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Conserved domains on  [gi|384381488|ref|NP_001244950|]
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glutamate receptor 1 isoform 5 [Homo sapiens]

Protein Classification

substrate-binding domain-containing protein; ABC transporter substrate-binding protein( domain architecture ID 10157284)

substrate-binding domain-containing protein similar to ionotropic glutamate receptor receptor (iGluR) subtypes, which contain the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain that is structurally homologous to the periplasmic-binding fold type 1 (PBP1), and the C-terminal ligand-binding domain that belongs to the PBP2 fold; 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_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
36-402 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: 820.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  36 EVWGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALH 115
Cdd:cd06390    1 QIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLTSFCGALH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 116 VCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGY 195
Cdd:cd06390   81 VCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 196 RMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAK 275
Cdd:cd06390  161 RMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVTGFQLVNYTDTIPAR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 276 IMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVR 355
Cdd:cd06390  241 IMQQWKNSDSRDLPRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVR 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 384381488 356 FEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAA 402
Cdd:cd06390  321 FEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKLVPAA 367
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
416-797 0e+00

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


:

Pssm-ID: 270447 [Multi-domain]  Cd Length: 260  Bit Score: 539.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13729    1 NRTYIVTTILESPYVMLKKNHEQFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETKMWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13729   81 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvS 655
Cdd:cd13729  118 -------------------------------------------------------------------------------S 118
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEY 735
Cdd:cd13729  119 PIESAEDLAKQTEIAYGTLDAGSTKEFFRRSKIAVFEKMWSYMKSADPSVFVKTTDEGVMRVRKSKGKYAYLLESTMNEY 198
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381488 736 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 797
Cdd:cd13729  199 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 260
 
Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
36-402 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: 820.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  36 EVWGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALH 115
Cdd:cd06390    1 QIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLTSFCGALH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 116 VCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGY 195
Cdd:cd06390   81 VCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 196 RMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAK 275
Cdd:cd06390  161 RMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVTGFQLVNYTDTIPAR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 276 IMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVR 355
Cdd:cd06390  241 IMQQWKNSDSRDLPRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVR 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 384381488 356 FEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAA 402
Cdd:cd06390  321 FEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKLVPAA 367
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
416-797 0e+00

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


Pssm-ID: 270447 [Multi-domain]  Cd Length: 260  Bit Score: 539.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13729    1 NRTYIVTTILESPYVMLKKNHEQFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETKMWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13729   81 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvS 655
Cdd:cd13729  118 -------------------------------------------------------------------------------S 118
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEY 735
Cdd:cd13729  119 PIESAEDLAKQTEIAYGTLDAGSTKEFFRRSKIAVFEKMWSYMKSADPSVFVKTTDEGVMRVRKSKGKYAYLLESTMNEY 198
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381488 736 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 797
Cdd:cd13729  199 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 260
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
548-826 1.28e-122

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


Pssm-ID: 459656 [Multi-domain]  Cd Length: 267  Bit Score: 372.41  E-value: 1.28e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  548 EIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEgrdqttsdqSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGG 627
Cdd:pfam00060   3 EVWLGILVAFLIVGVVLFLLERFSPYEWRGPLETE---------ENRFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  628 VWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFV 707
Cdd:pfam00060  74 VWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  708 RTTEEGMIRVRKSKGKYAYLLEstmNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLK 787
Cdd:pfam00060 154 ALNEEGVALVRNGIYAYALLSE---NYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLE 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 384381488  788 NKWWYDKGECGSggGDSKDKTSALSLSNVAGVFYILIGG 826
Cdd:pfam00060 231 KKWWPKSGECDS--KSSASSSSQLGLKSFAGLFLILGIG 267
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
47-384 2.32e-69

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


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 234.20  E-value: 2.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488   47 QEHAAFRFALSQLTEPPKLLPQID----IVNISDSFEMTYRFCSQFSKG-VYAIFGFYERRTVNMLTSFCGALHVCFITP 121
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPGTKleyiILDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPLISY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  122 SFPVDT-----SNQFVLQLRPE---LQDALISIIDHYKWQKFVYIY-DADRGLSVLQKVLDTAAEKNWQVTAVNIL---T 189
Cdd:pfam01094  81 GSTSPAlsdlnRYPTFLRTTPSdtsQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVIppaQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  190 TTEEGYRMLFQDLeKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILAN--LGFMDIDLNKFKESGANVTGFQLVN 267
Cdd:pfam01094 161 DDDEIARKLLKEV-KSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDglTTSLVILNPSTLEAAGGVLGFRLHP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  268 YTDTIPAKIMQqWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGdclanpavPWGQGIDI 347
Cdd:pfam01094 240 PDSPEFSEFFW-EKLSDEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRACGALG--------PWNGGQKL 310
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 384381488  348 QRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHD 384
Cdd:pfam01094 311 LRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
656-793 1.38e-51

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


Pssm-ID: 197504 [Multi-domain]  Cd Length: 133  Bit Score: 176.71  E-value: 1.38e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488   656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSaePSVFVRTTEEGMIRVRKSKgkYAYLLESTMNEY 735
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKS--PEVFVKSYAEGVQRVRVSN--YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 384381488   736 IEQRkPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYD 793
Cdd:smart00079  77 ELSR-NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
440-530 8.66e-14

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 71.55  E-value: 8.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 440 EGNDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPF 519
Cdd:COG0834   16 DEDGKLVGFDVDLARAIAKRLGLKVEFVPVP-------------WDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPY 82
                         90
                 ....*....|.
gi 384381488 520 MSLGISIMIKK 530
Cdd:COG0834   83 YTSGQVLLVRK 93
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
438-529 1.06e-07

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 53.98  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 438 QFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSK 517
Cdd:PRK09495  39 EFKQGDKYVGFDIDLWAAIAKELKLDYTLKPMD-------------FSGIIPALQTKNVDLALAGITITDERKKAIDFSD 105
                         90
                 ....*....|..
gi 384381488 518 PFMSLGISIMIK 529
Cdd:PRK09495 106 GYYKSGLLVMVK 117
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
250-385 3.37e-04

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


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 43.77  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 250 LNKFKESGANVTGFQLvNYTDTIPakIMQQWKNSDARDHTRVDW---------KRPKYTSALTYDGVKVMAEAfqsLRRq 320
Cdd:COG0683  189 LTKIKAAGPDAVFLAG-YGGDAAL--FIKQAREAGLKGPLNKAFvkaykakygREPSSYAAAGYDAALLLAEA---IEK- 261
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384381488 321 ridisrrgnAGDclANPAvpwgqgiDIQRALQQVRFEGLTGNVQFNEKGRRTNyTLHVIEMKHDG 385
Cdd:COG0683  262 ---------AGS--TDRE-------AVRDALEGLKFDGVTGPITFDPDGQGVQ-PVYIVQVKADG 307
 
Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
36-402 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: 820.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  36 EVWGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALH 115
Cdd:cd06390    1 QIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLTSFCGALH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 116 VCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGY 195
Cdd:cd06390   81 VCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 196 RMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAK 275
Cdd:cd06390  161 RMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVTGFQLVNYTDTIPAR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 276 IMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVR 355
Cdd:cd06390  241 IMQQWKNSDSRDLPRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVR 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 384381488 356 FEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVPAA 402
Cdd:cd06390  321 FEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKLVPAA 367
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
416-797 0e+00

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


Pssm-ID: 270447 [Multi-domain]  Cd Length: 260  Bit Score: 539.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13729    1 NRTYIVTTILESPYVMLKKNHEQFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETKMWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13729   81 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvS 655
Cdd:cd13729  118 -------------------------------------------------------------------------------S 118
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEY 735
Cdd:cd13729  119 PIESAEDLAKQTEIAYGTLDAGSTKEFFRRSKIAVFEKMWSYMKSADPSVFVKTTDEGVMRVRKSKGKYAYLLESTMNEY 198
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381488 736 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 797
Cdd:cd13729  199 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 260
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
416-797 1.87e-177

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


Pssm-ID: 270433 [Multi-domain]  Cd Length: 261  Bit Score: 513.44  E-value: 1.87e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNA--NQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVY 493
Cdd:cd13715    1 NRTYIVTTILEEPYVMMKKNHegEPLEGNERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARDADTGIWNGMVGELVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 494 GRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspy 573
Cdd:cd13715   81 GEADIAIAPLTITLVRERVIDFSKPFMSLGISIMIKKPV----------------------------------------- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 574 ewhseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 653
Cdd:cd13715      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 654 vsPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMN 733
Cdd:cd13715  120 --PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYDKMWEYMNSAEPSVFVRTTDEGIARVRKSKGKYAYLLESTMN 197
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384381488 734 EYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 797
Cdd:cd13715  198 EYINQRKPCDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC 261
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
36-399 2.64e-165

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: 486.83  E-value: 2.64e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  36 EVWGLFPNQQSQEHAAFRFALSQL-TEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGAL 114
Cdd:cd06389    1 QIGGLFPRGADQEYSAFRVGMVQFsTSEFRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITSFCGTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 115 HVCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTT--- 191
Cdd:cd06389   81 HVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGNINndk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 192 -EEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTD 270
Cdd:cd06389  161 kDETYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQIVDYDD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 271 TIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRA 350
Cdd:cd06389  241 SLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGVEIERA 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 384381488 351 LQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFV 399
Cdd:cd06389  321 LKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMV 369
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
416-797 1.80e-160

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


Pssm-ID: 270445 [Multi-domain]  Cd Length: 259  Bit Score: 469.90  E-value: 1.80e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13727    1 NRTVVVTTIMESPYVMYKKNHEMFEGNDKFEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDPETKIWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13727   81 AEIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQ------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvs 655
Cdd:cd13727      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEY 735
Cdd:cd13727  118 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMKSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMNEY 197
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381488 736 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 797
Cdd:cd13727  198 IEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
416-797 7.17e-159

