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Conserved domains on  [gi|1890342996|ref|NP_000819|]
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glutamate receptor 3 isoform 2 precursor [Homo sapiens]

Protein Classification

PBP1_iGluR_AMPA_GluR3 and PBP2_iGluR_AMPA domain-containing protein( domain architecture ID 10157275)

PBP1_iGluR_AMPA_GluR3 and PBP2_iGluR_AMPA domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
35-409 0e+00

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


:

Pssm-ID: 380610 [Multi-domain]  Cd Length: 375  Bit Score: 837.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  35 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLT 114
Cdd:cd06387     1 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 115 SFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVG 194
Cdd:cd06387    81 SFCGALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 195 NIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVN 274
Cdd:cd06387   161 NIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 275 NENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDI 354
Cdd:cd06387   241 NENPMVQQFLQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1890342996 355 ERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFS 409
Cdd:cd06387   321 ERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEYERFVPFS 375
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
422-805 5.27e-180

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: 519.22  E-value: 5.27e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNH--EQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVY 499
Cdd:cd13715     1 NRTYIVTTILEEPYVMMKKNHegEPLEGNERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARDADTGIWNGMVGELVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 500 GRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspy 579
Cdd:cd13715    81 GEADIAIAPLTITLVRERVIDFSKPFMSLGISIMIKKPV----------------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 580 ewhlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltve 659
Cdd:cd13715       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 660 rmvsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLEST 739
Cdd:cd13715   120 ----PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYDKMWEYMNSAEPSVFVRTTDEGIARVRKSKGKYAYLLEST 195
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890342996 740 MNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 805
Cdd:cd13715   196 MNEYINQRKPCDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC 261
 
Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
35-409 0e+00

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


Pssm-ID: 380610 [Multi-domain]  Cd Length: 375  Bit Score: 837.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  35 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLT 114
Cdd:cd06387     1 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 115 SFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVG 194
Cdd:cd06387    81 SFCGALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 195 NIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVN 274
Cdd:cd06387   161 NIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 275 NENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDI 354
Cdd:cd06387   241 NENPMVQQFLQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1890342996 355 ERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFS 409
Cdd:cd06387   321 ERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEYERFVPFS 375
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
422-805 5.27e-180

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: 519.22  E-value: 5.27e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNH--EQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVY 499
Cdd:cd13715     1 NRTYIVTTILEEPYVMMKKNHegEPLEGNERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARDADTGIWNGMVGELVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 500 GRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspy 579
Cdd:cd13715    81 GEADIAIAPLTITLVRERVIDFSKPFMSLGISIMIKKPV----------------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 580 ewhlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltve 659
Cdd:cd13715       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 660 rmvsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLEST 739
Cdd:cd13715   120 ----PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYDKMWEYMNSAEPSVFVRTTDEGIARVRKSKGKYAYLLEST 195
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890342996 740 MNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 805
Cdd:cd13715   196 MNEYINQRKPCDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC 261
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
554-834 2.43e-123

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: 373.57  E-value: 2.43e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 554 EIWMCIVFAYIGVSVVLFLVSRFSPYEWHlednneeprdpQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIV 633
Cdd:pfam00060   3 EVWLGILVAFLIVGVVLFLLERFSPYEWR-----------GPLETEENRFTLSNSLWFSFGALVQQGHRENPRSLSGRIV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 634 GGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSV 713
Cdd:pfam00060  72 VGVWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 714 FTKTTADGVARVRKSKGKFAFLLEstmNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDK 793
Cdd:pfam00060 152 KDALNEEGVALVRNGIYAYALLSE---NYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1890342996 794 LKNKWWYDKGECGSggGDSKDKTSALSLSNVAGVFYILVGG 834
Cdd:pfam00060 229 LEKKWWPKSGECDS--KSSASSSSQLGLKSFAGLFLILGIG 267
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
664-801 4.77e-53

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: 180.95  E-value: 4.77e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  664 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSaePSVFTKTTADGVARVRKSKgkFAFLLESTMNEY 743
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKS--PEVFVKSYAEGVQRVRVSN--YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996  744 IEQRkPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYD 801
Cdd:smart00079  77 ELSR-NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
46-391 1.76e-49

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: 178.73  E-value: 1.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  46 QEHSAFRFAVQLYNTNQNTtEKPFHLNYHVdhLDSSNSFSVTNAFCSQFSRG-VYAIFGFYDQMSMNTLTSFCGALHTSF 124
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGL-LPGTKLEYII--LDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 125 VTPSFPTDA--DVQ---FVIQMRP---ALKGAILSLLGHYKWEKFVYLY-DTERGFSILQAIMEAAVQNNWQVTARSV-- 193
Cdd:pfam01094  78 ISYGSTSPAlsDLNrypTFLRTTPsdtSQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVip 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 194 GNIKDVQEFRRIIEEMDRRqEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFT--DILLERVMHGGANITGFQ 271
Cdd:pfam01094 158 PAQDDDEIARKLLKEVKSR-ARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTslVILNPSTLEAAGGVLGFR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 272 IVNNENPMVQQFIQRWVRlDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGdclanpavPWSQG 351
Cdd:pfam01094 237 LHPPDSPEFSEFFWEKLS-DEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRACGALG--------PWNGG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1890342996 352 IDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVS 391
Cdd:pfam01094 308 QKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
434-536 1.00e-12

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 68.47  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 434 PYVMYKKNHEqlegnerYEGYCVDLAYEIAKhvRIKYKLSIVgdgkygardpETKiWNGMVGELVYGRADIAVAPLTITL 513
Cdd:COG0834    11 PFSFRDEDGK-------LVGFDVDLARAIAK--RLGLKVEFV----------PVP-WDRLIPALQSGKVDLIIAGMTITP 70
                          90       100
                  ....*....|....*....|...
gi 1890342996 514 VREEVIDFSKPFMSLGISIMIKK 536
Cdd:COG0834    71 EREKQVDFSDPYYTSGQVLLVRK 93
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
453-557 1.85e-07

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 53.57  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKHVRIKYKLSivgdgkygardpETKiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISI 532
Cdd:PRK11260   65 GFEVEFAEALAKHLGVKASLK------------PTK-WDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTVSGIQA 131
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1890342996 533 MIKkpqKSKPGVFSFLDPLA-----------YEIWM 557
Cdd:PRK11260  132 LVK---KGNEGTIKTAADLKgkkvgvglgtnYEQWL 164
 
Name Accession Description Interval E-value
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
35-409 0e+00

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


Pssm-ID: 380610 [Multi-domain]  Cd Length: 375  Bit Score: 837.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  35 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLT 114
Cdd:cd06387     1 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 115 SFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVG 194
Cdd:cd06387    81 SFCGALHTSFITPSFPTDADVQFVIQMRPALKGAILSLLAHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 195 NIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVN 274
Cdd:cd06387   161 NIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVN 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 275 NENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDI 354
Cdd:cd06387   241 NENPMVQQFLQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDI 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1890342996 355 ERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFS 409
Cdd:cd06387   321 ERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYWNEYERFVPFS 375
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit ...
36-406 0e+00

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


Pssm-ID: 380611 [Multi-domain]  Cd Length: 373  Bit Score: 541.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 115
Cdd:cd06388     2 IGGLFIRNTDQEYTAFRLAIFLHNTSPNASEAPFNLVPHVDNIETANSFAVTNAFCSQYSRGVFAIFGLYDKRSVHTLTS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 116 FCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGN 195
Cdd:cd06388    82 FCSALHISLITPSFPTEGESQFVLQLRPSLRGALLSLLDHYEWNRFVFLYDTDRGYSILQAIMEKAGQNGWQVSAICVEN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 196 IKDVQeFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNN 275
Cdd:cd06388   162 FNDAS-YRRLLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 276 ENPMVQQFIQRWVRLDEREFPEAKNAPlKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIE 355
Cdd:cd06388   241 NTPMVTKLMQRWKKLDQREYPGSETPP-KYTSALTYDGVLVMAETFRNLRRQKIDISRRGNAGDCLANPAAPWGQGIDME 319
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890342996 356 RALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFV 406
Cdd:cd06388   320 RTLKQVRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYWNDMDKLV 370
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
422-805 5.27e-180

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: 519.22  E-value: 5.27e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNH--EQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVY 499
Cdd:cd13715     1 NRTYIVTTILEEPYVMMKKNHegEPLEGNERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARDADTGIWNGMVGELVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 500 GRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspy 579
Cdd:cd13715    81 GEADIAIAPLTITLVRERVIDFSKPFMSLGISIMIKKPV----------------------------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 580 ewhlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltve 659
Cdd:cd13715       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 660 rmvsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLEST 739
Cdd:cd13715   120 ----PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYDKMWEYMNSAEPSVFVRTTDEGIARVRKSKGKYAYLLEST 195
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890342996 740 MNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 805
Cdd:cd13715   196 MNEYINQRKPCDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWYDKGEC 261
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
36-406 2.94e-174

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: 509.17  E-value: 2.94e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVQLYNTNQnttekpFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 115
Cdd:cd06389     2 IGGLFPRGADQEYSAFRVGMVQFSTSE------FRLTPHIDNLEVANSFAVTNAFCSQFSRGVYAIFGFYDKKSVNTITS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 116 FCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGN 195
Cdd:cd06389    76 FCGTLHVSFITPSFPTDGTHPFVIQMRPDLKGALLSLIEYYQWDKFAYLYDSDRGLSTLQAVLDSAAEKKWQVTAINVGN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 196 IKDVQE---FRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQI 272
Cdd:cd06389   156 INNDKKdetYRSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 273 VNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGI 352
Cdd:cd06389   236 VDYDDSLVSKFIERWSTLEEKEYPGAHTTTIKYTSALTYDAVQVMTEAFRNLRKQRIEISRRGNAGDCLANPAVPWGQGV 315
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 353 DIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFV 406
Cdd:cd06389   316 EIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYWSEVDKMV 369
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
422-805 4.34e-174

