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Conserved domains on  [gi|1039011994|gb|ANM61816|]
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glutamate receptor 3.5 [Arabidopsis thaliana]

Protein Classification

glutamate receptor( domain architecture ID 14448285)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
49-444 2.68e-150

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: 448.99  E-value: 2.68e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDSFIGRAAKLAFVAAIEDINADQSILRgTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHI 127
Cdd:cd19990     1 KIGAILDLNSRVGKEAKVAIEMAVSDFNSDSSSYG-TKLVLHVRDSKGDPLQAASAALDLIKNkKVEAIIGPQTSEEASF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKK 207
Cdd:cd19990    80 VAELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 208 RAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALDSMeplDP 287
Cdd:cd19990   160 GSRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNLLDSL---DS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 288 RALDLLQGVVAFRHYTPESDNKRQFKGRWKN-LRFKESLKSDDGFNSYALYAYDSVWLVARALDVFFSQGNTVTFSndps 366
Cdd:cd19990   237 STISSMQGVIGIKTYIPESSEFQDFKARFRKkFRSEYPEEENAEPNIYALRAYDAIWALAHAVEKLNSSGGNISVS---- 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 367 lrntndsgiklsklhifNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSNHTGFSVAP 444
Cdd:cd19990   313 -----------------DSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFEIVNVIGKGYRELGFWSPGSGFSEVL 373
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
485-828 7.97e-71

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


:

Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 234.34  E-value: 7.97e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 485 KPLKIGVPNRVSYKNYASKDKNPLG----VKGFCIDIFEAAIQLLPYPVPRTYILYGDgkkNPSYDNLISEVAANIFDVA 560
Cdd:cd13686     1 KKLRIGVPVKSGFKEFVKVTRDPITnstsVTGFCIDVFEAAVKRLPYAVPYEFIPFND---AGSYDDLVYQVYLKKFDAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 561 VGDVTIITNRTKFVDFTQPFIESGLVVVAPVKgaksspwsflkpftiemwavtgalflfvgaviwilehrfneefrgppr 640
Cdd:cd13686    78 VGDITITANRSLYVDFTLPYTESGLVMVVPVK------------------------------------------------ 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 641 rqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsRIEGMDTLIASNEPIGVQDG 720
Cdd:cd13686   110 ------------------------------------------------------------DVTDIEELLKSGEYVGYQRG 129
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 721 TFAWKFLVNELNiAPSRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSnSNCKFRT-VGQEFTRTGWGFAFQR 799
Cdd:cd13686   130 SFVREYLEEVLF-DESRLKPYGSPEEYAEALSKGS----IAAAFDEIPYLKLFLA-KYCKKYTmVGPTYKTGGFGFAFPK 203
                         330       340
                  ....*....|....*....|....*....
gi 1039011994 800 DSPLAVDMSTAILQLAEEGKLEKIRKKWL 828
Cdd:cd13686   204 GSPLVADVSRAILKVTEGGKLQQIENKWF 232
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
49-444 2.68e-150

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: 448.99  E-value: 2.68e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDSFIGRAAKLAFVAAIEDINADQSILRgTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHI 127
Cdd:cd19990     1 KIGAILDLNSRVGKEAKVAIEMAVSDFNSDSSSYG-TKLVLHVRDSKGDPLQAASAALDLIKNkKVEAIIGPQTSEEASF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKK 207
Cdd:cd19990    80 VAELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 208 RAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALDSMeplDP 287
Cdd:cd19990   160 GSRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNLLDSL---DS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 288 RALDLLQGVVAFRHYTPESDNKRQFKGRWKN-LRFKESLKSDDGFNSYALYAYDSVWLVARALDVFFSQGNTVTFSndps 366
Cdd:cd19990   237 STISSMQGVIGIKTYIPESSEFQDFKARFRKkFRSEYPEEENAEPNIYALRAYDAIWALAHAVEKLNSSGGNISVS---- 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 367 lrntndsgiklsklhifNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSNHTGFSVAP 444
Cdd:cd19990   313 -----------------DSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFEIVNVIGKGYRELGFWSPGSGFSEVL 373
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
63-426 1.30e-102

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: 323.95  E-value: 1.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  63 AAKLAFVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMENKVVAAIGPQSSGIGHIISHVANELHVPFLSF 142
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKGEVVAIIGPSCSSVASAVASLANEWKVPLISY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 143 AATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGA 221
Cdd:pfam01094  81 GSTSPALSDLNrYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPPAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 222 DNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALDSMEPLDpraLDLLQGVVAFRH 301
Cdd:pfam01094 161 DDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSLVILNPST---LEAAGGVLGFRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 302 YTPESDNKRQFKGrWKNLRFKESLKSDDGFN-SYALYAYDSVWLVARALDvffsqgntvtfsndpSLRNTNDSGIKLSKL 380
Cdd:pfam01094 238 HPPDSPEFSEFFW-EKLSDEKELYENLGGLPvSYGALAYDAVYLLAHALH---------------NLLRDDKPGRACGAL 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1039011994 381 HIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKST 426
Cdd:pfam01094 302 GPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
485-828 7.97e-71

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


Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 234.34  E-value: 7.97e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 485 KPLKIGVPNRVSYKNYASKDKNPLG----VKGFCIDIFEAAIQLLPYPVPRTYILYGDgkkNPSYDNLISEVAANIFDVA 560
Cdd:cd13686     1 KKLRIGVPVKSGFKEFVKVTRDPITnstsVTGFCIDVFEAAVKRLPYAVPYEFIPFND---AGSYDDLVYQVYLKKFDAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 561 VGDVTIITNRTKFVDFTQPFIESGLVVVAPVKgaksspwsflkpftiemwavtgalflfvgaviwilehrfneefrgppr 640
Cdd:cd13686    78 VGDITITANRSLYVDFTLPYTESGLVMVVPVK------------------------------------------------ 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 641 rqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsRIEGMDTLIASNEPIGVQDG 720
Cdd:cd13686   110 ------------------------------------------------------------DVTDIEELLKSGEYVGYQRG 129
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 721 TFAWKFLVNELNiAPSRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSnSNCKFRT-VGQEFTRTGWGFAFQR 799
Cdd:cd13686   130 SFVREYLEEVLF-DESRLKPYGSPEEYAEALSKGS----IAAAFDEIPYLKLFLA-KYCKKYTmVGPTYKTGGFGFAFPK 203
                         330       340
                  ....*....|....*....|....*....
gi 1039011994 800 DSPLAVDMSTAILQLAEEGKLEKIRKKWL 828
Cdd:cd13686   204 GSPLVADVSRAILKVTEGGKLQQIENKWF 232
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
606-860 3.42e-63

Ligand-gated ion channel; This family includes the four transmembrane regions of the ionotropic glutamate receptors and NMDA receptors.


Pssm-ID: 459656 [Multi-domain]  Cd Length: 267  Bit Score: 214.86  E-value: 3.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 606 TIEMWAVTGALFLFVGAVIWILEHRFNEEFRGP-----PRRQIITVFWFSFSTMFFS-HRENTVSTLGRFVLLVWLFVVL 679
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPleteeNRFTLSNSLWFSFGALVQQgHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 680 IINSSYTASLTSILTVQQLTSRIEGMDTLiASNEPIGVQDGTFAWKFLVNELNIAPSRIIPLKDEEEYLSALQRGPRGGG 759
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSPIQSLEDL-AKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 760 VAAIVDELPYIKALLSNS------NCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHE 833
Cdd:pfam00060 160 VALVRNGIYAYALLSENYylfqreCCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGE 239
                         250       260
                  ....*....|....*....|....*..
gi 1039011994 834 CTMQISDTENYQISVQSFWGLFLICGV 860
Cdd:pfam00060 240 CDSKSSASSSSQLGLKSFAGLFLILGI 266
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
701-830 2.45e-41

Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic homologues are represented by a separate alignment: PBPb


Pssm-ID: 197504 [Multi-domain]  Cd Length: 133  Bit Score: 147.82  E-value: 2.45e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  701 RIEGMDTLIAS-NEPIGVQDGTFAWKFLVNELNIAPSRIIPL-KDEEEYLSALQRGPRGGGVA--AIVDELPYIKALLSN 776
Cdd:smart00079   1 PITSVEDLAKQtKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYmKSPEVFVKSYAEGVQRVRVSnyAFIMESPYLDYELSR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039011994  777 sNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTY 830
Cdd:smart00079  81 -NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
48-431 8.31e-28

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: 115.03  E-value: 8.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  48 VNVGALFTY---DSFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSG 123
Cdd:COG0683     4 IKIGVLLPLtgpYAALGQPIKNGAELAVEEINAAGGVL-GRKIELVVEDDASDPDTAVAAARKLIDQdKVDAIVGPLSSG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 124 IGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSY-FRWREVVAIFVDDEYGRNGISVLG 201
Cdd:COG0683    83 VALAVAPVAEEAGVPLISPSATAPALTGPEcSPYVFRTAPSDAQQAEALADYLAKkLGAKKVALLYDDYAYGQGLAAAFK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 202 DALAKKRAKISYKAAFPPGAdnSSISDLLAsvNLMESR---IFVVHVNPDSGLnifsVAKSLGMMGsgyvwittdwllta 278
Cdd:COG0683   163 AALKAAGGEVVGEEYYPPGT--TDFSAQLT--KIKAAGpdaVFLAGYGGDAAL----FIKQAREAG-------------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 279 ldsmepldpraldlLQGVVAfrhytpesdnkRQFKGRWKNlrfkeslKSDDGFNSYALYAYDSVWLVARALDvffsQGNT 358
Cdd:COG0683   221 --------------LKGPLN-----------KAFVKAYKA-------KYGREPSSYAAAGYDAALLLAEAIE----KAGS 264
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011994 359 VTfsndpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYdILNIKSTGPLRV 431
Cdd:COG0683   265 TD-------------------------REAVRDALEGLKFDGVTGPITFDPDGQGVQPVY-IVQVKADGKFVV 311
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
700-831 3.02e-12

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 66.93  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 700 SRIEGMDTLiaSNEPIGVQDGTFAWKFLVNelNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDELPYIKALLS-NSN 778
Cdd:COG0834    96 SGIKSLADL--KGKTVGVQAGTTYEEYLKK--LGPNAEIVEFDSYAEALQALASG----RVDAVVTDEPVAAYLLAkNPG 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039011994 779 CKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKWLTYD 831
Cdd:COG0834   168 DDLKIVGEPLSGEPYGIAVRKGDPeLLEAVNKALAALKADGTLDKILEKWFGED 221
PRK15404 PRK15404
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
71-211 4.41e-03

high-affinity branched-chain amino acid ABC transporter substrate-binding protein;


Pssm-ID: 237959 [Multi-domain]  Cd Length: 369  Bit Score: 40.39  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINADQSIlRGTKLNIVFQDTNCSGFVGTMGAlqlmeNKVVaaigpqSSGIGHIISHVANELHVP-----------F 139
Cdd:PRK15404   52 AIEDINAKGGI-KGDKLEGVEYDDACDPKQAVAVA-----NKVV------NDGIKYVIGHLCSSSTQPasdiyedegilM 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 140 LSFAATDPTLSSLQYPYFLRTTQNDYFQ----MNAITDFVSYFRwrevVAIFVDDE-YGRNGISVLGDALAKKRAKI 211
Cdd:PRK15404  120 ITPAATAPELTARGYQLIFRTIGLDSDQgptaAKYILEKVKPKR----IAVLHDKQqYGEGLARSVKDGLKKAGANV 192
 
Name Accession Description Interval E-value
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
49-444 2.68e-150

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: 448.99  E-value: 2.68e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDSFIGRAAKLAFVAAIEDINADQSILRgTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHI 127
Cdd:cd19990     1 KIGAILDLNSRVGKEAKVAIEMAVSDFNSDSSSYG-TKLVLHVRDSKGDPLQAASAALDLIKNkKVEAIIGPQTSEEASF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKK 207
Cdd:cd19990    80 VAELGNKAQVPIISFSATSPTLSSLRWPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 208 RAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALDSMeplDP 287
Cdd:cd19990   160 GSRIEYRVALPPSSPEDSIEEELIKLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNLLDSL---DS 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 288 RALDLLQGVVAFRHYTPESDNKRQFKGRWKN-LRFKESLKSDDGFNSYALYAYDSVWLVARALDVFFSQGNTVTFSndps 366
Cdd:cd19990   237 STISSMQGVIGIKTYIPESSEFQDFKARFRKkFRSEYPEEENAEPNIYALRAYDAIWALAHAVEKLNSSGGNISVS---- 312
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 367 lrntndsgiklsklhifNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSNHTGFSVAP 444
Cdd:cd19990   313 -----------------DSGKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFEIVNVIGKGYRELGFWSPGSGFSEVL 373
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
63-426 1.30e-102

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: 323.95  E-value: 1.30e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  63 AAKLAFVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMENKVVAAIGPQSSGIGHIISHVANELHVPFLSF 142
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKGEVVAIIGPSCSSVASAVASLANEWKVPLISY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 143 AATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGA 221
Cdd:pfam01094  81 GSTSPALSDLNrYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPPAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 222 DNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALDSMEPLDpraLDLLQGVVAFRH 301
Cdd:pfam01094 161 DDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSLVILNPST---LEAAGGVLGFRL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 302 YTPESDNKRQFKGrWKNLRFKESLKSDDGFN-SYALYAYDSVWLVARALDvffsqgntvtfsndpSLRNTNDSGIKLSKL 380
Cdd:pfam01094 238 HPPDSPEFSEFFW-EKLSDEKELYENLGGLPvSYGALAYDAVYLLAHALH---------------NLLRDDKPGRACGAL 301
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1039011994 381 HIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKST 426
Cdd:pfam01094 302 GPWNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
485-828 7.97e-71

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


Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 234.34  E-value: 7.97e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 485 KPLKIGVPNRVSYKNYASKDKNPLG----VKGFCIDIFEAAIQLLPYPVPRTYILYGDgkkNPSYDNLISEVAANIFDVA 560
Cdd:cd13686     1 KKLRIGVPVKSGFKEFVKVTRDPITnstsVTGFCIDVFEAAVKRLPYAVPYEFIPFND---AGSYDDLVYQVYLKKFDAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 561 VGDVTIITNRTKFVDFTQPFIESGLVVVAPVKgaksspwsflkpftiemwavtgalflfvgaviwilehrfneefrgppr 640
Cdd:cd13686    78 VGDITITANRSLYVDFTLPYTESGLVMVVPVK------------------------------------------------ 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 641 rqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsRIEGMDTLIASNEPIGVQDG 720
Cdd:cd13686   110 ------------------------------------------------------------DVTDIEELLKSGEYVGYQRG 129
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 721 TFAWKFLVNELNiAPSRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSnSNCKFRT-VGQEFTRTGWGFAFQR 799
Cdd:cd13686   130 SFVREYLEEVLF-DESRLKPYGSPEEYAEALSKGS----IAAAFDEIPYLKLFLA-KYCKKYTmVGPTYKTGGFGFAFPK 203
                         330       340
                  ....*....|....*....|....*....
gi 1039011994 800 DSPLAVDMSTAILQLAEEGKLEKIRKKWL 828
Cdd:cd13686   204 GSPLVADVSRAILKVTEGGKLQQIENKWF 232
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
606-860 3.42e-63

Ligand-gated ion channel; This family includes the four transmembrane regions of the ionotropic glutamate receptors and NMDA receptors.


Pssm-ID: 459656 [Multi-domain]  Cd Length: 267  Bit Score: 214.86  E-value: 3.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 606 TIEMWAVTGALFLFVGAVIWILEHRFNEEFRGP-----PRRQIITVFWFSFSTMFFS-HRENTVSTLGRFVLLVWLFVVL 679
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPleteeNRFTLSNSLWFSFGALVQQgHRENPRSLSGRIVVGVWWFFAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 680 IINSSYTASLTSILTVQQLTSRIEGMDTLiASNEPIGVQDGTFAWKFLVNELNIAPSRIIPLKDEEEYLSALQRGPRGGG 759
Cdd:pfam00060  81 ILLSSYTANLAAFLTVERMQSPIQSLEDL-AKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKDALNEEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 760 VAAIVDELPYIKALLSNS------NCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHE 833
Cdd:pfam00060 160 VALVRNGIYAYALLSENYylfqreCCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKWWPKSGE 239
                         250       260
                  ....*....|....*....|....*..
gi 1039011994 834 CTMQISDTENYQISVQSFWGLFLICGV 860
Cdd:pfam00060 240 CDSKSSASSSSQLGLKSFAGLFLILGI 266
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
49-344 2.36e-45

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: 166.44  E-value: 2.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDSFIGRAAKL--AFVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIG 125
Cdd:cd06269     1 TIGALLPVHDYLESGAKVlpAFELALSDVNSRPDLLPKTTLGLAIRDSECNPTQALLSACDLLAAaKVVAILGPGCSASA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 126 HIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDAL 204
Cdd:cd06269    81 APVANLARHWDIPVLSYGATAPGLSDKSrYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEELF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 205 AKKRAKISYKAAFPPGADNsSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLltaLDSMEP 284
Cdd:cd06269   161 QEKGGLITSRQSFDENKDD-DLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFVIDGE---ASSSDE 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039011994 285 LDPRALDLLQGVVAFRHYTPESDNKRQF--KGRWKNLRFKESLKSDDGFNSYALYAYDSVWL 344
Cdd:cd06269   237 HGDEARQAAEGAITVTLIFPVVKEFLKFsmELKLKSSKRKQGLNEEYELNNFAAFFYDAVLA 298
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
701-830 2.45e-41

Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic homologues are represented by a separate alignment: PBPb


Pssm-ID: 197504 [Multi-domain]  Cd Length: 133  Bit Score: 147.82  E-value: 2.45e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  701 RIEGMDTLIAS-NEPIGVQDGTFAWKFLVNELNIAPSRIIPL-KDEEEYLSALQRGPRGGGVA--AIVDELPYIKALLSN 776
Cdd:smart00079   1 PITSVEDLAKQtKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYmKSPEVFVKSYAEGVQRVRVSnyAFIMESPYLDYELSR 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039011994  777 sNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTY 830
Cdd:smart00079  81 -NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
50-469 3.16e-37

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: 145.08  E-value: 3.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  50 VGALFTYDSFIGR--------AAKLAfvaaIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMEN--KVVAAIGP 119
Cdd:cd06366     2 IGGLFPLSGSKGWwggagilpAAEMA----LEHINNRSDILPGYNLELIWNDTQCDPGLGLKALYDLLYTppPKVMLLGP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 120 QSSGIGHIISHVANELHVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGIS 198
Cdd:cd06366    78 GCSSVTEPVAEASKYWNLVQLSYAATSPALSDrKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 199 VLGDALAKKRAKISYKAAFPPgadnssiSDLLASV-NLMES--RIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWI----- 270
Cdd:cd06366   158 DLEELLEEANITIVATESFSS-------EDPTDQLeNLKEKdaRIIIGLFYEDAARKVFCEAYKLGMYGPKYVWIlpgwy 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 271 TTDWLLTALDSMEPLDPRALDLLQGVVAFRHYTPESDNKRQFKGR----WKNLRFKESLKSDDGFNSYALYAYDSVWLVA 346
Cdd:cd06366   231 DDNWWDVPDNDVNCTPEQMLEALEGHFSTELLPLNPDNTKTISGLtaqeFLKEYLERLSNSNYTGSPYAPFAYDAVWAIA 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 347 RALDvffsqgNTVT--FSNDPSLRNTNDSGIKLSKLhifnegerFLQVILEMNYTGLTGQIEFNSEKNRInPAYDILNIK 424
Cdd:cd06366   311 LALN------KTIEklAEYNKTLEDFTYNDKEMADL--------FLEAMNSTSFEGVSGPVSFDSKGDRL-GTVDIEQLQ 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1039011994 425 STGPLRVGYWsnhtgfsvappetlysKPSNTSAKDQRLNEIIWPG 469
Cdd:cd06366   376 GGSYVKVGLY----------------DPNADSLLLLNESSIVWPG 404
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
485-828 9.76e-35

The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic binding protein type II superfamily; This subfamily represents the ligand binding of ionotropic glutamate receptors. iGluRs are heterotetrameric ion channels that comprises of three functionally distinct subtypes based on their pharmacology and structural similarities: AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid), NMDA (N-methyl-D-aspartate), and kainate receptors. All three types of channels are also activated by the physiological neurotransmitter, glutamate. iGluRs are concentrated at postsynaptic sites, where they exert a variety of different functions. While this ligand-binding domain of iGluRs is structurally homologous to the periplasmic binding fold type II superfamily, the N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain belongs to the periplasmic-binding fold type I.


