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Conserved domains on  [gi|164419751|ref|NP_062665|]
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glutamate receptor 4 isoform 1 precursor [Mus musculus]

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List of domain hits

Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR4 subunit ...
28-398 0e+00

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: 107383  Cd Length: 371  Bit Score: 795.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388    1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388   81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388  161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 268 NTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388  241 NTPMVTKLMQRWKKLDQREYPGSESPPKYTSALTYDGVLVMAEAFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419751 348 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVL 398
Cdd:cd06388  321 TLKQVRIQGLTGNIQFDHYGRRVNYTMDVFELKSNGPRKIGYWNDMDKLVL 371
PBPb cd00134
Bacterial periplasmic transport systems use membrane-bound complexes and substrate-bound, ...
417-528 8.67e-17

Bacterial periplasmic transport systems use membrane-bound complexes and substrate-bound, membrane-associated, periplasmic binding proteins (PBPs) to transport a wide variety of substrates, such as, amino acids, peptides, sugars, vitamins and inorganic ions. PBPs have two cell-membrane translocation functions: bind substrate, and interact with the membrane bound complex. A diverse group of periplasmic transport receptors for lysine/arginine/ornithine (LAO), glutamine, histidine, sulfate, phosphate, molybdate, and methanol are included in the PBPb CD.


:

Pssm-ID: 238078 [Multi-domain]  Cd Length: 218  Bit Score: 80.11  E-value: 8.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 417 VVVTTIMESPYVMYKKnhemfeGNDKYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEI 496
Cdd:cd00134    1 LTVGTAGTYPPFSFRD------ANGELTGFDVDLAKAIAKELGVKVKFVEVD-------------WDGLITALKSGKVDL 61
                         90       100       110
                 ....*....|....*....|....*....|..
gi 164419751 497 AIAPLTITLVREEVIDFSKPFMSLGISIMIKK 528
Cdd:cd00134   62 IAAGMTITPERAKQVDFSDPYYKSGQVILVKK 93
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
654-791 1.33e-53

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


:

Pssm-ID: 197504  Cd Length: 133  Bit Score: 182.87  E-value: 1.33e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   654 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSaePSVFTRTTAEGVARVRKSKgkFAFLLESTMNEY 733
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKS--PEVFVKSYAEGVQRVRVSN--YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 164419751   734 IEQRkPCDTMKVGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLKNKWWYD 791
Cdd:smart00079  77 ELSR-NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
546-825 8.84e-131

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


:

Pssm-ID: 249551 [Multi-domain]  Cd Length: 268  Bit Score: 395.87  E-value: 8.84e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  546 EIWMCIVFAYIGVSVVLFLVSRFSPYEWHteepedgkegPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGG 625
Cdd:pfam00060   1 EVWLCILAAYLIVGVVLFLVERFSPYEWR----------GPPEEPNQFTLSNSLWFSFGALVQQGHRELPRSLSGRIVVG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  626 VWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFT 705
Cdd:pfam00060  71 VWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQNKIGYGTLRGGSTFEFFTESKNPTYRRMWEYMISFKGEVNV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  706 RTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLK 785
Cdd:pfam00060 151 ESYEEGVQRVRKGNGLYAFLMESAYLEYEVSRDPCKLTTVGEVFATKGYGIAFPKGSPLRDKLSRAILELRESGELQKLE 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 164419751  786 NKWWYDKGECGPKDsgSKDKTSALSLSNVAGVFYILVGGL 825
Cdd:pfam00060 231 NKWWKKKGECSLKS--TAVSSSQLGLESFAGLFLILGIGL 268
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
39-380 1.50e-69

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: 250359 [Multi-domain]  Cd Length: 344  Bit Score: 235.45  E-value: 1.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   39 QEYTAFRLAIFLHNTSPNASEaPFNLVPHVDNIETaNSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLI 118
Cdd:pfam01094   1 QVLPAMRLAIEDINADPGLLP-GITLGYEDDDTCD-DSAAGAAADCLLKSKGVVAVIGPSCSSVAIAVARLAGAFGIPMI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  119 TPSFPTEGESQ-----FVLQLRPSLR---GALLSLLDHYEWNCFVFLYDTD----RGYSILQAIMEKAGQNGWHVSAicV 186
Cdd:pfam01094  79 SYGATSPELSDktrypTFARTVPSDSkqaRAIADILKHFGWKRVAVIYDDDdygeGGLEALEDALREAGLNVVAVAS--E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  187 ENFNDVSYRQLLEELDRRQEKK--FVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFK--DISLERFIHGGANVTGF 262
Cdd:pfam01094 157 VIASDDDFTALLKELKDIKSKArvIVVCGSPDDLRQILRQARELGLMSGGYVWILTDLWSDslLIDDDKAREAMKGVLGF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  263 QLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGnagdclanpaaPWGQG 342
Cdd:pfam01094 237 TLKPPDSPGFQEFLRRLKKLAARETPASDTEPNGYALLAYDAVYLLAHALNEALRDDPDITAGG-----------KWVDG 305
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 164419751  343 IDMERTLKQVRIQGLTGNVQFDH-YGRRVNYTMDVFELK 380
Cdd:pfam01094 306 SQLLEYLRNVNFEGLTGPVQFDDnGGRRPDYSLEILNWD 344
 
Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR4 subunit ...
28-398 0e+00

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: 107383  Cd Length: 371  Bit Score: 795.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388    1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388   81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388  161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 268 NTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388  241 NTPMVTKLMQRWKKLDQREYPGSESPPKYTSALTYDGVLVMAEAFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419751 348 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVL 398
Cdd:cd06388  321 TLKQVRIQGLTGNIQFDHYGRRVNYTMDVFELKSNGPRKIGYWNDMDKLVL 371
PBPb cd00134
Bacterial periplasmic transport systems use membrane-bound complexes and substrate-bound, ...
417-528 8.67e-17

Bacterial periplasmic transport systems use membrane-bound complexes and substrate-bound, membrane-associated, periplasmic binding proteins (PBPs) to transport a wide variety of substrates, such as, amino acids, peptides, sugars, vitamins and inorganic ions. PBPs have two cell-membrane translocation functions: bind substrate, and interact with the membrane bound complex. A diverse group of periplasmic transport receptors for lysine/arginine/ornithine (LAO), glutamine, histidine, sulfate, phosphate, molybdate, and methanol are included in the PBPb CD.


Pssm-ID: 238078 [Multi-domain]  Cd Length: 218  Bit Score: 80.11  E-value: 8.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 417 VVVTTIMESPYVMYKKnhemfeGNDKYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEI 496
Cdd:cd00134    1 LTVGTAGTYPPFSFRD------ANGELTGFDVDLAKAIAKELGVKVKFVEVD-------------WDGLITALKSGKVDL 61
                         90       100       110
                 ....*....|....*....|....*....|..
gi 164419751 497 AIAPLTITLVREEVIDFSKPFMSLGISIMIKK 528
Cdd:cd00134   62 IAAGMTITPERAKQVDFSDPYYKSGQVILVKK 93
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
654-791 1.33e-53

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


Pssm-ID: 197504  Cd Length: 133  Bit Score: 182.87  E-value: 1.33e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   654 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSaePSVFTRTTAEGVARVRKSKgkFAFLLESTMNEY 733
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKS--PEVFVKSYAEGVQRVRVSN--YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 164419751   734 IEQRkPCDTMKVGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLKNKWWYD 791
Cdd:smart00079  77 ELSR-NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
426-491 1.92e-29

