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Conserved domains on  [gi|1370459185|ref|XP_024304222|]
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glutamate receptor 4 isoform X6 [Homo sapiens]

Protein Classification

PBP1_iGluR_AMPA_GluR4 domain-containing protein( domain architecture ID 10157277)

PBP1_iGluR_AMPA_GluR4 domain-containing protein

Graphical summary

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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 ...
 28-400 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: 380611 [Multi-domain]  Cd Length: 373  Bit Score: 786.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388     1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388    81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388   161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 268 NTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388   241 NTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370459185 348 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 400
Cdd:cd06388   321 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 373
 
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 ...
 28-400 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: 380611 [Multi-domain]  Cd Length: 373  Bit Score: 786.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388     1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388    81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388   161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 268 NTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388   241 NTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370459185 348 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 400
Cdd:cd06388   321 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 373
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 39-382 4.77e-61

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 201.84  E-value: 4.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  39 QEYTAFRLAIFLHNTSPNASeAPFNLVPHVdnIETANSFAVTNAFCSQYSRG-VFAIFGLYDKRSVHTLTSFCSALHISL 117
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLL-PGTKLEYII--LDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 118 ITPSFPTEGES-----QFVLQLRPS---LRGALLSLLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAICV-- 186
Cdd:pfam01094  78 ISYGSTSPALSdlnryPTFLRTTPSdtsQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVip 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 187 -ENFNDVSYRQLLEELDRRqEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYI-----IANLGFKDISLERFIhggANVT 260
Cdd:pfam01094 158 pAQDDDEIARKLLKEVKSR-ARVIVVCCSSETARRLLKAARELGMMGEGYVWIatdglTTSLVILNPSTLEAA---GGVL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 261 GFQLVDFNTPMVIKLMdRWKKLDQREYP--GSETPPKYtSALTYDGVLVMAETFRSLRRQKIDISRRGNAGdclanpaaP 338
Cdd:pfam01094 234 GFRLHPPDSPEFSEFF-WEKLSDEKELYenLGGLPVSY-GALAYDAVYLLAHALHNLLRDDKPGRACGALG--------P 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1370459185 339 WGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKST 382
Cdd:pfam01094 304 WNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
 
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 ...
 28-400 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: 380611 [Multi-domain]  Cd Length: 373  Bit Score: 786.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388     1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388    81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388   161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 268 NTPMVIKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388   241 NTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370459185 348 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 400
Cdd:cd06388   321 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 373
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
 29-399 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: 380610 [Multi-domain]  Cd Length: 375  Bit Score: 585.45  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06387     2 IGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 109 FCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVEN 188
Cdd:cd06387    82 FCGALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 189 FNDV-SYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06387   162 IKDVqEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 268 NTPMVIKLMDRWKKLDQREYPGSETPP-KYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 346
Cdd:cd06387   242 ENPMVQQFLQRWVRLDEREFPEAKNAPlKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIE 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370459185 347 RTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLI 399
Cdd:cd06387   322 RALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEYERFVPF 374
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
 28-400 0e+00

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


Pssm-ID: 380612 [Multi-domain]  Cd Length: 372  Bit Score: 528.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPnaseapFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06389     1 QIGGLFPRGADQEYSAFRVGMVQFSTSE------FRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTIT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06389    75 SFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 188 NFN----DVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQ 263
Cdd:cd06389   155 NINndkkDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQ 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 264 LVDFNTPMVIKLMDRWKKLDQREYPGSETPP-KYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQG 342
Cdd:cd06389   235 IVDYDDSLVSKFIERWSTLEEKEYPGAHTTTiKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQG 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370459185 343 IDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 400
Cdd:cd06389   315 VEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMVVTL 372
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
 28-397 0e+00

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


Pssm-ID: 380613 [Multi-domain]  Cd Length: 367  Bit Score: 512.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNaseapfnLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06390     1 QIGGLFPNQQSQEHAAFRFALSQLTEPPK-------LLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06390    74 SFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNIL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06390   154 TTTEEGYRMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVTGFQLVNY 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 268 NTPMVIKLMDRWKKLDQREYPGSE-TPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 346
Cdd:cd06390   234 TDTIPARIMQQWKNSDSRDLPRVDwKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQ 313

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370459185 347 RTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLV 397
Cdd:cd06390   314 RALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKLV 364
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
 28-400 1.36e-164

