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Conserved domains on  [gi|164419765|ref|NP_001106656|]
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glutamate receptor 4 isoform 3 precursor [Rattus norvegicus]

Protein Classification

type 1 periplasmic-binding domain-containing protein; ABC transporter substrate-binding protein( domain architecture ID 10157277)

type 1 periplasmic-binding domain-containing protein such as the ligand binding domains of the LacI family of transcriptional regulators, the ABC transporter substrate-binding proteins, the family C GPCRs, membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal LIVBP-like domains of the ionotropic glutamate receptors (iGluRs); contains the Venus flytrap-like domain which undergoes transition from an open to a closed conformational state upon ligand binding; ABC transporter substrate-binding protein functions as the initial receptor in the transport of substrates like aromatic compounds, similar to Rhodopseudomonas palustris Rpa0668 which preferentially binds lignin-derived benzoate derivative compounds

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: 787.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388    1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388   81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388  161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 268 NTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388  241 NTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419765 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: 787.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388    1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388   81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388  161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 268 NTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388  241 NTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419765 348 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 400
Cdd:cd06388  321 TLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLVLIQ 373
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 39-382 7.42e-62

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


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 203.77  E-value: 7.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765   39 QEYTAFRLAIFLHNTSPNASeAPFNLVPHVdnIETANSFAVTNAFCSQYSRG-VFAIFGLYDKRSVHTLTSFCSALHISL 117
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLL-PGTKLEYII--LDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  118 ITPSFPTEGES-----QFVLQLRPS---LRGALLSLLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAICV-- 186
Cdd:pfam01094  78 ISYGSTSPALSdlnryPTFLRTTPSdtsQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVip 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  187 -ENFNDVSYRQLLEELDRRqEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYI-----IANLGFKDISLERFIhggANVT 260
Cdd:pfam01094 158 pAQDDDEIARKLLKEVKSR-ARVIVVCCSSETARRLLKAARELGMMGEGYVWIatdglTTSLVILNPSTLEAA---GGVL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  261 GFQLVDFNTPMVTKLMdRWKKLDQREYP--GSETPPKYtSALTYDGVLVMAETFRSLRRQKIDISRRGNAGdclanpaaP 338
Cdd:pfam01094 234 GFRLHPPDSPEFSEFF-WEKLSDEKELYenLGGLPVSY-GALAYDAVYLLAHALHNLLRDDKPGRACGALG--------P 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 164419765  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: 787.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06388    1 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06388   81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06388  161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 268 NTPMVTKLMDRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 347
Cdd:cd06388  241 NTPMVTKLMQRWKKLDQREYPGSETPPKYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDMER 320

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419765 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: 586.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06387    2 IGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 109 FCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVEN 188
Cdd:cd06387   82 FCGALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 189 FNDV-SYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06387  162 IKDVqEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNN 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 268 NTPMVTKLMDRWKKLDQREYPGSETPP-KYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 346
Cdd:cd06387  242 ENPMVQQFLQRWVRLDEREFPEAKNAPlKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIE 321

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 164419765 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: 529.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPnaseapFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06389    1 QIGGLFPRGADQEYSAFRVGMVQFSTSE------FRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTIT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06389   75 SFCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 188 NFN----DVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQ 263
Cdd:cd06389  155 NINndkkDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 264 LVDFNTPMVTKLMDRWKKLDQREYPGSETPP-KYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQG 342
Cdd:cd06389  235 IVDYDDSLVSKFIERWSTLEEKEYPGAHTTTiKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQG 314

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164419765 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: 514.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNaseapfnLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06390    1 QIGGLFPNQQSQEHAAFRFALSQLTEPPK-------LLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAICVE 187
Cdd:cd06390   74 SFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNIL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 188 NFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDF 267
Cdd:cd06390  154 TTTEEGYRMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVTGFQLVNY 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 268 NTPMVTKLMDRWKKLDQREYPGSE-TPPKYTSALTYDGVLVMAETFRSLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 346
Cdd:cd06390  234 TDTIPARIMQQWKNSDSRDLPRVDwKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQ 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164419765 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 7.98e-166