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: 504.17  E-value: 4.34e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 501
Cdd:cd13729     1 NRTYIVTTILESPYVMLKKNHEQFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETKMWNGMVGELVYGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13729    81 ADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPT------------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13729       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMN 741
Cdd:cd13729   118 -SPIESAEDLAKQTEIAYGTLDAGSTKEFFRRSKIAVFEKMWSYMKSADPSVFVKTTDEGVMRVRKSKGKYAYLLESTMN 196
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 742 EYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 805
Cdd:cd13729   197 EYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWYDKGEC 260
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
422-805 5.13e-172

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: 498.79  E-value: 5.13e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 501
Cdd:cd13727     1 NRTVVVTTIMESPYVMYKKNHEMFEGNDKFEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDPETKIWNGMVGELVYGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13727    81 AEIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQ------------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13727       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMN 741
Cdd:cd13727   118 --PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMKSAEPSVFTRTTAEGVARVRKSKGKFAFLLESTMN 195
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 742 EYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 805
Cdd:cd13727   196 EYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
36-407 1.79e-166

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: 489.07  E-value: 1.79e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVQLYNtnqntteKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 115
Cdd:cd06390     2 IGGLFPNQQSQEHAAFRFALSQLT-------EPPKLLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLTS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 116 FCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARsvgN 195
Cdd:cd06390    75 FCGALHVCFITPSFPVDTSNQFVLQLRPELQDALISVIEHYKWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAV---N 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 196 IKDVQE--FRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIV 273
Cdd:cd06390   152 ILTTTEegYRMLFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVTGFQLV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 274 NNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGID 353
Cdd:cd06390   232 NYTDTIPARIMQQWKNSDSRDLPRVDWKRPKYTSALTYDGVKVMAEAFQSLRRQRIDISRRGNAGDCLANPAVPWGQGID 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 354 IERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVP 407
Cdd:cd06390   312 IQRALQQVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDDKLVP 365
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
422-805 1.06e-164

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: 479.96  E-value: 1.06e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 501
Cdd:cd13728     1 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13728    81 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQ------------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13728       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMN 741
Cdd:cd13728   118 --PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMN 195
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 742 EYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 805
Cdd:cd13728   196 EYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
36-407 3.26e-162

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: 478.70  E-value: 3.26e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSsNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 115
Cdd:cd06380     2 IGAIFDSGEDQVQTAFRYAIDRHNSNNNNRFRLFPLTERIDITNA-DSFSVSRAICSQLSRGVFAIFGSSDASSLNTIQS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 116 FCGALHTSFVTPSFPTD---ADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQ-NNWQVTAR 191
Cdd:cd06380    81 YSDTFHMPYITPSFPKNepsDSNPFELSLRPSYIEAIVDLIRHYGWKKVVYLYDSDEGLLRLQQLYDYLKEkSNISVRVR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 192 SVGNIKDVQEFRRIIEEMDRRQE-KRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGF 270
Cdd:cd06380   161 RVRNVNDAYEFLRTLRELDREKEdKRIVLDLSSERYQKILEQIVEDGMNRRNYHYLLANLDFLDLDLERFLHGGVNITGF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 271 QIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDV----------SRRGSAGDC 340
Cdd:cd06380   241 QLVDTNNKTVKDFLQRWKKLDPREYPGAGTDTIPYEAALAVDAVLVIAEAFQSLLRQNDDIfrftfhgelyNNGSKGIDC 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996 341 LANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKV-SGSRKAGYWNEYERFVP 407
Cdd:cd06380   321 DPNPPLPWEHGKAIMKALKKVRFEGLTGNVQFDDFGQRKNYTLDVIELTSnRGLRKIGTWSEGDGFLL 388
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
422-805 7.66e-160

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: 467.58  E-value: 7.66e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 501
Cdd:cd13726     1 NKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKIWNGMVGELVYGK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13726    81 ADIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGT------------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13726       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMN 741
Cdd:cd13726   118 --PIESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSKGKYAYLLESTMN 195
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 742 EYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 805
Cdd:cd13726   196 EYIEQRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWYDKGEC 259
PBP1_iGluR_N_LIVBP-like cd06351
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
35-408 9.27e-159

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: 468.37  E-value: 9.27e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  35 SIGGLFMRNTVQEHSAFRFAVQLYNTNQNTtEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLT 114
Cdd:cd06351     1 HIGFIFEVNNEPAAKAFEVAVTYLKKNINT-RYGLSVQYDSIEANKSNAFVLLEAICNKYATGTPALILDTTKSSINSLT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 115 SFCGALHTSFVTPSFPTDAD--------VQFVIQMRP--ALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQN 184
Cdd:cd06351    80 SALGAPHISASYGQQGDLRQwrdldeakQKYLLQVRPpeALRSIVLHLNITNAWIKFVDSYDMEHYKSLLQNIQTRAVQN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 185 NWQVTARSVGNIK-------DVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILL 257
Cdd:cd06351   160 NVIVAIAKVGKREreeqldiNNFFILGTLQSIRMVLEVRPAYFERNFAWHAITQNEVEISSQSDNAHIMFMNPMAYDILL 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 258 ERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYlrrqrvdvsrrgsa 337
Cdd:cd06351   240 ETVYRDRLGLTRTTYNLNENPMVQQFIQRWVRLDEREFPEAKNAELQLSSAFYFDLALRSALAFKE-------------- 305
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1890342996 338 gdclanpavpwsqgidieralkmvqvqgmTGNIQFDTYGRRTNYTIDVYEMKVS-GSRKAGYWNEYERFVPF 408
Cdd:cd06351   306 -----------------------------TGYGTFDLQSTQPFNGHSFMKFEMDiNVRKIRGWSEYESVNSK 348
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
422-799 1.54e-145

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: 435.27  E-value: 1.54e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKiWNGMVGELVYGR 501
Cdd:cd13723     1 NRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQ-WNGMVKELIDHK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEW 581
Cdd:cd13723    80 ADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 HlednNEEPRDPQSPPdPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERM 661
Cdd:cd13723   160 Y----DAHPCNPGSEV-VENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERM 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 VSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMkSAEPSVFTKTTADGVARVRKSkgKFAFLLESTMN 741
Cdd:cd13723   235 ESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFM-SSKPSALVKNNEEGIQRALTA--DYALLMESTTI 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996 742 EYIEQRKpCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13723   312 EYVTQRN-CNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWW 368
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
35-409 9.24e-125

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: 380.17  E-value: 9.24e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  35 SIGGLFM-RNTVQEHSAFRFAVQLYNTNQNTtEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTL 113
Cdd:cd06368     1 KIGAIFNeVNDAHERAAFRYAVERLNTNIVK-LAYFRITYSIEAIDSNSHFDATDKACDLLEKGVVAIVGPSSSDSNNAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 114 TSFCGALHTSFVTPSFPTDADV-QFVIQMRP--ALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTA 190
Cdd:cd06368    80 QSICDALDVPHITVHDDPRLSKsQYSLSLYPrnQLSQAVSDLLKYWRWKRFVLVYDDDDRLRRLQELLEAARFSKRFVSV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 191 RSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDI-LLERVMHGGANITG 269
Cdd:cd06368   160 RKVDLDYKTLDETPLLKRKDCSLFSRILIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDLSLLlDLELFRYNHANITG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 270 FQIVNNeNPMVQQFIQRWVRLDEREFP----EAKNAPLKYTSALTHDAILVIAEAFRylrrqrvdvsrrgsagdclanpa 345
Cdd:cd06368   240 FQLVDN-NSMYKEDINRLAFNWSRFRQhikiESNLRGPPYEAALMFDAVLLLADAFR----------------------- 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 346 vpwsqgidieralkmvqvqgMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFS 409
Cdd:cd06368   296 --------------------RTGDLRFNGTGLRSNFTLRILELGYGGLRKIGFWDSNTRLAMNL 339
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
554-834 2.43e-123

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: 373.57  E-value: 2.43e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 554 EIWMCIVFAYIGVSVVLFLVSRFSPYEWHlednneeprdpQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIV 633
Cdd:pfam00060   3 EVWLGILVAFLIVGVVLFLLERFSPYEWR-----------GPLETEENRFTLSNSLWFSFGALVQQGHRENPRSLSGRIV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 634 GGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSV 713
Cdd:pfam00060  72 VGVWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 714 FTKTTADGVARVRKSKGKFAFLLEstmNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDK 793
Cdd:pfam00060 152 KDALNEEGVALVRNGIYAYALLSE---NYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1890342996 794 LKNKWWYDKGECGSggGDSKDKTSALSLSNVAGVFYILVGG 834
Cdd:pfam00060 229 LEKKWWPKSGECDS--KSSASSSSQLGLKSFAGLFLILGIG 267
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
422-799 8.42e-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: 371.48  E-value: 8.42e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 501
Cdd:cd13714     1 NKTLIVTTILEEPYVMLKESAKPLTGNDRFEGFCIDLLKELAKILGFNYTIRLVPDGKYGSYDPETGEWNGMVRELIDGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13714    81 ADLAVADLTITYERESVVDFTKPFMNLGISILYRKPT------------------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13714       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRksKGKFAFLLESTMN 741
Cdd:cd13714   118 --PIESADDLAKQTKIKYGTLRGGSTMTFFRDSNISTYQKMWNFMMSAKPSVFVKSNEEGVARVL--KGKYAFLMESTSI 193
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996 742 EYIEQRkPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13714   194 EYVTQR-NCNLTQIGGLLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKWW 250
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
422-799 1.35e-112

