRNGTISFIVDEVPYVKLFVAKHPSEFVIVETESVTNGFGFAFQKG-SPLVQKVSREIEKLRRTEKLKAIENWW 777
Cdd:cd13530 144 LKAGRIDAVITDAPVAKYYVKKNGPDLKVVGEPLTPEPYGIAVRKGnPELLDAINKALAELKADGTLDKLLEKW 217
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
134-426 1.33e-10

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


Pssm-ID: 380602  Cd Length: 364  Bit Score: 63.90  E-value: 1.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 134 KVPVI--SSFQvpSSLSlAKYNY--FIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQNAIHI 209
Cdd:cd06379  91 RIPVIgiSARD--SAFS-DKNIHvsFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETLAETKDIKI 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 210 EYKAEFSvsSNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAWILT--ARSMNNFQDtnylakee 287
Cdd:cd06379 168 EKVIEFE--PGEKNFTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIVTeqALAASNVPD-------- 237
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 288 meGVIGFKSYIPLTEELHnftLR---------WKRSLRLEEVVTRMSV-CSiwAHDIAWSLARAaevaklpglsvydLLE 357
Cdd:cd06379 238 --GVLGLQLIHGKNESAH---IRdsvsvvaqaIRELFRSSENITDPPVdCR--DDTNIWKSGQK-------------FFR 297
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30680330 358 AIPESAKHKGLSGDIKFIDK-KFISDKFEIVNMIGRGERS-VGLWNSGSFISNRRRRLSSTKaletIIWPG 426
Cdd:cd06379 298 VLKSVKLSDGRTGRVEFNDKgDRIGAEYDIINVQNPRKLVqVGIYVGSQRPTKSLLSLNDRK----IIWPG 364
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
476-783 3.77e-10

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: 60.76  E-value: 3.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 476 TGYCIDVFE--TSILPFNYEVEYIPWPGAINYknyndlvytLysQKDKYDAAVGDITITDNRSLYVDFTLPFTDMGLAVV 553
Cdd:COG0834  22 VGFDVDLARaiAKRLGLKVEFVPVPWDRLIPA---------L--QSGKVDLIIAGMTITPEREKQVDFSDPYYTSGQVLL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 554 TAKDKSmwiifkpltlslwltiasffiltgaivwlierhdnadfqgscfqqigtllcfgfstlvfahrerlqhnmsrfvv 633
Cdd:COG0834  91 VRKDNS-------------------------------------------------------------------------- 96
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 634 ivwifavliltsnytatltSVMTVQQIRGLKsnenIGFFSASIAANVVNDNptFQGPRYKGLKTADDFTNALRNGTISFI 713
Cdd:COG0834  97 -------------------GIKSLADLKGKT----VGVQAGTTYEEYLKKL--GPNAEIVEFDSYAEALQALASGRVDAV 151
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30680330 714 VDEVPYVKLFVAKHPS-EFVIVETESVTNGFGFAFQKGSP-LVQKVSREIEKLRRTEKLKAIENWWFQRQTT 783
Cdd:COG0834 152 VTDEPVAAYLLAKNPGdDLKIVGEPLSGEPYGIAVRKGDPeLLEAVNKALAALKADGTLDKILEKWFGEDVP 223
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
47-299 5.61e-10

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: 61.57  E-value: 5.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDM---GSMEGKLVTTSISMALSDFyhvN-----NGYRtrVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGG- 117
Cdd:cd06268   1 KIGVVVPLtgpYADYGEEILRGVALAVEEI---NaaggiNGRK--LELVIADDQGDPETAVAVARKLVDDDKVLAVVGHy 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 118 --QSLLEAKNLAelgEKTKVPVISSFQVPSSLSLAKYNYFIQATHDTSSEAKGIA-ALFSNFDWRTAVLIYEDDD---DW 191
Cdd:cd06268  76 ssSVTLAAAPIY---QEAGIPLISPGSTAPELTEGGGPYVFRTVPSDAMQAAALAdYLAKKLKGKKVAILYDDYDygkSL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 192 RESIQPlvgHFQQNAIHIeyKAEFSVSSNEECIMKQLRKFKASGIR-IFVAHISERIAN--RLfpcARRLGMMeegyAWI 268
Cdd:cd06268 153 ADAFKK---ALKALGGEI--VAEEDFPLGTTDFSAQLTKIKAAGPDvLFLAGYGADAANalKQ---ARELGLK----LPI 220
                       250       260       270
                ....*....|....*....|....*....|.
gi 30680330 269 LTARSMNNfQDTNYLAKEEMEGVIGFKSYIP 299
Cdd:cd06268 221 LGGDGLYS-PELLKLGGEAAEGVVVAVPWHP 250
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
34-269 6.98e-10