Pssm-ID: 270219 [Multi-domain]  Cd Length: 243  Bit Score: 132.88  E-value: 9.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 485 KPLKIGVPNRVSYKNYASKDKNPLGV---KGFCIDIFEAAIQLLPYPVprTYILYGDGK----KNPSYDNLISEVAANIF 557
Cdd:cd00998     1 KTLKVVVPLEPPFVMFVTGSNAVTGNgrfEGYCIDLLKELSQSLGFTY--EYYLVPDGKfgapVNGSWNGMVGEVVRGEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 558 DVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKsspwsflkpftiemwavtgalflfvgaviwilehrfneefrg 637
Cdd:cd00998    79 DLAVGPITITSERSVVIDFTQPFMTSGIGIMIPIRSID------------------------------------------ 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 638 pprrqiitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsiltvqqltsriegmDTLIASNEPIGV 717
Cdd:cd00998   117 --------------------------------------------------------------------DLKRQTDIEFGT 128
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 718 QDGTFAWKFLVNELNIAP--------SRIIPLKDEEEYLSALQRGPrgggVAAIVDELPYIKALLSNSNCKFRTVGQEFT 789
Cdd:cd00998   129 VENSFTETFLRSSGIYPFyktwmyseARVVFVNNIAEGIERVRKGK----VYAFIWDRPYLEYYARQDPCKLIKTGGGFG 204
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1039011994 790 RTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWL 828
Cdd:cd00998   205 SIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
66-342 1.66e-33

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: 132.80  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  66 LAFVAAIEDINADQSILRGTKLNIVFQDTnCSGFVGTMGAL------------------QLMENKVVAAIGPQSSGIGHI 127
Cdd:cd06350    31 EAMIYAIEEINNDSSLLPNVTLGYDIRDT-CSSSSVALESSleflldngikllansngqNIGPPNIVAVIGAASSSVSIA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAK 206
Cdd:cd06350   110 VANLLGLFKIPQISYASTSPELSdKIRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVSTVYSDDDYGRSGIEAFEREAKE 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 207 KRAKISYKAAFPPGADNSSISDLLASVNLMES-RIFVVHVNPDSGLNIFSVAKSLGMMgsGYVWITTD-WlltaLDSMEP 284
Cdd:cd06350   190 RGICIAQTIVIPENSTEDEIKRIIDKLKSSPNaKVVVLFLTESDARELLKEAKRRNLT--GFTWIGSDgW----GDSLVI 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 285 LDpRALDLLQGVVAFrhyTPESDNKRQFkgrwknlrfkeslksDDGFNSYALYAYDSV 342
Cdd:cd06350   264 LE-GYEDVLGGAIGV---VPRSKEIPGF---------------DDYLKSYAPYVIDAV 302
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
68-469 7.71e-32

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: 128.23  E-value: 7.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  68 FVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMENKVVAAI----GPQSSGIGHI-ISHVANELHVPFLSF 142
Cdd:cd06379    18 FREAVNEVNAHSHLPRKITLNATSITLDPNPIRTALSVCEDLIASQVYAVivshPPTPSDLSPTsVSYTAGFYRIPVIGI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 143 AATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGA 221
Cdd:cd06379    98 SARDSAFSDKNiHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETLAETKDIKIEKVIEFEPGE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 222 DNssISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTAldSMEPLDPRALDLLQGVVAFRH 301
Cdd:cd06379   178 KN--FTSLLEEMKELQSRVILLYASEDDAEIIFRDAAMLNMTGAGYVWIVTEQALAA--SNVPDGVLGLQLIHGKNESAH 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 302 ytpesdnkrqfkgrwknLRfkeslksddgfnsyalyayDSVWLVARALDVFFSQGNTVTFSndPslRNTNDSGiklsklH 381
Cdd:cd06379   254 -----------------IR-------------------DSVSVVAQAIRELFRSSENITDP--P--VDCRDDT------N 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 382 IFNEGERFLQVILEMNYT-GLTGQIEFNSEKNRINPAYDILNIKSTG-PLRVGYWSnhtgfsvappetlYSKPSNTSAKD 459
Cdd:cd06379   288 IWKSGQKFFRVLKSVKLSdGRTGRVEFNDKGDRIGAEYDIINVQNPRkLVQVGIYV-------------GSQRPTKSLLS 354
                         410
                  ....*....|
gi 1039011994 460 QRLNEIIWPG 469
Cdd:cd06379   355 LNDRKIIWPG 364
PBP1_ABC_ligand_binding-like cd06346
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
51-348 1.14e-30

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: 123.44  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  51 GALFTYDSFIGRAAKLAfvaaIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLME-NKVVAAIGPQSSGIGHIIS 129
Cdd:cd06346    10 GPLASLGPPMLAAAELA----VEEINAAGGVL-GKKVELVVEDSQTDPTAAVDAARKLVDvEGVPAIVGAASSGVTLAVA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 130 HVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRnGIS-VLGDALAKK 207
Cdd:cd06346    85 SVAVPNGVVQISPSSTSPALTTLEdKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVNNDYGQ-GLAdAFKKAFEAL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 208 RAKISYKAAFPPGAdnssiSDLLASVNlmesRIF------VVHV-NPDSGLNIFSVAKSLGMMGSgyVWITTDWLLtald 280
Cdd:cd06346   164 GGTVTASVPYEPGQ-----TSYRAELA----QAAaggpdaLVLIgYPEDGATILREALELGLDFT--PWIGTDGLK---- 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 281 SMEPLDPRALDLLQGVVAFRHYTPESDNKRQFKGRWKNlrfkeslKSDDGFNSYALYAYDSVWLVARA 348
Cdd:cd06346   229 SDDLVEAAGAEALEGMLGTAPGSPGSPAYEAFAAAYKA-------EYGDDPGPFAANAYDAVMLLALA 289
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
48-431 8.31e-28

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: 115.03  E-value: 8.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  48 VNVGALFTY---DSFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSG 123
Cdd:COG0683     4 IKIGVLLPLtgpYAALGQPIKNGAELAVEEINAAGGVL-GRKIELVVEDDASDPDTAVAAARKLIDQdKVDAIVGPLSSG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 124 IGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSY-FRWREVVAIFVDDEYGRNGISVLG 201
Cdd:COG0683    83 VALAVAPVAEEAGVPLISPSATAPALTGPEcSPYVFRTAPSDAQQAEALADYLAKkLGAKKVALLYDDYAYGQGLAAAFK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 202 DALAKKRAKISYKAAFPPGAdnSSISDLLAsvNLMESR---IFVVHVNPDSGLnifsVAKSLGMMGsgyvwittdwllta 278
Cdd:COG0683   163 AALKAAGGEVVGEEYYPPGT--TDFSAQLT--KIKAAGpdaVFLAGYGGDAAL----FIKQAREAG-------------- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 279 ldsmepldpraldlLQGVVAfrhytpesdnkRQFKGRWKNlrfkeslKSDDGFNSYALYAYDSVWLVARALDvffsQGNT 358
Cdd:COG0683   221 --------------LKGPLN-----------KAFVKAYKA-------KYGREPSSYAAAGYDAALLLAEAIE----KAGS 264
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011994 359 VTfsndpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYdILNIKSTGPLRV 431
Cdd:COG0683   265 TD-------------------------REAVRDALEGLKFDGVTGPITFDPDGQGVQPVY-IVQVKADGKFVV 311
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
49-444 1.47e-27

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: 115.92  E-value: 1.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDS----FIGRAAKLAFVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLME-NKVVAAIGPQSSG 123
Cdd:cd06352     1 KVGVLAPSNSqslpVGYARSAPAIDIAIERINSEGLLLPGFNFEFTYRDSCCDESEAVGAAADLIYkRNVDVFIGPACSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 124 IGHIISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEygrNGISVLGD 202
Cdd:cd06352    81 AADAVGRLATYWNIPIITWGAVSASFLDKSrYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDD---SKCFSIAN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 203 ALAKKRA-----KISYKaAFPPGADNSSISDLLASVNLmESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLT 277
Cdd:cd06352   158 DLEDALNqednlTISYY-EFVEVNSDSDYSSILQEAKK-RARIIVLCFDSETVRQFMLAAHDLGMTNGEYVFIFIELFKD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 278 A-----LDSMEPLDPRALDLLQgvvAFRH---------YTPESDN-KRQFKGRWKNLRFKESLKSDDGFNSYALYAYDSV 342
Cdd:cd06352   236 GfggnsTDGWERNDGRDEDAKQ---AYESllvislsrpSNPEYDNfSKEVKARAKEPPFYCYDASEEEVSPYAAALYDAV 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 343 WLVARALdvffsqgnTVTFSNDPSLRNtndsGIKLSKlHIFNegerflqvileMNYTGLTGQIEFNSEKNRiNPAYDILN 422
Cdd:cd06352   313 YLYALAL--------NETLAEGGNYRN----GTAIAQ-RMWN-----------RTFQGITGPVTIDSNGDR-DPDYALLD 367
                         410       420
                  ....*....|....*....|...
gi 1039011994 423 I-KSTGPLRVGYWSNHTGFSVAP 444
Cdd:cd06352   368 LdPSTGKFVVVLTYDGTSNGLVV 390
PBP1_mGluR cd06362
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ...
67-439 4.81e-26

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


Pssm-ID: 380585 [Multi-domain]  Cd Length: 460  Bit Score: 112.77  E-value: 4.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  67 AFVAAIEDINADQSILRGTKLNIVFQDTnCSGfvGTMG---ALQLMEN---------------------------KVVAA 116
Cdd:cd06362    35 AMLFAIDEINSRPDLLPNITLGFVILDD-CSS--DTTAleqALHFIRDsllsqesagfcqcsddppnldesfqfyDVVGV 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 117 IGPQSSGIghiiS-HVANEL---HVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDE 191
Cdd:cd06362   112 IGAESSSV----SiQVANLLrlfKIPQISYASTSDELSDkERYPYFLRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGS 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 192 YGRNGISVLgdalaKKRAK-----ISYKAAFPPGADNSS----ISDLLASVNlmeSRIFVVHVNPDSGLNIFSVAKSLGM 262
Cdd:cd06362   188 YGEEGYKAF-----KKLARkagicIAESERISQDSDEKDyddvIQKLLQKKN---ARVVVLFADQEDIRGLLRAAKRLGA 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 263 MGSgYVWITTDWLLTALDSMEPLdpraLDLLQGVVAFRHYTPESdnkRQFKGRWKNLR---------FKES--------- 324
Cdd:cd06362   260 SGR-FIWLGSDGWGTNIDDLKGN----EDVALGALTVQPYSEEV---PRFDDYFKSLTpsnntrnpwFREFwqelfqcsf 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 325 --------------LKSDDGFN--SYALYAYDSVWLVARALDVFfsqgntvtfsndpsLRN--TNDSGIKLSKLHIFNeG 386
Cdd:cd06362   332 rpsrenscnddkllINKSEGYKqeSKVSFVIDAVYAFAHALHKM--------------HKDlcPGDTGLCQDLMKCID-G 396
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039011994 387 ERFLQVILEMNYTGLTG-QIEFNsEKNRINPAYDILNIKSTGP-----LRVGYWSNHTG 439
Cdd:cd06362   397 SELLEYLLNVSFTGEAGgEIRFD-ENGDGPGRYDIMNFQRNNDgsyeyVRVGVWDQYTQ 454
PBP1_pheromone_receptor cd06365
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ...
66-442 4.01e-25

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


Pssm-ID: 380588 [Multi-domain]  Cd Length: 464  Bit Score: 110.04  E-value: 4.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  66 LAFVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMEN--------------KVVAAIGPQSSGIGHIISHV 131
Cdd:cd06365    40 LAFLFAIEEINKNPDLLPNITLGFHIYDSCSSERLALESSLSILSGnsepipnyscreqrKLVAFIGDLSSSTSVAMARI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 132 ANELHVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAK 210
Cdd:cd06365   120 LGLYKYPQISYGAFDPLLSDkVQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDDDYGEQFSQDLKKEMEKNGIC 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 211 ISYKAAFPpgADNSSISDLLASVNLMES--RIFVVHVNPDS-GLNIFSVAKSLgmmGSGYVWITTdwllTALDSMEPLDP 287
Cdd:cd06365   200 VAFVEKIP--TNSSLKRIIKYINQIIKSsaNVIIIYGDTDSlLELLFRLWEQL---VTGKVWITT----SQWDISTLPFE 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 288 RALDLLQGVVAFRHYTPE---------SDNKRQ--------------FKGRWK--------NLRFKESLKS------DDG 330
Cdd:cd06365   271 FYLNLFNGTLGFSQHSGEipgfkeflqSVHPSKypediflktlwesyFNCKWPdqnckslqNCCGNESLETldvhsfDMT 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 331 FNSYALYAYDSVWLVARAL-DVFFSQGNTVTFSNDpslrntNDSGIKLSKLHIFNEGERFLqvilemnyTGLTGQIEFNs 409
Cdd:cd06365   351 MSRLSYNVYNAVYAVAHALhEMLLCQPKTGPGNCS------DRRNFQPWQLHHYLKKVQFT--------NPAGDEVNFD- 415
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1039011994 410 EKNRINPAYDILNIKSTgplrvgywSNHTGFSV 442
Cdd:cd06365   416 EKGDLPTKYDILNWQIF--------PNGTGTKV 440
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
49-442 2.42e-24

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: 105.38  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDSFigrAAKLAFVAAIEDINADQSiLRGTKLN-IVFQDTNCSGFVGTMGALQLMENKVVAAIGPQSSGIGHI 127
Cdd:cd06382     1 RIGGIFDEDDE---DLEIAFKYAVDRINRERT-LPNTKLVpDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSDI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSfaatdpTLSSLQYPYFLRTTQN---DYFQMN-AITDFVSYFRWREVVAIFVDDEygrnGISVLGDA 203
Cdd:cd06382    77 VQSICDALEIPHIE------TRWDPKESNRDTFTINlypDPDALSkAYADLVKSLNWKSFTILYEDDE----GLIRLQEL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 204 LA---KKRAKISYKaAFPPGADNssiSDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALD 280
Cdd:cd06382   147 LKlpkPKDIPITVR-QLDPGDDY---RPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLD 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 281 sMEPldpraldLLQGVV---AFRHYTPESDNKRQFKGRWKNlRFKESLKSDDGFNSY----ALyAYDSVWLVARALDvff 353
Cdd:cd06382   223 -LEP-------FKYSGAnitGFRLVDPENPEVKNVLKDWSK-REKEGFNKDIGPGQIttetAL-MYDAVNLFANALK--- 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 354 sqgntvtfsndpslrntndsgiklsklhifnegerflqvilemnyTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGY 433
Cdd:cd06382   290 ---------------------------------------------EGLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGT 324

                  ....*....
gi 1039011994 434 WSNHTGFSV 442
Cdd:cd06382   325 WNPTDGLNI 333
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
58-347 3.59e-24

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: 103.95  E-value: 3.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd06268    13 ADYGEEILRGVALAVEEINAAGGIN-GRKLELVIADDQGDPETAVAVARKLVDDdKVLAVVGHYSSSVTLAAAPIYQEAG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 137 VPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSY-FRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKA 215
Cdd:cd06268    92 IPLISPGSTAPELTEGGGPYVFRTVPSDAMQAAALADYLAKkLKGKKVAILYDDYDYGKSLADAFKKALKALGGEIVAEE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 216 AFPPGADNssISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMmgsGYVWITTDWLLTaldsmEPLDPRALDLLQG 295
Cdd:cd06268   172 DFPLGTTD--FSAQLTKIKAAGPDVLFLAGYGADAANALKQARELGL---KLPILGGDGLYS-----PELLKLGGEAAEG 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039011994 296 VVAFRHYTPESDNKRQFKgrwKNLRFKEslKSDDGFNSYALYAYDSVWLVAR 347
Cdd:cd06268   242 VVVAVPWHPDSPDPPKQA---FVKAYKK--KYGGPPSWRAATAYDATQALAG 288
PBP1_ABC_ligand_binding-like cd19984
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
58-346 5.69e-24