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: 471.38  E-value: 7.98e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIEtANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06380    1 PIGAIFDSGEDQVQTAFRYAIDRHNSNNNNRFRLFPLTERIDITN-ADSFSVSRAICSQLSRGVFAIFGSSDASSLNTIQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLITPSFP---TEGESQFVLQLRPSLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNG-WHVSA 183
Cdd:cd06380   80 SYSDTFHMPYITPSFPknePSDSNPFELSLRPSYIEAIVDLIRHYGWKKVVYLYDSDEGLLRLQQLYDYLKEKSnISVRV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 184 ICVENFNDV-SYRQLLEELDRRQE-KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTG 261
Cdd:cd06380  160 RRVRNVNDAyEFLRTLRELDREKEdKRIVLDLSSERYQKILEQIVEDGMNRRNYHYLLANLDFLDLDLERFLHGGVNITG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 262 FQLVDFNTPMVTKLMDRWKKLDQREYPG-SETPPKYTSALTYDGVLVMAETFRSLRRQKIDI----------SRRGNAGD 330
Cdd:cd06380  240 FQLVDTNNKTVKDFLQRWKKLDPREYPGaGTDTIPYEAALAVDAVLVIAEAFQSLLRQNDDIfrftfhgelyNNGSKGID 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164419765 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 9.19e-92

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: 281.16  E-value: 9.19e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNaSEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06351    2 IGFIFEVNNEPAAKAFEVAVTYLKKNIN-TRYGLSVQYDSIEANKSNAFVLLEAICNKYATGTPALILDTTKSSINSLTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 109 FCSALHISLITPSFPTEGE--------SQFVLQLRP--SLRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNG 178
Cdd:cd06351   81 ALGAPHISASYGQQGDLRQwrdldeakQKYLLQVRPpeALRSIVLHLNITNAWIKFVDSYDMEHYKSLLQNIQTRAVQNN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 179 WHVSAICVEN--------FNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLE 250
Cdd:cd06351  161 VIVAIAKVGKrereeqldINNFFILGTLQSIRMVLEVRPAYFERNFAWHAITQNEVEISSQSDNAHIMFMNPMAYDILLE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 251 RFIHGGANVTGFQLVDFNTPMVTKLMDRWKKLDQREYP-GSETPPKYTSALTYDGVLVMAETFRSlrrqkidisrrgnag 329
Cdd:cd06351  241 TVYRDRLGLTRTTYNLNENPMVQQFIQRWVRLDEREFPeAKNAELQLSSAFYFDLALRSALAFKE--------------- 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164419765 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 4.76e-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: 224.79  E-value: 4.76e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  29 IGGLFIRNTDQEYTAFRLAIFLHNTSPNAseAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 108
Cdd:cd06382    2 IGGIFDEDDEDLEIAFKYAVDRINRERTL--PNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSDIVQS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 109 FCSALHISLI--TPSFPTEGESQFVLQLRPS---LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSA 183
Cdd:cd06382   80 ICDALEIPHIetRWDPKESNRDTFTINLYPDpdaLSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPKDIPITV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 184 ICVENFNDvsYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQ 263
Cdd:cd06382  160 RQLDPGDD--YRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANITGFR 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 264 LVDFNTPMVTKLMDRWKKLDQREYPGSETPPKYT--SALTYDGVLVMAETFRslrrqkidisrrgnagdclanpaapwgq 341
Cdd:cd06382  238 LVDPENPEVKNVLKDWSKREKEGFNKDIGPGQITteTALMYDAVNLFANALK---------------------------- 289

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 164419765 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 1.22e-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: 223.78  E-value: 1.22e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  29 IGGLF-IRNTDQEYTAFRLAIFLHNTSPNaSEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06368    2 IGAIFnEVNDAHERAAFRYAVERLNTNIV-KLAYFRITYSIEAIDSNSHFDATDKACDLLEKGVVAIVGPSSSDSNNALQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLITPSFPTEGE-SQFVLQLRPS--LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIMEKAGQNGWHVSAI 184
Cdd:cd06368   81 SICDALDVPHITVHDDPRLSkSQYSLSLYPRnqLSQAVSDLLKYWRWKRFVLVYDDDDRLRRLQELLEAARFSKRFVSVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 185 CVENFNDVS-YRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDIS-LERFIHGGANVTGF 262
Cdd:cd06368  161 KVDLDYKTLdETPLLKRKDCSLFSRILIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDLSLLLdLELFRYNHANITGF 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 263 QLVDFNtPMVTKLMDRWKKLDQREYPGSETP-----PKYTSALTYDGVLVMAETFRSlrrqkidisrrgnagdclanpaa 337
Cdd:cd06368  241 QLVDNN-SMYKEDINRLAFNWSRFRQHIKIEsnlrgPPYEAALMFDAVLLLADAFRR----------------------- 296

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 164419765 338 pwgqgidmertlkqvriqglTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWN 391
Cdd:cd06368  297 --------------------TGDLRFNGTGLRSNFTLRILELGYGGLRKIGFWD 330
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
 39-382 7.42e-62