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


Pssm-ID: 380603 [Multi-domain]  Cd Length: 390  Bit Score: 468.30  E-value: 1.36e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIEtANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06380     1 PIGAIFDSGEDQVQTAFRYAIDRHNSNNNNRFRLFPLTERIDITN-ADSFSVSRAICSQLSRGVFAIFGSSDASSLNTIQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLITPSFP---TEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNG-WHVSA 183
Cdd:cd06380    80 SYSDTFHMPYITPSFPknePSDSNPFELSLRPSYIEAIVDLIRHYGWKKVVYLYDSDEGLLRLQQLYDYLKEKSnISVRV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 184 ICVENFNDV-SYRQLLEELDRRQE-KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTG 261
Cdd:cd06380   160 RRVRNVNDAyEFLRTLRELDREKEdKRIVLDLSSERYQKILEQIVEDGMNRRNYHYLLANLDFLDLDLERFLHGGVNITG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 262 FQLVDFNTPMVIKLMDRWKKLDQREYPG-SETPPKYTSALTYDGVLVMAETFRSLRRQKIDI----------SRRGNAGD 330
Cdd:cd06380   240 FQLVDTNNKTVKDFLQRWKKLDPREYPGaGTDTIPYEAALAVDAVLVIAEAFQSLLRQNDDIfrftfhgelyNNGSKGID 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459185 331 CLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKST-GPRKVGYWNDMDKLVLIQ 400
Cdd:cd06380   320 CDPNPPLPWEHGKAIMKALKKVRFEGLTGNVQFDDFGQRKNYTLDVIELTSNrGLRKIGTWSEGDGFLLGE 390
PBP1_iGluR_N_LIVBP-like cd06351
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
 29-397 2.68e-91

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 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Glutamate mediates the majority of excitatory synaptic transmission in the central nervous system via two broad classes of ionotropic receptors characterized by their response to glutamate agonists: N-methyl-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: 380574  Cd Length: 348  Bit Score: 280.00  E-value: 2.68e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNaSEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06351     2 IGFIFEVNNEPAAKAFEVAVTYLKKNIN-TRYGLSVQYDSIEANKSNAFVLLEAICNKYATGTPALILDTTKSSINSLTS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 109 FCSALHISLITPSFPTEGE--------SQFVLQLRP--SLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNG 178
Cdd:cd06351    81 ALGAPHISASYGQQGDLRQwrdldeakQKYLLQVRPpeALRSIVLHLNITNAWIKFVDSYDMEHYKSLLQNIQTRAVQNN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 179 WHVSAICVEN--------FNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLE 250
Cdd:cd06351   161 VIVAIAKVGKrereeqldINNFFILGTLQSIRMVLEVRPAYFERNFAWHAITQNEVEISSQSDNAHIMFMNPMAYDILLE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 251 RFIHGGANVTGFQLVDFNTPMVIKLMDRWKKLDQREYP-GSETPPKYTSALTYDGVLVMAETFRSlrrqkidisrrgnag 329
Cdd:cd06351   241 TVYRDRLGLTRTTYNLNENPMVQQFIQRWVRLDEREFPeAKNAELQLSSAFYFDLALRSALAFKE--------------- 305

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370459185 330 dclanpaapwgqgidmertlkqvriqglTGNVQFDHYGRRVNYTMDVFELK-STGPRKVGYWNDMDKLV 397
Cdd:cd06351   306 ----------------------------TGYGTFDLQSTQPFNGHSFMKFEmDINVRKIRGWSEYESVN 346
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
 29-391 8.76e-70

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


Pssm-ID: 380605  Cd Length: 335  Bit Score: 224.02  E-value: 8.76e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNAseAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06382     2 IGGIFDEDDEDLEIAFKYAVDRINRERTL--PNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSDIVQS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 109 FCSALHISLI--TPSFPTEGESQFVLQLRPS---LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSA 183
Cdd:cd06382    80 ICDALEIPHIetRWDPKESNRDTFTINLYPDpdaLSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPKDIPITV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 184 ICVENFNDvsYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQ 263
Cdd:cd06382   160 RQLDPGDD--YRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANITGFR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 264 LVDFNTPMVIKLMDRWKKLDQREYPGSETPPKYT--SALTYDGVLVMAETFRslrrqkidisrrgnagdclanpaapwgq 341
Cdd:cd06382   238 LVDPENPEVKNVLKDWSKREKEGFNKDIGPGQITteTALMYDAVNLFANALK---------------------------- 289

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370459185 342 gidmertlkqvriQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWN 391
Cdd:cd06382   290 -------------EGLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGTWN 326
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
 29-391 2.08e-69