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: 348.16  E-value: 1.35e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGArdPETK-IWNGMVGELVYG 500
Cdd:cd13724     1 NTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGV--PEANgTWTGMVGELIAR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 501 RADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYE 580
Cdd:cd13724    79 KADLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 581 WHlednNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPrslsgrivggvwwfftliiissytanlaafltver 660
Cdd:cd13724   159 WY----SPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAP----------------------------------- 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 661 mvsPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSkgKFAFLLESTM 740
Cdd:cd13724   200 ---PIESVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNS--NYAFLLESTM 274
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1890342996 741 NEYIEQRKpCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13724   275 NEYYRQRN-CNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWW 332
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
422-800 5.63e-108

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: 333.00  E-value: 5.63e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHeqLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDpETKIWNGMVGELVYGR 501
Cdd:cd13685     1 NKTLRVTTILEPPFVMKKRDS--LSGNPRFEGYCIDLLEELAKILGFDYEIYLVPDGKYGSRD-ENGNWNGMIGELVRGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13685    78 ADIAVAPLTITAEREEVVDFTKPFMDTGISILMRKP-------------------------------------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13685       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKM--WSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLEST 739
Cdd:cd13685   114 -TPIESLEDLAKQSKIEYGTLKGSSTFTFFKNSKNPEYRRYeyTKIMSAMSPSVLVASAAEGVQRVRESNGGYAFIGEAT 192
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1890342996 740 MNEYIEQRkPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWY 800
Cdd:cd13685   193 SIDYEVLR-NCDLTKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGELEKLKEKWWN 252
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
427-799 5.74e-89

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: 286.89  E-value: 5.74e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 427 VTTILESPYVMYKKNheqleGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKiWNGMVGELVYGRADIAV 506
Cdd:cd13717     6 IGTVESPPFVYRDRD-----GSPIWEGYCIDLIEEISEILNFDYEIVEPEDGKFGTMDENGE-WNGLIGDLVRKEADIAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 507 APLTITLVREEVIDFSKPFMSL-GISIMIKKPqKSKPGVFSFLDPLAYEIWmcivfayigvsvvlflvsrfspyewhled 585
Cdd:cd13717    80 AALSVMAEREEVVDFTVPYYDLvGITILMKKP-ERPTSLFKFLTVLELEVW----------------------------- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 586 nneeprdpqsppdppNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPI 665
Cdd:cd13717   130 ---------------REFTLKESLWFCLTSLTPQGGGEAPKNLSGRLLVATWWLFVFIIIASYTANLAAFLTVSRLQTPV 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 666 ESAEDLAKQTEIAYGTLDSGSTKEFFRR--------------------------SKIAV--------YEKMWSYMKSAep 711
Cdd:cd13717   195 ESLDDLARQYKIQYTVVKNSSTHTYFERmknaedtlyemwkdmslndslspverAKLAVwdypvsekYTKIYQAMQEA-- 272
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 712 sVFTKTTADGVARVRKS-KGKFAFLLESTMNEYiEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGL 790
Cdd:cd13717   273 -GLVANAEEGVKRVREStSAGFAFIGDATDIKY-EILTNCDLQEVGEEFSRKPYAIAVQQGSPLKDELNYAILELQNDRF 350

                  ....*....
gi 1890342996 791 LDKLKNKWW 799
Cdd:cd13717   351 LEKLKAKWW 359
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
423-799 9.56e-80

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: 258.07  E-value: 9.56e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 423 RTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGArdPETKIWNGMVGELVYGRA 502
Cdd:cd00998     1 KTLKVVVPLEPPFVMFVTGSNAVTGNGRFEGYCIDLLKELSQSLGFTYEYYLVPDGKFGA--PVNGSWNGMVGEVVRGEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 503 DIAVAPLTITLVREEVIDFSKPFMSLGISIMIkkpqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewh 582
Cdd:cd00998    79 DLAVGPITITSERSVVIDFTQPFMTSGIGIMI------------------------------------------------ 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 583 lednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermv 662
Cdd:cd00998       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 663 sPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKsaEPSVFTKTTADGVARVRKSKGkFAFLLESTMNE 742
Cdd:cd00998   111 -PIRSIDDLKRQTDIEFGTVENSFTETFLRSSGIYPFYKTWMYSE--ARVVFVNNIAEGIERVRKGKV-YAFIWDRPYLE 186
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1890342996 743 YIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd00998   187 YYARQDPCKLIKTGGGFGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
422-799 1.37e-78

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: 255.33  E-value: 1.37e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGR 501
Cdd:cd13721     1 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAQDDVNGQWNGMVRELIDHK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13721    81 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKG-------------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13721       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSkgKFAFLLESTMN 741
Cdd:cd13721   117 -TPIDSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTS--DYAFLMESTTI 193
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996 742 EYIEQRKpCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13721   194 EFVTQRN-CNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWW 250
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
422-799 4.53e-72

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: 237.64  E-value: 4.53e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKiWNGMVGELVYGR 501
Cdd:cd13722     1 NRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFLYDVKLVPDGKYGAQNDKGE-WNGMVKELIDHR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13722    80 ADLAVAPLTITYVREKVIDFSKPFMTLGISILYRKG-------------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltverm 661
Cdd:cd13722       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 vSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSkgKFAFLLESTMN 741
Cdd:cd13722   116 -TPIDSADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVKNSDEGIQRVLTT--DYALLMESTSI 192
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996 742 EYIEQRKpCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13722   193 EYVTQRN-CNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWW 249
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
422-799 1.30e-70

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: 233.83  E-value: 1.30e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 422 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKiWNGMVGELVYGR 501
Cdd:cd13725     1 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGS-WTGMVGELINRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 502 ADIAVAPLTITLVREEVIDFSKPFMSLGISIMIkkpqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyew 581
Cdd:cd13725    80 ADLAVAAFTITAEREKVIDFSKPFMTLGISILY----------------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 582 hlednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltveRM 661
Cdd:cd13725   113 ------------------------------------------------------------------------------RV 114
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 662 VSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSkgKFAFLLESTMN 741
Cdd:cd13725   115 HMPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMN 192
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996 742 EYiEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13725   193 EY-HRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 249
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
36-400 4.55e-62

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: 213.24  E-value: 4.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVqlYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTS 115
Cdd:cd06382     2 IGGIFDEDDEDLEIAFKYAV--DRINRERTLPNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSDIVQS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 116 FCGALHTSFV--TPSFPTDADVQFVIQMRP---ALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTA 190
Cdd:cd06382    80 ICDALEIPHIetRWDPKESNRDTFTINLYPdpdALSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPKDIPITV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 191 RsvgNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGF 270
Cdd:cd06382   160 R---QLDPGDDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANITGF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 271 QIVNNENPMVQQFIQRWvRLDEREFPEAKNAPLKYT--SALTHDAILVIAEAFRylrrqrvdvsrrgsagdclanpavpw 348
Cdd:cd06382   237 RLVDPENPEVKNVLKDW-SKREKEGFNKDIGPGQITteTALMYDAVNLFANALK-------------------------- 289
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1890342996 349 sqgidieralkmvqvQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWN 400
Cdd:cd06382   290 ---------------EGLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGTWN 326
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
423-536 1.39e-57

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: 192.73  E-value: 1.39e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 423 RTIVVTTILESPYVMYKKNheqLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRA 502
Cdd:pfam10613   1 KTLIVTTILEPPFVMLKEN---LEGNDRYEGFCIDLLKELAEILGFKYEIRLVPDGKYGSLDPTTGEWNGMIGELIDGKA 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1890342996 503 DIAVAPLTITLVREEVIDFSKPFMSLGISIMIKK 536
Cdd:pfam10613  78 DLAVAPLTITSEREKVVDFTKPFMTLGISILMKK 111
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
664-801 4.77e-53

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: 180.95  E-value: 4.77e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  664 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSaePSVFTKTTADGVARVRKSKgkFAFLLESTMNEY 743
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYMKS--PEVFVKSYAEGVQRVRVSN--YAFIMESPYLDY 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996  744 IEQRkPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYD 801
Cdd:smart00079  77 ELSR-NCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
46-391 1.76e-49

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: 178.73  E-value: 1.76e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  46 QEHSAFRFAVQLYNTNQNTtEKPFHLNYHVdhLDSSNSFSVTNAFCSQFSRG-VYAIFGFYDQMSMNTLTSFCGALHTSF 124
Cdd:pfam01094   1 LVLLAVRLAVEDINADPGL-LPGTKLEYII--LDTCCDPSLALAAALDLLKGeVVAIIGPSCSSVASAVASLANEWKVPL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 125 VTPSFPTDA--DVQ---FVIQMRP---ALKGAILSLLGHYKWEKFVYLY-DTERGFSILQAIMEAAVQNNWQVTARSV-- 193
Cdd:pfam01094  78 ISYGSTSPAlsDLNrypTFLRTTPsdtSQADAIVDILKHFGWKRVALIYsDDDYGESGLQALEDALRERGIRVAYKAVip 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 194 GNIKDVQEFRRIIEEMDRRqEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFT--DILLERVMHGGANITGFQ 271
Cdd:pfam01094 158 PAQDDDEIARKLLKEVKSR-ARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTslVILNPSTLEAAGGVLGFR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 272 IVNNENPMVQQFIQRWVRlDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGdclanpavPWSQG 351
Cdd:pfam01094 237 LHPPDSPEFSEFFWEKLS-DEKELYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRACGALG--------PWNGG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1890342996 352 IDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVS 391
Cdd:pfam01094 308 QKLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNGS 347
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
427-798 4.12e-39