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


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 203.77  E-value: 7.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765   39 QEYTAFRLAIFLHNTSPNASeAPFNLVPHVdnIETANSFAVTNAFCSQYSRG-VFAIFGLYDKRSVHTLTSFCSALHISL 117
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLL-PGTKLEYII--LDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  118 ITPSFPTEGES-----QFVLQLRPS---LRGALLSLLDHYEWNCFVFLY-DTDRGYSILQAIMEKAGQNGWHVSAICV-- 186
Cdd:pfam01094  78 ISYGSTSPALSdlnryPTFLRTTPSdtsQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVip 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  187 -ENFNDVSYRQLLEELDRRqEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYI-----IANLGFKDISLERFIhggANVT 260
Cdd:pfam01094 158 pAQDDDEIARKLLKEVKSR-ARVIVVCCSSETARRLLKAARELGMMGEGYVWIatdglTTSLVILNPSTLEAA---GGVL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  261 GFQLVDFNTPMVTKLMdRWKKLDQREYP--GSETPPKYtSALTYDGVLVMAETFRSLRRQKIDISRRGNAGdclanpaaP 338
Cdd:pfam01094 234 GFRLHPPDSPEFSEFF-WEKLSDEKELYenLGGLPVSY-GALAYDAVYLLAHALHNLLRDDKPGRACGALG--------P 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 164419765  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 1.65e-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: 80.85  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPfNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06391    1 HIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTE-KITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLI--------TP--SFPTEGESQ---FVLQLRPS--LRGALLSLLDHYEWNCFVFLYDTDRGYSILQAIME 172
Cdd:cd06391   80 SLADAMHIPHLfiqrstagTPrsGCGLTRSNRnddYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 173 KAGQNGWHVSAICVE-NFNDV---SYRQL-LEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFK 245
Cdd:cd06391  160 KVSQQGMDVALQKVEnNINKMittLFDTMrIEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEIN 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 246 DISLERFIHggANVTGFQLVDFNTPMVTKLMDRWKKLDQReYPGSETPPK--------YTSALTYDGVLVMAETF-RSLR 316
Cdd:cd06391  240 DVDVQELVR--RSIGRLTIIRQTFPVPQNISQRCFRGNHR-ISSSLCDPKdpfaqnmeISNLYIYDTVLLLANAFhKKLE 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 317 RQKIdisRRGNAGDCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVF-----ELKSTGPRKVGYWN 391
Cdd:cd06391  317 DRKW---HSMASLSCIRKNSKPWQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILgtnygEELGRGVRKLGCWN 393


                 ....*
gi 164419765 392 DMDKL 396
Cdd:cd06391  394 PVTGL 398
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
 197-390 8.35e-16

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: 78.41  E-value: 8.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 197 LLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFIHGGANVTGFQLVDFNTPM----V 272
Cdd:cd06394  180 LLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQSNILGFSMFNTSHPFylefV 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 273 TKLMDRWKK-LDQREYPGsetpPKYTSALTYDGVLVMAETFRSLRR-QKIDISRRGnagdclANPAAPWGQGIDMERTLK 350
Cdd:cd06394  260 RSLNMSWREnCDASTYPG----PALSSALMFDAVHVVVSAVRELNRsQEIGVKPLS------CTSAQIWQHGTSLMNYLR 329

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 164419765 351 QVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYW 390
Cdd:cd06394  330 MVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 369
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
 28-391 2.21e-15

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: 77.34  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  28 QIGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPfNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 107
Cdd:cd06381    1 HIGAIFEENAAKDDRVFQLAVSDLSLNDDILQSE-KITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 108 SFCSALHISLI--------TPSF-----PTEGESQFVLQLRPSLR--GALLSLLDHYEWNCFVFLYDTDRGYSILQAIME 172
Cdd:cd06381   80 SLTDAMHIPHLfvqrnpggSPRTachlnPSPDGEAYTLASRPPVRlnDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFLD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 173 KAGQNGWHVSAICVEN-----FNDVSYRQLLEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFK 245
Cdd:cd06381  160 QASRLGLDVSLQKVDKnishvFTSLFTTMKTEELNRYRDtlRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEIS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 246 DISLERFIHggaNVTGFQLVDFNTPMVTKLMDRWKKLDQReYPGSETPPK--------YTSALTYDGVLVMAETF-RSLR 316
Cdd:cd06381  240 DPEILDLVH---SALGRMTVVRQIFPSAKDNQKCFRNNHR-ISSLLCDPQegylqmlqISNLYLYDSVLMLANAFhRKLE 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 317 RQKIDISRRGNagdCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYGRRVNYTMDVF-----ELKSTGPRKVGYWN 391
Cdd:cd06381  316 DRKWHSMASLN---CIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDSSNPYVQFEILgttysETFGKDMRKLATWD 392
PBP1_iGluR_delta_1 cd06392
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 ...
 29-367 9.77e-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: 75.43  E-value: 9.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  29 IGGLFIRNTDQEYTAFRLAI--FLHNTSPNASEAPFNlvpHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTL 106
Cdd:cd06392    2 IGAIFEENAAKDDRVFQLAVsdLSLNDDILQSEKITY---SIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 107 TSFCSALHISLI--------TPSF-----PTEGESQFVLQLRPSLR--GALLSLLDHYEWNCFVFLYDTDRGYSILQAIM 171
Cdd:cd06392   79 QSLTDAMHIPHLfvqrnsggSPRTachlnPSPEGEEYTLAARPPVRlnDVMLKLVTELRWQKFIVFYDSEYDIRGLQSFL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 172 EKAGQNGWHVSAICVEN-----FNDVSYRQLLEELDRRQE--KKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGF 244
Cdd:cd06392  159 DQASRLGLDVSLQKVDRnisrvFTNLFTTMKTEELNRYRDtlRRAILLLSPRGAQSFINEAVETNLASKDSHWVFVNEEI 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 245 KDISLERFIHGGANvtgfqlvdfNTPMVTKLMDRWKKLDQR----EYPGSETP--PK--YTSALT------YDGVLVMAE 310
Cdd:cd06392  239 SDPEILELVHSALG---------RMTVIRQIFPLSKDNNQRcmrnNHRISSLLcdPQegYLQMLQvsnlylYDSVLMLAN 309