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


Pssm-ID: 380591 [Multi-domain]  Cd Length: 339  Bit Score: 223.40  E-value: 2.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  29 IGGLF-IRNTDQEYTAFRLAIFLHNTSPNaSEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06368     2 IGAIFnEVNDAHERAAFRYAVERLNTNIV-KLAYFRITYSIEAIDSNSHFDATDKACDLLEKGVVAIVGPSSSDSNNALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLITPSFPTEGE-SQFVLQLRPS--LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAI 184
Cdd:cd06368    81 SICDALDVPHITVHDDPRLSkSQYSLSLYPRnqLSQAVSDLLKYWRWKRFVLVYDDDDRLRRLQELLEAARFSKRFVSVR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 185 CVENFNDVS-YRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDIS-LERFIHGGANVTGF 262
Cdd:cd06368   161 KVDLDYKTLdETPLLKRKDCSLFSRILIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDLSLLLdLELFRYNHANITGF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 263 QLVDFNtPMVIKLMDRWKKLDQREYPGSETP-----PKYTSALTYDGVLVMAETFRSlrrqkidisrrgnagdclanpaa 337
Cdd:cd06368   241 QLVDNN-SMYKEDINRLAFNWSRFRQHIKIEsnlrgPPYEAALMFDAVLLLADAFRR----------------------- 296

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370459185 338 pwgqgidmertlkqvriqglTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWN 391
Cdd:cd06368   297 --------------------TGDLRFNGTGLRSNFTLRILELGYGGLRKIGFWD 330
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 39-382 4.77e-61

Receptor family ligand binding region; This family includes extracellular ligand binding domains of a wide range of receptors. This family also includes the bacterial amino acid binding proteins of known structure.


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 201.84  E-value: 4.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  39 QEYTAFRLAIFLHNTSPNASeAPFNLVPHVdnIETANSFAVTNAFCSQYSRG-VFAIFGLYDKRSVHTLTSFCSALHISL 117
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLL-PGTKLEYII--LDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 118 ITPSFPTEGES-----QFVLQLRPS---LRGALLSLLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAICV-- 186
Cdd:pfam01094  78 ISYGSTSPALSdlnryPTFLRTTPSdtsQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVip 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 187 -ENFNDVSYRQLLEELDRRqEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYI-----IANLGFKDISLERFIhggANVT 260
Cdd:pfam01094 158 pAQDDDEIARKLLKEVKSR-ARVIVVCCSSETARRLLKAARELGMMGEGYVWIatdglTTSLVILNPSTLEAA---GGVL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 261 GFQLVDFNTPMVIKLMdRWKKLDQREYP--GSETPPKYtSALTYDGVLVMAETFRSLRRQKIDISRRGNAGdclanpaaP 338
Cdd:pfam01094 234 GFRLHPPDSPEFSEFF-WEKLSDEKELYenLGGLPVSY-GALAYDAVYLLAHALHNLLRDDKPGRACGALG--------P 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1370459185 339 WGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKST 382
Cdd:pfam01094 304 WNGGQKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
 28-396 3.28e-16

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


Pssm-ID: 380614 [Multi-domain]  Cd Length: 402  Bit Score: 80.08  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPfNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06391     1 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTE-KITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLI--------TP--SFPTEGESQ---FVLQLRPS--LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIME 172
Cdd:cd06391    80 SLADAMHIPHLfiqrstagTPrsGCGLTRSNRnddYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 173 KAGQNGWHVSAICVE-NFNDV---SYRQL-LEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFK 245
Cdd:cd06391   160 KVSQQGMDVALQKVEnNINKMittLFDTMrIEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 246 DISLERFIHggANVTGFQLVDFNTPMVIKLMDRWKKLDQReYPGSETPPK--------YTSALTYDGVLVMAETF-RSLR 316
Cdd:cd06391   240 DVDVQELVR--RSIGRLTIIRQTFPVPQNISQRCFRGNHR-ISSSLCDPKdpfaqnmeISNLYIYDTVLLLANAFhKKLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 317 RQKIdisRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVF-----ELKSTGPRKVGYWN 391
Cdd:cd06391   317 DRKW---HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILgtnygEELGRGVRKLGCWN 393


                  ....*
gi 1370459185 392 DMDKL 396
Cdd:cd06391   394 PVTGL 398
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
 28-391 9.31e-16