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: 145.47  E-value: 4.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 427 VTTILESPYVMYKKNheqlegneryEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDP-ETKIWNGMVGELVYGRADIA 505
Cdd:cd13687     6 VVTLEEAPFVYVKCC----------YGFCIDLLKKLAEDVNFTYDLYLVTDGKFGTVNKsINGEWNGMIGELVSGRADMA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 506 VAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhled 585
Cdd:cd13687    76 VASLTINPERSEVIDFSKPFKYTGITILVKKRNE---------------------------------------------- 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 586 nneeprdpqsppdppnefgifnslwfslgafmqqgcdisprsLSGrivggvwwfftliiissytanlaafLTVERMVSPI 665
Cdd:cd13687   110 ------------------------------------------LSG-------------------------INDPRLRNPS 122
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 666 ESaedlakqteIAYGTLDSGSTKEFFRRSkiavYEKMWSYMKSaepsvFTKTTA-DGVARVRksKGKF-AFLLESTMNEY 743
Cdd:cd13687   123 PP---------FRFGTVPNSSTERYFRRQ----VELMHRYMEK-----YNYETVeEAIQALK--NGKLdAFIWDSAVLEY 182
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1890342996 744 -IEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKW 798
Cdd:cd13687   183 eASQDEGCKLVTVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHESGFMEELDKKW 238
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
424-799 3.79e-36

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: 137.40  E-value: 3.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 424 TIVVTTILESPYVMYKKNheQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKiWNGMVGELVYGRAD 503
Cdd:cd13730     3 TLKVVTVLEEPFVMVAEN--ILGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGKYGHQLHNTS-WNGMIGELISKRAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 504 IAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhl 583
Cdd:cd13730    80 LAISAITITPERESVVDFSKRYMDYSVGILIKKPE--------------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 584 ednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvs 663
Cdd:cd13730       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 664 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRS------KIAVYEKMW---SYMKSAEPSVftKTTADGVARVRksKGKFAF 734
Cdd:cd13730   115 PIRTFQDLSKQVEMSYGTVRDSAVYEYFRAKgtnpleQDSTFAELWrtiSKNGGADNCV--SSPSEGIRKAK--KGNYAF 190
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1890342996 735 LLESTMNEYIE-QRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13730   191 LWDVAVVEYAAlTDDDCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKWW 256
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
424-799 2.14e-35

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: 135.35  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 424 TIVVTTILESPYVMYKKNheQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKiWNGMVGELVYGRAD 503
Cdd:cd13716     3 VLRVVTVLEEPFVMVSEN--VLGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHKYGSQQEDGT-WNGLIGELVFKRAD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 504 IAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhl 583
Cdd:cd13716    80 IGISALTITPERENVVDFTTRYMDYSVGVLLRKAE--------------------------------------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 584 ednneeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvs 663
Cdd:cd13716       --------------------------------------------------------------------------------
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 664 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKI------AVYEKMW---SYMKSAEPSVFTKTtadgvARVRKSK-GKFA 733
Cdd:cd13716   115 SIQSLQDLSKQTDIPYGTVLDSAVYEYVRSKGTnpferdSMYSQMWrmiNRSNGSENNVSESS-----EGIRKVKyGNYA 189
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890342996 734 FLLESTMNEYIEQRKP-CDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13716   190 FVWDAAVLEYVAINDDdCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 256
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
427-799 1.02e-30

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: 121.68  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 427 VTTILESPYVMYKKNheQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKiWNGMVGELVYGRADIAV 506
Cdd:cd13731     6 VVTVLEEPFVMVSEN--VLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGT-WNGLVGELVFKRADIGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 507 APLTITLVREEVIDFSKPFMSLGISIMIKKPQKskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhledn 586
Cdd:cd13731    83 SALTITPDRENVVDFTTRYMDYSVGVLLRRAES----------------------------------------------- 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 587 neeprdpqsppdppnefgifnslwfslgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvspIE 666
Cdd:cd13731   116 ------------------------------------------------------------------------------IQ 117
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 667 SAEDLAKQTEIAYGT-LDSGSTKEF-------FRRSkiAVYEKMWSYMKSAEPSvfTKTTADGVARVRKSK-GKFAFLLE 737
Cdd:cd13731   118 SLQDLSKQTDIPYGTvLDSAVYEHVrmkglnpFERD--SMYSQMWRMINRSNGS--ENNVLESQAGIQKVKyGNYAFVWD 193
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890342996 738 STMNEYIEQRKP-CDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13731   194 AAVLEYVAINDPdCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 256
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
453-798 8.35e-27

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: 111.27  E-value: 8.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISI 532
Cdd:cd13718    58 GFCIDILKKLAKDVGFTYDLYLVTNGKHGKKINGV--WNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 533 MIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvSRFSpyewHLEDNN-EEPRDpQSPPdppnefgifnslwf 611
Cdd:cd13718   136 MVARS------------------------------------NQVS----GLSDKKfQRPHD-QSPP-------------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 612 slgafmqqgcdisprslsgrivggvwwfftliiissytanlaafltvermvspiesaedlakqteIAYGTLDSGSTKEFF 691
Cdd:cd13718   161 -----------------------------------------------------------------FRFGTVPNGSTERNI 175
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 692 RRSkiavYEKMWSYMKsaepSVFTKTTADGVARVRksKGKF-AFLLESTMNEYIEQR-KPCDTMKVGGN--LDSKGYGVA 767
Cdd:cd13718   176 RNN----YPEMHQYMR----KYNQKGVEDALVSLK--TGKLdAFIYDAAVLNYMAGQdEGCKLVTIGSGkwFAMTGYGIA 245
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1890342996 768 TPKGSALRNAVNLAVLKLNEQGLLDKLKNKW 798
Cdd:cd13718   246 LQKNSKWKRPFDLALLQFRGDGELERLERLW 276
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
452-539 1.94e-26

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: 109.76  E-value: 1.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 452 EGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDP----ETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMS 527
Cdd:cd13719    50 YGYCIDLLIKLARKMNFTYELHLVADGQFGTQERvnnsNKKEWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKY 129
                          90
                  ....*....|..
gi 1890342996 528 LGISIMIKKPQK 539
Cdd:cd13719   130 QGLTILVKKEIR 141
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
434-498 1.45e-23

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: 94.62  E-value: 1.45e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1890342996  434 PYVMYKKNHEqlEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPEtKIWNGMVGELV 498
Cdd:smart00918   1 PYVMLKESPD--GGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLPN-GSWNGMVGELV 62
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
453-799 3.17e-21

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: 94.92  E-value: 3.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKHVRIKYKLSIVGDGKYGA-RDPEtkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGIS 531
Cdd:cd13720    67 GYCIDLLEKLAEDLGFDFDLYIVGDGKYGAwRNGR---WTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSLG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 532 IMIKkpqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfspyewhlednneePRDpqsppdppnefgifnslwf 611
Cdd:cd13720   144 ILVR------------------------------------------------------TRD------------------- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 612 slgafmqQGCDISPRSLSGRIVGgvwwfftliiissytanlaafltvERMVSPIESAEDlakqteiaygtldsgstkEFF 691
Cdd:cd13720   151 -------ELSGIHDPKLHHPSQG------------------------FRFGTVRESSAE------------------YYV 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 692 RRSkiavYEKMWSYMKSAEPSvftkTTADGVARVRKSKGKF-AFLLE-STMNEYIEQRKPCDTMKVGGNLDSKGYGVATP 769
Cdd:cd13720   182 KKS----FPEMHEHMRRYSLP----NTPEGVEYLKNDPEKLdAFIMDkALLDYEVSIDADCKLLTVGKPFAIEGYGIGLP 253
                         330       340       350
                  ....*....|....*....|....*....|
gi 1890342996 770 KGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13720   254 QNSPLTSNISELISQYKSNGFMDLLHDKWY 283
PBP1_iGluR_delta_2 cd06391
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta2 ...
36-400 8.82e-20

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: 92.80  E-value: 8.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVQLYNTNQNT--TEKpfhLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTL 113
Cdd:cd06391     2 IGAIFDESAKKDDEVFRTAVGDLNQNEEIlqTEK---ITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 114 TSFCGALHTSFV--------TP--SFPTDADVQ---FVIQMRPA--LKGAILSLLGHYKWEKFVYLYDTERGFSILQAIM 178
Cdd:cd06391    79 QSLADAMHIPHLfiqrstagTPrsGCGLTRSNRnddYTLSVRPPvyLNDVILRVVTEYAWQKFIIFYDSEYDIRGIQEFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 179 EAAVQNNWQVTARSV-GNIKDV--QEFRRI-IEEMDRRQE--KRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGF 252
Cdd:cd06391   159 DKVSQQGMDVALQKVeNNINKMitTLFDTMrIEELNRYRDtlRRAILVMNPATAKSFITEVVETNLVAFDCHWIIINEEI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 253 TDI-LLERVMHGGANITgfqIVNNENPMVQQFIQRWVRLDER--------EFPEAKNapLKYTSALTHDAILVIAEAFry 323
Cdd:cd06391   239 NDVdVQELVRRSIGRLT---IIRQTFPVPQNISQRCFRGNHRissslcdpKDPFAQN--MEISNLYIYDTVLLLANAF-- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 324 lRRQRVDVSRRGSAG-DCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVY-----EMKVSGSRKAG 397
Cdd:cd06391   312 -HKKLEDRKWHSMASlSCIRKNSKPWQGGRSMLETIKKGGVSGLTGLLEFGENGGNPNVHFEILgtnygEELGRGVRKLG 390