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: 256090  Cd Length: 65  Bit Score: 112.70  E-value: 1.92e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164419751  426 PYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDaDTKIWNGMVGELVY 491
Cdd:pfam10613   1 PYVMLKENGENLTGNERFEGYCIDLLDELAKILGFNYEIYLVPDGKYGSED-KTGEWNGMIGELIR 65
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
426-490 6.83e-25

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


Pssm-ID: 214911  Cd Length: 62  Bit Score: 99.63  E-value: 6.83e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164419751   426 PYVMYKKNHEmfEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADtKIWNGMVGELV 490
Cdd:smart00918   1 PYVMLKESPD--GGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLPN-GSWNGMVGELV 62
LivK COG0683
ABC-type branched-chain amino acid transport systems, periplasmic component [Amino acid ...
69-389 2.93e-06

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


Pssm-ID: 223755  Cd Length: 366  Bit Score: 48.97  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  69 DNIETANSFAVTNAFCSQysRGVFAIFGLYDKRSVHTLTSFCSALHISLITPS-----FPTEGESQFVLQLRPSLR--GA 141
Cdd:COG0683   59 DASDPATAAAVARKLITQ--DGVDAVVGPTTSGVALAASPVAEEAGVPLISPSatapqLTGRGLKPNVFRTGPTDNqqAA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 142 LLS--LLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELdRRQEKKFVI-DCEIER 217
Cdd:COG0683  137 AAAdyLVKKGGKKRVAIIGdDYAYGEGLADAFKAALKALGGEVVVEEVYAPGDTDFSALVAKI-KAAGPDAVLvGGYGPD 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 218 LQNILEQIVSVGkhVKGYHYIIAnlGFKDISLERFIHGGANVTGFQLVDFNTPMVT----KLMDRWKKLDqreypGSETP 293
Cdd:COG0683  216 AALFLRQAREQG--LKAKLIGGD--GAGTAEFEEIAGAGGAGAGLLATAYSTPDDSpankKFVEAYKAKY-----GDPAA 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 294 PKYTSALTYDGVLVMAETfrslrrqkidISRRGNAGDCLANPAApwgqgidmertLKQVRI-QGLTGNVQFDHYGRRVNY 372
Cdd:COG0683  287 PSYFAAAAYDAVKLLAKA----------IEKAGKSSDREAVAEA-----------LKGGKFfDTAGGPVTFDEKGDRGSK 345
                        330
                 ....*....|....*..
gi 164419751 373 TMDVFELKSTGPRKVGY 389
Cdd:COG0683  346 PVYVGQVQKGGDGKFVY 362
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
546-825 8.84e-131

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


Pssm-ID: 249551 [Multi-domain]  Cd Length: 268  Bit Score: 395.87  E-value: 8.84e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  546 EIWMCIVFAYIGVSVVLFLVSRFSPYEWHteepedgkegPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGG 625
Cdd:pfam00060   1 EVWLCILAAYLIVGVVLFLVERFSPYEWR----------GPPEEPNQFTLSNSLWFSFGALVQQGHRELPRSLSGRIVVG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  626 VWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFT 705
Cdd:pfam00060  71 VWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQNKIGYGTLRGGSTFEFFTESKNPTYRRMWEYMISFKGEVNV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  706 RTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLK 785
Cdd:pfam00060 151 ESYEEGVQRVRKGNGLYAFLMESAYLEYEVSRDPCKLTTVGEVFATKGYGIAFPKGSPLRDKLSRAILELRESGELQKLE 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 164419751  786 NKWWYDKGECGPKDsgSKDKTSALSLSNVAGVFYILVGGL 825
Cdd:pfam00060 231 NKWWKKKGECSLKS--TAVSSSQLGLESFAGLFLILGIGL 268
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
39-380 1.50e-69

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: 250359 [Multi-domain]  Cd Length: 344  Bit Score: 235.45  E-value: 1.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   39 QEYTAFRLAIFLHNTSPNASEaPFNLVPHVDNIETaNSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLI 118
Cdd:pfam01094   1 QVLPAMRLAIEDINADPGLLP-GITLGYEDDDTCD-DSAAGAAADCLLKSKGVVAVIGPSCSSVAIAVARLAGAFGIPMI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  119 TPSFPTEGESQ-----FVLQLRPSLR---GALLSLLDHYEWNCFVFLYDTD----RGYSILQAIMEKAGQNGWHVSAicV 186
Cdd:pfam01094  79 SYGATSPELSDktrypTFARTVPSDSkqaRAIADILKHFGWKRVAVIYDDDdygeGGLEALEDALREAGLNVVAVAS--E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  187 ENFNDVSYRQLLEELDRRQEKK--FVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFK--DISLERFIHGGANVTGF 262
Cdd:pfam01094 157 VIASDDDFTALLKELKDIKSKArvIVVCGSPDDLRQILRQARELGLMSGGYVWILTDLWSDslLIDDDKAREAMKGVLGF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  263 QLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGnagdclanpaaPWGQG 342
Cdd:pfam01094 237 TLKPPDSPGFQEFLRRLKKLAARETPASDTEPNGYALLAYDAVYLLAHALNEALRDDPDITAGG-----------KWVDG 305
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 164419751  343 IDMERTLKQVRIQGLTGNVQFDH-YGRRVNYTMDVFELK 380
Cdd:pfam01094 306 SQLLEYLRNVNFEGLTGPVQFDDnGGRRPDYSLEILNWD 344
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3;
435-528 1.58e-15

Bacterial extracellular solute-binding proteins, family 3;


Pssm-ID: 249906 [Multi-domain]  Cd Length: 220  Bit Score: 76.16  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  435 EMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFS 514
Cdd:pfam00497  13 EYVDENGKLVGFDVDLAKAIAKRLGVKVEFVPVS-------------WDGLIPALQSGKIDVIIAGMTITPERKKQVDFS 79
                          90
                  ....*....|....
gi 164419751  515 KPFMSLGISIMIKK 528
Cdd:pfam00497  80 DPYYTSGQVLVVRK 93
HisJ COG0834
ABC-type amino acid transport/signal transduction systems, periplasmic component/domain [Amino ...
396-541 8.13e-11

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


Pssm-ID: 223904 [Multi-domain]  Cd Length: 275  Bit Score: 62.33  E-value: 8.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 396 LVLIQDAPTLGNDTAAIENRTVVVTTIMESPYVMYKKnhemfEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGkygar 475
Cdd:COG0834   16 LLLAACAAADLLDKIKARGKLRVGTEATYAPPFEFLD-----AKGGKLVGFDVDLAKAIAKRLGGDKKVEFVPVA----- 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164419751 476 dadtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKpqKSKPGVFSFLD 541
Cdd:COG0834   86 ------WDGLIPALKAGKVDIIIAGMTITPERKKKVDFSDPYYYSGQVLLVKK--DSDIGIKSLED 143
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
435-528 1.82e-10

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 60.42  E-value: 1.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   435 EMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFS 514
Cdd:smart00062  14 SFADEDGELTGFDVDLAKAIAKELGLKVEFVEVS-------------FDSLLTALKSGKIDVVAAGMTITPERAKQVDFS 80
                           90
                   ....*....|....
gi 164419751   515 KPFMSLGISIMIKK 528
Cdd:smart00062  81 DPYYRSGQVILVRK 94
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
437-527 7.95e-09

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 55.91  E-value: 7.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 437 FEGNDKYEGYCVDLASEIAKHIGIKYKIaivpdgkygaRDADtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKP 516
Cdd:PRK09495  40 FKQGDKYVGFDIDLWAAIAKELKLDYTL----------KPMD---FSGIIPALQTKNVDLALAGITITDERKKAIDFSDG 106
                         90
                 ....*....|.
gi 164419751 517 FMSLGISIMIK 527
Cdd:PRK09495 107 YYKSGLLVMVK 117
3A0103s03R TIGR01096
lysine-arginine-ornithine-binding periplasmic protein; [Transport and binding proteins, Amino ...
439-528 1.14e-05

lysine-arginine-ornithine-binding periplasmic protein; [Transport and binding proteins, Amino acids, peptides and amines].