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


Pssm-ID: 380575 [Multi-domain]  Cd Length: 391  Bit Score: 61.99  E-value: 6.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  34 DNVDRLPVVYEdvRIGLVVDMGsmegklvttsISMALSDFYHVNNgyrTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEA 113
Cdd:cd06352   8 SNSQSLPVGYA--RSAPAIDIA----------IERINSEGLLLPG---FNFEFTYRDSCCDESEAVGAAADLIYKRNVDV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 114 LVG---GQSLLEAKNLAELgekTKVPVISSFQV-PSSLSLAKYNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDD 189
Cdd:cd06352  73 FIGpacSAAADAVGRLATY---WNIPIITWGAVsASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 190 D-WRESIQPLVGHF-QQNAIHIEYKAEFSVSSNEEcIMKQLRKFKASGiRIFVAHISERIANRLFPCARRLGMMEEGYAW 267
Cdd:cd06352 150 SkCFSIANDLEDALnQEDNLTISYYEFVEVNSDSD-YSSILQEAKKRA-RIIVLCFDSETVRQFMLAAHDLGMTNGEYVF 227

                ..
gi 30680330 268 IL 269
Cdd:cd06352 228 IF 229
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
476-778 5.83e-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: 57.30  E-value: 5.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   476 TGYCIDVFET--SILPFNYEVEYIPWPGAINYknyndlvytLysQKDKYDAAVGDITITDNRSLYVDFTLPFTDMGLAVV 553
Cdd:pfam00497  22 VGFDVDLAKAiaKRLGVKVEFVPVSWDGLIPA---------L--QSGKVDLIIAGMTITPERAKQVDFSDPYYYSGQVIL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   554 TAKDKSmwiifkpltlslWLTIASFFILTGAIVwlierhdnadfqgscfqqigtllcfgfstlvfahrerlqhnmsrfvv 633
Cdd:pfam00497  91 VRKKDS------------SKSIKSLADLKGKTV----------------------------------------------- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   634 ivwifAVLILTSNYTATLTSVMTVQQIRGLKSNEnigffsasiaanvvndnptfqgprykglktadDFTNALRNGTISFI 713
Cdd:pfam00497 112 -----GVQKGSTAEELLKNLKLPGAEIVEYDDDA--------------------------------EALQALANGRVDAV 154
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30680330   714 VDEVPYVKLFVAKHPSEFVIVETESVT-NGFGFAFQKGSP-LVQKVSREIEKLRRTEKLKAIENWWF 778
Cdd:pfam00497 155 VADSPVAAYLIKKNPGLNLVVVGEPLSpEPYGIAVRKGDPeLLAAVNKALAELKADGTLAKIYEKWF 221
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
82-410 8.00e-08

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: 55.31  E-value: 8.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  82 TRVSVLSRDSHGDPLQALAAAMDLLQtEQVEALVGGQSLLEAKNLAELGEKTKVPVISSFqvPSSLSLAKYNYFIQATHD 161
Cdd:cd06382  34 KLVPDIERVPRDDSFEASKKVCELLE-EGVAAIFGPSSPSSSDIVQSICDALEIPHIETR--WDPKESNRDTFTINLYPD 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 162 TSSEAKGIAALFSNFDWRTAVLIYEDDddwrES---IQPLVGHFQQNAIHI---EYKAEFSVSSneecimkQLRKFKASG 235
Cdd:cd06382 111 PDALSKAYADLVKSLNWKSFTILYEDD----EGlirLQELLKLPKPKDIPItvrQLDPGDDYRP-------VLKEIKKSG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 236 IRIFVAHISERIANRLFPCARRLGMMEEGYAWILTarsmnNFqDtnyLAKEEMEGVIGFKSYI-------PLTEELHNFT 308
Cdd:cd06382 180 ETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILT-----NL-D---LHTLDLEPFKYSGANItgfrlvdPENPEVKNVL 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 309 LRWKrSLRLEEVVTRMSVCSIWA-----HDIAWSLARAAevaklpglsvydlleaipesakHKGLSGDIKFIDKKFISD- 382
Cdd:cd06382 251 KDWS-KREKEGFNKDIGPGQITTetalmYDAVNLFANAL----------------------KEGLTGPIKFDEEGQRTDf 307
                       330       340
                ....*....|....*....|....*...
gi 30680330 383 KFEIVNMIGRGERSVGLWNSGSFISNRR 410
Cdd:cd06382 308 KLDILELTEGGLVKVGTWNPTDGLNITR 335
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
464-559 8.94e-08

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: 54.11  E-value: 8.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 464 VKTDFKTGVTAATGYCIDVFE--TSILPFNYEVEYIP------------WPGAINyknynDLVytlysqKDKYDAAVGDI 529
Cdd:cd13685  17 KKRDSLSGNPRFEGYCIDLLEelAKILGFDYEIYLVPdgkygsrdengnWNGMIG-----ELV------RGEADIAVAPL 85
                        90       100       110
                ....*....|....*....|....*....|
gi 30680330 530 TITDNRSLYVDFTLPFTDMGLAVVTAKDKS 559
Cdd:cd13685  86 TITAEREEVVDFTKPFMDTGISILMRKPTP 115
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
477-556 1.46e-07