                  ...
gi 1890342996 398 YWN 400
Cdd:cd06391   391 CWN 393
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
52-399 1.98e-18

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: 88.43  E-value: 1.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  52 RFAVQLYNTNQNT-TEKPFHLNYHVD--HLDSSNSFSVTNAFCSQFSRGVYAIFG-FYDQMSMNTLTSFCGAL---HTSF 124
Cdd:cd06394    19 RLALALAREQINSiIEVPAKARVEVDifELQRDSQYETTDTMCQILPKGVVSVLGpSSSPASASTVSHICGEKeipHIKV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 125 VTPSFPTDADVQFV-IQMRPA---LKGAILSLLGHY----------KWEKFVYLYDTERGFSILQAIMeaavqnnwqvta 190
Cdd:cd06394    99 GPEETPRLQYLRFAsVSLYPSnedISLAVSRILKSFnypsaslicaKAECLLRLEELVRQFLISKETL------------ 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 191 rSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGF 270
Cdd:cd06394   167 -SVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQSNILGF 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 271 QIVNNENPMVQQFIQRwVRLDEREFPEAKNAP-LKYTSALTHDAILVIAEAFRYLRR-QRVDVSRRGSAGdclanpAVPW 348
Cdd:cd06394   246 SMFNTSHPFYLEFVRS-LNMSWRENCDASTYPgPALSSALMFDAVHVVVSAVRELNRsQEIGVKPLSCTS------AQIW 318
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1890342996 349 SQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYW 399
Cdd:cd06394   319 QHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 369
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
424-798 5.10e-18

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: 83.84  E-value: 5.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 424 TIVVTTILE-SPYVMYKKNheqlegnERYEGYCVDLAYEIAKHVRIKYKLSIVGdgkygardpetkiWNGMVGELVYGRA 502
Cdd:cd13530     1 TLRVGTDADyPPFEYIDKN-------GKLVGFDVDLANAIAKRLGVKVEFVDTD-------------FDGLIPALQSGKI 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 503 DIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPqkskpgvfsfldplayeiwmcivfayigvsvvlflvsrfSPYEWH 582
Cdd:cd13530    61 DVAISGMTITPERAKVVDFSDPYYYTGQVLVVKKD---------------------------------------SKITKT 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 583 LEDnneeprdpqsppdppnefgifnslwfslgafmqqgcdisprsLSGRIVGgvwwfftlIIISSytanlaafltvermv 662
Cdd:cd13530   102 VAD------------------------------------------LKGKKVG--------VQAGT--------------- 116
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 663 spieSAEDLAkqteiaygtldsgstKEFFRRSKIAVYEkmwsymksaepsvftkTTADGVARVRKSKGKFAFLLESTMNE 742
Cdd:cd13530   117 ----TGEDYA---------------KKNLPNAEVVTYD----------------NYPEALQALKAGRIDAVITDAPVAKY 161
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1890342996 743 YIEQRKPcDTMKVGGNLDSKGYGVATPKG-SALRNAVNLAVLKLNEQGLLDKLKNKW 798
Cdd:cd13530   162 YVKKNGP-DLKVVGEPLTPEPYGIAVRKGnPELLDAINKALAELKADGTLDKLLEKW 217
PBP1_iGluR_delta-like cd06381
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of an orphan family ...
36-400 8.09e-18

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: 86.58  E-value: 8.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVQLYNTNQN--TTEKpfhLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTL 113
Cdd:cd06381     2 IGAIFEENAAKDDRVFQLAVSDLSLNDDilQSEK---ITYSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 114 TSFCGALHTS--FV------TPSF-----PTDADVQFVIQMRPA--LKGAILSLLGHYKWEKFVYLYDTERGFSILQAIM 178
Cdd:cd06381    79 QSLTDAMHIPhlFVqrnpggSPRTachlnPSPDGEAYTLASRPPvrLNDVMLRLVTELRWQKFVMFYDSEYDIRGLQSFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 179 EAAVQNNWQVTARSV-GNIKDV--QEFRRI-IEEMDRRQE--KRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGF 252
Cdd:cd06381   159 DQASRLGLDVSLQKVdKNISHVftSLFTTMkTEELNRYRDtlRRAILLLSPQGAHSFINEAVETNLASKDSHWVFVNEEI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 253 TDILLERVMHggANITGFQIVNNENPMvQQFIQRWVRLDER--------EFPEAKNapLKYTSALTHDAILVIAEAFryl 324
Cdd:cd06381   239 SDPEILDLVH--SALGRMTVVRQIFPS-AKDNQKCFRNNHRissllcdpQEGYLQM--LQISNLYLYDSVLMLANAF--- 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 325 RRQRVDVSRRGSAG-DCLANPAVPWSQGIDIERALKMVQVQGMTG-----------NIQFDTYGrrTNYTidvyEMKVSG 392
Cdd:cd06381   311 HRKLEDRKWHSMASlNCIRKSTKPWNGGRSMLDTIKKGHITGLTGvmefredssnpYVQFEILG--TTYS----ETFGKD 384

                  ....*...
gi 1890342996 393 SRKAGYWN 400
Cdd:cd06381   385 MRKLATWD 392
PBP1_iGluR_delta_1 cd06392
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 ...
36-372 2.31e-15

N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the delta1 receptor of an orphan glutamate receptor family. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Although the delta receptors are a member of the ionotropic glutamate receptor family, they cannot be activated by AMPA, kainate, NMDA, glutamate, or any other ligands. Phylogenetic analysis shows that both GluRdelta1 and GluRalpha2 may be closer related to non-NMDA receptors. In contrast to GluRdelta2, GluRdelta1 is expressed in many areas in the developing CNS, including the hippocampus and the caudate putamen. Furthermore, recent studies have shown that the orphan GluRdelta1 plays an essential role in high-frequency hearing and ionic homeostasis in the basal cochlea and that the locus encoding GluRdelta1 may be involved in congenial or acquired high-frequency hearing loss in humans.


Pssm-ID: 380615  Cd Length: 402  Bit Score: 79.28  E-value: 2.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLFMRNTVQEHSAFRFAVQLYNTNQNT--TEKPFhlnYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTL 113
Cdd:cd06392     2 IGAIFEENAAKDDRVFQLAVSDLSLNDDIlqSEKIT---YSIKVIEANNPFQAVQEACDLMTQGILALVTSTGCASANAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 114 TSFCGALHTSFVTPSFPTDADVQFVIQMRPALKG---------------AILSLLGHYKWEKFVYLYDTERGFSILQAIM 178
Cdd:cd06392    79 QSLTDAMHIPHLFVQRNSGGSPRTACHLNPSPEGeeytlaarppvrlndVMLKLVTELRWQKFIVFYDSEYDIRGLQSFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 179 EAAVQNNWQVTARSVG-NIKDVqeFRRII-----EEMDRRQE--KRYLIDCEVERINTILEQVVILGKHSRGYHYMLANL 250
Cdd:cd06392   159 DQASRLGLDVSLQKVDrNISRV--FTNLFttmktEELNRYRDtlRRAILLLSPRGAQSFINEAVETNLASKDSHWVFVNE 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 251 GFTDI-LLERVMHGGANITgfqIVNNENPMVQQFIQRWVRLDER------EFPEAKNAPLKYTSALTHDAILVIAEAFry 323
Cdd:cd06392   237 EISDPeILELVHSALGRMT---VIRQIFPLSKDNNQRCMRNNHRissllcDPQEGYLQMLQVSNLYLYDSVLMLANAF-- 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1890342996 324 lRRQRVDVSRRGSAG-DCLANPAVPWSQGIDIERALKMVQVQGMTGNIQF 372
Cdd:cd06392   312 -HRKLEDRKWHSMASlNCIRKSTKPWNGGRSMLDTIKKGHITGLTGVMEF 360
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
434-536 1.00e-12

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


Pssm-ID: 440596 [Multi-domain]  Cd Length: 223  Bit Score: 68.47  E-value: 1.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 434 PYVMYKKNHEqlegnerYEGYCVDLAYEIAKhvRIKYKLSIVgdgkygardpETKiWNGMVGELVYGRADIAVAPLTITL 513
Cdd:COG0834    11 PFSFRDEDGK-------LVGFDVDLARAIAK--RLGLKVEFV----------PVP-WDRLIPALQSGKVDLIIAGMTITP 70
                          90       100
                  ....*....|....*....|...
gi 1890342996 514 VREEVIDFSKPFMSLGISIMIKK 536
Cdd:COG0834    71 EREKQVDFSDPYYTSGQVLLVRK 93
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
434-549 2.25e-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: 67.32  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 434 PYVMYKKNHEqlegnerYEGYCVDLAYEIAKHVRIKYKLSIVGdgkygardpetkiWNGMVGELVYGRADIAVAPLTITL 513
Cdd:pfam00497  11 PFEYVDENGK-------LVGFDVDLAKAIAKRLGVKVEFVPVS-------------WDGLIPALQSGKVDLIIAGMTITP 70
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1890342996 514 VREEVIDFSKPFMSLGISIMIKKpQKSKPGVFSFLD 549
Cdd:pfam00497  71 ERAKQVDFSDPYYYSGQVILVRK-KDSSKSIKSLAD 105
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
446-536 7.37e-12