Pssm-ID: 233269 [Multi-domain]  Cd Length: 250  Bit Score: 46.58  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  439 GNDKYEGYCVDLASEIAKHIGIKYKiaivpdgkYGARDADTKIWNgmvgeLVYGKAEIAIAPLTITLVREEVIDFSKPFM 518
Cdd:TIGR01096  42 ANGKLVGFDVDLAKALCKRMKAKCK--------FVEQNFDGLIPS-----LKAKKVDAIMATMSITPKRQKQIDFSDPYY 108
                          90
                  ....*....|
gi 164419751  519 SLGISIMIKK 528
Cdd:TIGR01096 109 ATGQGFVVKK 118
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
745-789 1.03e-03

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 40.50  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 164419751 745 VGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLKNKWW 789
Cdd:PRK09495 198 VGDSLEAQQYGIAFPKGSELREKVNGALKTLKENGTYAEIYKKWF 242
 
Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR4 subunit ...
28-398 0e+00

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: 107383  Cd Length: 371  Bit Score: 795.77  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388    1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388   81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388  161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 268 NTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388  241 NTPMVTKLMQRWKKLDQREYPGSESPPKYTSALTYDGVLVMAEAFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419751 348 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVL 398
Cdd:cd06388  321 TLKQVRIQGLTGNIQFDHYGRRVNYTMDVFELKSNGPRKIGYWNDMDKLVL 371
PBPb cd00134
Bacterial periplasmic transport systems use membrane-bound complexes and substrate-bound, ...
417-528 8.67e-17

Bacterial periplasmic transport systems use membrane-bound complexes and substrate-bound, membrane-associated, periplasmic binding proteins (PBPs) to transport a wide variety of substrates, such as, amino acids, peptides, sugars, vitamins and inorganic ions. PBPs have two cell-membrane translocation functions: bind substrate, and interact with the membrane bound complex. A diverse group of periplasmic transport receptors for lysine/arginine/ornithine (LAO), glutamine, histidine, sulfate, phosphate, molybdate, and methanol are included in the PBPb CD.


Pssm-ID: 238078 [Multi-domain]  Cd Length: 218  Bit Score: 80.11  E-value: 8.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 417 VVVTTIMESPYVMYKKnhemfeGNDKYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEI 496
Cdd:cd00134    1 LTVGTAGTYPPFSFRD------ANGELTGFDVDLAKAIAKELGVKVKFVEVD-------------WDGLITALKSGKVDL 61
                         90       100       110
                 ....*....|....*....|....*....|..
gi 164419751 497 AIAPLTITLVREEVIDFSKPFMSLGISIMIKK 528
Cdd:cd00134   62 IAAGMTITPERAKQVDFSDPYYKSGQVILVKK 93
PBP1_iGluR_AMPA cd06380
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the AMPA receptor; ...
28-397 0e+00

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 I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107375  Cd Length: 382  Bit Score: 595.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNaSEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06380    1 PIGGLFDVDEDQEYSAFRFAISQHNTNPN-STAPFKLLPHVDNLDTSDSFALTNAICSQLSRGVFAIFGSYDKSSVNTLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 108 SFCSALHISLITPSFPTE---GESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNG--WHVS 182
Cdd:cd06380   80 SYSDALHVPFITPSFPTNdldDGNQFVLQMRPSLIQALVDLIEHYGWRKVVYLYDSDRGLLRLQQLLDYLREKDnkWQVT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 183 AICVENFNDV-SYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTG 261
Cdd:cd06380  160 ARRVDNVTDEeEFLRLLEDLDRRKEKRIVLDCESERLNKILEQIVDVGKNRKGYHYILANLGFDDIDLSKFLFGGVNITG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 262 FQLVDFNTPMVTKLMDRWKKLDQREYPGSET-PPKYTSALTYDGVLVMAETFRSLRRQK------IDISRRGNAGDCLAN 334
Cdd:cd06380  240 FQLVDNTNPTVQKFLQRWKKLDPREWPGAGTsPIKYTAALAHDAVLVMAEAFRSLRRQRgsgrhrIDISRRGNGGDCLAN 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164419751 335 PAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLV 397
Cdd:cd06380  320 PAVPWEHGIDIERALKKVQFEGLTGNVQFDEFGQRTNYTLDVVELKTRGLRKVGYWNEDDGLV 382
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR3 subunit ...
29-397 0e+00

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: 107382  Cd Length: 372  Bit Score: 565.43  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06387    2 IGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 109 FCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVEN 188
Cdd:cd06387   82 FCGALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 189 FNDV-SYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06387  162 IKDVqEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDISLERVMHGGANITGFQIVNN 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 268 NTPMVTKLMDRWKKLDQREYPGSETPP-KYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 346
Cdd:cd06387  242 ENPMVQQFLQRWVRLDEREFPEAKNSPlKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIE 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419751 347 RTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLV 397
Cdd:cd06387  322 RALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEYERFV 372
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR2 subunit ...
28-398 6.20e-179

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: 107384  Cd Length: 370  Bit Score: 524.58  E-value: 6.20e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPnaseapFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06389    1 QIGGLFPRGADQEYSAFRVGMVQFSTSE------FRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTIT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06389   75 SFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 188 NFN----DVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQ 263
Cdd:cd06389  155 NINndrkDEAYRSLFQDLENKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLSKIQFGGANVSGFQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 264 LVDFNTPMVTKLMDRWKKLDQREYPGSETPP-KYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQG 342
Cdd:cd06389  235 IVDYDDPLVSKFIQRWSTLEEKEYPGAHTKTiKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQG 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 164419751 343 IDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVL 398
Cdd:cd06389  315 VEIERALKQVQVEGLTGNIKFDQNGKRINYTINVMELKSNGPRKIGYWSEVDKMVV 370
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR1 subunit ...
28-397 8.32e-175

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: 107385  Cd Length: 364  Bit Score: 513.72  E-value: 8.32e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNaseapfnLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06390    1 QIGGLFPNQQSQEHAAFRFALSQLTEPPK-------LLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYDRKTVNMLT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06390   74 SFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNIL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06390  154 TTTEEGYRKLFQDLDKKKERLIVVDCESERLNAILNQIIKLEKNGIGYHYILANLGFMDIDLTKFRESGANVTGFQLVNY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 268 NTPMVTKLMDRWKKLDQREYPGSE-TPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 346
Cdd:cd06390  234 TDTTVSRIMQQWKNFDARDLPRVDwKRPKYTSALTYDGVRVMAEAFQNLRKQRIDISRRGNAGDCLANPAVPWGQGIDIQ 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419751 347 RTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLV 397
Cdd:cd06390  314 RALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDEKLV 364
PBP1_iGluR_non_NMDA_like cd06368
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the non-NMDA ...
28-397 4.48e-129