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: 53.88  E-value: 1.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 477 GYCIDVFE--TSILPFNYE---VEYIPWPGAINYKnYNDLVYTLYSQKdkYDAAVGDITITDNRSLYVDFTLPFTDMGLA 551
Cdd:cd13718  58 GFCIDILKklAKDVGFTYDlylVTNGKHGKKINGV-WNGMIGEVVYKR--ADMAVGSLTINEERSEVVDFSVPFVETGIS 134

                ....*
gi 30680330 552 VVTAK 556
Cdd:cd13718 135 VMVAR 139
PBP1_ABC_ligand_binding-like cd19984
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
65-303 1.51e-07

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: 53.76  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  65 SISMALSDFYHVNNGYRTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPVISSfqVP 144
Cdd:cd19984  22 GIELAVEEINAAGGINGKKIELIYEDSKCDPKKAVSAANKLINVDKVKAIIGGVCSSETLAIAPIAEQNKVVLISP--GA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 145 SSLSLAKY-NYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEdDDDWRESIqplvghfqQNAIHIEYKAEFSVSSNEEC 223
Cdd:cd19984 100 SSPEITKAgDYIFRNYPSDAYQGKVLAEFAYNKLYKKVAILYE-NNDYGVGL--------KDVFKKEFEELGGKIVASES 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 224 IMK-------QLRKFKASGIR-IFVAHISERIAnRLFPCARRLGMMEEgyawILTARSMNNfQDTNYLAKEEMEGVIGFK 295
Cdd:cd19984 171 FEQgetdfrtQLTKIKAANPDaIFLPGYPKEGG-LILKQAKELGIKAP----ILGSDGFED-PELLEIAGEAAEGVIFTY 244

                ....*...
gi 30680330 296 SYIPLTEE 303
Cdd:cd19984 245 PAFDDSSE 252
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
491-778 2.20e-07

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: 52.50  E-value: 2.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 491 NYEVEY--IPWPGainyknyndLVYTLysQKDKYDAAVGDITITDNRSLYVDFTLPFTDMGLAVVTAKDKSmwiifkplt 568
Cdd:cd13624  38 GFEVEFknMAFDG---------LIPAL--QSGKIDIIISGMTITEERKKSVDFSDPYYEAGQAIVVRKDST--------- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 569 lslwlTIASFFILTGAIVwlierhdnadfqGScfqQIGTllcfgfstlvfahrerlqhnmsrfvvivwifavliltsnyt 648
Cdd:cd13624  98 -----IIKSLDDLKGKKV------------GV---QIGT----------------------------------------- 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 649 atlTSVMTVQQIrglksnenigffsasiaanvvndnptFQGPRYKGLKTADDFTNALRNGTISFIVDEVPYVKLFVAKHP 728
Cdd:cd13624 117 ---TGAEAAEKI--------------------------LKGAKVKRFDTIPLAFLELKNGGVDAVVNDNPVAAYYVKQNP 167
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 30680330 729 S-EFVIVETESVTNGFGFAFQKG-SPLVQKVSREIEKLRRTEKLKAIENWWF 778
Cdd:cd13624 168 DkKLKIVGDPLTSEYYGIAVRKGnKELLDKINKALKKIKENGTYDKIYKKWF 219
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
94-270 6.97e-07

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-aspartate) subtypes of ionotropic glutamate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-D-asparate) subtypes of ionotropic glutamate receptors. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Glutamate mediates the majority of excitatory synaptic transmission in the central nervous system via two broad classes of ionotropic receptors, characterized by their response to glutamate agonists: N-methyl-D-aspartate (NMDA) and non-NMDA receptors. NMDA receptors have intrinsically slow kinetics, are highly permeable to Ca2+, and are blocked by extracellular Mg2+ in a voltage-dependent manner. Non-NMDA receptors have faster kinetics, are most often only weakly permeable to Ca2+, and are not blocked by extracellular Mg2+. While non-NMDA receptors typically mediate excitatory synaptic responses at resting membrane potentials, NMDA receptors contribute several forms of synaptic plasticity and are thought to play an important role in the development of synaptic pathways. Non-NMDA receptors include alpha-amino-3-hydroxy-5-methyl-4-isoxazole proprionate (AMPA) and kainate receptors.