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: 103.07  E-value: 5.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLME-NKVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd19984    13 ASYGEDMKNGIELAVEEINAAGGIN-GKKIELIYEDSKCDPKKAVSAANKLINvDKVKAIIGGVCSSETLAIAPIAEQNK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 137 VPFLSFAATDPTLSSLqYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAA 216
Cdd:cd19984    92 VVLISPGASSPEITKA-GDYIFRNYPSDAYQGKVLAEFAYNKLYKKVAILYENNDYGVGLKDVFKKEFEELGGKIVASES 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 217 FPPGA-DNSSISDLLASVNLMesRIFVVhVNPDSGLNIFSVAKSLGMMG---SGYVWITTDWLLTALDSMEpldpraldl 292
Cdd:cd19984   171 FEQGEtDFRTQLTKIKAANPD--AIFLP-GYPKEGGLILKQAKELGIKApilGSDGFEDPELLEIAGEAAE--------- 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039011994 293 lqGVV-AFRHYTPESDNKRQFKGRwknlRFKEslKSDDGFNSYALYAYDSVWLVA 346
Cdd:cd19984   239 --GVIfTYPAFDDSSEKKQKFFFY----RYKE--KYGKEPDIYAALAYDAVMILA 285
Peripla_BP_6 pfam13458
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ...
48-428 1.82e-23

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


Pssm-ID: 433225 [Multi-domain]  Cd Length: 342  Bit Score: 102.74  E-value: 1.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  48 VNVGALFTY---DSFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSG 123
Cdd:pfam13458   2 IKIGVLTPLsgpYASSGKSSRAGARAAIEEINAAGGVN-GRKIELVVADDQGDPDVAAAAARRLVDQdGVDAIVGGVSSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 124 IGHIISHVANELHVPFLSFAATDPTLSSlqyPYFLRTTQNDYFQMNAITDF-VSYFRWREVVAIFVDDEYGRNGISVLGD 202
Cdd:pfam13458  81 VALAVAEVLAKKGVPVIGPAALTGEKCS---PYVFSLGPTYSAQATALGRYlAKELGGKKVALIGADYAFGRALAAAAKA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 203 ALAKKRAKISYKAAFPPGADNssISDLLAsvNLMESR--IFVVHVNPDSGLNIFSVAKSLGMMGSGyvwITTDWLLTALD 280
Cdd:pfam13458 158 AAKAAGGEVVGEVRYPLGTTD--FSSQVL--QIKASGadAVLLANAGADTVNLLKQAREAGLDAKG---IKLVGLGGDEP 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 281 SMEPLDPRAldlLQGVVAFRHYTPESDNK--RQFKGRWKNlRFKEslksdDGFNSYALYAYDSVWLVARALDvffsQGNT 358
Cdd:pfam13458 231 DLKALGGDA---AEGVYATVPFFPDLDNPatRAFVAAFAA-KYGE-----APPTQFAAGGYIAADLLLAALE----AAGS 297
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 359 VTfsndpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGP 428
Cdd:pfam13458 298 PT-------------------------REAVIAALRALPYDGPFGPVGFRAEDHQAVHCMYLVQVKADGK 342
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
57-420 4.27e-22

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


Pssm-ID: 380565 [Multi-domain]  Cd Length: 334  Bit Score: 98.75  E-value: 4.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  57 DSFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMENKVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd06342    12 NAALGQDIRNGAELAVDEINAKGGGL-GFKIELVAQDDACDPAQAVAAAQKLVADGVVAVIGHYNSGAAIAAAPIYAEAG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 137 VPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVsyFRWREV--VAIfVDD--EYGRNGISVLGDALAKKRAKIS 212
Cdd:cd06342    91 IPMISPSATNPKLTEQGYKNFFRVVGTDDQQGPAAADYA--AKTLKAkrVAV-IHDgtAYGKGLADAFKKALKALGGTVV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 213 YKAAFPPGADNssISDLLASVnlMESR---IFVVHVNPDSGLnIFSVAKSLGM----MGSGyvwittdwlltALDSMEPL 285
Cdd:cd06342   168 GREGITPGTTD--FSALLTKI--KAANpdaVYFGGYYPEAGL-LLRQLREAGLkapfMGGD-----------GIVSPDFI 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 286 DpRALDLLQGVVAFRHYTPESDNKrqfkgRWKNL--RFKESLKSDDGfnSYALYAYDSVWLVARALDvffsQGNTVTfsn 363
Cdd:cd06342   232 K-AAGDAAEGVYATTPGAPPEKLP-----AAKAFlkAYKAKFGEPPG--AYAAYAYDAAQVLLAAIE----KAGSTD--- 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 364 dpslrntndsgiklsklhifneGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDI 420
Cdd:cd06342   297 ----------------------RAAVAAALRATDFDGVTGTISFDAKGDLTGPAFTV 331
PBP1_taste_receptor cd06363
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ...
66-276 2.85e-21

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


Pssm-ID: 380586 [Multi-domain]  Cd Length: 418  Bit Score: 97.76  E-value: 2.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  66 LAFVAAIEDINADQSILRGTKLNIVFQDTnCSGFVGTMGALQLM-----------------ENKVVAAIGPQSSG----I 124
Cdd:cd06363    46 QAMRFAVEEINNSSDLLPGVTLGYEIFDT-CSDAVNFRPTLSFLsqngshdievqcnytnyQPRVVAVIGPDSSElaltT 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 125 GHIISHVAnelhVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDA 203
Cdd:cd06363   125 AKLLGFFL----MPQISYGASSEELSnKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEK 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 204 LAKKRAKISYKAAFPPGADNSS-ISDLLASVNLMESRIFVVHVNPDSGLNIF--SVAKSLgmmgSGYVWI-TTDWLL 276
Cdd:cd06363   201 AANTGICVAYQGLIPTDTDPKPkYQDILKKINQTKVNVVVVFAPKQAAKAFFeeVIRQNL----TGKVWIaSEAWSL 273
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
49-350 7.03e-21

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: 96.16  E-value: 7.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGAL--FTYDSFIGRAAKL---AFVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMENKVVAAIGPQSS- 122
Cdd:cd06370     2 TIGYLtpYSGAGSYDRQGRVisgAITLAVDDVNNDPNLLPGHTLSFVWNDTRCDELLSIRAMTELWKRGVSAFIGPGCTc 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 123 GIGHIISHVANelhVPFLSFAATDPTLS-SLQYPYFLRTtqndYFQMNAITDFVS----YFRWREVVAIFVDDEYGRNGI 197
Cdd:cd06370    82 ATEARLAAAFN---LPMISYKCADPEVSdKSLYPTFART----IPPDSQISKSVIallkHFNWNKVSIVYENETKWSKIA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 198 SVLGDALAKKRAKISYKAAFPPGA-----DNSSISDLLASVnLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSG-YVWIT 271
Cdd:cd06370   155 DTIKELLELNNIEINHEEYFPDPYpyttsHGNPFDKIVEET-KEKTRIYVFLGDYSLLREFMYYAEDLGLLDNGdYVVIG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 272 TDW------------LLTALDSMEPLDPRALDLLQGVVAFrhyTPESDNKRQFKGRWKNLrfKESLKsDDGFNS------ 333
Cdd:cd06370   234 VELdqydvddpakypNFLSGDYTKNDTKEALEAFRSVLIV---TPSPPTNPEYEKFTKKV--KEYNK-LPPFNFpnpegi 307
                         330       340
                  ....*....|....*....|....*
gi 1039011994 334 --------YALYAYDSVWLVARALD 350
Cdd:cd06370   308 ektkevpiYAAYLYDAVMLYARALN 332
PBP1_CaSR cd06364
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ...
67-299 1.13e-19

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


Pssm-ID: 380587 [Multi-domain]  Cd Length: 473  Bit Score: 93.48  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  67 AFVAAIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLM--------------ENKVVAAIGPQSSGIGHIISHVA 132
Cdd:cd06364    41 TMIFAIEEINNSPDLLPNITLGYRIYDSCATISKALRAALALVngqeetnldercsgGPPVAAVIGESGSTLSIAVARTL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 133 NELHVPFLSFAATDPTLSS-LQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKI 211
Cdd:cd06364   121 GLFYIPQVSYFASCACLSDkKQFPSFLRTIPSDYYQSRALAQLVKHFGWTWVGAIASDDDYGRNGIKAFLEEAEKLGICI 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 212 SYKAAFPPGADNSSISDLLASVNLMESRIFVVHVnPDSGL----------NIfsvakslgmmgSGYVWITTD-WLLTALd 280
Cdd:cd06364   201 AFSETIPRTYSQEKILRIVEVIKKSTAKVIVVFS-SEGDLeplikelvrqNI-----------TGRQWIASEaWITSSL- 267
                         250
                  ....*....|....*....
gi 1039011994 281 smePLDPRALDLLQGVVAF 299
Cdd:cd06364   268 ---LATPEYFPVLGGTIGF 283
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
511-827 1.02e-18

GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270441 [Multi-domain]  Cd Length: 369  Bit Score: 88.98  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 511 KGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGL-V 586
Cdd:cd13723    31 EGYCIDLLKELAHILGFSYEIRLVedgKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVsI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 587 VVAPVKGAKSSPWSFLKPFTIEMWAVTGALFLFVGAVIWILEhRFN--EEFRGPP----------RRQIITVFWFSFSTM 654
Cdd:cd13723   111 LYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIA-RFSpyEWYDAHPcnpgsevvenNFTLLNSFWFGMGSL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 655 FFSHRENTVSTLG-RFVLLVWLFVVLIINSSYTASLTSILTVQQLTSRIEGMDTLIASN--EPIGVQDG----------- 720
Cdd:cd13723   190 MQQGSELMPKALStRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTkiEYGAVKDGatmtffkkski 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 721 -TFA--WKFLVNElniaPSRIIplKDEEEylsALQRGPRGGgvAAIVDELPYIKaLLSNSNCKFRTVGQEFTRTGWGFAF 797
Cdd:cd13723   270 sTFEkmWAFMSSK----PSALV--KNNEE---GIQRALTAD--YALLMESTTIE-YVTQRNCNLTQIGGLIDSKGYGIGT 337
                         330       340       350
                  ....*....|....*....|....*....|
gi 1039011994 798 QRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13723   338 PMGSPYRDKITIAILQLQEEDKLHIMKEKW 367
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
62-350 2.70e-18

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


Pssm-ID: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 87.28  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  62 RAAKLAfvaaIEDINADqSILRGTKLNIVFQDTNCSGFVGTMGALQLME-NKVVAAIGPQSSGIGHIISHVANELHVPFL 140
Cdd:cd19980    21 NGAKLA----VEEINAK-GGVLGRKLELVVEDDKCPPAEGVAAAKKLITdDKVPAIIGAWCSSVTLAVMPVAERAKVPLV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 141 SFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDF-VSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPP 219
Cdd:cd19980    96 VEISSAPKITEGGNPYVFRLNPTNSMLAKAFAKYlADKGKPKKVAFLAENDDYGRGAAEAFKKALKAKGVKVVATEYFDQ 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 220 GAdnSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGM----MGSGyVWITTDWLLTALDSMEpldpraldllqG 295
Cdd:cd19980   176 GQ--TDFTTQLTKLKAANPDAIFVVAETEDGALILKQARELGLkqqlVGTG-GTTSPDLIKLAGDAAE-----------G 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039011994 296 VVAFRHYTPESDNKRQFKgrwKNLRFKESLKSDDGFNSYAlyAYDSVWLVARALD 350
Cdd:cd19980   242 VYGASIYAPTADNPANKA---FVAAYKKKYGEPPDKFAAL--GYDAVMVIAEAIK 291
PBP1_ABC_HAAT-like cd19988
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
71-346 3.06e-18

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


Pssm-ID: 380643 [Multi-domain]  Cd Length: 302  Bit Score: 86.56  E-value: 3.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINAdQSILRGTKLNIVFQDTNCSGFVGTMGALQLM-ENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTL 149
Cdd:cd19988    26 AVEEINA-AGGILGIPIELVVEDDEGLPAASVSAAKKLIyQDKVWAIIGSINSSCTLAAIRVALKAGVPQINPGSSAPTI 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 150 SSLQYPYFLRTTQNDYFQMNAITDF-VSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADNssISD 228
Cdd:cd19988   105 TESGNPWVFRCTPDDRQQAYALVDYaFEKLKVTKIAVLYVNDDYGRGGIDAFKDAAKKYGIEVVVEESYNRGDKD--FSP 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 229 LLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMgsgyvwittdwlLTALDSMEPLDPRALDL----LQGVVAFRHYTP 304
Cdd:cd19988   183 QLEKIKDSGAQAIVMWGQYTEGALIAKQARELGLK------------QPLFGSDGLVTPKFIELagdaAEGAIATTPFLP 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039011994 305 ESDNKR--QFKGRWKNlRFKESLksddgfNSYALYAYDSVWLVA 346
Cdd:cd19988   251 DSDDPKvsAFVEKYKK-RYGEEP------DVFAAQAYDAMNILA 287
PBP1_ABC_ligand_binding-like cd06335
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
58-349 1.08e-17

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


Pssm-ID: 380558 [Multi-domain]  Cd Length: 348  Bit Score: 85.74  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd06335    13 AELGESARRGVELAVEEINAAGGIL-GRKIELVERDDEANPTKAVQNAQELIDKeKVVAIIGPTNSGVALATIPILQEAK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 137 VPFLSFAATDPTLSSL---QYPYFLRTTQNDYFQMNAITDFVSYFRWREvVAIFVDDE-YGRNGISVLGDALAKKRAKIS 212
Cdd:cd06335    92 IPLIIPVATGTAITKPpakPRNYIFRVAASDTLQADFLVDYAVKKGFKK-IAILHDTTgYGQGGLKDVEAALKKRGITPV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 213 YKAAFPPGADnssisDLLASVNLMESR----IFVVHVNPDSGLnifsVAKSLGMMGsGYVWITTDWLLtaldSMEPLDPR 288
Cdd:cd06335   171 ATESFKIGDT-----DMTPQLLKAKDAgadvILVYGLGPDLAQ----ILKAMEKLG-WKVPLVGSWGL----SMPNFIEL 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011994 289 ALDLLQGVVAFRHYTPESDNKRQfkgrWK-NLRFKESLKSDDGFNSY-ALYAYDSVWLVARAL 349
Cdd:cd06335   237 AGPLAEGTIMTQTFIEDYLTPRA----KKfIDAYKKKYGTDRIPSPVsAAQGYDAVYLLAAAI 295
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
61-442 1.27e-17

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: 85.49  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  61 GRAAKLAFVAAIEDINADQSILRGTKLNIVFQDTNC-SGFVGTMGALQLMENKVVAAIGPQSSGIGHIISHVANELHVPF 139
Cdd:cd06368    11 DAHERAAFRYAVERLNTNIVKLAYFRITYSIEAIDSnSHFDATDKACDLLEKGVVAIVGPSSSDSNNALQSICDALDVPH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 140 LSfaATDPTLSSLQYPYFLRTTQNDYFQmnAITDFVSYFRWREVVAIFVDDEygrnGISVLGDALakKRAKISYKAAFPP 219
Cdd:cd06368    91 IT--VHDDPRLSKSQYSLSLYPRNQLSQ--AVSDLLKYWRWKRFVLVYDDDD----RLRRLQELL--EAARFSKRFVSVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 220 GADNSSISD----LLASV-NLMESRIfVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALDSMEPLdpRALDL-L 293
Cdd:cd06368   161 KVDLDYKTLdetpLLKRKdCSLFSRI-LIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDLSLLLDLELF--RYNHAnI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 294 QGVVAFRHYTPESDNKRqfkgRW--KNLRFKESLKSD---DGFNSYALYAYDSVWLVARAldvffsqgntvtfsndpslr 368
Cdd:cd06368   238 TGFQLVDNNSMYKEDIN----RLafNWSRFRQHIKIEsnlRGPPYEAALMFDAVLLLADA-------------------- 293
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011994 369 ntndsgiklsklhiFNEgerflqvilemnytglTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSNHTGFSV 442
Cdd:cd06368   294 --------------FRR----------------TGDLRFNGTGLRSNFTLRILELGYGGLRKIGFWDSNTRLAM 337
PBP1_ABC_transporter_GPCR_C-like cd04509
Family C of G-protein coupled receptors and their close homologs, the type 1 ...
71-273 1.07e-16

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


Pssm-ID: 380490  Cd Length: 306  Bit Score: 81.97  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINADQSILRGTKLNIVFQDTNCSGFVGTMGALQLMEN-----------------------KVVAAIGPQSSGIGHI 127
Cdd:cd04509    36 ALDDINADPNLLPNNTLGIVIYDDCCDPKQALEQSNKFVNDliqkdtsdvrctngeppvfvkpeGIKGVIGHLCSSVTIP 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSFAATDPTLSSLQ-YPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAK 206
Cdd:cd04509   116 VSNILELFGIPQITYAATAPELSDDRgYQLFLRVVPLDSDQAPAMADIVKEKVWQYVSIVHDEGQYGEGGARAFQDGLKK 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 207 KRAKISYKAAFPPGADNSSISDLLASV-NLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSgYVWITTD 273
Cdd:cd04509   196 GGLCIAFSDGITAGEKTKDFDRLVARLkKENNIRFVVYFGYHPEMGQILRAARRAGLVGK-FQFMGSD 262
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
50-440 1.13e-16