N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the non-NMDA (N-methyl-d-asparate) 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 I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107363  Cd Length: 324  Bit Score: 393.95  E-value: 4.48e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASeAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06368    1 RIGAIFDEDARQEELAFRFAIDRINTNEEIL-AKFTLVPDIDELNTNDSFELTNKACDLLSQGVAAIFGPSSSSSANTVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 108 SFCSALHISLITPSFPTEG-ESQFVLQLRPSLR---GALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSA 183
Cdd:cd06368   80 SICDALEIPHITTSWSPNPkPRQFTINLYPSMRdlsDALLDLIKYFGWRKFVYIYDSDEGLLRLQELLDALSPKGIQVTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 184 ICVENFNDVsYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQ 263
Cdd:cd06368  160 RRLDDDTDM-YRPLLKEIKREKERRIILDCSPERLKEFLEQAVEVGMMSEYYHYILTNLDFHTLDLELFRYGGVNITGFR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 264 LVDFNTPMVTKLMDRWKKLDQREYPGSE-TPPKYTSALTYDGVLVMaetfrslrrqkidisrrgnagdclanpaapwgqg 342
Cdd:cd06368  239 LVDPDNPEVQKFIQRWERSDHRICPGSGlKPIKTESALTYDAVLLF---------------------------------- 284
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 164419751 343 idmertlkqvriqglTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLV 397
Cdd:cd06368  285 ---------------TGRIQFDENGQRSNFTLDILELKEGGLRKVGTWNPEDGLN 324
PBP1_iGluR_N_LIVBP_like cd06351
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
28-397 9.10e-89

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


Pssm-ID: 107346  Cd Length: 328  Bit Score: 287.48  E-value: 9.10e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNaSEAPFNLVPHVDNIETANSFAVTNAFCSQY-SRGVFAIFGLYDKRSVHTL 106
Cdd:cd06351    1 NIGAIFDRDARKEELAFRAAIDALNTENL-NALPTKLSVEVVEVNTNDPFSLLRAVCDLLvSQGVAAIFGPTSSESASAV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 107 TSFCSALHISLITPSFPTEG-----ESQFVLQLRPSLRG---ALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNG 178
Cdd:cd06351   80 QSICDALEIPHISISGGSEGlsdkeESSTTLQLYPSLEDladALLDLLEYYNWTKFAIIYDSDEGLSRLQELLDESGIKG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 179 WHVSAICVENFNDVsYRQLLEELDRRQEKKFVIDCE-IERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGA 257
Cdd:cd06351  160 IQVTVRRLDLDDDN-YRQLLKELKRSESRRIILDCSsEEEAKEILEQAVELGMMGYGYHWILTNLDLSDIDLEPFQYGPA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 258 NVTGFQLVDFNTPMVTKLMDRWkklDQREYPGSETPPKYTSALTYDGVLVMaetfrslrrqkidisrrgnagdclanpaa 337
Cdd:cd06351  239 NITGFRLVDPDSPDVSQFLQRW---LEESPGVNLRAPIYDAALLYDAVLLL----------------------------- 286
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164419751 338 pwgqgidmertlkqvriqglTGNVQFDHYGRRVNYTMDVFELK-STGPRKVGYWNDMDKLV 397
Cdd:cd06351  287 --------------------TGTVSFDEDGVRSNFTLDIIELNrSRGWRKVGTWNGSLDGL 327
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
654-791 1.33e-53

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


Pssm-ID: 197504  Cd Length: 133  Bit Score: 182.87  E-value: 1.33e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   654 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSaePSVFTRTTAEGVARVRKSKgkFAFLLESTMNEY 733
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKS--PEVFVKSYAEGVQRVRVSN--YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 164419751   734 IEQRkPCDTMKVGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLKNKWWYD 791
Cdd:smart00079  77 ELSR-NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP1_iGluR_Kainate cd06382
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the kainate ...
28-391 6.20e-53

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 I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107377  Cd Length: 327  Bit Score: 187.86  E-value: 6.20e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIR-NTDQEYTAFRLAIFLHNTsPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTL 106
Cdd:cd06382    1 RIGAIFDDdDDSGEELAFRYAIDRINR-EKELLANTTLEYDIKRVKPDDSFETTKKVCDLLQQGVAAIFGPSSSEASSIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 107 TSFCSAL---HISLiTPSFPTEGESQFVLQLRPS---LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWH 180
Cdd:cd06382   80 QSICDAKeipHIQT-RWDPEPKSNRQFTINLYPSnadLSRAYADIVKSFNWKSFTIIYESAEGLLRLQELLQAFGISGIT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 181 VSaicVENFNDVS-YRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANV 259
Cdd:cd06382  159 IT---VRQLDDDLdYRPLLKEIKNSGDNRIIIDCSADILIELLKQAQQVGMMSEYYHYIITNLDLHTLDLEDYRYSGVNI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 260 TGFQLVDFNTPMVTKLMDRWKKLDQREYPGSE-TPPKYTSALTYDGvlvmaetfrslrrqkidisrrgnagdclanpaap 338
Cdd:cd06382  236 TGFRLVDPDSPEVKEVIRSLELSWDEGCRILPsTGVTTESALMYDA---------------------------------- 281
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419751 339 wgqgidmertlkqVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWN 391
Cdd:cd06382  282 -------------VYLFGLTGRIEFDSSGQRSNFTLDVIELTESGLRKVGTWN 321
PBP1_ABC_transporter_GCPR_C_like cd04509
Family C of G-protein coupled receptors and their close homologs, the type I ...
28-307 2.03e-43

Family C of G-protein coupled receptors and their close homologs, the type I 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 I 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, phermone 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 - which is included in this CD - followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type II periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.


Pssm-ID: 107261 [Multi-domain]  Cd Length: 299  Bit Score: 160.35  E-value: 2.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTD-QEYTAFRLAIFLHNTSPNASE---APFNLVPHVDNIE--TANSFAVTNAFCSQYsrGVFAIFGLYDKR 101
Cdd:cd04509    1 KIGVLFPLSGPyAEYGAFRLAGAQLAVEEINAKggiPGRKLELVIYDDQsdPARALAAARRLCQQE--GVDALVGPVSSG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 102 SVHTLTSFCSALHISLITPSFPTEGESQ-----FVLQLRPSLR---GALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEK 173
Cdd:cd04509   79 VALAVAPVAEALKIPLISPGATAPGLTDkkgypYLFRTGPSDEqqaEALADYIKEYNWKKVAILYDDDSYGRGLLEAFKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 174 AGQNGWhVSAICVENF--NDVSYRQLLEELdRRQEKKFVIDCE-IERLQNILEQIVSVGKHvKGYHYIIANLGFKDISLE 250
Cdd:cd04509  159 AFKKKG-GTVVGEEYYplGTTDFTSLLQKL-KAAKPDVIVLCGsGEDAATILKQAAEAGLT-GGYPILGITLGLSDVLLE 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164419751 251 RFIH-GGANVTGFQLVDFNTPMVTKLMDRWKKldqREYPGSETPPKYTSALTYDGVLV 307
Cdd:cd04509  236 AGGEaAEGVLTGTPYFPGDPPPESFFFVRAAA---REKKKYEDQPDYFAALAYDAVLL 290
PBP1_glutamate_receptors_like cd06269
Family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the ...
28-263 6.25e-36