Pssm-ID: 380591 [Multi-domain]  Cd Length: 339  Bit Score: 52.37  E-value: 6.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  94 DPLQALAAAMDLLQtEQVEALVGGQSLLEAKNLAELGEKTKVPVIS-SFQVPSSLSLAKYNYFiqaTHDTSSEAkgIAAL 172
Cdd:cd06368  48 SHFDATDKACDLLE-KGVVAIVGPSSSDSNNALQSICDALDVPHITvHDDPRLSKSQYSLSLY---PRNQLSQA--VSDL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 173 FSNFDWRTAVLIYEDDDDWREsIQPLVGHFQQNaihieyKAEFSVSSN--------EECIMKQLRKFKASGIRIfvaHIS 244
Cdd:cd06368 122 LKYWRWKRFVLVYDDDDRLRR-LQELLEAARFS------KRFVSVRKVdldyktldETPLLKRKDCSLFSRILI---DLS 191
                       170       180
                ....*....|....*....|....*.
gi 30680330 245 ERIANRLFPCARRLGMMEEGYAWILT 270
Cdd:cd06368 192 PEKAYTFLLQALEMGMTIELYHYFLT 217
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
477-556 8.36e-07

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: 51.10  E-value: 8.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 477 GYCIDVFE--TSILPFNYEV------EYIPWPGAINyKNYNDLVYTLYSQKDkyDAAVGDITITDNRSLYVDFTLPFTDM 548
Cdd:cd13687  22 GFCIDLLKklAEDVNFTYDLylvtdgKFGTVNKSIN-GEWNGMIGELVSGRA--DMAVASLTINPERSEVIDFSKPFKYT 98

                ....*...
gi 30680330 549 GLAVVTAK 556
Cdd:cd13687  99 GITILVKK 106
PBP1_ABC_ligand_binding-like cd06341
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
83-260 9.50e-07

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: 380564 [Multi-domain]  Cd Length: 340  Bit Score: 51.92  E-value: 9.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  83 RVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAkNLAELGEKTKVPVISSFQVPSSLSLAKYNYFIQATHDT 162
Cdd:cd06341  40 KVEYVWCDDQSDPATNLQAARQLVEDEKVFALVGSSSAASG-SANDYLAQAGIPVVGGAGVSVWCFRNMFSNFFSLGGGG 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 163 SSEAKGIAAlfSNFDWRTAVLIYEDDDDW-RESIQPLVGhfQQNAIHIEYKAEFSVSSNEECIMKQLRKFKASGIRIFVA 241
Cdd:cd06341 119 STTTYGQYA--AALGGTKAAVVVTDIPAAsQQLAQQLAA--SLRAAGVEVVGTAPYAAAAPDYTAVAQAAKAAGADAVVG 194
                       170
                ....*....|....*....
gi 30680330 242 HISERIANRLFPCARRLGM 260
Cdd:cd06341 195 VLDPDVAARVLKAARAQGL 213
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
476-657 2.14e-06

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: 50.76  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 476 TGYCIDVFE--TSILPFNYEVEYIP------------WPGAINyknynDLVytlysqKDKYDAAVGDITITDNRSLYVDF 541
Cdd:cd13717  26 EGYCIDLIEeiSEILNFDYEIVEPEdgkfgtmdengeWNGLIG-----DLV------RKEADIALAALSVMAEREEVVDF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 542 TLPFTDM-GLAVVTAKDKSMWIIFKPLTL-------------SLWltiasfFILTgaivwlierhdnadfqgSCFQQIGT 607
Cdd:cd13717  95 TVPYYDLvGITILMKKPERPTSLFKFLTVlelevwreftlkeSLW------FCLT-----------------SLTPQGGG 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 30680330 608 llcfgfstlvFAHRerlqhNMS-RFVVIV-WIFAVLILTSnYTATLTSVMTV 657
Cdd:cd13717 152 ----------EAPK-----NLSgRLLVATwWLFVFIIIAS-YTANLAAFLTV 187
PBP1_SBP-like cd06328
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ...
47-172 8.09e-06

periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); Periplasmic substrate-binding domain of active transport proteins found in gram-negative and gram-positive bacteria. 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: 380551 [Multi-domain]  Cd Length: 336  Bit Score: 48.84  E-value: 8.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDM-GSME--GKLVTTSISMALsdfYHVNNGYRT----RVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQS 119
Cdd:cd06328   1 KIGVITSLtGPLAayGKQTERGFELGL---EYATDGTMEvdgrKIEVIVKDDQGDPDTAKAAATELIGDDGVDILVGTVS 77
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30680330 120 LLEAKNLAELGEKTKVPVISSFQVPSSLSLAKYN-YFIQATHDTSSEAKGIAAL 172
Cdd:cd06328  78 SAVALALAPVAEQNKKILIVGPAAADSITGENWNkYTFRTSRNSWQDAIAGAKA 131
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
477-556 1.08e-05