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


Pssm-ID: 380604 [Multi-domain]  Cd Length: 401  Bit Score: 78.49  E-value: 9.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPfNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06381     1 HIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSE-KITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 108 SFCSALHISLI--------TPSF-----PTEGESQFVLQLRPSLR--GALLSLLDHYEWNCFVFLYDTDRGYSILQAIME 172
Cdd:cd06381    80 SLTDAMHIPHLfvqrnpggSPRTachlnPSPDGEAYTLASRPPVRlnDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFLD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 173 KAGQNGWHVSAICVEN-----FNDVSYRQLLEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFK 245
Cdd:cd06381   160 QASRLGLDVSLQKVDKnishvFTSLFTTMKTEELNRYRDtlRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEIS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 246 DISLERFIHGGanvtgfqlvdFNTPMVIKLMDRWKKLDQREYPGSE------TPPK--------YTSALTYDGVLVMAET 311
Cdd:cd06381   240 DPEILDLVHSA----------LGRMTVVRQIFPSAKDNQKCFRNNHrissllCDPQegylqmlqISNLYLYDSVLMLANA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 312 F-RSLRRQKIDISRRGNagdCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVF-----ELKSTGPR 385
Cdd:cd06381   310 FhRKLEDRKWHSMASLN---CIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDSSNPYVQFEILgttysETFGKDMR 386


                  ....*.
gi 1370459185 386 KVGYWN 391
Cdd:cd06381   387 KLATWD 392
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
 197-390 1.56e-15

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


Pssm-ID: 380616  Cd Length: 379  Bit Score: 77.64  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 197 LLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPMVIK-- 274
Cdd:cd06394   180 LLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQSNILGFSMFNTSHPFYLEfv 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 275 --LMDRWKK-LDQREYPGsetpPKYTSALTYDGVLVMAETFRSLRR-QKIDISRRGnagdclANPAAPWGQGIDMERTLK 350
Cdd:cd06394   260 rsLNMSWREnCDASTYPG----PALSSALMFDAVHVVVSAVRELNRsQEIGVKPLS------CTSAQIWQHGTSLMNYLR 329

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370459185 351 QVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYW 390
Cdd:cd06394   330 MVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 369
PBP1_iGluR_delta_1 cd06392
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 ...
 29-367 6.15e-15

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 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 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: 380615  Cd Length: 402  Bit Score: 76.20  E-value: 6.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  29 IGGLFIRNTDQEYTAFRLAI--FLHNTSPNASEAPFNlvpHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTL 106
Cdd:cd06392     2 IGAIFEENAAKDDRVFQLAVsdLSLNDDILQSEKITY---SIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 107 TSFCSALHISLI--------TPSF-----PTEGESQFVLQLRPSLR--GALLSLLDHYEWNCFVFLYDTDRGYSILQAIM 171
Cdd:cd06392    79 QSLTDAMHIPHLfvqrnsggSPRTachlnPSPEGEEYTLAARPPVRlnDVMLKLVTELRWQKFIVFYDSEYDIRGLQSFL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 172 EKAGQNGWHVSAICVEN-----FNDVSYRQLLEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGF 244
Cdd:cd06392   159 DQASRLGLDVSLQKVDRnisrvFTNLFTTMKTEELNRYRDtlRRAILLLSPRGAQSFINEAVETNLASKDSHWVFVNEEI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 245 KDISLERFIH---GGANVTG--FQLVDFNTPMVIKLMDRWKKL--DQREypGSETPPKYTSALTYDGVLVMAETF-RSLR 316
Cdd:cd06392   239 SDPEILELVHsalGRMTVIRqiFPLSKDNNQRCMRNNHRISSLlcDPQE--GYLQMLQVSNLYLYDSVLMLANAFhRKLE 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370459185 317 RQKIDISRRGNagdCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYG 367
Cdd:cd06392   317 DRKWHSMASLN---CIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDG 364
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
 23-238 2.05e-04

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


Pssm-ID: 380573  Cd Length: 350  Bit Score: 43.05  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  23 FPSSVQIGGLfIRNTDqeytafrlaiflhNTSPNASEAPFNLVPHVDNIETANSFAVTNafcsqYSRGVFAIFGLYDKRS 102
Cdd:cd06350    46 LLPNVTLGYD-IRDTC-------------SSSSVALESSLEFLLDNGIKLLANSNGQNI-----GPPNIVAVIGAASSSV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 103 VHTLTSFCSALHISLITPS-----------FPTegesqF-------VLQLRpslrgALLSLLDHYEWNCFVFLY-DTDRG 163
Cdd:cd06350   107 SIAVANLLGLFKIPQISYAstspelsdkirYPY-----FlrtvpsdTLQAK-----AIADLLKHFNWNYVSTVYsDDDYG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 164 YSILQAIMEKAGQNGwhvsaICV-------ENFNDVSYRQLLEELDRRQEKK-FVIDCEIERLQNILEQIVSVGkhVKGY 235
Cdd:cd06350   177 RSGIEAFEREAKERG-----ICIaqtivipENSTEDEIKRIIDKLKSSPNAKvVVLFLTESDARELLKEAKRRN--LTGF 249