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: 66.10  E-value: 7.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 446 EGNERYEGYCVDLAYEIAKHVRIKYKLSIVgdgkygarDPETKIwngmvGELVYGRADIAVAPLTITLVREEVIDFSKPF 525
Cdd:cd13689    26 PKTREIVGFDVDLCKAIAKKLGVKLELKPV--------NPAARI-----PELQNGRVDLVAANLTYTPERAEQIDFSDPY 92
                          90
                  ....*....|.
gi 1890342996 526 MSLGISIMIKK 536
Cdd:cd13689    93 FVTGQKLLVKK 103
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
424-536 4.92e-10

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: 60.37  E-value: 4.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 424 TIVVTTILESPYVMYKKNHEqlegnerYEGYCVDLAYEIAKHVRIKYKLsivgdgkygardpETKIWNGMVGELVYGRAD 503
Cdd:cd00994     1 TLTVATDTTFVPFEFKQDGK-------YVGFDIDLWEAIAKEAGFKYEL-------------QPMDFKGIIPALQTGRID 60
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1890342996 504 IAVAPLTITLVREEVIDFSKPFMSLGISIMIKK 536
Cdd:cd00994    61 IAIAGITITEERKKVVDFSDPYYDSGLAVMVKA 93
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
424-534 5.33e-10

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: 60.43  E-value: 5.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 424 TIVVTTILESPYVMYkknheqleGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDgkygardpetkiWNGMVGELVYGRAD 503
Cdd:cd00997     4 TLTVATVPRPPFVFY--------NDGELTGFSIDLWRAIAERLGWETEYVRVDS------------VSALLAAVAEGEAD 63
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1890342996 504 IAVAPLTITLVREEVIDFSKPFMSLGISIMI 534
Cdd:cd00997    64 IAIAAISITAEREAEFDFSQPIFESGLQILV 94
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
444-536 6.53e-09

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: 57.26  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 444 QLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVgDGKYGARDPETKIwngmvgELVY-GRADIAVAPLTITLVREEVIDFS 522
Cdd:cd13688    23 YLDDNGKPVGYSVDLCNAIADALKKKLALPDL-KVRYVPVTPQDRI------PALTsGTIDLECGATTNTLERRKLVDFS 95
                          90
                  ....*....|....
gi 1890342996 523 KPFMSLGISIMIKK 536
Cdd:cd13688    96 IPIFVAGTRLLVRK 109
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
447-536 8.96e-09

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 56.57  E-value: 8.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  447 GNERYEGYCVDLAYEIAKhvRIKYKLSIVGDGkygardpetkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFM 526
Cdd:smart00062  18 EDGELTGFDVDLAKAIAK--ELGLKVEFVEVS-----------FDSLLTALKSGKIDVVAAGMTITPERAKQVDFSDPYY 84
                           90
                   ....*....|
gi 1890342996  527 SLGISIMIKK 536
Cdd:smart00062  85 RSGQVILVRK 94
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
442-541 1.73e-08

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: 55.81  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 442 HEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGdgkygardpetkiWNGMVGELVYGRADIAVAPLTITLVREEVIDF 521
Cdd:cd13620    20 QKMKDGKNQVVGADIDIAKAIAKELGVKLEIKSMD-------------FDNLLASLQSGKVDMAISGMTPTPERKKSVDF 86
                          90       100
                  ....*....|....*....|
gi 1890342996 522 SKPFMSLGISIMIKKPQKSK 541
Cdd:cd13620    87 SDVYYEAKQSLLVKKADLDK 106
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
453-536 3.49e-08

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: 55.02  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKhvRIKYKLSIVgdgkygardpETKiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISI 532
Cdd:cd13626    24 GFDVEVGREIAK--RLGLKVEFK----------ATE-WDGLLPGLNSGKFDVIANQVTITPEREEKYLFSDPYLVSGAQI 90

                  ....
gi 1890342996 533 MIKK 536
Cdd:cd13626    91 IVKK 94
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
446-536 9.22e-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: 53.83  E-value: 9.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 446 EGNErYEGYCVDLAYEIAKhvRIKYKLSivgdgkygardPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPF 525
Cdd:cd13713    18 EDNQ-LVGFDVDVAKAIAK--RLGVKVE-----------PVTTAWDGIIAGLWAGRYDIIIGSMTITEERLKVVDFSNPY 83
                          90
                  ....*....|.
gi 1890342996 526 MSLGISIMIKK 536
Cdd:cd13713    84 YYSGAQIFVRK 94
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
443-536 1.65e-07

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: 52.88  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 443 EQLEGNERYEGYCVDLAYEIAKhvRIKYKLSIVGDGkygardpetkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFS 522
Cdd:cd13624    14 EFVDENGKIVGFDIDLIKAIAK--EAGFEVEFKNMA-----------FDGLIPALQSGKIDIIISGMTITEERKKSVDFS 80
                          90
                  ....*....|....
gi 1890342996 523 KPFMSLGISIMIKK 536
Cdd:cd13624    81 DPYYEAGQAIVVRK 94
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
453-557 1.85e-07

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 53.57  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKHVRIKYKLSivgdgkygardpETKiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISI 532
Cdd:PRK11260   65 GFEVEFAEALAKHLGVKASLK------------PTK-WDGMLASLDSKRIDVVINQVTISDERKKKYDFSTPYTVSGIQA 131
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1890342996 533 MIKkpqKSKPGVFSFLDPLA-----------YEIWM 557
Cdd:PRK11260  132 LVK---KGNEGTIKTAADLKgkkvgvglgtnYEQWL 164
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
417-535 4.31e-07

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 52.05  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 417 SASSENRTIVVTTilESPYVMYkknhEQLEGNeRYEGYCVDLAYEIAKHVRIKYKLSIVGdgkygardpetkiWNGMVGE 496
Cdd:PRK09495   19 SSHAADKKLVVAT--DTAFVPF----EFKQGD-KYVGFDIDLWAAIAKELKLDYTLKPMD-------------FSGIIPA 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1890342996 497 LVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIK 535
Cdd:PRK09495   79 LQTKNVDLALAGITITDERKKAIDFSDGYYKSGLLVMVK 117
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
447-536 8.89e-07

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: 50.81  E-value: 8.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 447 GNERYEGYCVDLAYEIAKhvrikyklSIVGDG---KYGARDPETKIwngmvGELVYGRADIAVAPLTITLVREEVIDFSK 523
Cdd:cd13694    26 ENGKFQGFDIDLAKQIAK--------DLFGSGvkvEFVLVEAANRV-----PYLTSGKVDLILANFTVTPERAEVVDFAN 92
                          90
                  ....*....|...
gi 1890342996 524 PFMSLGISIMIKK 536
Cdd:cd13694    93 PYMKVALGVVSPK 105
PBP2_YxeM cd13709
Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein ...
448-544 1.00e-06

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: 50.81  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 448 NERYEGYCVDLAYEIAKhvRIKYKLSIVgdgkygardpeTKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMS 527
Cdd:cd13709    19 NGKLKGFEVDVWNAIGK--RTGYKVEFV-----------TADFSGLFGMLDSGKVDTIANQITITPERQEKYDFSEPYVY 85
                          90
                  ....*....|....*..
gi 1890342996 528 LGISIMIKKPQKSKPGV 544
Cdd:cd13709    86 DGAQIVVKKDNNSIKSL 102
PBP2_GlnP cd13619
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ...
451-540 1.51e-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: 50.01  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 451 YEGYCVDLAYEIAKHVRIKYKLSIVGdgkygardpetkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGI 530
Cdd:cd13619    22 YVGIDVDLLNAIAKDQGFKVELKPMG-------------FDAAIQAVQSGQADGVIAGMSITDERKKTFDFSDPYYDSGL 88
                          90
                  ....*....|
gi 1890342996 531 SIMIKKPQKS 540
Cdd:cd13619    89 VIAVKKDNTS 98
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
423-541 1.60e-06

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: 50.32  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 423 RTIVVTTILESPYVMYKKNHEQLEGNEryegycVDLAYEIAKHVRIKYKLSIVGdgkygardpetkiWNGMVGELVYGRA 502
Cdd:cd01004     2 GTLTVGTNPTYPPYEFVDEDGKLIGFD------VDLAKAIAKRLGLKVEIVNVS-------------FDGLIPALQSGRY 62
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1890342996 503 DIAVAPLTITLVREEVIDFSkPFMSLGISIMIKK--PQKSK 541
Cdd:cd01004    63 DIIMSGITDTPERAKQVDFV-DYMKDGLGVLVAKgnPKKIK 102
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
438-542 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 1890342996 438 YKKNHEQLEGNEryegycVDLAYEIAKHVRIKYKLSivgdgkygardpeTKIWNGMVGELVYGRADIAVAPLTITLVREE 517
Cdd:cd13712    15 FKDETGQLTGFE------VDVAKALAAKLGVKPEFV-------------TTEWSGILAGLQAGKYDVIINQVGITPERQK 75
                          90       100
                  ....*....|....*....|....*
gi 1890342996 518 VIDFSKPFMSLGISIMIKKPQKSKP 542
Cdd:cd13712    76 KFDFSQPYTYSGIQLIVRKNDTRTF 100
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
451-536 1.23e-05

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: 47.30  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 451 YEGYCVDLAYEIAKhvrikyklSIVGDG---KYGARDPETKIWNgmvgeLVYGRADIAVAPLTITLVREEVIDFSKPFMS 527
Cdd:cd01000    30 IQGFDVDVAKALAK--------DLLGDPvkvKFVPVTSANRIPA-----LQSGKVDLIIATMTITPERAKEVDFSVPYYA 96