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: 45.20  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330   477 GYCIDVFET--SILPFNYEVE------YipwpGAINYKNYND------LVytlysqKDKYDAAVGDITITDNRSLYVDFT 542
Cdd:pfam10613  28 GFCIDLLKElaEILGFKYEIRlvpdgkY----GSLDPTTGEWngmigeLI------DGKADLAVAPLTITSEREKVVDFT 97
                          90
                  ....*....|....
gi 30680330   543 LPFTDMGLAVVTAK 556
Cdd:pfam10613  98 KPFMTLGISILMKK 111
PBP1_ABC_ligand_binding-like cd06345
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
47-189 1.73e-05

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


Pssm-ID: 380568 [Multi-domain]  Cd Length: 356  Bit Score: 48.03  E-value: 1.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDMGSMEGKLVTTSISMALSDfyhVNN---GYRTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEA 123
Cdd:cd06345   1 KIGVLGPLSAPAGEAMERGAELAVEE---INAaggILGRKVELVVADTQGKPEDGVAAAERLITEDKVDAIVGGFRSEVV 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30680330 124 KNLAELGEKTKVPVISSfqVPSSLSLA--------KYNYFIQATHDTSSEAKGIAALFSN-----FDWRTAVLIYEDDD 189
Cdd:cd06345  78 LAAMEVAAEYKVPFIVT--GAASPAITkkvkkdyeKYKYVFRVGPNNSYLGATVAEFLKDllvekLGFKKVAILAEDAA 154
PBP1_ABC_ligand_binding-like cd19982
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
59-195 3.26e-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: 46.89  E-value: 3.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  59 GKLVTTSISMALSDFyHVNNGYRTR-VSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPV 137
Cdd:cd19982  16 GEMFKNGYEMALEEI-NAAGGIKGKkLELVIEDDQSKPQTALAAAEKLVSQDKVPLIVGGYSSGITLPVAAVAERQKIPL 94
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30680330 138 ISSFQVPSSLSLAKYNYFIQATHDTSSEAKGIAALFS-NFDWRTAVLIYEdDDDWRESI 195
Cdd:cd19982  95 LVPTAADDDITKPGYKYVFRLNPPASIYAKALFDFFKeLVKPKTIAILYE-NTAFGTSV 152
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
78-235 4.10e-05

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


Pssm-ID: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 46.77  E-value: 4.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  78 NGYRtrVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPVISSFQVPSSLSLAKYNYF-- 155
Cdd:cd06347  37 LGKK--IELIVYDNKSDPTEAANAAQKLIDEDKVVAIIGPVTSSIALAAAPIAQKAKIPMITPSATNPLVTKGGDYIFra 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 156 -----IQAThdtsseakgIAALF--SNFDWRTAVLIYEDDDDWRESiqpLVGHFQQNAIHIEYK--AEFSVSSNEECIMK 226
Cdd:cd06347 115 cftdpFQGA---------ALAKFayEELGAKKAAVLYDVSSDYSKG---LAKAFKEAFEKLGGEivAEETYTSGDTDFSA 182

                ....*....
gi 30680330 227 QLRKFKASG 235
Cdd:cd06347 183 QLTKIKAAN 191
PBP1_As_SBP-like cd06330
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
83-187 4.31e-05

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: 46.40  E-value: 4.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  83 RVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPVISSFQVPSSLSLAKYN-YFIQATHD 161
Cdd:cd06330  40 KIELVVRDDKGKPDEAVRAARELVLQEGVDFLIGTISSGVALAVAPVAEELKVLFIATDAATDRLTEENFNpYVFRTSPN 119
                        90       100
                ....*....|....*....|....*...
gi 30680330 162 TSSEAKGIAALFS--NFDWRTAVLIYED 187
Cdd:cd06330 120 TYMDAVAAALYAAkkPPDVKRWAGIGPD 147
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
690-777 6.80e-05

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


Pssm-ID: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 45.15  E-value: 6.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 690 PRYKGLKTAD-----DFTNALRNGTISFIVDEVPYVKLFVAKHPSEFVIVETESVTNGFGFAFQKGSPLVQKVSREIEKL 764
Cdd:cd13628 127 QPYPGLKTKLynrvnELVQALKSGRVDAAIVEDIVAETFAQKKN*LLESRYIPKEADGSAIAFPKGSPLRDDFNRWLKEM 206
                        90
                ....*....|...
gi 30680330 765 RRTEKLKAIENWW 777
Cdd:cd13628 207 GDSGELELMVRRW 219
PBP1_ABC_ligand_binding-like cd06326
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ...
73-193 1.24e-04

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: 45.23  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  73 FYHVN-----NGyrTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVG--GQSLLEAknLAELGEKTKVPVISSFQVPS 145
Cdd:cd06326  28 FDQVNaaggiNG--RKIRLVTLDDGYDPARTVENTRQLIEQDKVVALFGyvGTANVEA--VLPLLEEAGVPLVGPLTGAD 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 30680330 146 SL--SLAKYNYFIQATHDTssEAKGIAALFSNFDWRTAVLIYEDDDDWRE 193
Cdd:cd06326 104 SLrePGNPYVFHVRASYAD--EVEKIVRHLATLGLKRIAVVYQDDPFGKE 151
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
477-556 1.24e-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: 44.63  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 477 GYCIDVFE--TSILPFNYEVEYIP--WPGAINYKN--YNDLVYTLYSQKDkyDAAVGDITITDNRSLYVDFTLPFTDMGL 550
Cdd:cd13721  32 GYCIDLLRelSTILGFTYEIRLVEdgKYGAQDDVNgqWNGMVRELIDHKA--DLAVAPLAITYVREKVIDFSKPFMTLGI 109