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


Pssm-ID: 380603 [Multi-domain]  Cd Length: 390  Bit Score: 83.10  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  50 VGALFTYDSfigRAAKLAFVAAIEDINADQ-SILRGTKLNIVFQDTNCSGF-VGTmgAL-QLMENKVVAAIGPQSSGIGH 126
Cdd:cd06380     2 IGAIFDSGE---DQVQTAFRYAIDRHNSNNnNRFRLFPLTERIDITNADSFsVSR--AIcSQLSRGVFAIFGSSDASSLN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 127 IISHVANELHVPFLSFA-ATDPTLSSLQYPYFLRTtqnDYFQmnAITDFVSYFRWREVVAIFVDDEygrnGISVLGDAL- 204
Cdd:cd06380    77 TIQSYSDTFHMPYITPSfPKNEPSDSNPFELSLRP---SYIE--AIVDLIRHYGWKKVVYLYDSDE----GLLRLQQLYd 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 205 -AKKRAKISYKAAFPPGADNSSisDLLASVNLMESRI----FVVHVNPDSGLNIFSVAKSLGMMGSGYvwittDWLLTAL 279
Cdd:cd06380   148 yLKEKSNISVRVRRVRNVNDAY--EFLRTLRELDREKedkrIVLDLSSERYQKILEQIVEDGMNRRNY-----HYLLANL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 280 DsMEPLDPRALdlLQG---VVAFRHYTPESDNKRQFKGRWKNLRFKESLKSDDGFNSY--ALyAYDSVWLVARALDVFFS 354
Cdd:cd06380   221 D-FLDLDLERF--LHGgvnITGFQLVDTNNKTVKDFLQRWKKLDPREYPGAGTDTIPYeaAL-AVDAVLVIAEAFQSLLR 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 355 QGNTVTFSNDPSLRNTNDS-GIKLSKLHI--FNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKST-GPLR 430
Cdd:cd06380   297 QNDDIFRFTFHGELYNNGSkGIDCDPNPPlpWEHGKAIMKALKKVRFEGLTGNVQFDDFGQRKNYTLDVIELTSNrGLRK 376
                         410
                  ....*....|
gi 1039011994 431 VGYWSNHTGF 440
Cdd:cd06380   377 IGTWSEGDGF 386
PBP1_ABC_RPA1789-like cd06333
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ...
50-349 1.21e-16

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: 82.60  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  50 VGALFTY---DSFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQL-MENKVVAAIGPQSSGIG 125
Cdd:cd06333     2 IGAILSLtgpAASLGIPERNAVELLVEQINAAGGIN-GRKLELIVYDDESDPTKAVTNARKLiEEDKVDAIIGPSTTGES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 126 HIISHVANELHVPFLSFAATDPTLSSlQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALA 205
Cdd:cd06333    81 LAVAPIAEEAKVPLISLAGAAAIVEP-VRKWVFKTPQSDSLVAEAILDYMKKKGIKKVALLGDSDAYGQSGRAALKKLAP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 206 KKRAKISYKAAFPPGAdnSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGM-----MGSGYVwiTTDWLLTALD 280
Cdd:cd06333   160 EYGIEIVADERFARTD--TDMTAQLTKIRAAKPDAVLVWASGPPAALVAKNLRQLGYkgpiyQSHGAA--NQDFIKLAGK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 281 SME--------PLDPRALdllqgvvafrhytPESDNKR----QFKGRWKNlRFKEslksddGFNSYALYAYDSVWLVARA 348
Cdd:cd06333   236 AAEgvilpagkLLVADQL-------------PDSDPQKkvllEFVKAYEA-KYGE------GPSTFAGHAYDALLLLVEA 295

                  .
gi 1039011994 349 L 349
Cdd:cd06333   296 I 296
PBP1_ABC_HAAT-like cd19986
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
63-346 2.32e-16

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


Pssm-ID: 380641 [Multi-domain]  Cd Length: 297  Bit Score: 80.75  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  63 AAKLAfvaaIEDINADQSILrGTKLNIVFQDTNCSGfVGTMGALQLM--ENKVVAAIGPQSSGIGHIISHVANELHVPFL 140
Cdd:cd19986    22 GAQLA----LEEINAAGGVL-GRPLELVVEDDQGTN-TGAVNAVNKLisDDKVVAVIGPHYSTQVLAVSPLVKEAKIPVI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 141 sFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVS-YFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPP 219
Cdd:cd19986    96 -TGGTSPKLTEQGNPYMFRIRPSDSVSAKALAKYAVeELGAKKIAILYDNDDFGTGGADVVTAALKALGLEPVAVESYNT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 220 G-ADNSSIsdLLASVNLMESRIFVVHVNPDSGLnIFSVAKSLGM----MGSGyVWITTDWLLTALDSMEpldpraldllq 294
Cdd:cd19986   175 GdKDFTAQ--LLKLKNSGADVIIAWGHDAEAAL-IARQIRQLGLdvpvIGSS-SFATPTVLLLAGEALE----------- 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039011994 295 GVVAFRHYTPESDNKRQfKGRWKnlRFKESLKSDDGFNSyALYaYDSVWLVA 346
Cdd:cd19986   240 GIYSVTDFVPSDPDPKV-QAFVK--KYKAKYGEDPDLYS-AWY-YDAMYLLA 286
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
51-418 3.23e-16

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


Pssm-ID: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 81.05  E-value: 3.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  51 GALFTYDSFIGRAAKLAfvaaIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLM-ENKVVAAIGPQSSGIGHIIS 129
Cdd:cd06347    10 GEAAAYGQPALNGAELA----VDEINAAGGIL-GKKIELIVYDNKSDPTEAANAAQKLIdEDKVVAIIGPVTSSIALAAA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 130 HVANELHVPFLSFAATDPTLSSlQYPYFLRTTQNDYFQMNAITDFV-SYFRWREVVAIF-VDDEYGRNGISVLGDALAKK 207
Cdd:cd06347    85 PIAQKAKIPMITPSATNPLVTK-GGDYIFRACFTDPFQGAALAKFAyEELGAKKAAVLYdVSSDYSKGLAKAFKEAFEKL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 208 RAKISYKAAFPPGadNSSISDLLAsvNLMESR---IFVVHVNPDSGLnIFSVAKSLG----MMGsGYVWITTDWLLTALD 280
Cdd:cd06347   164 GGEIVAEETYTSG--DTDFSAQLT--KIKAANpdvIFLPGYYEEAAL-IIKQARELGitapILG-GDGWDSPELLELGGD 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 281 SMEpldpraldllqGVVAFRHYTPESDNK--RQFKGRWKNlRFKESLksddgfNSYALYAYDSVWLVARALdvffsqgNT 358
Cdd:cd06347   238 AVE-----------GVYFTTHFSPDDPSPevQEFVKAYKA-KYGEPP------NAFAALGYDAVMLLADAI-------KR 292
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 359 VTFSNDPSLRNtndsgiKLSKLhifnegerflqvileMNYTGLTGQIEFNSEKNRINPAY 418
Cdd:cd06347   293 AGSTDPEAIRD------ALAKT---------------KDFEGVTGTITFDPNGNPIKPAV 331
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
481-829 2.06e-15

The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the NR2 subunit of NMDA receptor family. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 270436 [Multi-domain]  Cd Length: 283  Bit Score: 77.76  E-value: 2.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 481 PENGKPLKIGVPNRVSYK--NYASKDKNP---LGVKGFCIDIFEAAIQLLPYpvprTYILY--GDGK----KNPSYDNLI 549
Cdd:cd13718    22 PLTGTCMRNTVPCRKQLNheNSTDADENRyvkKCCKGFCIDILKKLAKDVGF----TYDLYlvTNGKhgkkINGVWNGMI 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 550 SEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVApvkgAKSSpwsflkpftiemwAVTGalflfvgaviwILEH 629
Cdd:cd13718    98 GEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISVMV----ARSN-------------QVSG-----------LSDK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 630 RFNEEF-RGPPrrqiitvfwFSFSTMFFSHRENTvstlgrfvllvwlfvvliINSSYTAsltsiltvqqltsriegMDTL 708
Cdd:cd13718   150 KFQRPHdQSPP---------FRFGTVPNGSTERN------------------IRNNYPE-----------------MHQY 185
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 709 IASNEPIGVQDGtfawkflvnelniapsriiplkdeeeyLSALQRGPrgggvaaiVDELPYIKALLS-----NSNCKFRT 783
Cdd:cd13718   186 MRKYNQKGVEDA---------------------------LVSLKTGK--------LDAFIYDAAVLNymagqDEGCKLVT 230
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1039011994 784 VGQE--FTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLT 829
Cdd:cd13718   231 IGSGkwFAMTGYGIALQKNSKWKRPFDLALLQFRGDGELERLERLWLT 278
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
503-827 2.25e-15

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


Pssm-ID: 270435 [Multi-domain]  Cd Length: 360  Bit Score: 78.88  E-value: 2.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 503 KDKNPLGVKGFCIDIFEAAIQLLPYpvprTYILY--GDGK-----KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVD 575
Cdd:cd13717    18 DRDGSPIWEGYCIDLIEEISEILNF----DYEIVepEDGKfgtmdENGEWNGLIGDLVRKEADIALAALSVMAEREEVVD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 576 FTQPFIES-GLVVVAPVKGAKSSPWSFLKPFTIEMWAVtgalflfvgaviwilehrFNeefrgpprrqIITVFWF---SF 651
Cdd:cd13717    94 FTVPYYDLvGITILMKKPERPTSLFKFLTVLELEVWRE------------------FT----------LKESLWFcltSL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 652 STMFFSHRENTVStlGRFVLLVWLFVVLIINSSYTASLTSILTVQQLTSRIEGMDTLIASNEP-IGVQDGTFAWKFLVNE 730
Cdd:cd13717   146 TPQGGGEAPKNLS--GRLLVATWWLFVFIIIASYTANLAAFLTVSRLQTPVESLDDLARQYKIqYTVVKNSSTHTYFERM 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 731 LNI----------------------APSRI--IPLKD---------EEEYLS-----ALQRGPRGGGVA-AIVDELPYIK 771
Cdd:cd13717   224 KNAedtlyemwkdmslndslspverAKLAVwdYPVSEkytkiyqamQEAGLVanaeeGVKRVRESTSAGfAFIGDATDIK 303
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 772 ALLSNsNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13717   304 YEILT-NCDLQEVGEEFSRKPYAIAVQQGSPLKDELNYAILELQNDRFLEKLKAKW 358
PBP1_GPC6A-like cd06361
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ...
66-283 1.28e-14

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


Pssm-ID: 380584 [Multi-domain]  Cd Length: 401  Bit Score: 77.03  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  66 LAFVAAIEDINAdQSILRGTKLNIVFQDTnCSGFVGTMGALQ------------LMEN------KVVAAIGPQSSGIGHI 127
Cdd:cd06361    39 LAMIHAIEMINN-STLLPGIKLGYEIYDT-CSDVTKALQATLrllskfnssnelLECDytdyvpPVKAVIGASYSEISIA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAK 206
Cdd:cd06361   117 VARLLNLQLIPQISYESSAPILSdKLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDDDYGRSALESFIIQAEA 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 207 KRAKISYKAAFPPGAD----NSSISDLLASVNlMESRIFVVHV--NPDSGLNIFsvaKSLGMMGSGYVWITTD-----WL 275
Cdd:cd06361   197 ENVCIAFKEVLPAYLSdptmNVRINDTIQTIQ-SSSQVNVVVLflKPSLVKKLF---KEVIERNISKIWIASDnwstaRE 272

                  ....*...
gi 1039011994 276 LTALDSME 283
Cdd:cd06361   273 ILKMPNIN 280
PBP1_As_SBP-like cd06330
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
58-232 5.78e-14

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: 74.13  E-value: 5.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd06330    13 AVYGEPARNGAELAVEEINAAGGIL-GRKIELVVRDDKGKPDEAVRAARELVLQeGVDFLIGTISSGVALAVAPVAEELK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 137 VPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVS--YFRWREVVAIFVDDEYGRNGISVLGDALAKKR--AKI 211
Cdd:cd06330    92 VLFIATDAATDRLTeENFNPYVFRTSPNTYMDAVAAALYAAkkPPDVKRWAGIGPDYEYGRDSWAAFKAALKKLKpdVEV 171
                         170       180
                  ....*....|....*....|...
gi 1039011994 212 SYKAAFPPGA-D-NSSISDLLAS 232
Cdd:cd06330   172 VGELWPKLGAtDyTAYITALLAA 194
PBP1_SBP-like cd19989
periplasmic substrate-binding domain of active transport proteins; Periplasmic ...
62-354 8.83e-14

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: 73.08  E-value: 8.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  62 RAAKLAfvaaIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHIISHVANELHVPFL 140
Cdd:cd19989    21 RGAQLA----VEEINAAGGIL-GRPVELVVEDTEGKPATAVQKARKLVEQdGVDFLTGAVSSAVALAVAPKAAELKVPYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 141 -SFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPP 219
Cdd:cd19989    96 vTVAADDELTGENCNRYTFRVNTSDRMIARALAPWLAENGGKKWYIVYADYAWGQSSAEAFKEAIEELGGEVVGTLFAPL 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 220 GADN--SSISdllasvNLMESR---IFVVHVNPDSgLNIFSVAKSLGMMGSgYVWITTDWLLTALDSmEPLDPRALDLLQ 294
Cdd:cd19989   176 GTTDfsSYIT------QISDSGadgLLLALAGSDA-VNFLKQAGQFGLGKK-YKIVGGILSIEPLAL-PALGDAAEGVYG 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039011994 295 GVvaFRHYTPESDNKRQFKGRWKNlrfkeslKSDDGFNSYALYAYDSV-WLVARAL-DVFFS 354
Cdd:cd19989   247 GV--RYPPTLDTPANRAFVEAYEK-------EYGEAPDNFAGEAYEAMqALAHQAVqPGYIG 299
PBP1_ABC_ligand_binding-like cd06340
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
59-350 1.24e-13

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: 73.36  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  59 FIGRAAKLAFVAAIEDINADQSI--LRGTKLNIVFQDTNCSGFVGTMGALQLM-ENKVVAAIGPQSSGIGHIISHVANEL 135
Cdd:cd06340    14 LIGQEAKRGAELAVDEINAAGGIksLGGAKIELVVADTQSDPEVAASEAERLItQEGVVAIIGAYSSSVTLAASQVAERY 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 136 HVPFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNaitDFVSYFRW---------REVVAIFVDDEYGRNGISVLGDALAK 206
Cdd:cd06340    94 GVPFVTASAVADEITERGFKYVFRTAPTASQFAE---DAVDFLKElakkkgkkiKKVAIIYEDSAFGTSVAKGLKKAAKK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 207 KRAKISYKAAFPPGAdnssiSDLLASVN-LMESR---IFVVHVNPDSGLnIFSVAKSLG-----MMGSGYVWITTDWLlt 277
Cdd:cd06340   171 AGLEVVLDEPYPAGA-----TDLSSEVLkLKAAKpdvVFATSYTNDAIL-LLRTMKELGfkpkaIIGVGGGYSDPEFL-- 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 278 aldsmepldpRAL-DLLQGVVAFRHYTPESDNKRQfkgRWKNL--RFKESLKSDdgFNSYALYAYDSVWLVARALD 350
Cdd:cd06340   243 ----------KALgKDAEGVFSVVPWSPDLAKKKP---GAKEVneRYKKKYGED--MTGHAARAYTAAWVLADALE 303
PBP1_ABC_ligand_binding-like cd06345
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
50-411 1.27e-13

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


Pssm-ID: 380568 [Multi-domain]  Cd Length: 356  Bit Score: 73.45  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  50 VGALFTYDSFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLM-ENKVVAAIGPQSSGIGHII 128
Cdd:cd06345     2 IGVLGPLSAPAGEAMERGAELAVEEINAAGGIL-GRKVELVVADTQGKPEDGVAAAERLItEDKVDAIVGGFRSEVVLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 129 SHVANELHVPFLSFAATDPTLSSL------QYPYFLRTTQNDYFQMNAITDFVSYFRWREV----VAIFVDD-EYGRNGI 197
Cdd:cd06345    81 MEVAAEYKVPFIVTGAASPAITKKvkkdyeKYKYVFRVGPNNSYLGATVAEFLKDLLVEKLgfkkVAILAEDaAWGRGIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 198 SVLGDALAKKRAKISYKAAFPPGAdnssiSDLLASVNLMESRifvvhvNPDSGLNIFSvakslgmMGSGYVwITTDW--- 274
Cdd:cd06345   161 EALKKLLPEAGLEVVGVERFPTGT-----TDFTPILSKIKAS------GADVIVTIFS-------GPGGIL-LVKQWael 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 275 ---LLTALDSMEPLDPRALDLL----QGVVAFRHYTPES---DNKRQFKGrwknlRFKEslKSDDGFNSYALYAYDSVWL 344
Cdd:cd06345   222 gvpAPLVGINVPAQDPEFWENTggagEYEITLAFAAPKAkvtPKTKPFVD-----AYKK--KYGEAPNYTAYTAYDAIYI 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 345 VARALDvffsqgNTVTFSNDpslrntndsgiKLSKlhifnegerflqVILEMNYTGLTGQIEFNSEK 411
Cdd:cd06345   295 LAEAIE------RAGSTDPD-----------ALVK------------ALEKTDYEGVRGRIKFDKKD 332
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
487-827 1.55e-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: 67.66  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 487 LKIGVpnRVSYKNYASKDKNpLGVKGFCIDIFEAAIQLLpypvprtyilygdGKK----NPSYDNLISEVAANIFDVAVG 562
Cdd:cd13530     2 LRVGT--DADYPPFEYIDKN-GKLVGFDVDLANAIAKRL-------------GVKvefvDTDFDGLIPALQSGKIDVAIS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 563 DVTIITNRTKFVDFTQPFIESGLVVVAPvkgaKSSPwsflkpftiemwavtgalflfvgaviwilehrfneefrgpprrq 642
Cdd:cd13530    66 GMTITPERAKVVDFSDPYYYTGQVLVVK----KDSK-------------------------------------------- 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 643 iitvfwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltSILTVQQLTSRIegmdtliasnepIGVQDGTF 722
Cdd:cd13530    98 ------------------------------------------------ITKTVADLKGKK------------VGVQAGTT 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 723 AWKFLVNelNIAPSRIIPLKDEEEYLSALqrgpRGGGVAAIVDELPYIKALLSNSNCKFRTVGQEFTRTGWGFAF-QRDS 801
Cdd:cd13530   118 GEDYAKK--NLPNAEVVTYDNYPEALQAL----KAGRIDAVITDAPVAKYYVKKNGPDLKVVGEPLTPEPYGIAVrKGNP 191
                         330       340
                  ....*....|....*....|....*.
gi 1039011994 802 PLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13530   192 ELLDAINKALAELKADGTLDKLLEKW 217
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
700-831 3.02e-12