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


Pssm-ID: 270444 [Multi-domain]  Cd Length: 259  Bit Score: 465.65  E-value: 7.17e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13726    1 NKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13726   81 ADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvs 655
Cdd:cd13726      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEY 735
Cdd:cd13726  118 PIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMNEY 197
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381488 736 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 797
Cdd:cd13726  198 IEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
39-400 1.96e-156

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: 464.11  E-value: 1.96e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  39 GLFPNQQSQEHAAFRFALS------QLTEPP-KLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFC 111
Cdd:cd06387    4 GLFMRNTVQEHSAFRFAVQlyntnqNTTEKPfHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 112 GALHVCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAV---NIL 188
Cdd:cd06387   84 GALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARsvgNIK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 189 TTTEegYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNY 268
Cdd:cd06387  164 DVQE--FRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNN 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 269 TDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQ 348
Cdd:cd06387  242 ENPMVQQFLQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIE 321
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384381488 349 RALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFVP 400
Cdd:cd06387  322 RALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEYERFVP 373
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
39-400 1.31e-150

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: 449.42  E-value: 1.31e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  39 GLFPNQQSQEHAAFRFALSQLTEPP-------KLLPQIDIVNiSDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFC 111
Cdd:cd06380    4 AIFDSGEDQVQTAFRYAIDRHNSNNnnrfrlfPLTERIDITN-ADSFSVSRAICSQLSRGVFAIFGSSDASSLNTIQSYS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 112 GALHVCFITPSFPVD---TSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEK-NWQVTAVNI 187
Cdd:cd06380   83 DTFHMPYITPSFPKNepsDSNPFELSLRPSYIEAIVDLIRHYGWKKVVYLYDSDEGLLRLQQLYDYLKEKsNISVRVRRV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 188 -LTTTEEGYRMLFQDLEKKKE-RLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQL 265
Cdd:cd06380  163 rNVNDAYEFLRTLRELDREKEdKRIVLDLSSERYQKILEQIVEDGMNRRNYHYLLANLDFLDLDLERFLHGGVNITGFQL 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 266 VNYTDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDI----------SRRGNAGDCLA 335
Cdd:cd06380  243 VDTNNKTVKDFLQRWKKLDPREYPGAGTDTIPYEAALAVDAVLVIAEAFQSLLRQNDDIfrftfhgelyNNGSKGIDCDP 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384381488 336 NPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHD-GIRKIGYWNEDDKFVP 400
Cdd:cd06380  323 NPPLPWEHGKAIMKALKKVRFEGLTGNVQFDDFGQRKNYTLDVIELTSNrGLRKIGTWSEGDGFLL 388
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit ...
36-399 4.99e-150

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: 447.55  E-value: 4.99e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  36 EVWGLFPNQQSQEHAAFRFAL------SQLTEPP-KLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLT 108
Cdd:cd06388    1 QIGGLFIRNTDQEYTAFRLAIflhntsPNASEAPfNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 109 SFCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNIL 188
Cdd:cd06388   81 SFCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 189 TTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNY 268
Cdd:cd06388  161 NFNDASYRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 269 TDTIPAKIMQQWKNSDARDHTRVDwKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQ 348
Cdd:cd06388  241 NTPMVTKLMQRWKKLDQREYPGSE-TPPKYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384381488 349 RALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFV 399
Cdd:cd06388  320 RTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLV 370
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
416-791 4.44e-148

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


Pssm-ID: 270441 [Multi-domain]  Cd Length: 369  Bit Score: 442.21  E-value: 4.44e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDpDTKAWNGMVGELVYGR 495
Cdd:cd13723    1 NRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQD-DKGQWNGMVKELIDHK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEW 575
Cdd:cd13723   80 ADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 HSEEFEEGRDQTTSdqsNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVS 655
Cdd:cd13723  160 YDAHPCNPGSEVVE---NNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMES 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMkSAEPSVFVRTTEEGMIRVRKSkgKYAYLLESTMNEY 735
Cdd:cd13723  237 PIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFM-SSKPSALVKNNEEGIQRALTA--DYALLMESTTIEY 313
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384381488 736 IEQRKpCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13723  314 VTQRN-CNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWW 368
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
416-797 3.09e-147

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


Pssm-ID: 270446 [Multi-domain]  Cd Length: 259  Bit Score: 435.66  E-value: 3.09e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13728    1 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13728   81 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQ------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvs 655
Cdd:cd13728      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEY 735
Cdd:cd13728  118 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEY 197
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381488 736 IEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 797
Cdd:cd13728  198 IEQRKPCDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
416-791 1.33e-123

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


Pssm-ID: 270432 [Multi-domain]  Cd Length: 251  Bit Score: 374.18  E-value: 1.33e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13714    1 NKTLIVTTILEEPYVMLKESAKPLTGNDRFEGFCIDLLKELAKILGFNYTIRLVPDGKYGSYDPETGEWNGMVRELIDGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13714   81 ADLAVADLTITYERESVVDFTKPFMNLGISILYRKPT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvs 655
Cdd:cd13714      --------------------------------------------------------------------------------
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRksKGKYAYLLESTMNEY 735
Cdd:cd13714  118 PIESADDLAKQTKIKYGTLRGGSTMTFFRDSNISTYQKMWNFMMSAKPSVFVKSNEEGVARVL--KGKYAFLMESTSIEY 195
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384381488 736 IEQRkPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13714  196 VTQR-NCNLTQIGGLLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKWW 250
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
548-826 1.28e-122

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


Pssm-ID: 459656 [Multi-domain]  Cd Length: 267  Bit Score: 372.41  E-value: 1.28e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  548 EIWMCIVFAYIGVSVVLFLVSRFSPYEWHSEEFEEgrdqttsdqSNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGG 627
Cdd:pfam00060   3 EVWLGILVAFLIVGVVLFLLERFSPYEWRGPLETE---------ENRFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  628 VWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFV 707
Cdd:pfam00060  74 VWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  708 RTTEEGMIRVRKSKGKYAYLLEstmNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLK 787
Cdd:pfam00060 154 ALNEEGVALVRNGIYAYALLSE---NYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLE 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 384381488  788 NKWWYDKGECGSggGDSKDKTSALSLSNVAGVFYILIGG 826
Cdd:pfam00060 231 KKWWPKSGECDS--KSSASSSSQLGLKSFAGLFLILGIG 267
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
416-791 1.51e-110

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


Pssm-ID: 270442 [Multi-domain]  Cd Length: 333  Bit Score: 343.53  E-value: 1.51e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDtKAWNGMVGELVYGR 495
Cdd:cd13724    1 NTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEAN-GTWTGMVGELIARK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEW 575
Cdd:cd13724   80 ADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 HS-EEFEEGRDQTTsdqSNEFGIFNSLWFSLGAFMQQGCDISPrslsgrivggvwwfftliiissytanlaafltvermv 654
Cdd:cd13724  160 YSpHPCAQGRCNLL---VNQYSLGNSLWFPVGGFMQQGSTIAP------------------------------------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 655 sPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSkgKYAYLLESTMNE 734
Cdd:cd13724  200 -PIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNS--NYAFLLESTMNE 276
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 384381488 735 YIEQRKpCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13724  277 YYRQRN-CNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWW 332
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
416-792 1.26e-105

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


Pssm-ID: 270403 [Multi-domain]  Cd Length: 252  Bit Score: 327.22  E-value: 1.26e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNanQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDpDTKAWNGMVGELVYGR 495
Cdd:cd13685    1 NKTLRVTTILEPPFVMKKRD--SLSGNPRFEGYCIDLLEELAKILGFDYEIYLVPDGKYGSRD-ENGNWNGMIGELVRGE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13685   78 ADIAVAPLTITAEREEVVDFTKPFMDTGISILMRKP-------------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvS 655
Cdd:cd13685  114 -------------------------------------------------------------------------------T 114
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKM--WTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMN 733
Cdd:cd13685  115 PIESLEDLAKQSKIEYGTLKGSSTFTFFKNSKNPEYRRYeyTKIMSAMSPSVLVASAAEGVQRVRESNGGYAFIGEATSI 194
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 384381488 734 EYIEQRkPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWY 792
Cdd:cd13685  195 DYEVLR-NCDLTKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGELEKLKEKWWN 252
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
416-791 8.77e-88

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


Pssm-ID: 270435 [Multi-domain]  Cd Length: 360  Bit Score: 284.19  E-value: 8.77e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNanqfeGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKaWNGMVGELVYGR 495
Cdd:cd13717    1 RRVYRIGTVESPPFVYRDRD-----GSPIWEGYCIDLIEEISEILNFDYEIVEPEDGKFGTMDENGE-WNGLIGDLVRKE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSL-GISIMIKKPqKSKPGVFSFLDPLAYEIWmcivfayigvsvvlflvsrfspye 574
Cdd:cd13717   75 ADIALAALSVMAEREEVVDFTVPYYDLvGITILMKKP-ERPTSLFKFLTVLELEVW------------------------ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 575 whseefeegrdqttsdqsNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMV 654
Cdd:cd13717  130 ------------------REFTLKESLWFCLTSLTPQGGGEAPKNLSGRLLVATWWLFVFIIIASYTANLAAFLTVSRLQ 191
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 655 SPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIA--VFEKMWTYMK-----------------------------SAEP 703
Cdd:cd13717  192 TPVESLDDLARQYKIQYTVVKNSSTHTYFERMKNAedTLYEMWKDMSlndslspveraklavwdypvsekytkiyqAMQE 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 704 SVFVRTTEEGMIRVRKS-KGKYAYLLESTMNEYiEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGL 782
Cdd:cd13717  272 AGLVANAEEGVKRVREStSAGFAFIGDATDIKY-EILTNCDLQEVGEEFSRKPYAIAVQQGSPLKDELNYAILELQNDRF 350

                 ....*....
gi 384381488 783 LDKLKNKWW 791
Cdd:cd13717  351 LEKLKAKWW 359
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
416-791 1.69e-80