                ....*.
gi 30680330 551 AVVTAK 556
Cdd:cd13721 110 SILYRK 115
PBP1_ABC_ligand_binding-like cd06340
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
83-189 2.09e-04

type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), 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: 44.47  E-value: 2.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  83 RVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGG-QSLLeAKNLAELGEKTKVPVISSFQVPSSLSLAKYNYFIQATHD 161
Cdd:cd06340  43 KIELVVADTQSDPEVAASEAERLITQEGVVAIIGAySSSV-TLAASQVAERYGVPFVTASAVADEITERGFKYVFRTAPT 121
                        90       100       110
                ....*....|....*....|....*....|....
gi 30680330 162 TSSEAKGIAALF------SNFDWRTAVLIYEDDD 189
Cdd:cd06340 122 ASQFAEDAVDFLkelakkKGKKIKKVAIIYEDSA 155
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
477-556 2.42e-04

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: 43.89  E-value: 2.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 477 GYCIDVFE--TSILPFNYEVEYIP--WPGAINYK-NYNDLVYTLYSQKDkyDAAVGDITITDNRSLYVDFTLPFTDMGLA 551
Cdd:cd13722  32 GYCLDLLKelSNILGFLYDVKLVPdgKYGAQNDKgEWNGMVKELIDHRA--DLAVAPLTITYVREKVIDFSKPFMTLGIS 109

                ....*
gi 30680330 552 VVTAK 556
Cdd:cd13722 110 ILYRK 114
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
703-778 2.56e-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: 43.42  E-value: 2.56e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30680330 703 NALRNGTISFIVDEVPYVKLFVAKHPSEFVIVETESVT-NGFGFAFQKGSPLVQKVSREIEKLRRTEKLKAIENWWF 778
Cdd:cd00994 141 MELETGRADAVVHDTPNVLYYAKTAGKGKVKVVGEPLTgEQYGIAFPKGSELREKVNAALKTLKADGTYDEIYKKWF 217
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
109-296 2.67e-04

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


Pssm-ID: 380573  Cd Length: 350  Bit Score: 44.21  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 109 EQVEALVGGQSLLEAKNLAELGEKTKVPVISSFQVPSSLS-LAKYNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYED 187
Cdd:cd06350  93 PNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSdKIRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVSTVYSD 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 188 DDDWRESIQPLVGHFQQNAIHIEYKAEFSVSSNEEC---IMKQLRKFKAsgIRIFVAHISERIANRLFPCARRLGMMeeG 264
Cdd:cd06350 173 DDYGRSGIEAFEREAKERGICIAQTIVIPENSTEDEikrIIDKLKSSPN--AKVVVLFLTESDARELLKEAKRRNLT--G 248
                       170       180       190
                ....*....|....*....|....*....|..
gi 30680330 265 YAWILTARSMNNFQDTNyLAKEEMEGVIGFKS 296
Cdd:cd06350 249 FTWIGSDGWGDSLVILE-GYEDVLGGAIGVVP 279
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
468-557 3.53e-04

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 42.70  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330    468 FKTGVTAATGYCIDVFETSILPFNYEVEYIP--WPGAINyknynDLvytlysQKDKYDAAVGDITITDNRSLYVDFTLPF 545
Cdd:smart00062  15 FADEDGELTGFDVDLAKAIAKELGLKVEFVEvsFDSLLT-----AL------KSGKIDVVAAGMTITPERAKQVDFSDPY 83
                           90
                   ....*....|..
gi 30680330    546 TDMGLAVVTAKD 557
Cdd:smart00062  84 YRSGQVILVRKD 95
PBP1_ABC_ligand_binding-like cd06346
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
47-189 4.76e-04