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 66.93  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 700 SRIEGMDTLiaSNEPIGVQDGTFAWKFLVNelNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDELPYIKALLS-NSN 778
Cdd:COG0834    96 SGIKSLADL--KGKTVGVQAGTTYEEYLKK--LGPNAEIVEFDSYAEALQALASG----RVDAVVTDEPVAAYLLAkNPG 167
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039011994 779 CKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKWLTYD 831
Cdd:COG0834   168 DDLKIVGEPLSGEPYGIAVRKGDPeLLEAVNKALAALKADGTLDKILEKWFGED 221
PBP1_ABC_HAAT-like cd06344
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
71-349 4.47e-12

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


Pssm-ID: 380567 [Multi-domain]  Cd Length: 332  Bit Score: 68.41  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMENK-VVAAIGPQSSGIGHIISHVANELHVPFLSFAATDPTL 149
Cdd:cd06344    24 AVEEINAAGGVL-GRKIRLVEYDDEASVDKGLAIAQRFADNPdVVAVIGHRSSYVAIPASIIYERAGLLMLSPGATAPKL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 150 SSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFppGADNSSISDL 229
Cdd:cd06344   103 TQHGFKYIFRNIPSDEDIARQLARYAARQGYKRIVIYYDDDSYGKGLANAFEEEARELGITIVDRRSY--SSDEEDFRRL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 230 LASVNLMESR--IFVVHVNPDSGLNIfsvaKSLGMMGSGYVWITTDwlltALDSMEPLDpraldlLQGVVAFRHYTPES- 306
Cdd:cd06344   181 LSKWKALDFFdaIFLAGSMPEGAEFI----KQARELGIKVPIIGGD----GLDSPELIE------IAGKAAEGVVVATVf 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1039011994 307 DNKRQfkgRWKNLRFKESLKSDDGF--NSYALYAYDSVWLVARAL 349
Cdd:cd06344   247 DPDDP---RPEVRAFVEAFRKKYGRepDVWAAQGYDAVKLLAEAI 288
PBP1_mGluR_groupIII cd06376
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ...
67-437 4.65e-12

ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain of the group III metabotropic glutamate receptor, a family which contains mGlu4R, mGluR6R, mGluR7, and mGluR8; all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.


Pssm-ID: 380599 [Multi-domain]  Cd Length: 467  Bit Score: 69.45  E-value: 4.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  67 AFVAAIEDINADQSILRGTKLNIVFQDTnCS----------GFVGTM--------------GALQLMENKVVAAIGPQSS 122
Cdd:cd06376    39 AMLYALDQINSDPDLLPNVTLGARILDT-CSrdtyaleqslTFVQALiqkdtsdvrctngdPPVFVKPEKVVGVIGASAS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 123 GIGHIISHVANELHVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVL- 200
Cdd:cd06376   118 SVSIMVANILRLFQIPQISYASTAPELSdDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGNYGEKGVESFv 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 201 ------GDALAKKRAKISYKAAfpPGADNSSISDLLASVNlmeSRIFVVHVNPDSGLNIFSVAKSLGMMGSgYVWITTD- 273
Cdd:cd06376   198 qisreaGGVCIAQSEKIPRERR--TGDFDKIIKRLLETPN---ARAVVIFADEDDIRRVLAAAKRANKTGH-FLWVGSDs 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 274 W--LLTALDSMEPLDPRALDLL---QGVVAFRHY----TPEsDNKRQ--FKGRWK---NLRF----------------KE 323
Cdd:cd06376   272 WgaKISPVLQQEDVAEGAITILpkrASIEGFDAYftsrTLE-NNRRNvwFAEFWEenfNCKLtssgskkedtlrkctgQE 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 324 SLKSDDGFNSYAL--YAYDSVWLVARALDvffsqgntvtfsndpSLRNT---NDSGIKLSKLHIfnEGERFLQVILEMNY 398
Cdd:cd06376   351 RIGRDSGYEQEGKvqFVVDAVYAMAHALH---------------NMNKDlcpGYRGLCPEMEPA--GGKKLLKYIRNVNF 413
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1039011994 399 TGLTGQ-IEFNseKNRINPA-YDIL-----NIKSTGPLRVGYWSNH 437
Cdd:cd06376   414 NGSAGTpVMFN--KNGDAPGrYDIFqyqttNGSNYGYRLIGQWTDE 457
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
511-828 6.20e-12

The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; The ligand-binding domain of the ionotropic NMDA subtype is structurally homologous to the periplasmic-binding fold type II superfamily, while the N-terminal domain belongs to the periplasmic-binding fold type I. The function of the NMDA subtype receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer comprising two NR1 and two NR2 (A, B, C, and D) or NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 270405 [Multi-domain]  Cd Length: 239  Bit Score: 66.51  E-value: 6.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 511 KGFCIDIFEAaiqlLPYPVPRTYILY--GDGK---KNPSYDN----LISEVAANIFDVAVGDVTIITNRTKFVDFTQPFI 581
Cdd:cd13687    21 YGFCIDLLKK----LAEDVNFTYDLYlvTDGKfgtVNKSINGewngMIGELVSGRADMAVASLTINPERSEVIDFSKPFK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 582 ESGLVVVApvkgAKSSpwsflkpftiemwAVTGalflfvgaviwILEHRFneefrgppRRQIITvfwFSFSTMFFSHREN 661
Cdd:cd13687    97 YTGITILV----KKRN-------------ELSG-----------INDPRL--------RNPSPP---FRFGTVPNSSTER 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 662 TvstlgrfvllvwlfvvliINSSYTASLTSILTVQQLTSriegmdtliasnepigvqdgtfawkflvnelniapsriipl 741
Cdd:cd13687   138 Y------------------FRRQVELMHRYMEKYNYETV----------------------------------------- 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 742 kdeEEYLSALQRGPrgggvaaiVDELPYIKALL-----SNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAE 816
Cdd:cd13687   159 ---EEAIQALKNGK--------LDAFIWDSAVLeyeasQDEGCKLVTVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHE 227
                         330
                  ....*....|..
gi 1039011994 817 EGKLEKIRKKWL 828
Cdd:cd13687   228 SGFMEELDKKWL 239
PBP1_ABC_ligand_binding-like cd19982
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
60-221 2.53e-11

type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. 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: 65.77  E-value: 2.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  60 IGRAAKLAFVAAIEDINADQSIlRGTKLNIVFQDTNCSGFVGTMGALQLM-ENKVVAAIGPQSSGIGHIISHVANELHVP 138
Cdd:cd19982    15 FGEMFKNGYEMALEEINAAGGI-KGKKLELVIEDDQSKPQTALAAAEKLVsQDKVPLIVGGYSSGITLPVAAVAERQKIP 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 139 FLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDeyGRNGISVL--GDALAKKRA-KISYKA 215
Cdd:cd19982    94 LLVPTAADDDITKPGYKYVFRLNPPASIYAKALFDFFKELVKPKTIAILYEN--TAFGTSVAkaARRFAKKRGiEVVADE 171

                  ....*.
gi 1039011994 216 AFPPGA 221
Cdd:cd19982   172 SYDKGA 177
PBP1_mGluR_groupI cd06374
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ...
67-433 3.67e-11

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


Pssm-ID: 380597 [Multi-domain]  Cd Length: 474  Bit Score: 66.60  E-value: 3.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  67 AFVAAIEDINADQSILRGTKLNIVFQDT-------------------------NCSGFVGTMGALQLMENK--VVAAIGP 119
Cdd:cd06374    46 AMFRTLDKINKDPNLLPNITLGIEIRDScwyspvaleqsiefirdsvasvedeKDTQNTPDPTPLSPPENRkpIVGVIGP 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 120 QSSgigHIISHVANEL---HVPFLSFAATDPTLSSL-QYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVDDEYGRN 195
Cdd:cd06374   126 GSS---SVTIQVQNLLqlfHIPQIGYSATSIDLSDKsLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGES 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 196 GISVLGDALAKKRAKISYKAAFPPGADNSSISDLLAsvNLME----SRIFVVHVNPDSGLNIFSVAKSLGMMGsGYVWIT 271
Cdd:cd06374   203 GIEAFKELAAEEGICIAHSDKIYSNAGEEEFDRLLR--KLMNtpnkARVVVCFCEGETVRGLLKAMRRLNATG-HFLLIG 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 272 TDWLLTALDSMEPLDPRAldllQG----------VVAF-RHYT---PESdNKRQ--FKGRWKNlRFKESLKSDDGFNSYa 335
Cdd:cd06374   280 SDGWADRKDVVEGYEDEA----AGgitikihspeVESFdEYYFnlkPET-NSRNpwFREFWQH-RFDCRLPGHPDENPY- 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 336 lyaYDSVWLVARALDVFFSQGNTVTFSNDP-------------SLRNTNDSGIKLSKLHIfnEGERFLQVILEMNYTGLT 402
Cdd:cd06374   353 ---FKKCCTGEESLLGNYVQDSKLGFVINAiyamahalhrmqeDLCGGYSVGLCPAMLPI--NGSLLLDYLLNVSFVGVS 427
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1039011994 403 GQ-IEFNseKNRINPA-YDILNIKSTGPLRVGY 433
Cdd:cd06374   428 GDtIMFD--ENGDPPGrYDIMNFQKTGEGSYDY 458
PBP1_ABC_HAAT-like cd06349
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
61-424 1.26e-10

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


Pssm-ID: 380572 [Multi-domain]  Cd Length: 338  Bit Score: 64.13  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  61 GRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHIISHVANELHVPF 139
Cdd:cd06349    16 GQQFKNGVELAVDEINAAGGVN-GRKLELVVYDDQGDPKEAVNIAQKFVSDdKVVAVIGDFSSSCSMAAAPIYEEAGLVQ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 140 LSFAATDPTLSSLqYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIF-VDDEYGRNGISVLGDALAKKRAKISYKAAFP 218
Cdd:cd06349    95 ISPTASHPDFTKG-GDYVFRNSPTQAVEAPFLADYAVKKLGAKKIAIIyLNTDWGVSAADAFKKAAKALGGEIVATEAYL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 219 PGAD--NSSISdllasvNLMESR---IFVVHVNPDSGLnIFSVAKSLG----MMGSGYVwITTDWLLTALDSMEpldpra 289
Cdd:cd06349   174 PGTKdfSAQIT------KIKNANpdaIYLAAYYNDAAL-IAKQARQLGwdvqIFGSSSL-YSPEFIELAGDAAE------ 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 290 ldllqGVVAFRHYTPESDNKrqfkgRWKNlrFKESLKSDDGF--NSYALYAYDSVWLVARAldvffsqgntvtfsndpsL 367
Cdd:cd06349   240 -----GVYLSSPFFPESPDP-----EVKE--FVKAYKAKYGEdpDDFAARAYDAVNILAEA------------------I 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 368 RNTNDSGiklsklhifnEGERflQVILEM-NYTGLTGQIEFNSEKNRINpAYDILNIK 424
Cdd:cd06349   290 EKAGTDR----------EAIR--DALANIkDFSGLTGTITFDENGDVLK-SLTILVVK 334
PBP1_ABC_ligand_binding-like cd06343
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
58-349 2.07e-10

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


Pssm-ID: 380566 [Multi-domain]  Cd Length: 355  Bit Score: 63.36  E-value: 2.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSIlRGTKLNIVFQDTNCSGFVGTMGALQLME-NKVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd06343    20 AAYGKPVRAGAAAYFDEVNAAGGI-NGRKIELIVEDDGYDPARAVAAVRKLVEqDKVFAIVGGLGTPTNLAVRPYLNEAG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 137 VPFLSFAATDPTLSSLQYPYfLRTTQNDY-FQMNAITDF-VSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYK 214
Cdd:cd06343    99 VPQLFPATGASALSPPPKPY-TFGVQPSYeDEGRILADYiVETLPAAKVAVLYQNDDFGKDGLEGLKEALKAYGLEVVAE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 215 AAFPPGAdnssiSDLLASV-NLMESR--IFVVHVNPDSGLNIFSVAKSLGMmgsgyvwiTTDWLLTA----LDSMEPLDP 287
Cdd:cd06343   178 ETYEPGD-----TDFSSQVlKLKAAGadVVVLGTLPKEAAAALKEAAKLGW--------KPTFLGSSvsadPTTLAKAGG 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039011994 288 RALDLLQGVVAFRHYTPESDNKRQfkgrwknlRFKESLK---SDDGFNSYALYAYDSVWLVARAL 349
Cdd:cd06343   245 DAAEGVYSASYLKDPTDADDPAVK--------EFREAYKkyfPDDPPNAYALYGYAAAQVFVEAL 301
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
511-827 2.44e-10

The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily; This subfamily represents the ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate receptors including AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) receptors (GluR1-4), kainate receptors (GluR5-7 and KA1/2), and orphan receptors delta 1/2. iGluRs form tetrameric ligand-gated ion channels, which are concentrated at postsynaptic sites in excitatory synapses where they fulfill a variety of different functions. While this ligand-binding domain of iGluRs is structurally homologous to the periplasmic binding fold type II superfamily, the N-terminal leucine/isoleucine/valine#binding protein (LIVBP)-like domain belongs to the periplasmic-binding fold type I.


Pssm-ID: 270403 [Multi-domain]  Cd Length: 252  Bit Score: 61.82  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 511 KGFCIDIFEAAIQLLP-----YPVPRTyiLYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGL 585
Cdd:cd13685    29 EGYCIDLLEELAKILGfdyeiYLVPDG--KYGSRDENGNWNGMIGELVRGEADIAVAPLTITAEREEVVDFTKPFMDTGI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 586 VVVapvkgaksspwsFLKPFTIEmwavtgalflfvgaviwilehrfneEFRGPPRRQIItvfwfSFSTmffshrentvst 665
Cdd:cd13685   107 SIL------------MRKPTPIE-------------------------SLEDLAKQSKI-----EYGT------------ 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 666 lgrfvllvwlfvvliINSSYTasltsiltvqqltsriegMDTLIASNEPIGVQDGTfaWKFLVNElniapSRIIPLKDEE 745
Cdd:cd13685   133 ---------------LKGSST------------------FTFFKNSKNPEYRRYEY--TKIMSAM-----SPSVLVASAA 172
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 746 EylsALQRGPRGGGVAAIVDELPYIKaLLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRK 825
Cdd:cd13685   173 E---GVQRVRESNGGYAFIGEATSID-YEVLRNCDLTKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGELEKLKE 248

                  ..
gi 1039011994 826 KW 827
Cdd:cd13685   249 KW 250
PBP1_iGluR_NMDA cd06367
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the ionotropic ...
102-434 7.10e-10

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


Pssm-ID: 380590 [Multi-domain]  Cd Length: 357  Bit Score: 61.87  E-value: 7.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 102 TMGALQLMENKVVAAI----GPQSSGIGHIISHVANELHVPFL------SFAATDPTLSSLqypyFLRTTQNDYFQMNAI 171
Cdd:cd06367    52 ITRICDLLSDSKVQGVvfsdDTDQEAIAQILDFIAAQTLTPVLglhgrsSMIMADKSEHSM----FLQFGPPIEQQASVM 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 172 TDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAFPPGADN--SSISDLLASVNLMESRIFVVHVNPDS 249
Cdd:cd06367   128 LNIMEEYDWYIVSLVTTYFPGYQDFVNKLRSTIENSGWELEEVLQLDMSLDDgdSKLQAQLKKLQSPEARVILLYCTKEE 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 250 GLNIFSVAKSLGMMGSGYVWIttdwlltaLDSMEPLDPRALDLL-QGVVafrhytpesdnkrqfkgrwknlrfkeSLKSD 328
Cdd:cd06367   208 ATYVFEVAASVGLTGYGYTWL--------VGSLVAGTDTVPAEFpTGLI--------------------------SLSYD 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 329 DGFNSYAlYAYDSVWLVARALDVFFSQGNTVTfsnDPSLRNTNDSGIKLSKLHIFNegeRFLqvileMNYTGLTGQIEFN 408
Cdd:cd06367   254 EWYNLPA-RIRDGVAIVATAASEMLSEHEQIP---DPPSSCVNNQEIRKYTGPMLK---RYL-----INVTFEGRDLSFS 321
                         330       340
                  ....*....|....*....|....*..
gi 1039011994 409 SEKNRINPAYDILNIKSTGPL-RVGYW 434
Cdd:cd06367   322 EDGYQMHPKLVIILLNNERKWeRVGKW 348
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
49-441 1.15e-09