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


Pssm-ID: 270439 [Multi-domain]  Cd Length: 251  Bit Score: 260.72  E-value: 1.69e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGR 495
Cdd:cd13721    1 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13721   81 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKG-------------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvS 655
Cdd:cd13721  117 -------------------------------------------------------------------------------T 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSkgKYAYLLESTMNEY 735
Cdd:cd13721  118 PIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTS--DYAFLMESTTIEF 195
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384381488 736 IEQRKpCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13721  196 VTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWW 250
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
417-791 1.30e-76

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


Pssm-ID: 270219 [Multi-domain]  Cd Length: 243  Bit Score: 249.98  E-value: 1.30e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 417 RTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGArdPDTKAWNGMVGELVYGRA 496
Cdd:cd00998    1 KTLKVVVPLEPPFVMFVTGSNAVTGNGRFEGYCIDLLKELSQSLGFTYEYYLVPDGKFGA--PVNGSWNGMVGEVVRGEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 497 DVAVAPLTITLVREEVIDFSKPFMSLGISIMIkkpqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewh 576
Cdd:cd00998   79 DLAVGPITITSERSVVIDFTQPFMTSGIGIMI------------------------------------------------ 110
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 577 seefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvsP 656
Cdd:cd00998  111 -------------------------------------------------------------------------------P 111
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 657 IESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKsaEPSVFVRTTEEGMIRVRKSKGkYAYLLESTMNEYI 736
Cdd:cd00998  112 IRSIDDLKRQTDIEFGTVENSFTETFLRSSGIYPFYKTWMYSE--ARVVFVNNIAEGIERVRKGKV-YAFIWDRPYLEYY 188
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 384381488 737 EQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd00998  189 ARQDPCKLIKTGGGFGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
416-791 5.95e-74

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


Pssm-ID: 270440 [Multi-domain]  Cd Length: 250  Bit Score: 243.03  E-value: 5.95e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDpDTKAWNGMVGELVYGR 495
Cdd:cd13722    1 NRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFLYDVKLVPDGKYGAQN-DKGEWNGMVKELIDHR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13722   80 ADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKG-------------------------------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvS 655
Cdd:cd13722  116 -------------------------------------------------------------------------------T 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSkgKYAYLLESTMNEY 735
Cdd:cd13722  117 PIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVKNSDEGIQRVLTT--DYALLMESTSIEY 194
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384381488 736 IEQRKpCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13722  195 VTQRN-CNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWW 249
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
416-791 1.84e-72

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


Pssm-ID: 270443 [Multi-domain]  Cd Length: 250  Bit Score: 239.22  E-value: 1.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 416 NRTYIVTTILEDPYVMLKKNANQFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDtKAWNGMVGELVYGR 495
Cdd:cd13725    1 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPN-GSWTGMVGELINRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 496 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIkkpqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 575
Cdd:cd13725   80 ADLAVAAFTITAEREKVIDFSKPFMTLGISILY----------------------------------------------- 112
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 576 hseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltveRMVS 655
Cdd:cd13725  113 ----------------------------------------------------------------------------RVHM 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSkgKYAYLLESTMNEY 735
Cdd:cd13725  117 PVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMNEY 194
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 384381488 736 iEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13725  195 -HRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 249
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
47-384 2.32e-69

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


Pssm-ID: 460062 [Multi-domain]  Cd Length: 347  Bit Score: 234.20  E-value: 2.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488   47 QEHAAFRFALSQLTEPPKLLPQID----IVNISDSFEMTYRFCSQFSKG-VYAIFGFYERRTVNMLTSFCGALHVCFITP 121
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGLLPGTKleyiILDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPLISY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  122 SFPVDT-----SNQFVLQLRPE---LQDALISIIDHYKWQKFVYIY-DADRGLSVLQKVLDTAAEKNWQVTAVNIL---T 189
Cdd:pfam01094  81 GSTSPAlsdlnRYPTFLRTTPSdtsQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVIppaQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  190 TTEEGYRMLFQDLeKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILAN--LGFMDIDLNKFKESGANVTGFQLVN 267
Cdd:pfam01094 161 DDDEIARKLLKEV-KSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDglTTSLVILNPSTLEAAGGVLGFRLHP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  268 YTDTIPAKIMQqWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGdclanpavPWGQGIDI 347
Cdd:pfam01094 240 PDSPEFSEFFW-EKLSDEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRACGALG--------PWNGGQKL 310
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 384381488  348 QRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHD 384
Cdd:pfam01094 311 LRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
PBP1_iGluR_N_LIVBP-like cd06351
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
39-400 4.26e-67

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: 228.00  E-value: 4.26e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  39 GLFPNQQSQEHAAFRFALSQLT------EPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCG 112
Cdd:cd06351    4 FIFEVNNEPAAKAFEVAVTYLKknintrYGLSVQYDSIEANKSNAFVLLEAICNKYATGTPALILDTTKSSINSLTSALG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 113 ALHVCFITPSFPVDTS--------NQFVLQLRPE--LQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQV 182
Cdd:cd06351   84 APHISASYGQQGDLRQwrdldeakQKYLLQVRPPeaLRSIVLHLNITNAWIKFVDSYDMEHYKSLLQNIQTRAVQNNVIV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 183 TAVNILTTTEEGYRMLF--------QDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFK 254
Cdd:cd06351  164 AIAKVGKREREEQLDINnffilgtlQSIRMVLEVRPAYFERNFAWHAITQNEVEISSQSDNAHIMFMNPMAYDILLETVY 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 255 ESGANVTGFQLVNYTDTIPAKIMQQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSlrrqridisrrgnagdcl 334
Cdd:cd06351  244 RDRLGLTRTTYNLNENPMVQQFIQRWVRLDEREFPEAKNAELQLSSAFYFDLALRSALAFKE------------------ 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384381488 335 anpavpwgqgidiqralqqvrfeglTGNVQFNEKGRRTNYTLHVIEMKHD-GIRKIGYWNEDDKFVP 400
Cdd:cd06351  306 -------------------------TGYGTFDLQSTQPFNGHSFMKFEMDiNVRKIRGWSEYESVNS 347
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
46-394 5.20e-65

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: 221.86  E-value: 5.20e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  46 SQEHAAFRFALSQLTEPPKLLP------QIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFI 119
Cdd:cd06368   12 AHERAAFRYAVERLNTNIVKLAyfritySIEAIDSNSHFDATDKACDLLEKGVVAIVGPSSSDSNNALQSICDALDVPHI 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 120 TPSFPVDTSN-QFVLQLRP--ELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTA----VNILTTTE 192
Cdd:cd06368   92 TVHDDPRLSKsQYSLSLYPrnQLSQAVSDLLKYWRWKRFVLVYDDDDRLRRLQELLEAARFSKRFVSVrkvdLDYKTLDE 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 193 EGYrmlfqdLEKKKERL---VVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDI-DLNKFKESGANVTGFQLVNy 268
Cdd:cd06368  172 TPL------LKRKDCSLfsrILIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDLSLLlDLELFRYNHANITGFQLVD- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 269 TDTIPAKIMQQW--KNSDARDHTRVDWKR--PKYTSALTYDGVKVMAEAFQSlrrqridisrrgnagdclanpavpwgqg 344
Cdd:cd06368  245 NNSMYKEDINRLafNWSRFRQHIKIESNLrgPPYEAALMFDAVLLLADAFRR---------------------------- 296
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 384381488 345 idiqralqqvrfeglTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNE 394
Cdd:cd06368  297 ---------------TGDLRFNGTGLRSNFTLRILELGYGGLRKIGFWDS 331
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
39-399 2.22e-64

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: 220.17  E-value: 2.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  39 GLFPNQQSQEHAAFRFALS-----QLTEPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGA 113
Cdd:cd06382    4 GIFDEDDEDLEIAFKYAVDrinreRTLPNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSDIVQSICDA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 114 LHVCFI--TPSFPVDTSNQFVLQLRPE---LQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNIl 188
Cdd:cd06382   84 LEIPHIetRWDPKESNRDTFTINLYPDpdaLSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPKDIPITVRQL- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 189 tTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNY 268
Cdd:cd06382  163 -DPGDDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANITGFRLVDP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 269 TDTIPAKIMQQWKNSDaRDHTRVDWKRPKYT--SALTYDGVKVMAEAFQslrrqridisrrgnagdclanpavpwgqgid 346
Cdd:cd06382  242 ENPEVKNVLKDWSKRE-KEGFNKDIGPGQITteTALMYDAVNLFANALK------------------------------- 289
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 384381488 347 iqralqqvrfEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKFV 399
Cdd:cd06382  290 ----------EGLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGTWNPTDGLN 332
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
417-530 6.49e-58

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


Pssm-ID: 463166 [Multi-domain]  Cd Length: 111  Bit Score: 193.50  E-value: 6.49e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  417 RTYIVTTILEDPYVMLKKNanqFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKAWNGMVGELVYGRA 496
Cdd:pfam10613   1 KTLIVTTILEPPFVMLKEN---LEGNDRYEGFCIDLLKELAEILGFKYEIRLVPDGKYGSLDPTTGEWNGMIGELIDGKA 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 384381488  497 DVAVAPLTITLVREEVIDFSKPFMSLGISIMIKK 530
Cdd:pfam10613  78 DLAVAPLTITSEREKVVDFTKPFMTLGISILMKK 111
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
656-793 1.38e-51

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


Pssm-ID: 197504 [Multi-domain]  Cd Length: 133  Bit Score: 176.71  E-value: 1.38e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488   656 PIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSaePSVFVRTTEEGMIRVRKSKgkYAYLLESTMNEY 735
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKS--PEVFVKSYAEGVQRVRVSN--YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 384381488   736 IEQRkPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYD 793
Cdd:smart00079  77 ELSR-NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
421-790 3.74e-41