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: 43.32  E-value: 4.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDM-GSME--GKLVTTSISMALSdfyHVNN--GYRTR-VSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSL 120
Cdd:cd06346   1 KIGALLPLtGPLAslGPPMLAAAELAVE---EINAagGVLGKkVELVVEDSQTDPTAAVDAARKLVDVEGVPAIVGAASS 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30680330 121 LEAKNLAELGEKTKVPVISsfqvPSSLS-----LAKYNYFIQ-ATHDtSSEAKGIAALFSNFDWRTAVLIYEDDD 189
Cdd:cd06346  78 GVTLAVASVAVPNGVVQIS----PSSTSpalttLEDKGYVFRtAPSD-ALQGVVLAQLAAERGFKKVAVIYVNND 147
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
686-778 5.97e-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: 42.32  E-value: 5.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 686 TFQGPRYKGLKTADDFTNALRNGTISFIVDEVPyVKLFVAKHPSEFVIVETESV--TNGFGFAFQKGSPLVQKVSREIEK 763
Cdd:cd00997 124 RRHDIDVVEVPNLEAAYTALQDKDADAVVFDAP-VLRYYAAHDGNGKAEVTGSVflEENYGIVFPTGSPLRKPINQALLN 202
                        90
                ....*....|....*
gi 30680330 764 LRRTEKLKAIENWWF 778
Cdd:cd00997 203 LREDGTYDELYEKWF 217
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
477-549 6.29e-04

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: 42.52  E-value: 6.29e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30680330 477 GYCIDVFE--TSILPFNYEVEYIPWP--GAINYKN--YNDLVYTLysQKDKYDAAVGDITITDNRSLYVDFTLPFTDMG 549
Cdd:cd13714  32 GFCIDLLKelAKILGFNYTIRLVPDGkyGSYDPETgeWNGMVREL--IDGRADLAVADLTITYERESVVDFTKPFMNLG 108
PBP1_RPA0668_benzoate-like cd20014
type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the ...
83-151 1.27e-03

type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the active transport of lignin-derived benzoate derivative compounds, and its close homologs; This group includes RPA0668 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0668 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. 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: 380667 [Multi-domain]  Cd Length: 346  Bit Score: 41.84  E-value: 1.27e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30680330  83 RVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPVISSFQVPSSLSLAK 151
Cdd:cd20014  38 PIELVKEDDEADPDVALQKARKLIEQDKVDVLVGPVSSGVALAIRDVVEQAKVPLIVANAGANALTRAA 106
PBP1_ABC_HAAT-like cd06348
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
47-191 1.97e-03

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


Pssm-ID: 380571 [Multi-domain]  Cd Length: 342  Bit Score: 41.45  E-value: 1.97e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  47 RIGLVVDM---GSMEGKLVTTSISMALSDFyhvNNGYR---TRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSL 120
Cdd:cd06348   1 KIGVALSLtgpGALYGQSQKNGAQLAVEEI---NAAGGvggVKIELIVEDTAGDPEQAINAFQKLINQDKVLAILGPTLS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 121 LEAKNLAELGEKTKVPVISsfqvpsslslakynyfiqathdTSSEAKGIAA----LFSN------------------FDW 178
Cdd:cd06348  78 SEAFAADPIAQQAKVPVVG----------------------ISNTAPGITDigpyIFRNslpedkvipptvkaakkkYGI 135
                       170
                ....*....|...
gi 30680330 179 RTAVLIYEDDDDW 191
Cdd:cd06348 136 KKVAVLYDQDDAF 148
PBP1_SBP-like cd19989
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
84-171 2.27e-03

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: 41.11  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  84 VSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPVISSFQVPSSLSLAKYN-YFIQATHDT 162
Cdd:cd19989  41 VELVVEDTEGKPATAVQKARKLVEQDGVDFLTGAVSSAVALAVAPKAAELKVPYLVTVAADDELTGENCNrYTFRVNTSD 120

                ....*....
gi 30680330 163 SSEAKGIAA 171
Cdd:cd19989 121 RMIARALAP 129
PBP2_mlr5654_like cd13702
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
518-560 2.56e-03

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


Pssm-ID: 270420 [Multi-domain]  Cd Length: 223  Bit Score: 40.38  E-value: 2.56e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 30680330 518 QKDKYDAAVGDITITDNRSLYVDFTLPFTDMGLAVVTAKDKSM 560
Cdd:cd13702  58 QAKKFDAIIASMSITPERKKQVDFTDPYYTNPLVFVAPKDSTI 100
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
477-591 3.79e-03

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: 40.38  E-value: 3.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 477 GYCIDVFE--TSILPFNYEVEYIP-----WPGAINykNYNDLVYTLYSQKDkyDAAVGDITITDNRSLYVDFTLPFTDMG 549
Cdd:cd13724  32 GFCVDMLKelAEILRFNYKIRLVGdgvygVPEANG--TWTGMVGELIARKA--DLAVAGLTITAEREKVIDFSKPFMTLG 107
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30680330 550 LAVV----TAKDKSMWIIFKPLTLSLWLTIASFFILTGAIVWLIER 591
Cdd:cd13724 108 ISILyrvhMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVAR 153
PBP1_ABC_ligand_binding-like cd06337
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
76-141 4.26e-03

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


Pssm-ID: 380560 [Multi-domain]  Cd Length: 354  Bit Score: 40.36  E-value: 4.26e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30680330  76 VNNGYRTRVSVLSRDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPVISSF 141
Cdd:cd06337  36 KVGGKKYPVEIVVRDSQSDPNRAGEAARDLILRDKVDLMLASGTPDTVNPVADQCEANGVPCISTD 101
PBP1_Nba-like cd06359
type 1 periplasmic binding component of active transport systems predicted to be involved in ...
84-171 4.54e-03

type 1 periplasmic binding component of active transport systems predicted to be involved in 2-nitrobenzoic acid degradation pathway; This group includes the type 1 periplasmic binding component of active transport systems that are predicted to be involved in 2-nitrobenzoic acid degradation pathway; their substrate specificities are not well characterized.