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 recep; 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 I family. The family C GPCRs consist of metabotropic glutamate receptor (mGluR) receptors, a calcium-sensing receptor (CaSR), gamma-aminobutyric receptors (GABAb), 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: 153137  Cd Length: 298  Bit Score: 138.80  E-value: 6.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  28 QIGGLFIRNTDQ---EYTAFRLAIFLHNT-SPNASEAPFNLVPHVDNIE--TANSFAVTNAFCSQ--YSRGVFAIFGLYD 99
Cdd:cd06269    1 RIGGLFPLHSGGrfgEEGAFRAAAALFAVeEINNDLPNTTLGYEIYDSCcsPSDAFSAALDLCSLleKSRGVVAVIGPSS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 100 KRSVHTLTSFCSALHISLIT-----PSFPTEGESQFVLQLRPSLR---GALLSLLDHYEWNCFVFLYDTDRGYSILQAIM 171
Cdd:cd06269   81 SSSAEAVASLLGALHIPQISysatsPLLSDKEQFPSFLRTVPSDSsqaQAIVDLLKHFGWTWVGLVYSDDDYGRRLLELL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 172 EKAGQnGWHVSAICVENFNDVS--YRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHvKGYHYIIANLGFKD-IS 248
Cdd:cd06269  161 EEELE-KNGICVAFVESIPDGSedIRRLLKELKSSTARVIVVFSSEEDALRLLEEAVELGMM-TGYHWIITDLWLTScLD 238
                        250
                 ....*....|....*
gi 164419751 249 LERFIHGGANVTGFQ 263
Cdd:cd06269  239 LELLEYFPGNLTGFG 253
PBP1_iGluR_Kainate_GluR5_7 cd06393
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR5-7 ...
27-391 1.23e-35

N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR5-7 subunits of Kainate receptor; N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the GluR5-7 subunits of Kainate receptor. While this N-terminal domain belongs to the periplasmic-binding fold type I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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 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: 107388  Cd Length: 384  Bit Score: 139.77  E-value: 1.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  27 VQIGGLF----IRNTD---QEYTAFRLAIFLHNTS----PNASeapfnLVPHVDNIETANSFAVTNAFCSQYSRGVFAIF 95
Cdd:cd06393    3 IRIGGIFeyldGPNNQvmsAEELAFRFSANIINRNrtllPNTT-----LTYDIQRIHFHDSFEATKKACDQLALGVVAIF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  96 GLYDKRSVHTLTSFCSAL---HISLITPSFPTEGESQFVLQLRP---SLRGALLSLLDHYEWNCFVFLYDTDRGYSILQA 169
Cdd:cd06393   78 GPSQGSCTNAVQSICNALevpHIQLRWKHHPLDNKDTFYVNLYPdyaSLSHAILDLVQYLKWRSATVVYDDSTGLIRLQE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 170 IMEKAGQNGWHVSAICVENFNDVSyRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISL 249
Cdd:cd06393  158 LIMAPSRYNIRLKIRQLPTDSDDA-RPLLKEMKRGREFRIIFDCSHQMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 250 ERFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYPGSETP-----PKYTSALTYDGVLVMAETFRslRRQKIDIsr 324
Cdd:cd06393  237 EPYRYSGVNLTGFRILNVDNPHVSSIVEKWSMERLQAAPKPETGlldgvMMTDAALLYDAVHMVSVCYQ--RAPQMTV-- 312
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164419751 325 rgNAGDClaNPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHY-GRRVNYTMDVFELKSTGPRKVGYWN 391
Cdd:cd06393  313 --NSLQC--HRHKAWRFGGRFMNFIKEAQWEGLTGRIVFNKTsGLRTDFDLDIISLKEDGLEKVGVWN 376
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
426-491 1.92e-29

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: 256090  Cd Length: 65  Bit Score: 112.70  E-value: 1.92e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164419751  426 PYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDaDTKIWNGMVGELVY 491
Cdd:pfam10613   1 PYVMLKENGENLTGNERFEGYCIDLLDELAKILGFNYEIYLVPDGKYGSED-KTGEWNGMIGELIR 65
Periplasmic_Binding_Protein_Type_1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
29-315 3.08e-25

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine/isoleucine/valine- binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands, while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


Pssm-ID: 107248 [Multi-domain]  Cd Length: 269  Bit Score: 106.51  E-value: 3.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  29 IGGLFIRNTDQEYTAFRLAIFLHNtspnASEAPFNLVPHVDNIET--ANSFAVTNAFCSQysrGVFAIFGLYDKRSVHTL 106
Cdd:cd01391    2 IGVLLPLSGSAPFGAQLLAGIELA----AEEIGRGLEVILADSQSdpERALEALRDLIQQ---GVDGIIGPPSSSSALAV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 107 TSFCSALHISLITPSFPTEGESQF--VLQLRPSLR---GALLSLLDHYEWNCFVFLYDTDRGYS-ILQAIMEKAGQNGW- 179
Cdd:cd01391   75 VELAAAAGIPVVSLDATAPDLTGYpyVFRVGPDNEqagEAAAEYLAEKGWKRVALIYGDDGAYGrERLEGFKAALKKAGi 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 180 -HVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFkDISLERFIHGGAN 258
Cdd:cd01391  155 eVVAIEYGDLDTEKGFQALLQLLKAAPKPDAIFACNDEMAAGALKAAREAGLTPGDISIIGFDGSP-AALLAAGEAGPGL 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 164419751 259 VTGFQLVDFNTPmvtklmdrwkkldqreypgseTPPKYTSALTYDGVLVMAETFRSL 315
Cdd:cd01391  234 TTVAQPFPGDDP---------------------DQPDYPAALGYDAVLLGVRLPYVL 269
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
426-490 6.83e-25

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


Pssm-ID: 214911  Cd Length: 62  Bit Score: 99.63  E-value: 6.83e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164419751   426 PYVMYKKNHEmfEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDADtKIWNGMVGELV 490
Cdd:smart00918   1 PYVMLKESPD--GGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLPN-GSWNGMVGELV 62
PBP1_iGluR_delta_2 cd06391
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the delta2 ...
29-396 1.66e-15

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 I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107386  Cd Length: 400  Bit Score: 78.14  E-value: 1.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPfNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06391    2 IGAIFDESAKKDDEVFRMAVADLNQNNEILQTE-KITVSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 109 FCSALHISLITPSFPTEGESQ-------------FVLQLRPS--LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEK 173
Cdd:cd06391   81 LADAMHIPHLFIQRSTAGTPRsscgltrsnrnddYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDTDYDIRGIQEFLDK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 174 AGQNGWHVSAICVENFNDVSYRQL-----LEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKD 246
Cdd:cd06391  161 VSQQGMDVALQKVENNINKMITGLfrtmrIEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEISD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 247 ISLERFIHggANVTGFQLVDFNTPMVTKLMDRWKKLDQReYPGSETPPK--------YTSALTYDGVLVMAETF-RSLRR 317
Cdd:cd06391  241 MDVQELVR--RSIGRLTIIRQTFPLPQNISQRCFRGNHR-ISSSLCDPKdpfaqmmeISNLYIYDTVLLLANAFhKKLED 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 318 QKIdisRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVF-----ELKSTGPRKVGYWND 392
Cdd:cd06391  318 RKW---HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGELEFNENGGNPNVHFEILgtnygEDLGRGVRKLGCWNP 394

                 ....
gi 164419751 393 MDKL 396
Cdd:cd06391  395 ITGL 398
PBP1_iGluR_delta_1 cd06392
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the delta1 ...
29-367 1.54e-13

N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family; N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family. While this N-terminal domain belongs to the periplasmic-binding fold type I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 may be closer related to non-NMDA receptors. In contrast to GluRdelta2, GluRdelta1 is expressed in many areas in the developing CNS, including the hippocampus and the caudate putamen. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans.