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


Pssm-ID: 380604 [Multi-domain]  Cd Length: 401  Bit Score: 61.55  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDsfigrAAK--LAFVAAIEDINADQSILRGTKL--NIVFQDTNcSGFVGTMGALQLMENKVVAAIGPQSSGI 124
Cdd:cd06381     1 HIGAIFEEN-----AAKddRVFQLAVSDLSLNDDILQSEKItySIKVIEAN-NPFQAVQEACDLMTQGILALVTSTGCAS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 125 GHIISHVANELHVPFLsFAATDPTLSSLQYPYFLRTTQNDYFQM---------NAITDFVSYFRWREVVaIFVDDEYGRN 195
Cdd:cd06381    75 ANALQSLTDAMHIPHL-FVQRNPGGSPRTACHLNPSPDGEAYTLasrppvrlnDVMLRLVTELRWQKFV-MFYDSEYDIR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 196 GI-------SVLGDALAKKRAKISYKAAFPPGADNSSISDLLASVNLMESRIFVVhvNPDSGLNIFSVAKSLGMMGSGYV 268
Cdd:cd06381   153 GLqsfldqaSRLGLDVSLQKVDKNISHVFTSLFTTMKTEELNRYRDTLRRAILLL--SPQGAHSFINEAVETNLASKDSH 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 269 WITTDwlltaldsMEPLDPRALDLLQG-----VVAFRHYTPESDNKRQFKGrwkNLRFKESL-KSDDGFNSYA----LYA 338
Cdd:cd06381   231 WVFVN--------EEISDPEILDLVHSalgrmTVVRQIFPSAKDNQKCFRN---NHRISSLLcDPQEGYLQMLqisnLYL 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 339 YDSVWLVARALDVFFSQGNTVTFSNDPSLRNTNDSgiklsklhiFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAY 418
Cdd:cd06381   300 YDSVLMLANAFHRKLEDRKWHSMASLNCIRKSTKP---------WNGGRSMLDTIKKGHITGLTGVMEFREDSSNPYVQF 370
                         410       420
                  ....*....|....*....|....*...
gi 1039011994 419 DILNIK-----STGPLRVGYWSNHTGFS 441
Cdd:cd06381   371 EILGTTysetfGKDMRKLATWDSEKGLN 398
PBP1_GC_G-like cd06372
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ...
71-390 3.07e-09

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


Pssm-ID: 380595 [Multi-domain]  Cd Length: 390  Bit Score: 60.20  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINADQSILRGTKLNIVFQDTNC------SGFVGtmgalQLMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAA 144
Cdd:cd06372    26 AVDKVNSEPSLLGNYSLDFVYTDCGCnakeslGAFID-----QVQKENISALFGPACPEAAEVTGLLASEWNIPMFGFVG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 145 TDPTLSSlqypyflRTTQNDYFQM--------NAITDFVSYFRWrEVVAIF-----------VDDEYGrngisVLGDALa 205
Cdd:cd06372   101 QSPKLDD-------RDVYDTYVKLvpplqrigEVLVKTLQFFGW-THVAMFggssatstwdkVDELWK-----SVENQL- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 206 KKRAKISYKAAFppgadNSSISDLLaSVNLME----SRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTD------WL 275
Cdd:cd06372   167 KFNFNVTAKVKY-----DTSNPDLL-QENLRYissvARVIVLICSSEDARSILLEAEKLGLMDGEYVFFLLQqfedsfWK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 276 LTALDSMEPLDPRALD--LLQGVVAFRHYTpESDNKRQFKGRWKNLRFKESLKSDDGFNSYALYAYDSVWLVARALDVFF 353
Cdd:cd06372   241 EVLNDEKNQVFLKAYEmvFLIAQSSYGTYG-YSDFRKQVHQKLRRAPFYSSISSEDQVSPYSAYLHDAVLLYAMGLKEML 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1039011994 354 SQGntvtfsNDP--------SLRNTNDS---GIKLSkLHIFNEGERFL 390
Cdd:cd06372   320 KDG------KDPrdgrallqTLRGYNQTtfyGITGL-VYLDVQGERHM 360
PBP1_mGluR_groupII cd06375
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ...
56-274 8.39e-09

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


Pssm-ID: 380598 [Multi-domain]  Cd Length: 462  Bit Score: 59.07  E-value: 8.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  56 YDSFIGRAAKLAFvaAIEDINADQSILRGTKLNIVFQDTnCSGfvGTMGALQLME------NKVV--------------- 114
Cdd:cd06375    30 EDRGIQRLEAMLF--AIDRINRDPHLLPGVRLGVHILDT-CSR--DTYALEQSLEfvraslTKVDdseymcpddgsyaiq 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 115 -AAIGPQSSGIGHIIS----HVANEL---HVPFLSFAATDPTLS-SLQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVA 185
Cdd:cd06375   105 eDSPLPIAGVIGGSYSsvsiQVANLLrlfQIPQISYASTSAKLSdKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVST 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 186 IFVDDEYGRNGISVLGD---------ALAKKRAKISYKAAFppgadNSSISDLLASVNlmeSRIFVVHVNPDSGLNIFSV 256
Cdd:cd06375   185 VASEGDYGETGIEAFEQearlrniciATAEKVGRSADRKSF-----DGVIRELLQKPN---ARVVVLFTRSDDARELLAA 256
                         250
                  ....*....|....*....
gi 1039011994 257 AKSLGMmgsGYVWITTD-W 274
Cdd:cd06375   257 AKRLNA---SFTWVASDgW 272
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
487-828 1.80e-08

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: 55.76  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 487 LKIGVpnRVSYKNYASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYIlygdgkkNPSYDNLISEVAANIFDVAVGDVTI 566
Cdd:pfam00497   1 LRVGT--DGDYPPFEYVDENG-KLVGFDVDLAKAIAKRLGVKV--EFV-------PVSWDGLIPALQSGKVDLIIAGMTI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 567 ITNRTKFVDFTQPFIESGLVVVAPVKGAKSSpwsflkpftiemwavtgalflfvgaviwilehrfneefrgpprrqiitv 646
Cdd:pfam00497  69 TPERAKQVDFSDPYYYSGQVILVRKKDSSKS------------------------------------------------- 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 647 fwfsfstmffshrentvstlgrfvllvwlfvvliinssytasltsILTVQQLTSRIegmdtliasnepIGVQDGTFAWKF 726
Cdd:pfam00497 100 ---------------------------------------------IKSLADLKGKT------------VGVQKGSTAEEL 122
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 727 LVNeLNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDELPYIKALLSNSNCKFRTV-GQEFTRTGWGFAFQRDSP-LA 804
Cdd:pfam00497 123 LKN-LKLPGAEIVEYDDDAEALQALANG----RVDAVVADSPVAAYLIKKNPGLNLVVvGEPLSPEPYGIAVRKGDPeLL 197
                         330       340
                  ....*....|....*....|....
gi 1039011994 805 VDMSTAILQLAEEGKLEKIRKKWL 828
Cdd:pfam00497 198 AAVNKALAELKADGTLAKIYEKWF 221
PBP1_ABC_ligand_binding-like cd06336
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
62-349 2.36e-08

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


Pssm-ID: 380559 [Multi-domain]  Cd Length: 345  Bit Score: 56.86  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  62 RAAKLAfvaaIEDINADQSIL-RGT--KLNIVFQDTNCSGFVGTMGALQLM-ENKVVAAIGPQSSGIGHIISHVANELHV 137
Cdd:cd06336    21 RGLELA----ADEINAAGGIKvGGKkyKVEVVSYDDKYTPAEAVAAARRLVsQDGVKFIFGPGGSAIAAAVQPVTERNKV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 138 pFLSFAATDPTLSSLQYPYFLRTTQNDYFQMNAITDFV-SYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAA 216
Cdd:cd06336    97 -LLLTAAFSDPILGPDNPLLFRIPPTPYEYAPPFIKWLkKNGPIKTVALIAPNDATGKDWAAAFVAAWKAAGGEVVAEEF 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 217 FPPGADNSS--ISDLLASvnlmesrifvvhvNPD-----------SGLnIFSVAKSLGMMGsgyVWITTDWlltalDSME 283
Cdd:cd06336   176 YDRGTTDFYpvLTKILAL-------------KPDaldlggsspgpAGL-IIKQARELGFKG---PFVSEGG-----AKAD 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 284 PLDPRA-LDLLQGVVAFRHYTPE---SDNKRQFKGRWKNlRFKESLksddgfNSYALYAYDSVWLVARAL 349
Cdd:cd06336   234 EILKEVgGEAAEGFIGVLPADDDpiaSPGAKAFVERYKK-KYGEPP------NSESALFYDAAYILVKAM 296
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
511-638 2.38e-08

The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the KA1 subunit of kainate receptor. While this ligand-binding domain is structurally homologous to the periplasmic binding fold type II superfamily, the N_terminal domain of kainate receptors belongs to the periplasmic-binding fold type I. There are five types of kainate receptors, GluR5, GluR6, GluR7, KA1, and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined.


Pssm-ID: 270442 [Multi-domain]  Cd Length: 333  Bit Score: 56.94  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 511 KGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVV 587
Cdd:cd13724    31 EGFCVDMLKELAEILRFNYKIRLVgdgVYGVPEANGTWTGMVGELIARKADLAVAGLTITAEREKVIDFSKPFMTLGISI 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039011994 588 VAPVK-GAKSSPWSFLKPFTIEMWAVTGALFLFVGAVIWILEHRFNEEFRGP 638
Cdd:cd13724   111 LYRVHmGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWYSP 162
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
48-438 4.34e-08

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


Pssm-ID: 380616  Cd Length: 379  Bit Score: 56.46  E-value: 4.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  48 VNVGALFTYDSFIGRAAKLAFVAAIEDINADQSILRGTKLNI-VFQDTNCSGFVGTMGALQLMENKVVAAIGPQSS-GIG 125
Cdd:cd06394     2 LRMAAILDDQTVCGRGERLALALAREQINSIIEVPAKARVEVdIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSpASA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 126 HIISHVANELHVPFLSFAATD-PTLSSLQYPYFLRTTQNDYFQMnAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDAL 204
Cdd:cd06394    82 STVSHICGEKEIPHIKVGPEEtPRLQYLRFASVSLYPSNEDISL-AVSRILKSFNYPSASLICAKAECLLRLEELVRQFL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 205 AKKRAkISYKAAfppgADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITT--DWLLTALDSM 282
Cdd:cd06394   161 ISKET-LSVRML----DDSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTtmDFPLLHLDGI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 283 epldpraLDLLQGVVAFRHYTPESDNKRQFKgRWKNLRFKESLKSDDgFNSYALYA---YDSVWLVARALDvffsqgntv 359
Cdd:cd06394   236 -------VDDQSNILGFSMFNTSHPFYLEFV-RSLNMSWRENCDAST-YPGPALSSalmFDAVHVVVSAVR--------- 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 360 tfsndpSLRNTNDSGIK---LSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYW-S 435
Cdd:cd06394   298 ------ELNRSQEIGVKplsCTSAQIWQHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWyS 371

                  ...
gi 1039011994 436 NHT 438
Cdd:cd06394   372 NRT 374
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
49-441 6.25e-08

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


Pssm-ID: 380614 [Multi-domain]  Cd Length: 402  Bit Score: 56.20  E-value: 6.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDSfigRAAKLAFVAAIEDINADQSILRGTKL--NIVFQDTNcSGFVGTMGALQLMENKV---VAAIGPQSSG 123
Cdd:cd06391     1 HIGAIFDESA---KKDDEVFRTAVGDLNQNEEILQTEKItfSVTFVDGN-NPFQAVQEACELMNQGIlalVSSIGCTSAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 124 IghiISHVANELHVPFLsFAATDPTLSSLQYPYFLRTTQNDYFQM---------NAITDFVSYFRWREVVaIFVDDEYGR 194
Cdd:cd06391    77 S---LQSLADAMHIPHL-FIQRSTAGTPRSGCGLTRSNRNDDYTLsvrppvylnDVILRVVTEYAWQKFI-IFYDSEYDI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 195 NGISVLGDALAKKRAKISYKAAfpPGADNSSISDLLASVNLMES-------RIFVVHVNPDSGLNIFSVAKSLGMMGSGY 267
Cdd:cd06391   152 RGIQEFLDKVSQQGMDVALQKV--ENNINKMITTLFDTMRIEELnryrdtlRRAILVMNPATAKSFITEVVETNLVAFDC 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 268 VWITTDWLLTALDSMEpLDPRALDLLQgVVAFRHYTPESDNKRQFKGrwkNLRFKESL-KSDDGFNSYA----LYAYDSV 342
Cdd:cd06391   230 HWIIINEEINDVDVQE-LVRRSIGRLT-IIRQTFPVPQNISQRCFRG---NHRISSSLcDPKDPFAQNMeisnLYIYDTV 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 343 WLVARALDVFFSQGNTVTFSNDPSLRNTNDSgiklsklhiFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILN 422
Cdd:cd06391   305 LLLANAFHKKLEDRKWHSMASLSCIRKNSKP---------WQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILG 375
                         410       420
                  ....*....|....*....|....
gi 1039011994 423 I-----KSTGPLRVGYWSNHTGFS 441
Cdd:cd06391   376 TnygeeLGRGVRKLGCWNPVTGLN 399
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
512-584 6.43e-08

Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the S1 domain, is the luminal domain just upstream of the first, M1, transmembrane region of transmembrane ion-channel proteins, and it binds L-glutamate and glycine. It is found in association with Lig_chan, pfam00060.


Pssm-ID: 463166 [Multi-domain]  Cd Length: 111  Bit Score: 51.75  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 512 GFCIDIFEAAIQLLPYpvprTYILY--GDGK------KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIES 583
Cdd:pfam10613  28 GFCIDLLKELAEILGF----KYEIRlvPDGKygsldpTTGEWNGMIGELIDGKADLAVAPLTITSEREKVVDFTKPFMTL 103

                  .
gi 1039011994 584 G 584
Cdd:pfam10613 104 G 104
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit ...
126-436 1.44e-07

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


Pssm-ID: 380611 [Multi-domain]  Cd Length: 373  Bit Score: 54.64  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 126 HIISHVANELHVPFLSfaATDPTLSSLQYPYFLRTTQNdyfqmNAITDFVSYFRWREVVAIFVDDEygrnGISVLgDALA 205
Cdd:cd06388    77 HTLTSFCSALHISLIT--PSFPTEGESQFVLQLRPSLR-----GALLSLLDHYEWNRFVFLYDTDR----GYSIL-QAIM 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 206 KKRAKISYK--AAFPPGADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALdSME 283
Cdd:cd06388   145 EKAGQNGWQvsAICVENFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDI-SLE 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 284 pldpRALDLLQGVVAFRHYTPESDNKRQFKGRWKNLRFKESLKSDDGFNSYALYAYDSVWLVARALDVFFSQGNTVTfsn 363
Cdd:cd06388   224 ----RFMHGGANVTGFQLVDFNTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDIS--- 296
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011994 364 dpslRNTNDSGIKLSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSN 436
Cdd:cd06388   297 ----RRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWND 365
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
128-435 1.62e-07

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


Pssm-ID: 380612 [Multi-domain]  Cd Length: 372  Bit Score: 54.64  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 128 ISHVANELHVPFLSfaATDPTLSSLQYPYFLRTTQNdyfqmNAITDFVSYFRWREVVAIFvDDEYGRNGISVLGDALAKK 207
Cdd:cd06389    73 ITSFCGTLHVSFIT--PSFPTDGTHPFVIQMRPDLK-----GALLSLIEYYQWDKFAYLY-DSDRGLSTLQAVLDSAAEK 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 208 RAKISykaAFPPGADNSSISD-----LLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTaldsm 282
Cdd:cd06389   145 KWQVT---AINVGNINNDKKDetyrsLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFT----- 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 283 eplDPRALDLLQG---VVAFRHYTPESDNKRQFKGRWKNLRFKESLKSDDGFNSY-ALYAYDSVWLVARALDVFFSQGNT 358
Cdd:cd06389   217 ---DGDLLKIQFGganVSGFQIVDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYtSALTYDAVQVMTEAFRNLRKQRIE 293
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 359 VTfsndpslRNTNDSGIKLSKLHIFNEGERFLQVILEMNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWS 435
Cdd:cd06389   294 IS-------RRGNAGDCLANPAVPWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWS 363
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
496-615 2.49e-07

The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the KA2 subunit of kainate receptor. While this ligand-binding domain is structurally homologous to the periplasmic binding fold type II superfamily, the N_terminal domain of kainate receptors belongs to the periplasmic-binding fold type I. There are five types of kainate receptors, GluR5, GluR6, GluR7, KA1, and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined.


Pssm-ID: 270443 [Multi-domain]  Cd Length: 250  Bit Score: 53.17  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 496 SYKNYASKDKnplgVKGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTK 572
Cdd:cd13725    20 NFQALSGNER----FEGFCVDMLRELAELLRFRYRLRLVedgLYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREK 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039011994 573 FVDFTQPFIESGLVVVAPVKGAKSSPWSFLKPFTIEMWAVTGA 615
Cdd:cd13725    96 VIDFSKPFMTLGISILYRVHMPVESADDLADQTNIEYGTIHAG 138
PBP1_NPR-like cd06373
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ...
71-273 5.21e-07

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


Pssm-ID: 380596 [Multi-domain]  Cd Length: 394  Bit Score: 53.05  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINAdQSILRGTKLNIVFQDTNCSGFVGTMGALQLMENKVVAAI-GPqssGIGHIISHVA------NelhVPFLSFA 143
Cdd:cd06373    26 ALRRVER-RGFLPGWRFQVHYRDTKCSDTLAPLAAVDLYCAKKVDVFlGP---VCEYALAPVAryaghwN---VPVLTAG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 144 ATDPTLS-SLQYPYFLRTTQNdYFQMN-AITDFVSYFRWREVVAIFVDDEYGRNGISV-------LGDALAKKRAKISYK 214
Cdd:cd06373    99 GLAAGFDdKTEYPLLTRMGGS-YVKLGeFVLTLLRHFGWRRVALLYHDNLRRKAGNSNcyftlegIFNALTGERDSIHKS 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 215 aaFP-PGADNSSISDLLASVNlMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTD 273
Cdd:cd06373   178 --FDeFDETKDDFEILLKRVS-NSARIVILCASPDTVREIMLAAHELGMINGEYVFFNID 234
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
49-444 8.45e-07

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


Pssm-ID: 380610 [Multi-domain]  Cd Length: 375  Bit Score: 52.33  E-value: 8.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  49 NVGALFTYDSFIGRAAklaFVAAIEDINADQSIL-RGTKLNIVFQDTNCS-GFVGTMGALQLMENKVVAAIGPQSSGIGH 126
Cdd:cd06387     1 SIGGLFMRNTVQEHSA---FRFAVQLYNTNQNTTeKPFHLNYHVDHLDSSnSFSVTNAFCSQFSRGVYAIFGFYDQMSMN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 127 IISHVANELHVPFLSfaATDPTLSSLQYPYFLRTTQNdyfqmNAITDFVSYFRWREVVAIFvDDEYGRNGISVLGDALAK 206
Cdd:cd06387    78 TLTSFCGALHTSFIT--PSFPTDADVQFVIQMRPALK-----GAILSLLAHYKWEKFVYLY-DTERGFSILQAIMEAAVQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 207 KRAKISYKAAfppG--ADNSSISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITTDWLLTALdSMEP 284
Cdd:cd06387   150 NNWQVTARSV---GniKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDI-LLER 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 285 LDPRALDllqgVVAFRHYTPESDNKRQFKGRWKNL---RFKESLKSDDGFNSyALyAYDSVWLVARALDVFFSQgntvtf 361
Cdd:cd06387   226 VMHGGAN----ITGFQIVNNENPMVQQFLQRWVRLderEFPEAKNAPLKYTS-AL-THDAILVIAEAFRYLRRQ------ 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 362 SNDPSLRNTndSGIKLSKLHI-FNEG---ERFLQVIlemNYTGLTGQIEFNSEKNRINPAYDILNIKSTGPLRVGYWSNH 437
Cdd:cd06387   294 RVDVSRRGS--AGDCLANPAVpWSQGidiERALKMV---QVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEY 368

                  ....*..
gi 1039011994 438 TGFSVAP 444
Cdd:cd06387   369 ERFVPFS 375
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
777-834 1.92e-06

The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand binding domain of the NR1, an essential channel-forming subunit of the NMDA receptor. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer ccomposed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. When co-expressed with NR1, the NR3 subunits form receptors that are activated by glycine alone and therefore can be classified as excitatory glycine receptors. NR1/NR3 receptors are calcium-impermeable and unaffected by ligands acting at the NR2 glutamate-binding site.