                  ....*....
gi 1890342996 528 LGISIMIKK 536
Cdd:cd01000    97 DGQGLLVRK 105
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
452-549 1.35e-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: 47.29  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 452 EGYCVDLAYEIAKhvRIKYKLSIVgdgkygardpeTKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGIS 531
Cdd:cd01001    25 VGFDIDLANALCK--RMKVKCEIV-----------TQPWDGLIPALKAGKYDAIIASMSITDKRRQQIDFTDPYYRTPSR 91
                          90
                  ....*....|....*...
gi 1890342996 532 IMIKKPQKSKPGVFSFLD 549
Cdd:cd01001    92 FVARKDSPITDTTPAKLK 109
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
453-549 1.54e-05

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: 47.18  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKHVRIKYKLSIVGdgkygardpetkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISI 532
Cdd:cd13629    24 GFDVDLAKALAKDLGVKVEFVNTA-------------WDGLIPALQTGKFDLIISGMTITPERNLKVNFSNPYLVSGQTL 90
                          90
                  ....*....|....*..
gi 1890342996 533 MIKKPQKSKPGVFSFLD 549
Cdd:cd13629    91 LVNKKSAAGIKSLEDLN 107
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
445-529 4.17e-05

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: 45.79  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 445 LEGNERYEGYCVDLAYEIAKhvRIKYKLSIVgdgkygardPETkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKP 524
Cdd:cd01069    26 RDNQGQYEGYDIDMAEALAK--SLGVKVEFV---------PTS--WPTLMDDLAADKFDIAMGGISITLERQRQAFFSAP 92

                  ....*
gi 1890342996 525 FMSLG 529
Cdd:cd01069    93 YLRFG 97
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
443-544 5.94e-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: 5.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 443 EQLEGNERYEGYCVDLAYEIAKhvRIKYKLSIVgdgkygardpeTKIWNGMVGELVYGRADIaVAPLTITLVREEVIDFS 522
Cdd:cd13704    16 EFLDENGNPTGFNVDLLRAIAE--EMGLKVEIR-----------LGPWSEVLQALENGEIDV-LIGMAYSEERAKLFDFS 81
                          90       100
                  ....*....|....*....|..
gi 1890342996 523 KPFMSLGISIMIKKPQKSKPGV 544
Cdd:cd13704    82 DPYLEVSVSIFVRKGSSIINSL 103
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
421-527 6.45e-05

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 46.21  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 421 ENRTIVVTTIlESPYVMYkknheqlEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDgkygardpetkiWNGMVGELVYG 500
Cdd:COG4623    20 ERGVLRVLTR-NSPTTYF-------IYRGGPMGFEYELAKAFADYLGVKLEIIVPDN------------LDELLPALNAG 79
                          90       100
                  ....*....|....*....|....*..
gi 1890342996 501 RADIAVAPLTITLVREEVIDFSKPFMS 527
Cdd:COG4623    80 EGDIAAAGLTITPERKKQVRFSPPYYS 106
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
450-536 7.80e-05

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: 44.95  E-value: 7.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 450 RYEGYCVDLAYEIAKhvrikyklSIVGDGK--------YGARdpETKIWNGMVgelvygraDIAVAPLTITLVREEVIDF 521
Cdd:cd13690    30 EFEGFDVDIARAVAR--------AIGGDEPkvefrevtSAER--EALLQNGTV--------DLVVATYSITPERRKQVDF 91
                          90
                  ....*....|....*
gi 1890342996 522 SKPFMSLGISIMIKK 536
Cdd:cd13690    92 AGPYYTAGQRLLVRA 106
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
424-525 7.86e-05

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: 44.77  E-value: 7.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 424 TIVVTTILESPYVMYKknheqlEGNER-YEGYCVDLAYEIAKHVRIKYKLSiVGDgkygardpetkiWNGMVGELVYGRA 502
Cdd:cd13628     1 TLNMGTSPDYPPFEFK------IGDRGkIVGFDIELAKTIAKKLGLKLQIQ-EYD------------FNGLIPALASGQA 61
                          90       100
                  ....*....|....*....|...
gi 1890342996 503 DIAVAPLTITLVREEVIDFSKPF 525
Cdd:cd13628    62 DLALAGITPTPERKKVVDFSEPY 84
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
755-799 1.04e-04

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 44.74  E-value: 1.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1890342996 755 VGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:PRK09495  198 VGDSLEAQQYGIAFPKGSELREKVNGALKTLKENGTYAEIYKKWF 242
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
741-799 1.42e-04

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: 44.02  E-value: 1.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 741 NEYIEQRKPCDTMKVGGNLDSKGYGVATPKG-SALRNAVNLAVLKLNEQGLLDKLKNKWW 799
Cdd:cd13624   160 AYYVKQNPDKKLKIVGDPLTSEYYGIAVRKGnKELLDKINKALKKIKENGTYDKIYKKWF 219
PBP2_OccT_like cd13699
Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding ...
490-534 2.30e-04

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: 43.52  E-value: 2.30e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1890342996 490 WNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMI 534
Cdd:cd13699    50 WDGMIPALNAGKFDVIMDAMSITAERKKVIDFSTPYAATPNSFAV 94
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
446-527 2.77e-04

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: 43.35  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 446 EGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDgkygardpetkiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPF 525
Cdd:cd01009    16 IDRGGPRGFEYELAKAFADYLGVELEIVPADN------------LEELLEALEEGKGDLAAAGLTITPERKKKVDFSFPY 83

                  ..
gi 1890342996 526 MS 527
Cdd:cd01009    84 YY 85
PBP2_Peb1a_like cd13691
Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 ...
450-541 2.78e-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: 43.21  E-value: 2.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 450 RYEGYCVDLAYEIAKhvrikyklsiVGDG---KYGARDPETKiwngmvGELV-YGRADIAVAPLTITLVREEVIDFSKPF 525
Cdd:cd13691    30 KYEGMEVDLARKLAK----------KGDGvkvEFTPVTAKTR------GPLLdNGDVDAVIATFTITPERKKSYDFSTPY 93
                          90
                  ....*....|....*.
gi 1890342996 526 MSLGISIMIKKPQKSK 541
Cdd:cd13691    94 YTDAIGVLVEKSSGIK 109
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
452-536 3.04e-04

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: 43.14  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 452 EGYCVDLAYEIAKhvRIKYKLSIVgdgkygardpETKIWNgMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGIS 531
Cdd:cd13696    31 VGYDVDYAKDLAK--ALGVKPEIV----------ETPSPN-RIPALVSGRVDVVVANTTRTLERAKTVAFSIPYVVAGMV 97

                  ....*
gi 1890342996 532 IMIKK 536
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 ...
443-549 3.35e-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: 42.91  E-value: 3.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 443 EQLEGNERYEGYCVDLAYEIAKHVRIKYKLSivgdgkygardpETKIWNGMVGELVYGRADIaVAPLTITLVREEVIDFS 522
Cdd:cd01007    16 EFIDEGGEPQGIAADYLKLIAKKLGLKFEYV------------PGDSWSELLEALKAGEIDL-LSSVSKTPEREKYLLFT 82
                          90       100
                  ....*....|....*....|....*..
gi 1890342996 523 KPFMSLGISIMIKkpqKSKPGVFSFLD 549
Cdd:cd01007    83 KPYLSSPLVIVTR---KDAPFINSLSD 106
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
663-798 3.91e-04

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


Pssm-ID: 270406 [Multi-domain]  Cd Length: 238  Bit Score: 43.01  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 663 SPIESAEDLAKQTeiaYGTLDSGSTKEFFRRskiaVYEKMWSYMKSaepsVFTKTTADGVARVRKSKGKfAFLLEST--M 740
Cdd:cd13688   111 SGLNSLEDLAGKT---VGVTAGTTTEDALRT----VNPLAGLQASV----VPVKDHAEGFAALETGKAD-AFAGDDIllA 178
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1890342996 741 NEYIEQRKPCDTMKVGGNLDSKGYGVATPKG-SALRNAVNLAVLKLNEQGLLDKLKNKW 798
Cdd:cd13688   179 GLAARSKNPDDLALIPRPLSYEPYGLMLRKDdPDFRLLVDRALAQLYQSGEIEKLYDKW 237
PBP2_ArtJ cd00999
The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold ...
648-798 7.05e-04

The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold protein superfamily; An arginine-binding protein found in Chlamydiae trachomatis (CT-ArtJ) and pneumoniae (CPn-ArtJ) and its closely related proteins. CT- and CPn-ArtJ are shown to have different immunogenic properties despite a high sequence similarity. The ArtJ proteins display the type 2 periplasmic binding fold organized in two alpha-beta domains with arginine-binding region at their interface.