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164419765 311 TF-RSLRRQKIDISRRGNagdCLANPAAPWGQGIDMERTLKQVRIQGLTGNVQFDHYG 367
Cdd:cd06392  310 AFhRKLEDRKWHSMASLN---CIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDG 364
PBP1_GPCR_family_C-like cd06350
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ...
 23-238 1.49e-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: 43.82  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  23 FPSSVQIGGLfIRNTDqeytafrlaiflhNTSPNASEAPFNLVPHVDNIETANSFAVTNafcsqYSRGVFAIFGLYDKRS 102
Cdd:cd06350   46 LLPNVTLGYD-IRDTC-------------SSSSVALESSLEFLLDNGIKLLANSNGQNI-----GPPNIVAVIGAASSSV 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 103 VHTLTSFCSALHISLITPS-----------FPTegesqF-------VLQLRpslrgALLSLLDHYEWNCFVFLY-DTDRG 163
Cdd:cd06350  107 SIAVANLLGLFKIPQISYAstspelsdkirYPY-----FlrtvpsdTLQAK-----AIADLLKHFNWNYVSTVYsDDDYG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 164 YSILQAIMEKAGQNGwhvsaICV-------ENFNDVSYRQLLEELDRRQEKK-FVIDCEIERLQNILEQIVSVGkhVKGY 235
Cdd:cd06350  177 RSGIEAFEREAKERG-----ICIaqtivipENSTEDEIKRIIDKLKSSPNAKvVVLFLTESDARELLKEAKRRN--LTGF 249


                 ...
gi 164419765 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 4.07e-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: 42.40  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765  29 IGGLFIRNTDQEYTAFRLAIFLHntSPNASEAPFNLVPHVD---NIET--ANSFAVTNAFCS-QYSRGVFAIFGLYDKRS 102
Cdd:cd06269    2 IGALLPVHDYLESGAKVLPAFEL--ALSDVNSRPDLLPKTTlglAIRDseCNPTQALLSACDlLAAAKVVAILGPGCSAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 103 VHTLTSFCSALHISLIT-----PSFPTEGESQFVLQLRPS---LRGALLSLLDHYEWNCFVFLYDTDR-GYSILQAIMEK 173
Cdd:cd06269   80 AAPVANLARHWDIPVLSygataPGLSDKSRYAYFLRTVPPdskQADAMLALVRRLGWNKVVLIYSDDEyGEFGLEGLEEL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 174 AGQ-NGWHVSAICVENFNDVSYRQLLEELDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYI-----IANLGFKDI 247
Cdd:cd06269  160 FQEkGGLITSRQSFDENKDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFvidgeASSSDEHGD 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164419765 248 SLERFIHGG-------ANVTGFQlvDFNTPMVTKLMDRWKKLDQREYPGSEtppkytSALTYDGVLVMAET 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 4.40e-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: 4.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 164419765 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 5.17e-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: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164419765 279 WKKLDQREYPGSETPPKYtSALTYDGVLVMAETFRSLRrQKIDISRRGNAGDCLANPAapWGQGIdMErTLKQVRIQGLT 358
Cdd:cd06366  281 LKEYLERLSNSNYTGSPY-APFAYDAVWAIALALNKTI-EKLAEYNKTLEDFTYNDKE--MADLF-LE-AMNSTSFEGVS 354

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 164419765 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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