Pssm-ID: 270437 [Multi-domain]  Cd Length: 277  Bit Score: 50.44  E-value: 1.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011994 777 SNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYdHEC 834
Cdd:cd13719   220 QDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWIRY-QEC 276
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
693-828 3.99e-06

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


Pssm-ID: 270344 [Multi-domain]  Cd Length: 219  Bit Score: 48.85  E-value: 3.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 693 LTVQQLTSRIEGMDTLiaSNEPIGVQDGTfAWKFLVNELNIaPSRIIPLKDEEEYLSALQRGpRGGgvAAIVDELpYIKA 772
Cdd:cd13626    90 IIVKKDNTIIKSLEDL--KGKVVGVSLGS-NYEEVARDLAN-GAEVKAYGGANDALQDLANG-RAD--ATLNDRL-AALY 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 773 LLSNSNCKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKWL 828
Cdd:cd13626   162 ALKNSNLPLKIVGDIVSTAKVGFAFRKDNPeLRKKVNKALAEMKADGTLKKLSEKWF 218
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
715-827 6.21e-06

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


Pssm-ID: 270216 [Multi-domain]  Cd Length: 218  Bit Score: 48.43  E-value: 6.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 715 IGVQDGTFAWKFLVNELNIAPSRIIPlKDEEEYLSAlqrgpRGGGVAAIVDELP----YIKallSNSNCKFRTVGQEFTR 790
Cdd:cd00994   109 VAVKTGTTSVDYLKENFPDAQLVEFP-NIDNAYMEL-----ETGRADAVVHDTPnvlyYAK---TAGKGKVKVVGEPLTG 179
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039011994 791 TGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd00994   180 EQYGIAFPKGSELREKVNAALKTLKADGTYDEIYKKW 216
PBP1_ABC_ligand_binding-like cd06338
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ...
58-349 7.52e-06

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


Pssm-ID: 380561 [Multi-domain]  Cd Length: 347  Bit Score: 49.12  E-value: 7.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSI---LRGTKLNIVFQD--TNcsgfVGTMGAL--QLM-ENKVVAAIGPQSSGIGHIIS 129
Cdd:cd06338    13 AGEGKAQKRGYELWVEDVNAAGGVkggGKKRPVELVYYDdqSD----PATAVRLyeKLItEDKVDLLLGPYSSGLTLAAA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 130 HVANELHVPFLSFAATDPTLSSLQYPYflrttqndYFQMNAITD--FVSYFR-WREV------VAIF-VDDEYGRNGISV 199
Cdd:cd06338    89 PVAEKYGIPMIAGGAASDSIFERGYKY--------VFGVLPPASdyAKGLLDlLAELgpkpktVAIVyEDDPFGKEVAEG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 200 LGDALAKKRAKISYKAAFPPGADNssISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLG----MMGSGYVWITTDWl 275
Cdd:cd06338   161 AREAAKKAGLEVVYDESYPPGTTD--FSPLLTKVKAANPDILLVGGYPPDAITLVRQMKELGynpkAFFLTVGPAFPAF- 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 276 ltaldsmepldPRAL-DLLQGVVAFRHYTPESDNKrqFKGRWKNL--RFKESLKSDDGFnsYALYAYDSVWLVARAL 349
Cdd:cd06338   238 -----------REALgKDAEGVLGPSQWEPSLPYK--VFPGAKEFvkAYKEKFGEEPSY--HAAAAYAAGQVLQQAI 299
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
715-828 3.63e-05

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


Pssm-ID: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 46.18  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 715 IGVQDGTFAWKFLvNELNIAPSRIIPLkdeEEYLSALQRGprggGVAAIVDELP----YIKallSNSNCKFRTVGQEFTR 790
Cdd:cd00997   111 VATVAGSTAADYL-RRHDIDVVEVPNL---EAAYTALQDK----DADAVVFDAPvlryYAA---HDGNGKAEVTGSVFLE 179
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039011994 791 TGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWL 828
Cdd:cd00997   180 ENYGIVFPTGSPLRKPINQALLNLREDGTYDELYEKWF 217
PBP2_Arg_3 cd13622
Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding ...
484-603 5.29e-05

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


Pssm-ID: 270340 [Multi-domain]  Cd Length: 222  Bit Score: 45.37  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 484 GKPLKIGVPnrvSYKN-YASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYILYgdgkknpSYDNLISEVAANIFDVAVG 562
Cdd:cd13622     1 SKPLIVGVG---KFNPpFEMQGTNN-ELFGFDIDLMNEICKRIQRTC--QYKPM-------RFDDLLAALNNGKVDVAIS 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039011994 563 DVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKSSPWSFLK 603
Cdd:cd13622    68 SISITPERSKNFIFSLPYLLSYSQFLTNKDNNISSFLEDLK 108
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
135-435 5.51e-05

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


Pssm-ID: 380613 [Multi-domain]  Cd Length: 367  Bit Score: 46.47  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 135 LHVPFL--SFaatdPTLSSLQYPYFLRTTQNDyfqmnAITDFVSYFRWREVVAIFVDDeygrNGISVLG---DALAKKRA 209
Cdd:cd06390    79 LHVCFItpSF----PVDTSNQFVLQLRPELQD-----ALISVIEHYKWQKFVYIYDAD----RGLSVLQkvlDTAAEKNW 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 210 KIS-------YKAAFppgadnssisdLLASVNLMESRIFVVHVNPDSG-LN-IFSVAKSLGMMGSGYVWITTDWLLTALD 280
Cdd:cd06390   146 QVTavnilttTEEGY-----------RMLFQDLDKKKERLVVVDCESErLNaILGQIVKLEKNGIGYHYILANLGFMDID 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 281 SMEPLDPRAldllqGVVAFR--HYTP-----------ESDNKRQFKGRWKNLRFKESLksddgfnsyalyAYDSVWLVAR 347
Cdd:cd06390   215 LTKFKESGA-----NVTGFQlvNYTDtiparimqqwkNSDSRDLPRVDWKRPKYTSAL------------TYDGVKVMAE 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 348 ALDVFFSQ-------GNTVTFSNDPSLrnTNDSGIKLsklhifnegERFLQvilEMNYTGLTGQIEFNSEKNRINPAYDI 420
Cdd:cd06390   278 AFQSLRRQridisrrGNAGDCLANPAV--PWGQGIDI---------QRALQ---QVRFEGLTGNVQFNEKGRRTNYTLHV 343
                         330
                  ....*....|....*
gi 1039011994 421 LNIKSTGPLRVGYWS 435
Cdd:cd06390   344 IEMKHDGIRKIGYWN 358
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
512-590 5.99e-05

The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the NR3 subunit of NMDA receptor family. The ionotropic N-methyl-d-asparate (NMDA) subtype of glutamate receptors serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 270438 [Multi-domain]  Cd Length: 283  Bit Score: 46.00  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 512 GFCIDIFEAAIQLLPYpvprTYILY--GDGK----KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGL 585
Cdd:cd13720    67 GYCIDLLEKLAEDLGF----DFDLYivGDGKygawRNGRWTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSL 142

                  ....*.
gi 1039011994 586 -VVVAP 590
Cdd:cd13720   143 gILVRT 148
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
541-588 6.26e-05

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


Pssm-ID: 270342 [Multi-domain]  Cd Length: 219  Bit Score: 45.18  E-value: 6.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039011994 541 KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVV 588
Cdd:cd13624    44 KNMAFDGLIPALQSGKIDIIISGMTITEERKKSVDFSDPYYEAGQAIV 91
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
487-590 6.70e-05

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 45.01  E-value: 6.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  487 LKIGVpnRVSYKNYASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYILYgdgkknpSYDNLISEVAANIFDVAVGDVTI 566
Cdd:smart00062   2 LRVGT--NGDYPPFSFADEDG-ELTGFDVDLAKAIAKELGLKV--EFVEV-------SFDSLLTALKSGKIDVVAAGMTI 69
                           90       100
                   ....*....|....*....|....
gi 1039011994  567 ITNRTKFVDFTQPFIESGLVVVAP 590
Cdd:smart00062  70 TPERAKQVDFSDPYYRSGQVILVR 93
PBP1_ABC_HAAT-like cd19981
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
61-220 6.76e-05

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


Pssm-ID: 380636 [Multi-domain]  Cd Length: 297  Bit Score: 45.74  E-value: 6.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  61 GRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHIISHVANELHVPF 139
Cdd:cd19981    16 GKSALHGAELAVEQINAAGGIN-GKKVELVVYDDQASPKQAVNIAQKLIEQdKVVAVVSGSYSGPTRAAAPIFQEAKVPM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 140 LSFAATDPTLSSlQYPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIF-VDDEYGRNGISVLGDALAKKRAKISYKAAFP 218
Cdd:cd19981    95 VSAYAVHPDITK-AGDYVFRVAFLGPVQGRAGAEYAVKDLGAKKVAILtIDNDFGKSLAAGFKEEAKKLGAEIVSEYAYA 173

                  ..
gi 1039011994 219 PG 220
Cdd:cd19981   174 LG 175
PBP1_ABC_ligand_binding-like cd19978
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ...
58-223 9.12e-05

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


Pssm-ID: 380633 [Multi-domain]  Cd Length: 341  Bit Score: 45.64  E-value: 9.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSIlRGTKLNIVFQDTNCSGFVGTMGALQLMEN-KVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd19978    14 AELGNEMKRGIEAAFNEVNAQGGV-NGRKIKLIALDDGYEPDRTVKNTKKLIEEdKVFALIGYVGTPTALAALPLANEKK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 137 VPFLSFAATDPTLSSLQYPY--FLRTTQNDyfQMNAITD-FVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISY 213
Cdd:cd19978    93 IPLFGPFTGAEFLRTPFLPYvfNLRASYAD--ETEALVDyLVKTLGPKRIAIFYQNDAFGLAGLEGAKKALKKRGLTPVA 170
                         170
                  ....*....|
gi 1039011994 214 KAAFPPGADN 223
Cdd:cd19978   171 EGSYTRNTLD 180
PBP1_sensory_GC_DEF-like cd06371
ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are ...
63-186 9.84e-05

ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues; This group includes the ligand-binding domain of membrane guanylyl cyclases (GC-D, GC-E, and GC-F) that are specifically expressed in sensory tissues. They share a similar topology with an N-terminal extracellular ligand-binding domain, a single transmembrane domain, and a C-terminal cytosolic region that contains kinase-like and catalytic domains. GC-D is specifically expressed in a subpopulation of olfactory sensory neurons. GC-E and GC-F are colocalized within the same photoreceptor cells of the retina and have important roles in phototransduction. Unlike the other family members, GC-E and GC-F have no known extracellular ligands. Instead, they are activated under low calcium conditions by guanylyl cyclase activating proteins called GCAPs. GC-D expressing neurons have been implicated in pheromone detection and GC-D is phylogenetically more similar to the Ca2+-regulated GC-E and GC-F than to receptor GC-A, -B and -C which are activated by peptide ligands. Moreover, these olfactory GCs and retinal GCs share characteristic sequence similarity in a regulatory domain that is involved in the binding of GCAPs, suggesting GC-D activity may be regulated by an unknown extracellular ligand and intracellular Ca2+. Rodent GC-D-expressing neurons have been implicated in pheromone detection and were recently shown to respond to atmospheric CO2 which is an olfactory stimulus for many invertebrates and regulates some insect innate behavior, such as the location of food and hosts.


Pssm-ID: 380594 [Multi-domain]  Cd Length: 379  Bit Score: 45.77  E-value: 9.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  63 AAKLAfvaaIEDINADQSILRGTKLNIVFQDTNCSGfVGTMGALQLMENKVVAAIGPQSSGIGHIISHVANELHVPFLSF 142
Cdd:cd06371    22 AARLA----VSRINKDPSLDLGYWFDYVILPEDCET-SKALAAFSSAEGRASGFVGPVNPGYCEAASLLAQEWDKALFSW 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1039011994 143 AATDPTLSSlqYPYFLRTTQndyFQMNAITDFVSYFRWREVVAI 186
Cdd:cd06371    97 GCVNHELNS--YPTFARTLP---PPADVLYTVLRYFRWAHVAVV 135
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
778-827 9.93e-05

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


Pssm-ID: 270432 [Multi-domain]  Cd Length: 251  Bit Score: 44.84  E-value: 9.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039011994 778 NCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13714   200 NCNLTQIGGLLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKW 249
PBP1_ABC_HAAT-like cd19983
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
71-346 1.21e-04

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


Pssm-ID: 380638 [Multi-domain]  Cd Length: 303  Bit Score: 45.27  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINADQSIlRGTKLNIVFQDTNcsgfvGTMGALQ-----LMENKVVAAIGPQSSGIGHIISHVANELHVPFLSFAAT 145
Cdd:cd19983    26 AVEEINAAGGI-NGRPVELIIRDDQ-----QDPEAAKaadreLIAGGVVAIIGHMTSAMTVAVLPVINEAKVLMISPTVS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 146 DPTLSSLQyPYFLRTTQNDYFQMNAITDFVSYFRWREVVAIFVD---DEYGRNGISVLGDALAKKRAKISYKAAFPPGAD 222
Cdd:cd19983   100 TPELSGKD-DYFFRVTPTTRESAQALARYAYNRGGLRRVAVIYDlsnRAYSESWLDNFRSEFEALGGRIVAEIPFSSGAD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 223 nSSISDLLASvnLMESR---IFVVHVNPDSGLnifsVAKSLGMMGSGYVWITTDWLLTaldsmepldpraLDLLQ----- 294
Cdd:cd19983   179 -VDFSDLARR--LLASKpdgLLLVASAVDTAM----LAQQIRKLGSKIPLFSSAWAAT------------EELLElggka 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 295 --GVVAFRHYTPESDNKR--QFKGRWKNlRFKEslksDDGFnsYALYAYDSVWLVA 346
Cdd:cd19983   240 veGMLFSQAYDRNSSNPRylAFKEAYEE-RFGR----EPSF--AAAYAYEAAMVLA 288
PBP1_AmiC-like cd06331
type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system ...
58-160 1.33e-04

type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF); This group includes the type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF), found in bacteria and Archaea. AmiC controls expression of the amidase operon by a ligand-triggered conformational switch. In the absence of ligand or presence of butyramide (repressor), AmiC (the ligand sensor and negative regulator) adopts an open conformation and inhibits the transcription antitermination function of AmiR by direct protein-protein interaction. In the presence of inducing ligands such as acetamide, AmiC adopts a closed conformation which disrupts a silencing AmiC-AmiR complex and the expression of amidase and other genes of the operon is induced. FmdDEF is predicted to be an ATP-dependent transporter and closely resembles the periplasmic binding protein and the two transmembrane proteins present in various hydrophobic amino acid-binding transport systems.