Pssm-ID: 107387  Cd Length: 400  Bit Score: 72.34  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  29 IGGLFIRNTDQEYTAFRLAI--FLHNTSPNASEAPFNlvpHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTL 106
Cdd:cd06392    2 IGAIFEENAAKDDRVFQLAVsdLSLNDDILQSEKITY---SIKSIEANNPFQAVQEACDLMTQGILALVTSTGCASANAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 107 TSFCSALHISLI--------TPSF-----PTEGESQFVLQLRPSLR--GALLSLLDHYEWNCFVFLYDTDRGYSILQAIM 171
Cdd:cd06392   79 QSLTDAMHIPHLfvqrnsggSPRTachlnPSPEGEEYTLAARPPVRlnDVMLKLVTELRWQKFIVFYDSEYDIRGLQSFL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 172 EKAGQNGWHVSAICVEN-----FNDVSYRQLLEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGF 244
Cdd:cd06392  159 DQASRLGLDVSLQKVDRnisrvFTNLFTTMKTEELNRYRDtlRRAILLLSPRGAQTFINEAVETNLASKDSHWVFVNEEI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 245 KDISLERFIH---GGANVTG--FQLVDFNTPMVTKLMDRWKKL--DQREypGSETPPKYTSALTYDGVLVMAETF-RSLR 316
Cdd:cd06392  239 SDTEILELVHsalGRMTVIRqiFPLSKDNNQRCIRNNHRISSLlcDPQE--GYLQMLQVSNLYLYDSVLMLANAFhRKLE 316
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419751 317 RQKIDISRRGNagdCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYG 367
Cdd:cd06392  317 DRKWHSMASLN---CIRKSTKPWNGGRSMLETIKKGHITGLTGVMEFKEDG 364
PBP1_iGluR_AMPA_Like cd06383
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of uncharacterized ...
66-373 7.77e-13

N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of uncharacterized AMPA-like receptors; N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of uncharacterized AMPA-like receptors. While this N-terminal domain belongs to the periplasmic-binding fold type I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107378  Cd Length: 368  Bit Score: 69.83  E-value: 7.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  66 PHVDNIETANSFAVT-NAFCSQYSRGVF--AIFGLYDKRSVHTLTSFCSALHISLITPSFPTEGESQ--FVLQLRPS--- 137
Cdd:cd06383   40 VETNAEVNRNDVKVAlIEVCDKADSAIVphLVLDTTTCGDASEIKSVTGALGIPTFSASYGQEGDLEqpYLIQLMPPadd 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 138 LRGALLSLLDHYEWNCFVFLYDTDRGYSIL--QAIMEKAGQNGWHVSAICVEnfnDVsyRQLLEELDRRQEKKFVIDC-E 214
Cdd:cd06383  120 IVEAIRDIVSYYNITNAAILYDDDFVMDHKykSLLQNWPTRHVITIINSIID---EV--REQIKRLRNLDIKNIFILGsT 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 215 IERLQNILEQIVSVGKHVKGYHYIIANlgfKDISLERFIHGGanvtgfqlVDFNTPMVTKLMDRWKKLDQREYPGSETPP 294
Cdd:cd06383  195 EEIIRYVLDQALAEGFMGRKYAWFLGN---PDLGIYDDLSCQ--------LRNASIFVTRPMMDYQSSVRGALLRTDEPT 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 295 KYTSA---------LTYDGVLVMAETFRSLRrqkIDISRRGNAGDCLAN-----PAAPW-GQGIDMERTLKQVRIQGLTG 359
Cdd:cd06383  264 LRPVFyfewafrlfLAYDAVLAVGEWPRRMR---KKRVEDGSTGTSVLPgfgisPESPLmTLQSSPFNGSSEIKFEMLAG 340
                        330
                 ....*....|....
gi 164419751 360 NVQFDHYGRRVNYT 373
Cdd:cd06383  341 RVAIDEGSSVSTKT 354
PBP1_iGluR_NMDA cd06367
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the ionotropic ...
102-393 3.48e-11

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 I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107362  Cd Length: 362  Bit Score: 64.63  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 102 SVHTLTSFCSALHISLITPSFPTEGESQfvLQLRPSLRG---ALLSLLDHYEWNCFVFLYDTDRGY-SILQAIMEKAGQN 177
Cdd:cd06367   86 SAQTRIPVVGISGRESIFMSDKNIHSLF--LQTGPSLEQqadVMLEILEEYDWHQFSVVTSRDPGYrDFLDRVETTLEES 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 178 --GWHVSAICV----ENFNDVSYRQLLEELDRRqekkfVI--DCEIERLQNILEQIVSVGKHVKGYHYIIANLgfkdisl 249
Cdd:cd06367  164 fvGWEFQLVLTldlsDDDGDARLLRQLKKLESR-----VIllYCSKEEAERIFEAAASLGLTGPGYVWIVGEL------- 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 250 erfihggANVTGFQLVDFNTPMVTKLMDRWKKLDQReypgsetppkytsalTYDGVLVMAETFRSLRRQKIDISRrgNAG 329
Cdd:cd06367  232 -------ALGSGLAPEGLPVGLLGVGLDTWYSLEAR---------------VRDAVAIVARAAESLLRDKGALPE--PPV 287
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164419751 330 DCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFEL-KSTGPRKVGYWNDM 393
Cdd:cd06367  288 NCYDTANKRESSGQYLARFLMNVTFDGETGDVSFNEDGYLSNPKLVIINLrRNRKWERVGSWENG 352
PBP1_GABAb_receptor cd06366
Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
42-396 9.09e-09

Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb). 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: 107361 [Multi-domain]  Cd Length: 350  Bit Score: 56.89  E-value: 9.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  42 TAFRLAIFLHNtSPNASEAPFNLVPHVDNiETANSFAVTNAFCSQ-YSRGVFAIFGLYDKRSVHTLTSFCSALHISLI-- 118
Cdd:cd06366   19 PAIEMALEDVN-ADNSILPGYRLVLHVRD-SKCDPVQAASAALDLlENKPVVAIIGPQCSSVAEFVAEVANEWNVPVLsf 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 119 ---TPSFPTEGESQFVLQLRPSLR---GALLSLLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAICV--ENF 189
Cdd:cd06366   97 aatSPSLSSRLQYPYFFRTTPSDSsqnPAIAALLKKFGWRRVATIYeDDDYGSGGLPDLVDALQEAGIEISYRAAfpPSA 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 190 NDVSYRQLLEELDRRQEKKFVID----------CEIERLqnileqivsvGKHVKGY---------HYIIANLGFKDISLE 250
Cdd:cd06366  177 NDDDITDALKKLKEKDSRVIVVHfspdlarrvfCEAYKL----------GMMGKGYvwiltdwlsSNWWSSSDCTDEEML 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 251 RFIHGganVTGFQLVDFNTPMVTK-LMDRWKKLDQREYPGSETPPKYtSALTYDGVlvmaetfrslrrqkidisrrgnag 329
Cdd:cd06366  247 EAMQG---VIGVRSYVPNSSMTLQeFTSRWRKRFGNENPELTEPSIY-ALYAYDAV------------------------ 298
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164419751 330 dclanpaapWGqgidmertlkQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKL 396
Cdd:cd06366  299 ---------WA----------STNFNGLSGPVQFDGGRRLASPAFEIINIIGKGYRKIGFWSSESGL 346
PBP1_iGluR_delta_like cd06381
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of an orphan family ...
29-391 3.07e-08