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


Pssm-ID: 270405 [Multi-domain]  Cd Length: 239  Bit Score: 151.25  E-value: 3.74e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 421 VTTILEDPYVMLKKNanqfegndryEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTKA-WNGMVGELVYGRADVA 499
Cdd:cd13687    6 VVTLEEAPFVYVKCC----------YGFCIDLLKKLAEDVNFTYDLYLVTDGKFGTVNKSINGeWNGMIGELVSGRADMA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 500 VAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhsee 579
Cdd:cd13687   76 VASLTINPERSEVIDFSKPFKYTGITILVKKRNE---------------------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 580 feegrdqttsdqsnefgifnslwfslgafmqqgcdisprsLSGrivggvwwfftliiissytanlaafLTVERMVSPIES 659
Cdd:cd13687  110 ----------------------------------------LSG-------------------------INDPRLRNPSPP 124
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 660 aedlakqteIAYGTLEAGSTKEFFRRSkiavFEKMWTYMKSAEpsvfVRTTEEGMIRVRKSKGKyAYLLESTMNEY-IEQ 738
Cdd:cd13687  125 ---------FRFGTVPNSSTERYFRRQ----VELMHRYMEKYN----YETVEEAIQALKNGKLD-AFIWDSAVLEYeASQ 186
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 384381488 739 RKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKW 790
Cdd:cd13687  187 DEGCKLVTVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHESGFMEELDKKW 238
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
418-791 2.50e-38

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


Pssm-ID: 270448 [Multi-domain]  Cd Length: 257  Bit Score: 143.94  E-value: 2.50e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 418 TYIVTTILEDPYVMLKKNAnqFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTkAWNGMVGELVYGRAD 497
Cdd:cd13730    3 TLKVVTVLEEPFVMVAENI--LGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGKYGHQLHNT-SWNGMIGELISKRAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 498 VAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhs 577
Cdd:cd13730   80 LAISAITITPERESVVDFSKRYMDYSVGILIKKPE--------------------------------------------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 578 eefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvsPI 657
Cdd:cd13730  115 ------------------------------------------------------------------------------PI 116
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 658 ESAEDLAKQTEIAYGTLEAGSTKEFFRRS------KIAVFEKMW-TYMKSAEPSVFVRTTEEGmirVRKSK-GKYAYLLE 729
Cdd:cd13730  117 RTFQDLSKQVEMSYGTVRDSAVYEYFRAKgtnpleQDSTFAELWrTISKNGGADNCVSSPSEG---IRKAKkGNYAFLWD 193
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384381488 730 STMNEYIE-QRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13730  194 VAVVEYAAlTDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKWW 256
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
421-791 2.95e-38

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


Pssm-ID: 270434 [Multi-domain]  Cd Length: 257  Bit Score: 143.44  E-value: 2.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 421 VTTILEDPYVMLKKNAnqFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTkAWNGMVGELVYGRADVAV 500
Cdd:cd13716    6 VVTVLEEPFVMVSENV--LGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHKYGSQQEDG-TWNGLIGELVFKRADIGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 501 APLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhseef 580
Cdd:cd13716   83 SALTITPERENVVDFTTRYMDYSVGVLLRKAE------------------------------------------------ 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 581 eegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvsPIESA 660
Cdd:cd13716  115 ---------------------------------------------------------------------------SIQSL 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 661 EDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYM-------KSAEPSVFVRTTEEGmirVRKSK-GKYAYLLESTM 732
Cdd:cd13716  120 QDLSKQTDIPYGTVLDSAVYEYVRSKGTNPFERDSMYSqmwrminRSNGSENNVSESSEG---IRKVKyGNYAFVWDAAV 196
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 733 NEYIEQRKP-CDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13716  197 LEYVAINDDdCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 256
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
421-791 3.12e-32

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


Pssm-ID: 270449 [Multi-domain]  Cd Length: 257  Bit Score: 126.30  E-value: 3.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 421 VTTILEDPYVMLKKNAnqFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDtKAWNGMVGELVYGRADVAV 500
Cdd:cd13731    6 VVTVLEEPFVMVSENV--LGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQED-GTWNGLVGELVFKRADIGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 501 APLTITLVREEVIDFSKPFMSLGISIMIKKPQKskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhseef 580
Cdd:cd13731   83 SALTITPDRENVVDFTTRYMDYSVGVLLRRAES----------------------------------------------- 115
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 581 eegrdqttsdqsnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvspIESA 660
Cdd:cd13731  116 ----------------------------------------------------------------------------IQSL 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 661 EDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEK--MWTYM-----KSAEPSVFVRTTEEGmirVRKSK-GKYAYLLESTM 732
Cdd:cd13731  120 QDLSKQTDIPYGTVLDSAVYEHVRMKGLNPFERdsMYSQMwrminRSNGSENNVLESQAG---IQKVKyGNYAFVWDAAV 196
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 733 NEYIEQRKP-CDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13731  197 LEYVAINDPdCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 256
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
421-790 1.89e-28

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


Pssm-ID: 270437 [Multi-domain]  Cd Length: 277  Bit Score: 115.92  E-value: 1.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 421 VTTILEDPYVMLKK----------------NANQFEGNDRY---EGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDP-- 479
Cdd:cd13719    6 IVTIHEEPFVYVRPtpsdgtcreeftvncpNFNISGRPTVPfccYGYCIDLLIKLARKMNFTYELHLVADGQFGTQERvn 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 480 --DTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKskpgvfsfldplayeiwmcivfay 557
Cdd:cd13719   86 nsNKKEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILVKKEIR------------------------ 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 558 igvsvvlflvsrfspyewhseefeegrdqttsdqsnefgifnslwfslgafmqqgcdisprsLSGrivggvwwfftliii 637
Cdd:cd13719  142 --------------------------------------------------------------LTG--------------- 144
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 638 ssytanlaafLTVERMVSPIEsaedlakqtEIAYGTLEAGSTKEFFRRSkiAVFEKMWTYMKSAEpsvfVRTTEEGMIRV 717
Cdd:cd13719  145 ----------INDPRLRNPSE---------KFIYATVKGSSVDMYFRRQ--VELSTMYRHMEKHN----YETAEEAIQAV 199
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384381488 718 RKSKGKyAYLLESTMNEYiEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKW 790
Cdd:cd13719  200 RDGKLH-AFIWDSSRLEF-EASQDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTW 270
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
447-790 3.27e-25

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


Pssm-ID: 270436 [Multi-domain]  Cd Length: 283  Bit Score: 106.65  E-value: 3.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 447 GYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDTkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISI 526
Cdd:cd13718   58 GFCIDILKKLAKDVGFTYDLYLVTNGKHGKKINGV--WNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 527 MIKKpqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhseefeegrdqttsdqSNEFgifnslwfslg 606
Cdd:cd13718  136 MVAR-------------------------------------------------------------SNQV----------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 607 afmqqgcdisprslSGrivggvwwfftliiissytanlaafLTVERMVSPIEsaedlaKQTEIAYGTLEAGSTKEFFRRS 686
Cdd:cd13718  144 --------------SG-------------------------LSDKKFQRPHD------QSPPFRFGTVPNGSTERNIRNN 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 687 kiavFEKMWTYMKsaepSVFVRTTEEGMIRVRKSKGKyAYLLESTMNEYIEQR-KPCDTMKVGGN--LDSKGYGIATPKG 763
Cdd:cd13718  179 ----YPEMHQYMR----KYNQKGVEDALVSLKTGKLD-AFIYDAAVLNYMAGQdEGCKLVTIGSGkwFAMTGYGIALQKN 249
                        330       340
                 ....*....|....*....|....*..
gi 384381488 764 SALRNPVNLAVLKLNEQGLLDKLKNKW 790
Cdd:cd13718  250 SKWKRPFDLALLQFRGDGELERLERLW 276
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
428-492 1.06e-22

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


Pssm-ID: 214911 [Multi-domain]  Cd Length: 62  Bit Score: 91.93  E-value: 1.06e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384381488   428 PYVMLKKNAnqFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGARDPDtKAWNGMVGELV 492
Cdd:smart00918   1 PYVMLKESP--DGGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLPN-GSWNGMVGELV 62
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
198-392 1.15e-20

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: 94.98  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 198 LFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDIDLNKFKESGANVTGFQLVNYTDTIPAKIM 277
Cdd:cd06394  180 LLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQSNILGFSMFNTSHPFYLEFV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 278 QQWKNSDARDHTRVDWKRPKYTSALTYDGVKVMAEAFQSLRR-QRIDISRRGnagdclANPAVPWGQGIDIQRALQQVRF 356
Cdd:cd06394  260 RSLNMSWRENCDASTYPGPALSSALMFDAVHVVVSAVRELNRsQEIGVKPLS------CTSAQIWQHGTSLMNYLRMVEY 333
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 384381488 357 EGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYW 392
Cdd:cd06394  334 DGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 369
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
447-791 2.70e-20

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


Pssm-ID: 270438 [Multi-domain]  Cd Length: 283  Bit Score: 92.22  E-value: 2.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 447 GYCVELAAEIAKHVGYSYRLEIVSDGKYGArDPDTKaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISI 526
Cdd:cd13720   67 GYCIDLLEKLAEDLGFDFDLYIVGDGKYGA-WRNGR-WTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSLGI 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 527 MIkKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhseefeegrdqttsdqsnefgifnslwfslg 606
Cdd:cd13720  145 LV-RTR-------------------------------------------------------------------------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 607 afmQQGCDISPRSLSGRIVGgvwwfftliiissytanlaafltvERMVSPIESAEDlakqteiaygtleagstkEFFRRS 686
Cdd:cd13720  150 ---DELSGIHDPKLHHPSQG------------------------FRFGTVRESSAE------------------YYVKKS 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 687 kiavFEKMWTYMKSAEpsvfVRTTEEGMIRVRKSKGKYAYLLEST--MNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGS 764
Cdd:cd13720  185 ----FPEMHEHMRRYS----LPNTPEGVEYLKNDPEKLDAFIMDKalLDYEVSIDADCKLLTVGKPFAIEGYGIGLPQNS 256
                        330       340
                 ....*....|....*....|....*..
gi 384381488 765 ALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13720  257 PLTSNISELISQYKSNGFMDLLHDKWY 283
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
39-393 1.40e-19