Pssm-ID: 380554 [Multi-domain]  Cd Length: 333  Bit Score: 45.29  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINADQSILrGTKLNIVFQDTNCSGFVGTMGALQLM-ENKVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd06331    13 SVYGRAIANGAELAVEEINAAGGVL-GRPVELVVEDDASDPATAVAAARRLIqQDKVDAIVGPITSATRNAVAPVAERAK 91
                          90       100
                  ....*....|....*....|....
gi 1039011994 137 VPFLSFAATDPTLSSlqyPYFLRT 160
Cdd:cd06331    92 VPLLYPTFYEGGECS---PYLFCF 112
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
779-834 1.40e-04

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR2 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR2, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270444 [Multi-domain]  Cd Length: 259  Bit Score: 44.63  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 779 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 834
Cdd:cd13726   204 CDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
543-598 1.43e-04

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


Pssm-ID: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 44.25  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 543 PSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKSSP 598
Cdd:cd00997    48 DSVSALLAAVAEGEADIAIAAISITAEREAEFDFSQPIFESGLQILVPNTPLINSV 103
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
541-600 2.62e-04

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


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 43.33  E-value: 2.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 541 KNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKSSPWS 600
Cdd:cd13629    44 VNTAWDGLIPALQTGKFDLIISGMTITPERNLKVNFSNPYLVSGQTLLVNKKSAAGIKSL 103
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
690-828 2.70e-04

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


Pssm-ID: 270406 [Multi-domain]  Cd Length: 238  Bit Score: 43.40  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 690 TSILTVQQltSRIEGMDTLiaSNEPIGVQDGTFAWKFL--VNELNIAPSRIIPLKDEEEYLSALQRGprggGVAAIVDE- 766
Cdd:cd13688   103 TRLLVRKD--SGLNSLEDL--AGKTVGVTAGTTTEDALrtVNPLAGLQASVVPVKDHAEGFAALETG----KADAFAGDd 174
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 767 --LPYIKALLSNSNcKFRTVGQEFTRTGWGFAFQRDSP---LAVDmsTAILQLAEEGKLEKIRKKWL 828
Cdd:cd13688   175 ilLAGLAARSKNPD-DLALIPRPLSYEPYGLMLRKDDPdfrLLVD--RALAQLYQSGEIEKLYDKWF 238
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
758-828 4.58e-04

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


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 42.56  E-value: 4.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039011994 758 GGVAAIVDELPYIKALLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVD-MSTAILQLAEEGKLEKIRKKWL 828
Cdd:cd13629   150 GKADAFIYDQPTPARFAKKNDPTLVALLEPFTYEPLGFAIRKGDPDLLNwLNNFLKQIKGDGTLDELYDKWF 221
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
512-587 5.42e-04

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


Pssm-ID: 270216 [Multi-domain]  Cd Length: 218  Bit Score: 42.26  E-value: 5.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 512 GFCIDIFEAAIQLLPYPVPRTYIlygdgkknpSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVV 587
Cdd:cd00994    23 GFDIDLWEAIAKEAGFKYELQPM---------DFKGIIPALQTGRIDIAIAGITITEERKKVVDFSDPYYDSGLAV 89
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
773-827 5.95e-04

GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270439 [Multi-domain]  Cd Length: 251  Bit Score: 42.70  E-value: 5.95e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039011994 773 LLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13721   195 FVTQRNCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKW 249
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
496-588 6.40e-04

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


Pssm-ID: 270431 [Multi-domain]  Cd Length: 218  Bit Score: 42.27  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 496 SYKNyaskDKNPLgvKGFCIDIFEA-AIQLLPYPVPRTyilygdgkknPSYDNLISEVAANIFDVAVGDVTIITNRTKFV 574
Cdd:cd13713    14 NFLD----EDNQL--VGFDVDVAKAiAKRLGVKVEPVT----------TAWDGIIAGLWAGRYDIIIGSMTITEERLKVV 77
                          90
                  ....*....|....
gi 1039011994 575 DFTQPFIESGLVVV 588
Cdd:cd13713    78 DFSNPYYYSGAQIF 91
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
772-827 6.56e-04

The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the delta1 receptor of an orphan glutamate receptor family. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of delta receptors belongs to the periplasmic-binding fold type I. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRdelta2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans.


Pssm-ID: 270448 [Multi-domain]  Cd Length: 257  Bit Score: 42.64  E-value: 6.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 772 ALLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13730   200 AALTDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKW 255
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
779-834 6.90e-04

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR1 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR1, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270447 [Multi-domain]  Cd Length: 260  Bit Score: 42.71  E-value: 6.90e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 779 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 834
Cdd:cd13729   205 CDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 260
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
779-834 8.60e-04

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR4 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR4, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I.The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270445 [Multi-domain]  Cd Length: 259  Bit Score: 42.33  E-value: 8.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 779 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 834
Cdd:cd13727   204 CDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP1_ABC_HAAT-like cd06348
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
58-418 1.15e-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: 42.22  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINAdQSILRGTKLNIVFQDTNcsgfvGT-MGALQLM-----ENKVVAAIGPQSSGIGHIISHV 131
Cdd:cd06348    13 ALYGQSQKNGAQLAVEEINA-AGGVGGVKIELIVEDTA-----GDpEQAINAFqklinQDKVLAILGPTLSSEAFAADPI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 132 ANELHVPFLSFAATDPTLSSLQyPYFLRTTQNDYFQM-NAITDFVSYFRWREVVAIF-VDDEYGRNGISVLGDALAKKRA 209
Cdd:cd06348    87 AQQAKVPVVGISNTAPGITDIG-PYIFRNSLPEDKVIpPTVKAAKKKYGIKKVAVLYdQDDAFTVSGTKVFPAALKKNGV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 210 KISYKAAFPPGaDnssiSDLLASVNLmesrifVVHVNPD----SGL-----NIFSVAKSLGMMG---SGYVWITTDWLLT 277
Cdd:cd06348   166 EVLDTETFQTG-D----TDFSAQLTK------IKALNPDaiviSALaqegaLIVKQARELGLKGpivGGNGFNSPDLIKL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 278 ALDSMEpldpraldllqGVVAFRHYTPESDNKrqfKGRWKNLRFKESLKSDDgfNSYALYAYDSVWLVARALDvffsqgn 357
Cdd:cd06348   235 AGKAAE-----------GVIVGSAWSPDNPDP---KNQAFVAAYKEKYGKEP--DQFAAQAYDAAYILAEAIK------- 291
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039011994 358 tvtfsndpslrnTNDSGIKLSKLhifnegERFL-QVILEMNYTGLTGQIEFNSEKNRINPAY 418
Cdd:cd06348   292 ------------KAGSTTDRADL------RDALaRILIAKDFEGPLGPFSFDADRDGIQPPV 335
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
507-582 1.24e-03

The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the type 2 periplasmic-binding fold protein superfamily; This group contains the ligand-binding domain of the delta1 receptor of an orphan glutamate receptor family. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of delta receptors belongs to the periplasmic-binding fold type I. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetical analysis shows that both GluRdelta1 and GluRdelta2 are more homologous to non-NMDA receptors. GluRdelta2 was shown to function as an AMPA-like receptor by mutation analysis. Moreover, targeted disruption of GluRdelta2 gene caused motor coordination impairment, Purkinje cell maturation, and long-term depression of synaptic transmission. It has been suggested that GluRdelta2 is the receptor for cerebellin 1, a glycoprotein of the Clq, and the tumor necrosis factor family which is secreted from cerebellar granule cells. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans.


Pssm-ID: 270448 [Multi-domain]  Cd Length: 257  Bit Score: 41.87  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 507 PLGVKGFCIDIFEAAIQLLP-----YPVPRTYilYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFI 581
Cdd:cd13730    25 PKRYKGFSIDVLDALAKALGfkyeiYQAPDGK--YGHQLHNTSWNGMIGELISKRADLAISAITITPERESVVDFSKRYM 102

                  .
gi 1039011994 582 E 582
Cdd:cd13730   103 D 103
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
485-584 1.42e-03

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


Pssm-ID: 270231 [Multi-domain]  Cd Length: 232  Bit Score: 41.17  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 485 KPLKIGVPNrvSYKNYASKDKNPlGVKGFCIDIFEAAIQLLPYPVprTYIlygdgkkNPSYDNLISEVAANIFDVAVGDV 564
Cdd:cd01069    10 GVLRVGTTG--DYKPFTYRDNQG-QYEGYDIDMAEALAKSLGVKV--EFV-------PTSWPTLMDDLAADKFDIAMGGI 77
                          90       100
                  ....*....|....*....|
gi 1039011994 565 TIITNRTKFVDFTQPFIESG 584
Cdd:cd01069    78 SITLERQRQAFFSAPYLRFG 97
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
767-827 1.45e-03

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


Pssm-ID: 270449 [Multi-domain]  Cd Length: 257  Bit Score: 41.55  E-value: 1.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039011994 767 LPYIKalLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13731   197 LEYVA--INDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 255
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
772-827 1.47e-03

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


Pssm-ID: 270434 [Multi-domain]  Cd Length: 257  Bit Score: 41.37  E-value: 1.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 772 ALLSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13716   200 VAINDDDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKW 255
PBP1_SBP-like cd06329
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ...
58-176 1.65e-03

periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); 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: 380552 [Multi-domain]  Cd Length: 343  Bit Score: 41.88  E-value: 1.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  58 SFIGRAAKLAFVAAIEDINAdQSILRGTKLNIVFQDTNCSGfVGTMGALQLM-ENKVVAAIGPQSSGIGHIISHVANELH 136
Cdd:cd06329    13 ASVGEIYLKGLQFAIEEINA-GGGLLGRKIELVPFDNKGSP-QEALIQLKKAiDQGIRFVLQGNSSAVAGALIDAIEKHN 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1039011994 137 -------VPFLSFAATDPTLSSLQY-PYFLRTTQNDYFQMNAITDFVS 176
Cdd:cd06329    91 qrnpdkrVLFLNYGAEAPELTGAKCsFWHFRFDANADMKMAALADYMK 138
PBP1_ABC_HAAT-like cd19985
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
62-230 1.80e-03

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


Pssm-ID: 380640 [Multi-domain]  Cd Length: 321  Bit Score: 41.49  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  62 RAAKLAfvaaIEDINADQSIlRGTKLNIVFQDTNCSGFVGTMGALQLMENKVVAAIGPQSSGIghiiSHVANELH----V 137
Cdd:cd19985    21 RGAELY----IDQINAAGGI-NGKKVKLDVFDDQNDPDAARKAAQIIVSDKALAVIGHYYSSA----SIAAGKIYkkagI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 138 PFLSFAATDP--TLSSlqyPYFLRTTQNDYFQMNAITDFVSYFRWREVVA-IFVDDEYGRNgisvLGDALAK--KRAKIS 212
Cdd:cd19985    92 PAITPSATADavTRDN---PWYFRVIFNDSLQGRFLANYAKKVLKKDKVSiIYEEDSYGKS----LASVFEAtaRALGLK 164
                         170
                  ....*....|....*...
gi 1039011994 213 YKAAFPPGADNSSISDLL 230
Cdd:cd19985   165 VLKKWSFDTDSSQLDQNL 182
PBP2_Arg_STM4351 cd13700
Substrate binding domain of arginine-specific ABC transporter; type 2 periplasmic-binding ...
542-596 1.85e-03

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


Pssm-ID: 270418 [Multi-domain]  Cd Length: 222  Bit Score: 40.89  E-value: 1.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039011994 542 NPSYDNLISEVAANIFDVAVGDVTIITNRTKFVDFTQPFIESGLVVVAPVKGAKS 596
Cdd:cd13700    47 NQAFDSLIPSLKFKKFDAVISGMDITPEREKQVSFSTPYYENSAVVIAKKDTYKT 101
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
779-834 1.99e-03

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtypes of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This family represents the ligand-binding domain of the AMPA receptor subunits, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current.


Pssm-ID: 270433 [Multi-domain]  Cd Length: 261  Bit Score: 41.19  E-value: 1.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 779 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 834
Cdd:cd13715   206 CDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC 261
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
774-827 2.07e-03

GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270440 [Multi-domain]  Cd Length: 250  Bit Score: 40.80  E-value: 2.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039011994 774 LSNSNCKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13722   195 VTQRNCNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKW 248
PBP1_YraM_LppC_lipoprotein-like cd06339
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup ...
60-231 3.61e-03

periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup includes periplasmic binding component of lipoprotein LppC, an immunodominant antigen, whose molecular function is not characterized. Members of this subgroup are predicted to be involved in transport of lipid compounds, and they are sequence similar to the family of ABC-type hydrophobic amino acid transporters (HAAT).


Pssm-ID: 380562 [Multi-domain]  Cd Length: 331  Bit Score: 40.72  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  60 IGRAAKLAFVAAIEDINadqsilrGTKLNIVFQDTNCSGFVGTMgALQLMENKVVAAIGP-QSSGIGHIIShVANELHVP 138
Cdd:cd06339    15 AGQAIRDGIELALFDAG-------GSRPELRVYDTGGPEGAAAA-YQQAVAEGADLIIGPlLKSSVAALAA-AAQALGVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 139 FLSF-AATDPTLSSLQYPYFLRTTQndyfQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISYKAAF 217
Cdd:cd06339    86 VLALnNDESATAGPGLFQFGLSPED----EARQAARYAVQQGLRRFAVLAPDNAYGQRVANAFREAWQALGGTVVAVESY 161
                         170
                  ....*....|....*.
gi 1039011994 218 PPGADN--SSISDLLA 231
Cdd:cd06339   162 DPDETDfsAAIRRLLG 177
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
497-589 3.68e-03

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


Pssm-ID: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 39.76  E-value: 3.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 497 YKNYASKDKNPLGVKGFCIDIFEAAIQLLPYPVPRTYIlygdgkknpSYDNLISEVAANIFDVAVGDVTIITNRTKFVDF 576
Cdd:cd13628    10 YPPFEFKIGDRGKIVGFDIELAKTIAKKLGLKLQIQEY---------DFNGLIPALASGQADLALAGITPTPERKKVVDF 80
                          90
                  ....*....|...
gi 1039011994 577 TQPFIESGLVVVA 589
Cdd:cd13628    81 SEPYYEASDTIVS 93
PBP1_ABC_ligand_binding-like cd06326
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ...
60-223 3.72e-03

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


Pssm-ID: 380549 [Multi-domain]  Cd Length: 339  Bit Score: 40.60  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  60 IGRAAKLAFVAAIEDINADQSIlRGTKLNIVFQDTncsGFVGTMGA---LQLMEN-KVVAAIGPQSSGIGHIISHVANEL 135
Cdd:cd06326    16 LGREYLAGAKAYFDQVNAAGGI-NGRKIRLVTLDD---GYDPARTVentRQLIEQdKVVALFGYVGTANVEAVLPLLEEA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 136 HVPFLSFAATDPTLSSLQYPY--FLRTTQNDyfQMNAITDFVSYFRWREVVAIFVDDEYGRNGISVLGDALAKKRAKISY 213
Cdd:cd06326    92 GVPLVGPLTGADSLREPGNPYvfHVRASYAD--EVEKIVRHLATLGLKRIAVVYQDDPFGKEGLAAAEAALAARGLEPVA 169
                         170
                  ....*....|
gi 1039011994 214 KAAFPPGADN 223
Cdd:cd06326   170 TAAVARNAAD 179
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
685-827 4.35e-03

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


Pssm-ID: 270430 [Multi-domain]  Cd Length: 219  Bit Score: 39.68  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 685 YTASLTSILTVQQLTSRIEGMDTLiaSNEPIGVQDGTFAWKFLVNELNIAPSRIIPlkDEEEYLSALQRGPRGggvAAIV 764
Cdd:cd13712    83 YTYSGIQLIVRKNDTRTFKSLADL--KGKKVGVGLGTNYEQWLKSNVPGIDVRTYP--GDPEKLQDLAAGRID---AALN 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011994 765 DELpyIKALLSNSNCKFRTVGQEFTRTGWGFAFQRDSP-LAVDMSTAILQLAEEGKLEKIRKKW 827
Cdd:cd13712   156 DRL--AANYLVKTSLELPPTGGAFARQKSGIPFRKGNPkLKAAINKAIEDLRADGTLAKLSEKW 217
PRK15404 PRK15404
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
71-211 4.41e-03

high-affinity branched-chain amino acid ABC transporter substrate-binding protein;


Pssm-ID: 237959 [Multi-domain]  Cd Length: 369  Bit Score: 40.39  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994  71 AIEDINADQSIlRGTKLNIVFQDTNCSGFVGTMGAlqlmeNKVVaaigpqSSGIGHIISHVANELHVP-----------F 139
Cdd:PRK15404   52 AIEDINAKGGI-KGDKLEGVEYDDACDPKQAVAVA-----NKVV------NDGIKYVIGHLCSSSTQPasdiyedegilM 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011994 140 LSFAATDPTLSSLQYPYFLRTTQNDYFQ----MNAITDFVSYFRwrevVAIFVDDE-YGRNGISVLGDALAKKRAKI 211
Cdd:PRK15404  120 ITPAATAPELTARGYQLIFRTIGLDSDQgptaAKYILEKVKPKR----IAVLHDKQqYGEGLARSVKDGLKKAGANV 192
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
497-588 4.47e-03

GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group contains glutamate receptor domain GluR. These domains are found in the GluR proteins that have been shown to function as L-glutamate activated potassium channels, also known ionotropic glutamate receptors or iGluRs. In addition to two ligand binding core domains, iGluRs typically have a channel-like domain inserted in the middle of the GluR-like domain. Animal iGluRs mediate the ion flux in the synapses of the CNS and can be subdivided into several classes depending on the neurotransmitter specificity and ion conductance properties. Their plant homologs have been shown to function in light signal transduction and calcium homeostasis. The GluR proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270440 [Multi-domain]  Cd Length: 250  Bit Score: 40.03  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011994 497 YKNYASKDKNPLG---VKGFCIDIFEAAIQLLPYPVPRTYI---LYGDGKKNPSYDNLISEVAANIFDVAVGDVTIITNR 570
Cdd:cd13722    14 YVMYRKSDKPLYGndrFEGYCLDLLKELSNILGFLYDVKLVpdgKYGAQNDKGEWNGMVKELIDHRADLAVAPLTITYVR 93
                          90
                  ....*....|....*...
gi 1039011994 571 TKFVDFTQPFIESGLVVV 588
Cdd:cd13722    94 EKVIDFSKPFMTLGISIL 111
PBP1_iGluR_NMDA_NR2 cd06378
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR2 subunit of ...
225-272 6.46e-03

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


Pssm-ID: 380601  Cd Length: 356  Bit Score: 39.97  E-value: 6.46e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039011994 225 SISDLLASVNLMESRIFVVHVNPDSGLNIFSVAKSLGMMGSGYVWITT 272
Cdd:cd06378   180 SDAKTLRQLKKIEAQVILLYCTKEEAQYIFEAAEEAGLTGYGYVWIVP 227
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
779-834 8.96e-03

The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic acid) subtype GluR3 of ionotropic glutamate receptors, a member of the type 2 periplasmic binding fold protein superfamily; This group contains the ligand-binding domain of the AMPA receptor subunit GluR3, a member of non-NMDA (N-methyl-D-aspartate) type iGluRs which are ligand-gated ion channels that mediate excitatory synaptic transmission in the central nervous system. While this ligand-binding domain is structurally homologous to the periplasmic-binding fold type II superfamily, the N-terminal domain of AMPA receptors belongs to the periplasmic-binding fold type I. The AMPA receptors are the most commonly found receptor in the nervous system and sensitive to the artificial glutamate analog, AMPA. They consist of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current


Pssm-ID: 270446 [Multi-domain]  Cd Length: 259  Bit Score: 38.90  E-value: 8.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011994 779 CKFRTVGQEFTRTGWGFAFQRDSPLAVDMSTAILQLAEEGKLEKIRKKWLTYDHEC 834
Cdd:cd13728   204 CDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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