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 I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107376  Cd Length: 363  Bit Score: 55.20  E-value: 3.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  29 IGGLFIRNTDQEYTAFRLAIF-LHNTSPNASEAPFNLvpHVDNIETANSF-AVTNAfCSQYSRGVFAIFGLYDKRSVHTL 106
Cdd:cd06381    2 IGAIFSESALEDDEVFAVAVIdLNINEQILQTEKITL--SISFIDLNNHFdAVQEA-CDLMNQGILALVTSTGCASAIAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 107 TSFCSALHISLIT-------------PSFPTEGESQFVLQLRPSLR--GALLSLLDHYEWNCFVFLYDTDRGYSILQAIM 171
Cdd:cd06381   79 QSLTDAMHIPHLFiqrgyggsprtacGLNPSPRGQQYTLALRPPVRlnDVMLRLVTEWRWQKFVYFYDNDYDIRGLQEFL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 172 EKAGQNGWHVSAICVEN-----FNDVSYRQLLEELDRRQEKK--FVIDCEIERLQNILEQIVSVGKHVKGYHYIIAN--- 241
Cdd:cd06381  159 DQLSRQGIDVLLQKVDLniskmATALFTTMRCEELNRYRDTLrrALLLLSPNGAYTFIDASVETNLAIKDSHWFLINeei 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 242 LGFKDISLERFIHGGANVTGFQLVDFNT---------PMVTKLMDRWkkldqreyPGSETPPKYTSALTYDGVLVMAEtf 312
Cdd:cd06381  239 SDTEIDELVRYAHGRMTVIRQTFSKEKTnqrclrnnhRISSLLCDPK--------DGYLQMLEISNLYIYDSVLLLLE-- 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 313 rslrrqkidisrrgnagdclanpaapwgqgidmerTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGP-----RKV 387
Cdd:cd06381  309 -----------------------------------TIKKGPITGLTGKLEFNEGGDNSNVQFEILGTGYSETlgkdgRWL 353

                 ....
gi 164419751 388 GYWN 391
Cdd:cd06381  354 ATWN 357
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of the KA1 and KA2 ...
197-398 1.22e-06

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 I superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type II. 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: 107389  Cd Length: 333  Bit Score: 50.26  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 197 LLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLvdFNTP------ 270
Cdd:cd06394  178 LLKEIRDDKTATIIIDANASMSHTILLKASELGMTSAFYKYILTTMDFPLLRLDSIVDDRSNILGFSM--FNQShafyqe 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 271 MVTKLMDRWKK-LDQREYPGsetpPKYTSALTYDGVLVMaetfrslrrqkidisrrgnagdclanpaapwgqgidmertl 349
Cdd:cd06394  256 FIRSLNQSWREnCDHSPYTG----PALSSALLFDAVYAV----------------------------------------- 290
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 164419751 350 kqvriqGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVL 398
Cdd:cd06394  291 ------GLTGRIEFNSKGQRSNYTLKILQKTRSGFRQIGQWHSNETLSM 333
LivK COG0683
ABC-type branched-chain amino acid transport systems, periplasmic component [Amino acid ...
69-389 2.93e-06

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


Pssm-ID: 223755  Cd Length: 366  Bit Score: 48.97  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  69 DNIETANSFAVTNAFCSQysRGVFAIFGLYDKRSVHTLTSFCSALHISLITPS-----FPTEGESQFVLQLRPSLR--GA 141
Cdd:COG0683   59 DASDPATAAAVARKLITQ--DGVDAVVGPTTSGVALAASPVAEEAGVPLISPSatapqLTGRGLKPNVFRTGPTDNqqAA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 142 LLS--LLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAICVENFNDVSYRQLLEELdRRQEKKFVI-DCEIER 217
Cdd:COG0683  137 AAAdyLVKKGGKKRVAIIGdDYAYGEGLADAFKAALKALGGEVVVEEVYAPGDTDFSALVAKI-KAAGPDAVLvGGYGPD 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 218 LQNILEQIVSVGkhVKGYHYIIAnlGFKDISLERFIHGGANVTGFQLVDFNTPMVT----KLMDRWKKLDqreypGSETP 293
Cdd:COG0683  216 AALFLRQAREQG--LKAKLIGGD--GAGTAEFEEIAGAGGAGAGLLATAYSTPDDSpankKFVEAYKAKY-----GDPAA 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 294 PKYTSALTYDGVLVMAETfrslrrqkidISRRGNAGDCLANPAApwgqgidmertLKQVRI-QGLTGNVQFDHYGRRVNY 372
Cdd:COG0683  287 PSYFAAAAYDAVKLLAKA----------IEKAGKSSDREAVAEA-----------LKGGKFfDTAGGPVTFDEKGDRGSK 345
                        330
                 ....*....|....*..
gi 164419751 373 TMDVFELKSTGPRKVGY 389
Cdd:COG0683  346 PVYVGQVQKGGDGKFVY 362
PBP1_GPCR_family_C_like cd06350
Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
29-281 2.69e-05

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 recep; 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 devided 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: 153138  Cd Length: 348  Bit Score: 45.82  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  29 IGGLFIRNTDQE-------------YTAFRLAIFLHNTSPNASEAPFN--LVPHV----DNIETA---------NSFAVT 80
Cdd:cd06350    2 IGGLFPLHSGSEsvslkcgrfgkkgLQAAEAMLFAVEEINNDPDLLPNitLGYHIydscCSPAVAlraaldlllSGEGTT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  81 NAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLIT-----PSFPTEGESQFVLQLRPS---LRGALLSLLDHYEWN 152
Cdd:cd06350   82 PPYSCRKQPKVVAVIGPGSSSVSMAVAELLGLFKIPQISygatsPLLSDKLQFPSFFRTVPSdtsQALAIVALLKHFGWT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 153 CFVFLY-DTDRGYSILQAIMEKAGQNGwhvsaICVE-------NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQ 224
Cdd:cd06350  162 WVGLVYsDDDYGRSGLSDLEEELEKNG-----ICIAfveaippSSTEEDIKRILKKLKSSTARVIVVFGDEDDALRLFCE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164419751 225 IVSVGkhVKGYhYIIANLGF-----KDISLERFIHGganVTGFQLVDFNTPMVTKLMDRWKK 281
Cdd:cd06350  237 AYKLG--MTGK-YWIISTDWdtstcLLLFTLDAFQG---VLGFSGHAPRSGEIPGFKDFLRK 292
PBP1_Speract_GC_like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
141-224 6.57e-03

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


Pssm-ID: 107365  Cd Length: 404  Bit Score: 38.47  E-value: 6.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 141 ALLSLLDHYEWNCFVFLYDTDRGY-SILQAIMEKAGQNGWHVSAICVENFNDVSyrqlleeldrrqekkfvIDCEIERLQ 219
Cdd:cd06370  126 SVIALLKHFNWNKFSVVYENDSKYsSVFETLKEEAELRNITISHVEYYADFYPP-----------------DPIMDNPFE 188

                 ....*
gi 164419751 220 NILEQ 224
Cdd:cd06370  189 DIIQR 193
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
546-825 8.84e-131

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


Pssm-ID: 249551 [Multi-domain]  Cd Length: 268  Bit Score: 395.87  E-value: 8.84e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  546 EIWMCIVFAYIGVSVVLFLVSRFSPYEWHteepedgkegPSDQPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGG 625
Cdd:pfam00060   1 EVWLCILAAYLIVGVVLFLVERFSPYEWR----------GPPEEPNQFTLSNSLWFSFGALVQQGHRELPRSLSGRIVVG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  626 VWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFT 705
Cdd:pfam00060  71 VWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQNKIGYGTLRGGSTFEFFTESKNPTYRRMWEYMISFKGEVNV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  706 RTTAEGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLK 785
Cdd:pfam00060 151 ESYEEGVQRVRKGNGLYAFLMESAYLEYEVSRDPCKLTTVGEVFATKGYGIAFPKGSPLRDKLSRAILELRESGELQKLE 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 164419751  786 NKWWYDKGECGPKDsgSKDKTSALSLSNVAGVFYILVGGL 825
Cdd:pfam00060 231 NKWWKKKGECSLKS--TAVSSSQLGLESFAGLFLILGIGL 268
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
39-380 1.50e-69