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: 92.03  E-value: 1.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  39 GLFPNQQSQEHAAFRFALSQLT------EPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCG 112
Cdd:cd06391    4 AIFDESAKKDDEVFRTAVGDLNqneeilQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLAD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 113 ALHV--CFI------TP--SFPVDTSNQ---FVLQLRPE--LQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAE 177
Cdd:cd06391   84 AMHIphLFIqrstagTPrsGCGLTRSNRnddYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQ 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 178 KNWQVTA------VNILTTTEegYR-MLFQDLEKKKE--RLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDI 248
Cdd:cd06391  164 QGMDVALqkvennINKMITTL--FDtMRIEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEINDV 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 249 DLNKF-KESGANVTgfqLVNYTDTIPAKIMQQ-WKNSDARDHTRVDWKRPK-----YTSALTYDGVKVMAEAFQslrRQR 321
Cdd:cd06391  242 DVQELvRRSIGRLT---IIRQTFPVPQNISQRcFRGNHRISSSLCDPKDPFaqnmeISNLYIYDTVLLLANAFH---KKL 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384381488 322 IDISRRGNAG-DCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVI-----EMKHDGIRKIGYWN 393
Cdd:cd06391  316 EDRKWHSMASlSCIRKNSKPWQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILgtnygEELGRGVRKLGCWN 393
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
418-530 2.42e-16

Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This domain is found in solute binding proteins that serve as initial receptors in the ABC transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1, but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 270248 [Multi-domain]  Cd Length: 217  Bit Score: 78.83  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 418 TYIVTTILED-PYVMlkknanqFEGNDRYEGYCVELAAEIAKHVGYsyRLEIVsdgkygardpDTkAWNGMVGELVYGRA 496
Cdd:cd13530    1 TLRVGTDADYpPFEY-------IDKNGKLVGFDVDLANAIAKRLGV--KVEFV----------DT-DFDGLIPALQSGKI 60
                         90       100       110
                 ....*....|....*....|....*....|....
gi 384381488 497 DVAVAPLTITLVREEVIDFSKPFMSLGISIMIKK 530
Cdd:cd13530   61 DVAISGMTITPERAKVVDFSDPYYYTGQVLVVKK 94
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
40-393 4.99e-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: 81.19  E-value: 4.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  40 LFPNQQSQEHAAFRFALSQLT------EPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGA 113
Cdd:cd06381    5 IFEENAAKDDRVFQLAVSDLSlnddilQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQSLTDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 114 LHV----------------CFITPSfpvDTSNQFVLQLRP--ELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTA 175
Cdd:cd06381   85 MHIphlfvqrnpggsprtaCHLNPS---PDGEAYTLASRPpvRLNDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFLDQA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 176 AEKNWQVTAVNILTTTEEGYRMLF-----QDLEKKKE--RLVVVDCESERLNAILGQIIKLEKNGIGYHYILANLGFMDI 248
Cdd:cd06381  162 SRLGLDVSLQKVDKNISHVFTSLFttmktEELNRYRDtlRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEISDP 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 249 DLNKFKESGanvTGFQLVNYTDTIPAKIMQQ-WKNSDARDHTRVDWKRP-----KYTSALTYDGVKVMAEAFQslrRQRI 322
Cdd:cd06381  242 EILDLVHSA---LGRMTVVRQIFPSAKDNQKcFRNNHRISSLLCDPQEGylqmlQISNLYLYDSVLMLANAFH---RKLE 315
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 384381488 323 DISRRGNAG-DCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVI-----EMKHDGIRKIGYWN 393
Cdd:cd06381  316 DRKWHSMASlNCIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDSSNPYVQFEILgttysETFGKDMRKLATWD 392
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
440-530 8.66e-14

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 71.55  E-value: 8.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 440 EGNDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPF 519
Cdd:COG0834   16 DEDGKLVGFDVDLARAIAKRLGLKVEFVPVP-------------WDRLIPALQSGKVDLIIAGMTITPEREKQVDFSDPY 82
                         90
                 ....*....|.
gi 384381488 520 MSLGISIMIKK 530
Cdd:COG0834   83 YTSGQVLLVRK 93
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
428-543 1.67e-12

Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognizes Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 425719 [Multi-domain]  Cd Length: 221  Bit Score: 67.70  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  428 PYVMLKKNanqfegnDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITL 507
Cdd:pfam00497  11 PFEYVDEN-------GKLVGFDVDLAKAIAKRLGVKVEFVPVS-------------WDGLIPALQSGKVDLIIAGMTITP 70
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 384381488  508 VREEVIDFSKPFMSLGISIMIKKpQKSKPGVFSFLD 543
Cdd:pfam00497  71 ERAKQVDFSDPYYYSGQVILVRK-KDSSKSIKSLAD 105
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
438-790 1.23e-11

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


Pssm-ID: 270216 [Multi-domain]  Cd Length: 218  Bit Score: 64.99  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 438 QFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSK 517
Cdd:cd00994   14 EFKQDGKYVGFDIDLWEAIAKEAGFKYELQPMD-------------FKGIIPALQTGRIDIAIAGITITEERKKVVDFSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 518 PFMSLGISIMIKKPQKSKPGvfsfLDPLAYEiwmcIVFAYIGVSVVLFLVSRFSPyewhseefeegrdqttsdqsnefgi 597
Cdd:cd00994   81 PYYDSGLAVMVKADNNSIKS----IDDLAGK----TVAVKTGTTSVDYLKENFPD------------------------- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 598 fnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytANLAAFLTVERMvspiesaedlakqteiaYGTLEAG 677
Cdd:cd00994  128 --------------------------------------------AQLVEFPNIDNA-----------------YMELETG 146
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 678 stkeffrRSKIAVFEKmwtymksaePSV--FVRTTEEGMIRVrkskgkyayllestmneyieqrkpcdtmkVGGNLDSKG 755
Cdd:cd00994  147 -------RADAVVHDT---------PNVlyYAKTAGKGKVKV-----------------------------VGEPLTGEQ 181
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 384381488 756 YGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKW 790
Cdd:cd00994  182 YGIAFPKGSELREKVNAALKTLKADGTYDEIYKKW 216
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
440-530 2.96e-11

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


Pssm-ID: 270407 [Multi-domain]  Cd Length: 229  Bit Score: 64.18  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 440 EGNDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardPDTKawngmVGELVYGRADVAVAPLTITLVREEVIDFSKPF 519
Cdd:cd13689   26 PKTREIVGFDVDLCKAIAKKLGVKLELKPVN--------PAAR-----IPELQNGRVDLVAANLTYTPERAEQIDFSDPY 92
                         90
                 ....*....|.
gi 384381488 520 MSLGISIMIKK 530
Cdd:cd13689   93 FVTGQKLLVKK 103
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
440-535 5.01e-10

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


Pssm-ID: 270338 [Multi-domain]  Cd Length: 227  Bit Score: 60.43  E-value: 5.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 440 EGNDRYEGYCVELAAEIAKHVGYsyRLEIVSdgkygardpdtKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPF 519
Cdd:cd13620   24 DGKNQVVGADIDIAKAIAKELGV--KLEIKS-----------MDFDNLLASLQSGKVDMAISGMTPTPERKKSVDFSDVY 90
                         90
                 ....*....|....*.
gi 384381488 520 MSLGISIMIKKPQKSK 535
Cdd:cd13620   91 YEAKQSLLVKKADLDK 106
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
418-528 1.13e-09

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


Pssm-ID: 270218 [Multi-domain]  Cd Length: 218  Bit Score: 59.27  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 418 TYIVTTILEDPYVMlkknanqfEGNDRYEGYCVELAAEIAKHVGYSYrlEIVSDGKYGArdpdtkawngMVGELVYGRAD 497
Cdd:cd00997    4 TLTVATVPRPPFVF--------YNDGELTGFSIDLWRAIAERLGWET--EYVRVDSVSA----------LLAAVAEGEAD 63
                         90       100       110
                 ....*....|....*....|....*....|.
gi 384381488 498 VAVAPLTITLVREEVIDFSKPFMSLGISIMI 528
Cdd:cd00997   64 IAIAAISITAEREAEFDFSQPIFESGLQILV 94
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
439-530 2.50e-09

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


Pssm-ID: 270344 [Multi-domain]  Cd Length: 219  Bit Score: 58.48  E-value: 2.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGNDRYEGYCVELAAEIAKHVGYSYrleivsdgkygarDPDTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKP 518
Cdd:cd13626   16 KDEDGKLTGFDVEVGREIAKRLGLKV-------------EFKATEWDGLLPGLNSGKFDVIANQVTITPEREEKYLFSDP 82
                         90
                 ....*....|..
gi 384381488 519 FMSLGISIMIKK 530
Cdd:cd13626   83 YLVSGAQIIVKK 94
PBP1_iGluR_delta_1 cd06392
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 ...
40-369 4.28e-09