                  ...
gi 1370459185 236 HYI 238
Cdd:cd06350   250 TWI 252
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
 29-311 4.69e-04

ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as natriuretic peptide receptors (NPRs), and N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of ionotropic glutamate rece; This CD represents the ligand-binding domain of the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic glutamate receptors, all of which are structurally similar and related to the periplasmic-binding fold type 1 family. The family C GPCRs consists of metabotropic glutamate receptor (mGluR), a calcium-sensing receptor (CaSR), gamma-aminobutyric acid receptor (GABAbR), the promiscuous L-alpha-amino acid receptor GPR6A, families of taste and pheromone receptors, and orphan receptors. Truncated splicing variants of the orphan receptors are not included in this CD. The family C GPCRs are activated by endogenous agonists such as amino acids, ions, and sugar based molecules. Their amino terminal ligand-binding region is homologous to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). The ionotropic glutamate receptors (iGluRs) have an integral ion channel and are subdivided into three major groups based on their pharmacology and structural similarities: NMDA receptors, AMPA receptors, and kainate receptors. The family of membrane bound guanylyl cyclases is further divided into three subfamilies: the ANP receptor (GC-A)/C-type natriuretic peptide receptor (GC-B), the heat-stable enterotoxin receptor (GC-C)/sensory organ specific membrane GCs such as retinal receptors (GC-E, GC-F), and olfactory receptors (GC-D and GC-G).


Pssm-ID: 380493 [Multi-domain]  Cd Length: 332  Bit Score: 42.02  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185  29 IGGLFIRNTDQEYTAFRLAIFLHntSPNASEAPFNLVPHVD---NIET--ANSFAVTNAFCS-QYSRGVFAIFGLYDKRS 102
Cdd:cd06269     2 IGALLPVHDYLESGAKVLPAFEL--ALSDVNSRPDLLPKTTlglAIRDseCNPTQALLSACDlLAAAKVVAILGPGCSAS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 103 VHTLTSFCSALHISLIT-----PSFPTEGESQFVLQLRPS---LRGALLSLLDHYEWNCFVFLYDTDR-GYSILQAIMEK 173
Cdd:cd06269    80 AAPVANLARHWDIPVLSygataPGLSDKSRYAYFLRTVPPdskQADAMLALVRRLGWNKVVLIYSDDEyGEFGLEGLEEL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 174 AGQ-NGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYI-----IANLGFKDI 247
Cdd:cd06269   160 FQEkGGLITSRQSFDENKDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFvidgeASSSDEHGD 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370459185 248 SLERFIHGG-------ANVTGFQlvDFNTPMVIKLMDRWKKLDQREYPGSEtppkytSALTYDGVLVMAET 311
Cdd:cd06269   240 EARQAAEGAitvtlifPVVKEFL--KFSMELKLKSSKRKQGLNEEYELNNF------AAFFYDAVLADRPG 302
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
 141-194 4.71e-03

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


Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 39.15  E-value: 4.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370459185 141 ALLSLLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAicVENFNDVSY 194
Cdd:cd06370   127 SVIALLKHFNWNKVSIVYeNETKWSKIADTIKELLELNNIEINH--EEYFPDPYP 179
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
 279-399 5.36e-03

ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA); Ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for gamma-aminobutyric acid (GABA). GABA is the major inhibitory neurotransmitter in the mammalian CNS and, like glutamate and other transmitters, acts via both ligand gated ion channels (GABAa receptors) and G-protein coupled receptors (GABAb receptor or GABAbR). GABAa receptors are members of the ionotropic receptor superfamily which includes alpha-adrenergic and glycine receptors. The GABAb receptor is a member of a receptor superfamily which includes the mGlu receptors. The GABAb receptor is coupled to G alpha-i proteins, and activation causes a decrease in calcium, an increase in potassium membrane conductance, and inhibition of cAMP formation. The response is thus inhibitory and leads to hyperpolarization and decreased neurotransmitter release, for example.


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 38.77  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370459185 279 WKKLDQREYPGSETPPKYtSALTYDGVLVMAETFRSLRrQKIDISRRGNAGDCLANPAapWGQGIdMErTLKQVRIQGLT 358
Cdd:cd06366   281 LKEYLERLSNSNYTGSPY-APFAYDAVWAIALALNKTI-EKLAEYNKTLEDFTYNDKE--MADLF-LE-AMNSTSFEGVS 354

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370459185 359 GNVQFDHYGRRVnYTMDVFELKSTGPRKVGYWN-DMDKLVLI 399
Cdd:cd06366   355 GPVSFDSKGDRL-GTVDIEQLQGGSYVKVGLYDpNADSLLLL 395
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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