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: 250359 [Multi-domain]  Cd Length: 344  Bit Score: 235.45  E-value: 1.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   39 QEYTAFRLAIFLHNTSPNASEaPFNLVPHVDNIETaNSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTSFCSALHISLI 118
Cdd:pfam01094   1 QVLPAMRLAIEDINADPGLLP-GITLGYEDDDTCD-DSAAGAAADCLLKSKGVVAVIGPSCSSVAIAVARLAGAFGIPMI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  119 TPSFPTEGESQ-----FVLQLRPSLR---GALLSLLDHYEWNCFVFLYDTD----RGYSILQAIMEKAGQNGWHVSAicV 186
Cdd:pfam01094  79 SYGATSPELSDktrypTFARTVPSDSkqaRAIADILKHFGWKRVAVIYDDDdygeGGLEALEDALREAGLNVVAVAS--E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  187 ENFNDVSYRQLLEELDRRQEKK--FVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFK--DISLERFIHGGANVTGF 262
Cdd:pfam01094 157 VIASDDDFTALLKELKDIKSKArvIVVCGSPDDLRQILRQARELGLMSGGYVWILTDLWSDslLIDDDKAREAMKGVLGF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  263 QLVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGnagdclanpaaPWGQG 342
Cdd:pfam01094 237 TLKPPDSPGFQEFLRRLKKLAARETPASDTEPNGYALLAYDAVYLLAHALNEALRDDPDITAGG-----------KWVDG 305
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 164419751  343 IDMERTLKQVRIQGLTGNVQFDH-YGRRVNYTMDVFELK 380
Cdd:pfam01094 306 SQLLEYLRNVNFEGLTGPVQFDDnGGRRPDYSLEILNWD 344
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3;
435-528 1.58e-15

Bacterial extracellular solute-binding proteins, family 3;


Pssm-ID: 249906 [Multi-domain]  Cd Length: 220  Bit Score: 76.16  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  435 EMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFS 514
Cdd:pfam00497  13 EYVDENGKLVGFDVDLAKAIAKRLGVKVEFVPVS-------------WDGLIPALQSGKIDVIIAGMTITPERKKQVDFS 79
                          90
                  ....*....|....
gi 164419751  515 KPFMSLGISIMIKK 528
Cdd:pfam00497  80 DPYYTSGQVLVVRK 93
HisJ COG0834
ABC-type amino acid transport/signal transduction systems, periplasmic component/domain [Amino ...
396-541 8.13e-11

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


Pssm-ID: 223904 [Multi-domain]  Cd Length: 275  Bit Score: 62.33  E-value: 8.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 396 LVLIQDAPTLGNDTAAIENRTVVVTTIMESPYVMYKKnhemfEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGkygar 475
Cdd:COG0834   16 LLLAACAAADLLDKIKARGKLRVGTEATYAPPFEFLD-----AKGGKLVGFDVDLAKAIAKRLGGDKKVEFVPVA----- 85
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164419751 476 dadtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKpqKSKPGVFSFLD 541
Cdd:COG0834   86 ------WDGLIPALKAGKVDIIIAGMTITPERKKKVDFSDPYYYSGQVLLVKK--DSDIGIKSLED 143
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
435-528 1.82e-10

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 60.42  E-value: 1.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751   435 EMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFS 514
Cdd:smart00062  14 SFADEDGELTGFDVDLAKAIAKELGLKVEFVEVS-------------FDSLLTALKSGKIDVVAAGMTITPERAKQVDFS 80
                           90
                   ....*....|....
gi 164419751   515 KPFMSLGISIMIKK 528
Cdd:smart00062  81 DPYYRSGQVILVRK 94
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
437-527 7.95e-09

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 55.91  E-value: 7.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 437 FEGNDKYEGYCVDLASEIAKHIGIKYKIaivpdgkygaRDADtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKP 516
Cdd:PRK09495  40 FKQGDKYVGFDIDLWAAIAKELKLDYTL----------KPMD---FSGIIPALQTKNVDLALAGITITDERKKAIDFSDG 106
                         90
                 ....*....|.
gi 164419751 517 FMSLGISIMIK 527
Cdd:PRK09495 107 YYKSGLLVMVK 117
PRK11260 PRK11260
cystine transporter subunit; Provisional
437-549 9.55e-09

cystine transporter subunit; Provisional


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 55.88  E-value: 9.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 437 FEGND-KYEGYCVDLASEIAKHIGIKYKIAIVPdgkygardadtkiWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSK 515
Cdd:PRK11260  56 FQGEDgKLTGFEVEFAEALAKHLGVKASLKPTK-------------WDGMLASLDSKRIDVVINQVTISDERKKKYDFST 122
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 164419751 516 PFMSLGISIMIKkpqKSKPGVFSFLDPLA-----------YEIWM 549
Cdd:PRK11260 123 PYTVSGIQALVK---KGNEGTIKTAADLKgkkvgvglgtnYEQWL 164
3A0103s03R TIGR01096
lysine-arginine-ornithine-binding periplasmic protein; [Transport and binding proteins, Amino ...
439-528 1.14e-05

lysine-arginine-ornithine-binding periplasmic protein; [Transport and binding proteins, Amino acids, peptides and amines].


Pssm-ID: 233269 [Multi-domain]  Cd Length: 250  Bit Score: 46.58  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751  439 GNDKYEGYCVDLASEIAKHIGIKYKiaivpdgkYGARDADTKIWNgmvgeLVYGKAEIAIAPLTITLVREEVIDFSKPFM 518
Cdd:TIGR01096  42 ANGKLVGFDVDLAKALCKRMKAKCK--------FVEQNFDGLIPS-----LKAKKVDAIMATMSITPKRQKQIDFSDPYY 108
                          90
                  ....*....|
gi 164419751  519 SLGISIMIKK 528
Cdd:TIGR01096 109 ATGQGFVVKK 118
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
745-789 1.03e-03

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 40.50  E-value: 1.03e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 164419751 745 VGGNLDSKGYGVATPKGSSLGTPVNLAVLKLSEAGVLDKLKNKWW 789
Cdd:PRK09495 198 VGDSLEAQQYGIAFPKGSELREKVNGALKTLKENGTYAEIYKKWF 242
PRK10859 PRK10859
membrane-bound lytic transglycosylase F; Provisional
410-519 1.11e-03

membrane-bound lytic transglycosylase F; Provisional


Pssm-ID: 236778 [Multi-domain]  Cd Length: 482  Bit Score: 41.01  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419751 410 AAIENRTV-VVTTImESPyvmykknHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDgkygardadtkiWNGMVGE 488
Cdd:PRK10859  37 EQIQERGElRVGTI-NSP-------LTYYIGNDGPTGFEYELAKRFADYLGVKLEIKVRDN------------ISQLFDA 96
                         90       100       110
                 ....*....|....*....|....*....|.
gi 164419751 489 LVYGKAEIAIAPLTITLVREEVIDFSKPFMS 519
Cdd:PRK10859  97 LDKGKADLAAAGLTYTPERLKQFRFGPPYYS 127
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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