Pssm-ID: 380582 [Multi-domain]  Cd Length: 333  Bit Score: 40.32  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  84 VSVLSRDSHGDPLQALAAAMDLLQTEQVEALVG--GQSLLEA--KNLAelgeKTKVPVISSFQVPSSL--SLAKYNYFIQ 157
Cdd:cd06359  39 VEVVVEDDQLKPDVAKQAAERLIERDKVDFVTGiiFSNVMLAvvKPVV----DSKVFYISANAGPSDLagKGCNPNFFVT 114
                        90
                ....*....|....*
gi 30680330 158 ATH-DTSSEAKGIAA 171
Cdd:cd06359 115 SWQnDQLHEAAGKYA 129
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
712-778 5.66e-03

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


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 39.09  E-value: 5.66e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30680330 712 FIVDEvPYVKLFVAKHPSEFVIVETESVTNGFGFAFQKGSP-LVQKVSREIEKLRRTEKLKAIENWWF 778
Cdd:cd13629 155 FIYDQ-PTPARFAKKNDPTLVALLEPFTYEPLGFAIRKGDPdLLNWLNNFLKQIKGDGTLDELYDKWF 221
PBP1_ABC_RPA1789-like cd06333
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ...
78-199 7.13e-03

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: 39.45  E-value: 7.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  78 NGYRTRVSVLsrDSHGDPLQALAAAMDLLQTEQVEALVGGQSLLEAKNLAELGEKTKVPVISsfQVPSS-LSLAKYNYFI 156
Cdd:cd06333  37 NGRKLELIVY--DDESDPTKAVTNARKLIEEDKVDAIIGPSTTGESLAVAPIAEEAKVPLIS--LAGAAaIVEPVRKWVF 112
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30680330 157 QATHDTSSEAKGIAALFSNFDWRTAVLIYEDD---DDWRESIQPLV 199
Cdd:cd06333 113 KTPQSDSLVAEAILDYMKKKGIKKVALLGDSDaygQSGRAALKKLA 158
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
58-216 8.79e-03

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: 39.54  E-value: 8.79e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  58 EGKLVTTSISMALSDfyhVNN------GYRtrVSVLSRDSHGDPLQALAAAMDLLqTEQVEALVG--GQSLLEAKNLAEL 129
Cdd:cd06370  18 QGRVISGAITLAVDD---VNNdpnllpGHT--LSFVWNDTRCDELLSIRAMTELW-KRGVSAFIGpgCTCATEARLAAAF 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 130 gektKVPVISSF---QVPSSLSLakYNYFIQaTHDTSSE-AKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVGHFQQN 205
Cdd:cd06370  92 ----NLPMISYKcadPEVSDKSL--YPTFAR-TIPPDSQiSKSVIALLKHFNWNKVSIVYENETKWSKIADTIKELLELN 164
                       170
                ....*....|.
gi 30680330 206 AIHIEYKAEFS 216
Cdd:cd06370 165 NIEINHEEYFP 175
PBP1_NPR_C cd06386
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ...
62-267 9.08e-03

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


Pssm-ID: 380609 [Multi-domain]  Cd Length: 391  Bit Score: 39.46  E-value: 9.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330  62 VTTSISMALSDFYHVNNGYR-TRVSVLSRDSH-GDplQALAAAMDL--LQTEQVEALVGGQSLLEAKNLAELGEKTKVPV 137
Cdd:cd06386  22 VRPAIEYALRSVEGNGLLPPgTRFNVAYEDSDcGN--RALFSLVDRvaQKRAKPDLILGPVCEYAAAPVARLASHWNLPM 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30680330 138 ISSFQVPSSLSLAK--YNYFIQATHDTSSEAKGIAALFSNFDWRTAVLIYEDDDDWRESIQPLVG-H--FQQNAIHIeyk 212
Cdd:cd06386 100 LSAGALAAGFSHKDseYSHLTRVAPAYAKMGEMFLALFRHHHWSRAFLVYSDDKLERNCYFTLEGvHevFQEEGLHT--- 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30680330 213 AEFSVSSNEECIMKQLRKFKASGIRIFVAHISERIANRLFPCARRLGMMEEGYAW 267
Cdd:cd06386 177 SIYSFDETKDLDLEEIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTNGDYAF 231
 
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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