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: 59.64  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  40 LFPNQQSQEHAAFRFALSQLT------EPPKLLPQIDIVNISDSFEMTYRFCSQFSKGVYAIFGFYERRTVNMLTSFCGA 113
Cdd:cd06392    5 IFEENAAKDDRVFQLAVSDLSlnddilQSEKITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANALQSLTDA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 114 LHV----------------CFITPSfpvDTSNQFVLQLRP--ELQDALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTA 175
Cdd:cd06392   85 MHIphlfvqrnsggsprtaCHLNPS---PEGEEYTLAARPpvRLNDVMLKLVTELRWQKFIVFYDSEYDIRGLQSFLDQA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 176 A-----------EKNWQVTAVNILTT--TEEGYRmlFQDLEKKKERLVvvdceSER-LNAILGQIIKLEKNGIGYHYILA 241
Cdd:cd06392  162 SrlgldvslqkvDRNISRVFTNLFTTmkTEELNR--YRDTLRRAILLL-----SPRgAQSFINEAVETNLASKDSHWVFV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 242 NLGFMDIDLNKFKESGANVTgfqlvnytdTIPAKIMQQWKNSDA---RDHTRVD----------WKRPKYTSALTYDGVK 308
Cdd:cd06392  235 NEEISDPEILELVHSALGRM---------TVIRQIFPLSKDNNQrcmRNNHRISsllcdpqegyLQMLQVSNLYLYDSVL 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 384381488 309 VMAEAFQslrRQRIDISRRGNAG-DCLANPAVPWGQGIDIQRALQQVRFEGLTGNVQFNEKG 369
Cdd:cd06392  306 MLANAFH---RKLEDRKWHSMASlNCIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEFREDG 364
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
441-530 4.74e-09

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 57.72  E-value: 4.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488   441 GNDRYEGYCVELAAEIAKHVGYSyrLEIVsdgkygardpdTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFM 520
Cdd:smart00062  18 EDGELTGFDVDLAKAIAKELGLK--VEFV-----------EVSFDSLLTALKSGKIDVVAAGMTITPERAKQVDFSDPYY 84
                           90
                   ....*....|
gi 384381488   521 SLGISIMIKK 530
Cdd:smart00062  85 RSGQVILVRK 94
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
440-530 1.47e-08

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


Pssm-ID: 270342 [Multi-domain]  Cd Length: 219  Bit Score: 55.96  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 440 EGNDRYEGYCVELAAEIAKHVGYsyRLEIVSdgkygardpdtKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPF 519
Cdd:cd13624   17 DENGKIVGFDIDLIKAIAKEAGF--EVEFKN-----------MAFDGLIPALQSGKIDIIISGMTITEERKKSVDFSDPY 83
                         90
                 ....*....|.
gi 384381488 520 MSLGISIMIKK 530
Cdd:cd13624   84 YEAGQAIVVRK 94
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
446-530 5.52e-08

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


Pssm-ID: 270431 [Multi-domain]  Cd Length: 218  Bit Score: 54.21  E-value: 5.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 446 EGYCVELAAEIAKHVGYsyRLEIVsdgkygardpdTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGIS 525
Cdd:cd13713   23 VGFDVDVAKAIAKRLGV--KVEPV-----------TTAWDGIIAGLWAGRYDIIIGSMTITEERLKVVDFSNPYYYSGAQ 89

                 ....*
gi 384381488 526 IMIKK 530
Cdd:cd13713   90 IFVRK 94
PBP2_YxeM cd13709
Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein ...
439-538 8.37e-08

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


Pssm-ID: 270427 [Multi-domain]  Cd Length: 227  Bit Score: 53.89  E-value: 8.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGNDRYEGYCVELAAEIAKHVGYsyRLEIVsdgkygardpdTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKP 518
Cdd:cd13709   16 FKENGKLKGFEVDVWNAIGKRTGY--KVEFV-----------TADFSGLFGMLDSGKVDTIANQITITPERQEKYDFSEP 82
                         90       100
                 ....*....|....*....|
gi 384381488 519 FMSLGISIMIKKPQKSKPGV 538
Cdd:cd13709   83 YVYDGAQIVVKKDNNSIKSL 102
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
438-529 1.06e-07

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 53.98  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 438 QFEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSK 517
Cdd:PRK09495  39 EFKQGDKYVGFDIDLWAAIAKELKLDYTLKPMD-------------FSGIIPALQTKNVDLALAGITITDERKKAIDFSD 105
                         90
                 ....*....|..
gi 384381488 518 PFMSLGISIMIK 529
Cdd:PRK09495 106 GYYKSGLLVMVK 117
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
439-551 1.60e-07

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 53.57  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGND-RYEGYCVELAAEIAKHVGYSYRLEivsdgkygardpDTKaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSK 517
Cdd:PRK11260  56 FQGEDgKLTGFEVEFAEALAKHLGVKASLK------------PTK-WDGMLASLDSKRIDVVINQVTISDERKKKYDFST 122
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 384381488 518 PFMSLGISIMIKkpqKSKPGVFSFLDPLA-----------YEIWM 551
Cdd:PRK11260 123 PYTVSGIQALVK---KGNEGTIKTAADLKgkkvgvglgtnYEQWL 164
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
447-519 9.21e-07

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


Pssm-ID: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 50.93  E-value: 9.21e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 384381488 447 GYCVELAAEIAKHVGYSYRleiVSDGkygardpdtkAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPF 519
Cdd:cd13628   25 GFDIELAKTIAKKLGLKLQ---IQEY----------DFNGLIPALASGQADLALAGITPTPERKKVVDFSEPY 84
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
439-521 1.03e-06

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 51.99  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKP 518
Cdd:COG4623   36 FIYRGGPMGFEYELAKAFADYLGVKLEIIVPDN------------LDELLPALNAGEGDIAAAGLTITPERKKQVRFSPP 103

                 ...
gi 384381488 519 FMS 521
Cdd:COG4623  104 YYS 106
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
439-543 1.09e-06

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


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 50.65  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGND---RYEGYCVELAAEIAKHVGYsyRLEIVsdgkygardpdTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDF 515
Cdd:cd13629   13 FEMTDkkgELIGFDVDLAKALAKDLGV--KVEFV-----------NTAWDGLIPALQTGKFDLIISGMTITPERNLKVNF 79
                         90       100
                 ....*....|....*....|....*...
gi 384381488 516 SKPFMSLGISIMIKKPQKSKPGVFSFLD 543
Cdd:cd13629   80 SNPYLVSGQTLLVNKKSAAGIKSLEDLN 107
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
447-536 1.61e-06

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


Pssm-ID: 270430 [Multi-domain]  Cd Length: 219  Bit Score: 50.08  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 447 GYCVELAAEIAKHVGYSYRLEivsdgkygardpdTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISI 526
Cdd:cd13712   24 GFEVDVAKALAAKLGVKPEFV-------------TTEWSGILAGLQAGKYDVIINQVGITPERQKKFDFSQPYTYSGIQL 90
                         90
                 ....*....|
gi 384381488 527 MIKKPQKSKP 536
Cdd:cd13712   91 IVRKNDTRTF 100
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
439-521 1.85e-06

The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold protein superfamily; This subfamily includes the solute binding domain YfhD_N. These domains are found in the YfhD proteins that are predicted to function as lytic transglycosylases that cleave the glycosidic bond between N-acetylmuramic acid and N-acetylglucosamin in peptidoglycan, while the YfhD_N domain might act as an auxiliary or regulatory subunit. In addition to periplasmic solute binding domain, they have an SLT domain, typically found in soluble lytic transglycosylases, and a C-terminal low complexity domain. The YfhD proteins might have been recruited to create localized cell wall openings required for transport of large substrates such as DNA. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270230 [Multi-domain]  Cd Length: 223  Bit Score: 49.90  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKP 518
Cdd:cd01009   15 YIDRGGPRGFEYELAKAFADYLGVELEIVPADN------------LEELLEALEEGKGDLAAAGLTITPERKKKVDFSFP 82

                 ...
gi 384381488 519 FMS 521
Cdd:cd01009   83 YYY 85
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
36-243 3.78e-06

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: 50.11  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488  36 EVWGLFPNQQSQEHA-----AFRFALSQLTEPPKLLPQIDI-VNISDS----FEMTYRFCS-QFSKGVYAIFGFYERRTV 104
Cdd:cd06269    1 TIGALLPVHDYLESGakvlpAFELALSDVNSRPDLLPKTTLgLAIRDSecnpTQALLSACDlLAAAKVVAILGPGCSASA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 105 NMLTSFCGALHVCFIT-----PSFPVDTSNQFVLQLRPE---LQDALISIIDHYKWQKFVYIYDADR-GLSVLQKVLDTA 175
Cdd:cd06269   81 APVANLARHWDIPVLSygataPGLSDKSRYAYFLRTVPPdskQADAMLALVRRLGWNKVVLIYSDDEyGEFGLEGLEELF 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384381488 176 AEKNWQVTAV-NILTTTEEGYRMLFQDLEKKKERLVVVDCESERLNAILGQIIKLEKNGIGYHYILANL 243
Cdd:cd06269  161 QEKGGLITSRqSFDENKDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFVIDG 229
PBP2_GlnP cd13619
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ...
438-534 4.55e-06

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


Pssm-ID: 270337 [Multi-domain]  Cd Length: 220  Bit Score: 48.85  E-value: 4.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 438 QFEGND-RYEGYCVELAAEIAKHVGYSYRLeivsdgkygaRDPDtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFS 516
Cdd:cd13619   14 EFQNDDgKYVGIDVDLLNAIAKDQGFKVEL----------KPMG---FDAAIQAVQSGQADGVIAGMSITDERKKTFDFS 80
                         90
                 ....*....|....*...
gi 384381488 517 KPFMSLGISIMIKKPQKS 534
Cdd:cd13619   81 DPYYDSGLVIAVKKDNTS 98
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
439-530 6.75e-06

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


Pssm-ID: 270412 [Multi-domain]  Cd Length: 229  Bit Score: 48.12  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGNDRYEGYCVELAAEIAKHV-GYSYRLEIVSdgkygardpdTKAWNgMVGELVYGRADVAVAPLTITLVREEVIDFSK 517
Cdd:cd13694   24 VDENGKFQGFDIDLAKQIAKDLfGSGVKVEFVL----------VEAAN-RVPYLTSGKVDLILANFTVTPERAEVVDFAN 92
                         90
                 ....*....|...
gi 384381488 518 PFMSLGISIMIKK 530
Cdd:cd13694   93 PYMKVALGVVSPK 105
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
440-530 6.82e-06

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


Pssm-ID: 270406 [Multi-domain]  Cd Length: 238  Bit Score: 48.40  E-value: 6.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 440 EGNDRYEGYCVELAAEIAKHVGYSYRLEIVsDGKYGARDPDTkawngMVGELVYGRADVAVAPLTITLVREEVIDFSKPF 519
Cdd:cd13688   25 DDNGKPVGYSVDLCNAIADALKKKLALPDL-KVRYVPVTPQD-----RIPALTSGTIDLECGATTNTLERRKLVDFSIPI 98
                         90
                 ....*....|.
gi 384381488 520 MSLGISIMIKK 530
Cdd:cd13688   99 FVAGTRLLVRK 109
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
142-393 1.56e-05

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: 48.40  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 142 ALISIIDHYKWQKFVYIYDAD-RGLSV---LQKVLDtaaEKNWQVTAVNILTTTEegyrmLFQDLEKKKE---RLVVVDC 214
Cdd:cd06366  129 ARIALLKHFGWKRVATIYQNDeVFSSTaedLEELLE---EANITIVATESFSSED-----PTDQLENLKEkdaRIIIGLF 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 215 ESERLNAILGQIIKLEKNGIGYHYILanLGFMDIDLNKFKESGANVTGFQL----------------VNYTDTIPAKIMQ 278
Cdd:cd06366  201 YEDAARKVFCEAYKLGMYGPKYVWIL--PGWYDDNWWDVPDNDVNCTPEQMlealeghfstellplnPDNTKTISGLTAQ 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 279 QWKN-SDARDHTrVDWKRPKYtSALTYDGVKVMAEAFQSLRrQRIDISRRGNAGDCLANPAVPWGqgidIQRALQQVRFE 357
Cdd:cd06366  279 EFLKeYLERLSN-SNYTGSPY-APFAYDAVWAIALALNKTI-EKLAEYNKTLEDFTYNDKEMADL----FLEAMNSTSFE 351
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 384381488 358 GLTGNVQFNEKGRRTnYTLHVIEMKHDGIRKIGYWN 393
Cdd:cd06366  352 GVSGPVSFDSKGDRL-GTVDIEQLQGGSYVKVGLYD 386
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
733-791 1.84e-05

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


Pssm-ID: 270342 [Multi-domain]  Cd Length: 219  Bit Score: 46.72  E-value: 1.84e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 733 NEYIEQRKPCDTMKVGGNLDSKGYGIATPKG-SALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:cd13624  160 AYYVKQNPDKKLKIVGDPLTSEYYGIAVRKGnKELLDKINKALKKIKENGTYDKIYKKWF 219
PBP2_OccT_like cd13699
Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding ...
482-528 3.11e-05

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


Pssm-ID: 270417 [Multi-domain]  Cd Length: 211  Bit Score: 46.21  E-value: 3.11e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 384381488 482 KAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMI 528
Cdd:cd13699   48 QDWDGMIPALNAGKFDVIMDAMSITAERKKVIDFSTPYAATPNSFAV 94
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
447-535 3.28e-05

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


Pssm-ID: 270225 [Multi-domain]  Cd Length: 230  Bit Score: 46.08  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 447 GYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSkPFMSLGISI 526
Cdd:cd01004   26 GFDVDLAKAIAKRLGLKVEIVNVS-------------FDGLIPALQSGRYDIIMSGITDTPERAKQVDFV-DYMKDGLGV 91
                         90
                 ....*....|.
gi 384381488 527 MIKK--PQKSK 535
Cdd:cd01004   92 LVAKgnPKKIK 102
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
747-791 3.69e-05

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 46.28  E-value: 3.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 384381488 747 VGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWW 791
Cdd:PRK09495 198 VGDSLEAQQYGIAFPKGSELREKVNGALKTLKENGTYAEIYKKWF 242
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
446-543 5.28e-05

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


Pssm-ID: 270222 [Multi-domain]  Cd Length: 228  Bit Score: 45.75  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 446 EGYCVELAAEIAKHVGYSYRLEivsdgkygardpdTKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGIS 525
Cdd:cd01001   25 VGFDIDLANALCKRMKVKCEIV-------------TQPWDGLIPALKAGKYDAIIASMSITDKRRQQIDFTDPYYRTPSR 91
                         90
                 ....*....|....*...
gi 384381488 526 IMIKKPQKSKPGVFSFLD 543
Cdd:cd01001   92 FVARKDSPITDTTPAKLK 109
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
428-538 6.39e-05

The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding fold protein; This subfamily includes the periplasmic sensor domain of the histidine kinase receptors (HisK) which are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes. Typically, the two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. The two-component systems serve as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. Extracellular stimuli such as small molecule ligands and ions are detected by the N-terminal periplasmic sensing domain of the sensor kinase receptor, which regulate the catalytic activity of the cytoplasmic kinase domain and promote ATP-dependent autophosphorylation of a conserved histidine residue. The phosphate is then transferred to a conserved aspartate in the response regulator through a phospho-transfer mechanism, and the activity of the response regulator is in turn regulated. The sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space through their function as an initial high-affinity binding component. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270422 [Multi-domain]  Cd Length: 220  Bit Score: 45.27  E-value: 6.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 428 PYVMLkknanqfEGNDRYEGYCVELAAEIAKHVGYsyRLEIVSDgkygardpdtkAWNGMVGELVYGRADVaVAPLTITL 507
Cdd:cd13704   14 PYEFL-------DENGNPTGFNVDLLRAIAEEMGL--KVEIRLG-----------PWSEVLQALENGEIDV-LIGMAYSE 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 384381488 508 VREEVIDFSKPFMSLGISIMIKKPQKSKPGV 538
Cdd:cd13704   73 ERAKLFDFSDPYLEVSVSIFVRKGSSIINSL 103
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
429-542 7.61e-05

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


Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 45.20  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 429 YVMLKKNANQfeGNDRYEGYCVELAAEIAKHVGYSYRLEIVSDGKYGArdpdtkaWNGMVGELVYGRADVAVAPLTITLV 508
Cdd:cd13686   16 FVKVTRDPIT--NSTSVTGFCIDVFEAAVKRLPYAVPYEFIPFNDAGS-------YDDLVYQVYLKKFDAAVGDITITAN 86
                         90       100       110
                 ....*....|....*....|....*....|....
gi 384381488 509 REEVIDFSKPFMSLGISIMIkkPQKSKPGVFSFL 542
Cdd:cd13686   87 RSLYVDFTLPYTESGLVMVV--PVKDVTDIEELL 118
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
446-530 8.39e-05

The substrate binding domain of putative amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Agrobacterium tumefaciens and its related proteins. The putative Atu4678-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270414 [Multi-domain]  Cd Length: 227  Bit Score: 45.06  E-value: 8.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 446 EGYCVELAAEIAKHVGYsyRLEIVsdgkygardpDTKAWNgMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGIS 525
Cdd:cd13696   31 VGYDVDYAKDLAKALGV--KPEIV----------ETPSPN-RIPALVSGRVDVVVANTTRTLERAKTVAFSIPYVVAGMV 97

                 ....*
gi 384381488 526 IMIKK 530
Cdd:cd13696   98 VLTRK 102
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
439-543 1.58e-04

The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine kinase receptors, and related proteins; This family comprises the periplasmic sensor domain of the two-component sensor-kinase systems, such as the sensor protein BvgS of Bordetella pertussis and histidine kinase receptors (HisK), and uncharacterized related proteins. Typically, the two-component system consists of a membrane spanning sensor-kinase and a cytoplasmic response regulator. It serves as a stimulus-response coupling mechanism to enable microorganisms to sense and respond to changes in environmental conditions. The N-terminal sensing domain of the sensor kinase detects extracellular signals, such as small molecule ligands and ions, which then modulate the catalytic activity of the cytoplasmic kinase domain through a phosphorylation cascade. The periplasmic sensor domain belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 44.06  E-value: 1.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGNDRYEGYCVELAAEIAKHVGYsyRLEIVSdgkygardpdTKAWNGMVGELVYGRADVaVAPLTITLVREEVIDFSKP 518
Cdd:cd01007   18 IDEGGEPQGIAADYLKLIAKKLGL--KFEYVP----------GDSWSELLEALKAGEIDL-LSSVSKTPEREKYLLFTKP 84
                         90       100
                 ....*....|....*....|....*
gi 384381488 519 FMSLGISIMIKkpqKSKPGVFSFLD 543
Cdd:cd01007   85 YLSSPLVIVTR---KDAPFINSLSD 106
PBP2_AA_binding_like_2 cd13627
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
447-535 1.79e-04

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


Pssm-ID: 270345 [Multi-domain]  Cd Length: 243  Bit Score: 43.93  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 447 GYCVELAAEIAKHVGYsyRLEIVSdgkygardpdtKAWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISI 526
Cdd:cd13627   37 GYDVQIAKKLAEKLDM--KLVIKK-----------IEWNGLIPALNSGDIDLIIAGMSKTPEREKTIDFSDPYYISNIVM 103

                 ....*....
gi 384381488 527 MIKKPQKSK 535
Cdd:cd13627  104 VVKKDSAYA 112
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
433-523 2.12e-04

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


Pssm-ID: 270231 [Multi-domain]  Cd Length: 232  Bit Score: 43.87  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 433 KKNANQFEGNDryegycVELAAEIAKHVGYsyRLEIVSdgkygardpdtKAWNGMVGELVYGRADVAVAPLTITLVREEV 512
Cdd:cd01069   26 RDNQGQYEGYD------IDMAEALAKSLGV--KVEFVP-----------TSWPTLMDDLAADKFDIAMGGISITLERQRQ 86
                         90
                 ....*....|.
gi 384381488 513 IDFSKPFMSLG 523
Cdd:cd01069   87 AFFSAPYLRFG 97
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
304-398 2.63e-04

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


Pssm-ID: 380645 [Multi-domain]  Cd Length: 373  Bit Score: 44.14  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 304 YDGVKVMAEAFQSLRRQRIDISRRGNagdclanpavpwgqGIDIQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKH 383
Cdd:cd19990  289 YDAIWALAHAVEKLNSSGGNISVSDS--------------GKKLLEEILSTKFKGLSGEVQFVDGQLAPPPAFEIVNVIG 354
                         90
                 ....*....|....*
gi 384381488 384 DGIRKIGYWNEDDKF 398
Cdd:cd19990  355 KGYRELGFWSPGSGF 369
PBP2_Peb1a_like cd13691
Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 ...
444-535 2.70e-04

Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 periplasmic-binding protein fold; This group includes periplasmic aspartate/glutamate binding domain Peb1a and its closely related protein. The Peb1a is an important virulence factor in the food-borne human pathogen Campylobacter jejuni, which has a major role in adherence and host colonization. The Peb1a domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270409 [Multi-domain]  Cd Length: 228  Bit Score: 43.60  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 444 RYEGYCVELAAEIAKHVGYSyrleivsDGKYGARDPDTKawngmvGELV-YGRADVAVAPLTITLVREEVIDFSKPFMSL 522
Cdd:cd13691   30 KYEGMEVDLARKLAKKGDGV-------KVEFTPVTAKTR------GPLLdNGDVDAVIATFTITPERKKSYDFSTPYYTD 96
                         90
                 ....*....|...
gi 384381488 523 GISIMIKKPQKSK 535
Cdd:cd13691   97 AIGVLVEKSSGIK 109
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
442-530 2.86e-04

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


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 43.45  E-value: 2.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 442 NDRYEGYCVELAAEIAKHVGysyrleivsdgkygaRDPDTKAWNGMVGE-----LVYGRADVAVAPLTITLVREEVIDFS 516
Cdd:cd01000   27 NGKIQGFDVDVAKALAKDLL---------------GDPVKVKFVPVTSAnripaLQSGKVDLIIATMTITPERAKEVDFS 91
                         90
                 ....*....|....
gi 384381488 517 KPFMSLGISIMIKK 530
Cdd:cd01000   92 VPYYADGQGLLVRK 105
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
141-396 2.99e-04

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


Pssm-ID: 380602  Cd Length: 364  Bit Score: 44.25  E-value: 2.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 141 DALISIIDHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNI-LTTTEEGYRMLFQDLEKKKERLVVVDCESERL 219
Cdd:cd06379  125 DVWAEMLRHFEWKQVIVIHSDDQDGRALLGRLETLAETKDIKIEKVIeFEPGEKNFTSLLEEMKELQSRVILLYASEDDA 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 220 NAILGQIIKLEKNGIGYHYILANlgfmdidlnkfKESGAN-----VTGFQLVNytdtipakimqqwkNSDARDHTRvdwk 294
Cdd:cd06379  205 EIIFRDAAMLNMTGAGYVWIVTE-----------QALAASnvpdgVLGLQLIH--------------GKNESAHIR---- 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 295 rpkytsaltyDGVKVMAEAFQSLRRQRIDISRRGNagDCLANPAVpWGQGIDIQRALQQVRFE-GLTGNVQFNEKGRRTN 373
Cdd:cd06379  256 ----------DSVSVVAQAIRELFRSSENITDPPV--DCRDDTNI-WKSGQKFFRVLKSVKLSdGRTGRVEFNDKGDRIG 322
                        250       260
                 ....*....|....*....|....
gi 384381488 374 YTLHVIEMKHDGIRK-IGYWNEDD 396
Cdd:cd06379  323 AEYDIINVQNPRKLVqVGIYVGSQ 346
LivK COG0683
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ...
250-385 3.37e-04

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


Pssm-ID: 440447 [Multi-domain]  Cd Length: 314  Bit Score: 43.77  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 250 LNKFKESGANVTGFQLvNYTDTIPakIMQQWKNSDARDHTRVDW---------KRPKYTSALTYDGVKVMAEAfqsLRRq 320
Cdd:COG0683  189 LTKIKAAGPDAVFLAG-YGGDAAL--FIKQAREAGLKGPLNKAFvkaykakygREPSSYAAAGYDAALLLAEA---IEK- 261
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384381488 321 ridisrrgnAGDclANPAvpwgqgiDIQRALQQVRFEGLTGNVQFNEKGRRTNyTLHVIEMKHDG 385
Cdd:COG0683  262 ---------AGS--TDRE-------AVRDALEGLKFDGVTGPITFDPDGQGVQ-PVYIVQVKADG 307
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
444-530 3.48e-04

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


Pssm-ID: 270408 [Multi-domain]  Cd Length: 231  Bit Score: 43.03  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 444 RYEGYCVELAAEIAKHVGYS-----YRlEIVSDGKYGARDpdtkawNGMVgelvygraDVAVAPLTITLVREEVIDFSKP 518
Cdd:cd13690   30 EFEGFDVDIARAVARAIGGDepkveFR-EVTSAEREALLQ------NGTV--------DLVVATYSITPERRKQVDFAGP 94
                         90
                 ....*....|..
gi 384381488 519 FMSLGISIMIKK 530
Cdd:cd13690   95 YYTAGQRLLVRA 106
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
725-790 5.00e-04

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


Pssm-ID: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 42.46  E-value: 5.00e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384381488 725 AYLLESTMNEYIEQRKPCDTMK--VGGNLDskGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKW 790
Cdd:cd13628  154 AAIVEDIVAETFAQKKN*LLESryIPKEAD--GSAIAFPKGSPLRDDFNRWLKEMGDSGELELMVRRW 219
PBP2_SMa0082_like cd01072
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ...
446-535 1.02e-03

The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic binding protein fold; This group includes the periplamic-binding protein component of a putative amino acid ABC transporter from Sinorhizobium meliloti and its related proteins. The putative SMa0082-like domain belongs to the type 2 periplasmic binding protein fold superfamily (PBP2), whose many members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 270233 [Multi-domain]  Cd Length: 238  Bit Score: 41.86  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 446 EGYCVELAAEIAKHVGYsyRLEIVsdgkygardPDTKAwnGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGIS 525
Cdd:cd01072   36 QGYDVDVAKLLAKDLGV--KLELV---------PVTGA--NRIPYLQTGKVDMLIASLGITPERAKVVDFSQPYAAFYLG 102
                         90
                 ....*....|
gi 384381488 526 IMIKKPQKSK 535
Cdd:cd01072  103 VYGPKDAKVK 112
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
445-539 1.12e-03

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


Pssm-ID: 270214 [Multi-domain]  Cd Length: 196  Bit Score: 41.02  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 445 YEGYCVELAAEIAKHVGYSYRLEivsdgkygardpDTKAWNGMVGELVYGRADVAVAPLTITL------VREEVIDFSKP 518
Cdd:cd00648   12 YAGFAEDAAKQLAKETGIKVELV------------PGSSIGTLIEALAAGDADVAVGPIAPALeaaadkLAPGGLYIVPE 79
                         90       100
                 ....*....|....*....|.
gi 384381488 519 FMSLGISIMIKKPQKSKPGVF 539
Cdd:cd00648   80 LYVGGYVLVVRKGSSIKGLLA 100
PBP2_Ngo0372_TcyA cd13711
Substrate binding domain of ABC transporters involved in cystine import; the type 2 ...
447-530 1.30e-03

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


Pssm-ID: 270429 [Multi-domain]  Cd Length: 222  Bit Score: 41.13  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 447 GYCVELAAEIAKHVGYsyRLEIVsdgkygardpDTKaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISI 526
Cdd:cd13711   25 GFDVEVARAVAKKLGV--KVEFV----------ETQ-WDSMIAGLDAGRFDVVANQVGITDERKKKYDFSTPYIYSRAVL 91

                 ....
gi 384381488 527 MIKK 530
Cdd:cd13711   92 IVRK 95
PBP2_ml15202_like cd13701
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
483-536 2.93e-03

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


Pssm-ID: 270419 [Multi-domain]  Cd Length: 227  Bit Score: 40.14  E-value: 2.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 384381488 483 AWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKP 536
Cdd:cd13701   50 AWDGIIPALQSGKIDMIWNSMSITDERKKVIDFSDPYYETPTAIVGAKSDDRRV 103
PBP2_AA_binding_like_1 cd13625
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
743-790 3.88e-03

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


Pssm-ID: 270343 [Multi-domain]  Cd Length: 230  Bit Score: 40.05  E-value: 3.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 384381488 743 DTMKVGGNLDSKGY-GIATPKGSA-LRNPVNLAVLKLNEQGLLDKLKNKW 790
Cdd:cd13625  181 GVFALVGPVGGPTYfAWVIRKGDAeLRKAINDALLALKKSGKLAALQQKW 230
PBP2_AA_binding_like_1 cd13625
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
439-518 5.47e-03

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


Pssm-ID: 270343 [Multi-domain]  Cd Length: 230  Bit Score: 39.28  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 439 FEGNDRYEGYCVELAAEIAKHVGYSYRLEIVSdgkygardpdtkaWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKP 518
Cdd:cd13625   20 FVENGKIVGFDRDLLDEMAKKLGVKVEQQDLP-------------WSGILPGLLAGKFDMVATSVTITKERAKRFAFTLP 86
PBP1_ABC_LIVBP-like cd06342
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ...
300-379 5.73e-03

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


Pssm-ID: 380565 [Multi-domain]  Cd Length: 334  Bit Score: 39.82  E-value: 5.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384381488 300 SALTYDGVKVMAEAfqslrrqridISRRGNAgdclaNPAvpwgqgiDIQRALQQVRFEGLTGNVQFNEKGRRTN--YTLH 377
Cdd:cd06342  275 AAYAYDAAQVLLAA----------IEKAGST-----DRA-------AVAAALRATDFDGVTGTISFDAKGDLTGpaFTVY 332

                 ..
gi 384381488 378 VI 379
Cdd:cd06342  333 QV 334
 
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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