Pssm-ID: 270220 [Multi-domain]  Cd Length: 223  Bit Score: 41.93  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 648 YTANLAAFLTVERmVSPIESAEDLAKQTeiayGTLDSGSTKEFFRRSkiavyekmwsyMKSAEPSVFTKTTaDGVARVRK 727
Cdd:cd00999    87 YGESVSAFVTVSD-NPIKPSLEDLKGKS----VAVQTGTIQEVFLRS-----------LPGVEVKSFQKTD-DCLREVVL 149
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890342996 728 SKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSK--GYGVATPKGS-ALRNAVNLAVLKLNEQGLLDKLKNKW 798
Cdd:cd00999   150 GRSDAAVMDPTVAKVYLKSKDFPGKLATAFTLPEWglGKALAVAKDDpALKEAVNKALDELKKEGELAALRKKW 223
PBP2_AA_binding_like_2 cd13627
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
453-541 9.78e-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: 42.00  E-value: 9.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKhvrikyKLSivgdgkygaRDPE-TKI-WNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGI 530
Cdd:cd13627    37 GYDVQIAKKLAE------KLD---------MKLViKKIeWNGLIPALNSGDIDLIIAGMSKTPEREKTIDFSDPYYISNI 101
                          90
                  ....*....|.
gi 1890342996 531 SIMIKKPQKSK 541
Cdd:cd13627   102 VMVVKKDSAYA 112
PBP1_glutamate_receptors-like cd06269
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ...
36-320 1.15e-03

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


Pssm-ID: 380493 [Multi-domain]  Cd Length: 332  Bit Score: 42.02  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  36 IGGLF-----MRNTVQEHSAFRFAVQLYNTNQNTTEKpFHLNY-HVDHldSSNSFSVTNAFCS-QFSRGVYAIFGFYDQM 108
Cdd:cd06269     2 IGALLpvhdyLESGAKVLPAFELALSDVNSRPDLLPK-TTLGLaIRDS--ECNPTQALLSACDlLAAAKVVAILGPGCSA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 109 SMNTLTSFCGALHT---SFVTPS--FPTDADVQFVIQMRPA---LKGAILSLLGHYKWEKFVYLY-DTERGFSILQAIME 179
Cdd:cd06269    79 SAAPVANLARHWDIpvlSYGATApgLSDKSRYAYFLRTVPPdskQADAMLALVRRLGWNKVVLIYsDDEYGEFGLEGLEE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 180 AAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLAN-----LGFTD 254
Cdd:cd06269   159 LFQEKGGLITSRQSFDENKDDDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFVIDgeassSDEHG 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1890342996 255 ILLERVMHGganITGFQIVNNENPMVQQFIQRWVRLDEREFP-EAKNAPLKYTSALTHDAILVIAEA 320
Cdd:cd06269   239 DEARQAAEG---AITVTLIFPVVKEFLKFSMELKLKSSKRKQgLNEEYELNNFAAFFYDAVLADRPG 302
PBP2_AA_binding_like_1 cd13625
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
751-798 1.39e-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: 41.21  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1890342996 751 DTMKVGGNLDSKGY-GVATPKGSA-LRNAVNLAVLKLNEQGLLDKLKNKW 798
Cdd:cd13625   181 GVFALVGPVGGPTYfAWVIRKGDAeLRKAINDALLALKKSGKLAALQQKW 230
PBP2_Ngo0372_TcyA cd13711
Substrate binding domain of ABC transporters involved in cystine import; the type 2 ...
453-536 1.44e-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: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 453 GYCVDLAYEIAKH--VRIKYKlsivgdgkygardpETKiWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGI 530
Cdd:cd13711    25 GFDVEVARAVAKKlgVKVEFV--------------ETQ-WDSMIAGLDAGRFDVVANQVGITDERKKKYDFSTPYIYSRA 89

                  ....*.
gi 1890342996 531 SIMIKK 536
Cdd:cd13711    90 VLIVRK 95
PBP1_SAP_GC-like cd06370
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ...
148-254 1.67e-03

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


Pssm-ID: 380593 [Multi-domain]  Cd Length: 400  Bit Score: 41.85  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 148 AILSLLGHYKWEKFVYLYDTERGFS-ILQAIMEAAVQNNWQVTAR------SVGNIKDVQEFRRIIEEMdrrQEKrylid 220
Cdd:cd06370   127 SVIALLKHFNWNKVSIVYENETKWSkIADTIKELLELNNIEINHEeyfpdpYPYTTSHGNPFDKIVEET---KEK----- 198
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1890342996 221 cevERIntileqVVILGKHSRGYHYMLA--NLGFTD 254
Cdd:cd06370   199 ---TRI------YVFLGDYSLLREFMYYaeDLGLLD 225
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
717-798 2.76e-03

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: 40.30  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 717 TTADGVARVRKSKGKFAFLLESTMNEYIEQRKpcDTMKVGG--NLDSKGYGVATPKGS-ALRNAVNLAVLKLNEQGLLDK 793
Cdd:cd01004   146 DQADALQALRSGRADAYLSDSPTAAYAVKQSP--GKLELVGevFGSPAPIGIAVKKDDpALADAVQAALNALIADGTYKK 223

                  ....*
gi 1890342996 794 LKNKW 798
Cdd:cd01004   224 ILKKW 228
PBP2_Arg_3 cd13622
Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding ...
425-526 3.62e-03

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


Pssm-ID: 270340 [Multi-domain]  Cd Length: 222  Bit Score: 39.98  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 425 IVVTTILESPYVMYKKNHEqlegnerYEGYCVDLAYEIAKhvRIKYKLsivgdgKYGARDPEtkiwnGMVGELVYGRADI 504
Cdd:cd13622     5 IVGVGKFNPPFEMQGTNNE-------LFGFDIDLMNEICK--RIQRTC------QYKPMRFD-----DLLAALNNGKVDV 64
                          90       100
                  ....*....|....*....|..
gi 1890342996 505 AVAPLTITLVREEVIDFSKPFM 526
Cdd:cd13622    65 AISSISITPERSKNFIFSLPYL 86
Periplasmic_Binding_Protein_Type_2 cd00648
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
451-545 5.35e-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: 39.09  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 451 YEGYCVDLAYEIAKHVRIKYKLSIVGDgkygardpetkiWNGMVGELVYGRADIAVAPLTITL------VREEVIDFSKP 524
Cdd:cd00648    12 YAGFAEDAAKQLAKETGIKVELVPGSS------------IGTLIEALAAGDADVAVGPIAPALeaaadkLAPGGLYIVPE 79
                          90       100
                  ....*....|....*....|.
gi 1890342996 525 FMSLGISIMIKKPQKSKPGVF 545
Cdd:cd00648    80 LYVGGYVLVVRKGSSIKGLLA 100
PBP2_AatB_like cd00996
Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong ...
737-798 5.55e-03

Polar amino acids-binding domain of ATP-binding cassette transporter-like systems that belong to the type 2 periplasmic binding fold protein superfamily; This subfamily includes periplasmic binding domain of ATP-binding cassette transporter-like systems that serve as initial receptors in the ABC transport of amino acids and their derivatives in eubacteria. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically-located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The Abp proteins belong to the PBPI 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: 270217 [Multi-domain]  Cd Length: 227  Bit Score: 39.48  E-value: 5.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890342996 737 ESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGS-ALRNAVNLAVLKLNEQGLLDKLKNKW 798
Cdd:cd00996   163 EVYARYYIKKKPLDDYKILDESFGSEEYGVGFRKEDtELKEKINKALDEMKADGTAAKISQKW 225
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
61-383 6.65e-03

ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of membrane guanylyl-cyclase receptors. Membrane guanylyl cyclases (GC) have a single membrane-spanning region and are activated by endogenous and exogenous peptides. This family can be divided into three major subfamilies: the natriuretic peptide receptors (NPRs), sensory organ-specific membrane GCs, and the enterotoxin/guanylin receptors. The binding of peptide ligands to the receptor results in the activation of the cytosolic catalytic domain. Three types of NPRs have been cloned from mammalian tissues: NPR-A/GC-A, NPR-B/ GC-B, and NPR-C. In addition, two of the GCs, GC-D and GC-G, appear to be pseudogenes in humans. Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are produced in the heart, and both bind to the NPR-A. NPR-C, also termed the clearance receptor, binds each of the natriuretic peptides and can alter circulating levels of these peptides. The ligand binding domain of the NPRs exhibits strong structural similarity to the type 1 periplasmic binding fold protein family.


Pssm-ID: 380575 [Multi-domain]  Cd Length: 391  Bit Score: 40.03  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996  61 NQNTTEKPFH-LNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFG---FYDQMSMNTLTSF-------CGALHTSFVTPS- 128
Cdd:cd06352    32 NSEGLLLPGFnFEFTYRDSCCDESEAVGAAADLIYKRNVDVFIGpacSAAADAVGRLATYwnipiitWGAVSASFLDKSr 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 129 FPTdadvqfVIQMRPALKG---AILSLLGHYKWEKFVYLYDTE--RGFSILQAImEAAVQNNWQVTARSVG--NIKDVQE 201
Cdd:cd06352   112 YPT------LTRTSPNSLSlaeALLALLKQFNWKRAAIIYSDDdsKCFSIANDL-EDALNQEDNLTISYYEfvEVNSDSD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 202 FRRIIEEMDRRqekrylidcevERIntileqVVIL--GKHSRgyHYMLA--NLGFTD-----ILLERVMHG-GANITGFQ 271
Cdd:cd06352   185 YSSILQEAKKR-----------ARI------IVLCfdSETVR--QFMLAahDLGMTNgeyvfIFIELFKDGfGGNSTDGW 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 272 IVNNE---------------------NPMVQQFIQRwVRLDEREFP----EAKNAPLKYTSALTHDAILVIAEAFRylrr 326
Cdd:cd06352   246 ERNDGrdedakqayesllvislsrpsNPEYDNFSKE-VKARAKEPPfycyDASEEEVSPYAAALYDAVYLYALALN---- 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1890342996 327 qrvdvsRRGSAGDCLANpavpwsqGIDIERALKMVQVQGMTGNIQFDTYG-RRTNYTI 383
Cdd:cd06352   321 ------ETLAEGGNYRN-------GTAIAQRMWNRTFQGITGPVTIDSNGdRDPDYAL 365
PBP1_ABC_LivK_ligand_binding-like cd06347
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
263-373 7.09e-03

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


Pssm-ID: 380570 [Multi-domain]  Cd Length: 334  Bit Score: 39.45  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 263 GGANITGFQIVN-----NENPMVQQFIQRWvrldEREFPEAKNAPlkytSALTHDAILVIAEAfrylrrqrvdVSRRGSa 337
Cdd:cd06347   235 GGDAVEGVYFTThfspdDPSPEVQEFVKAY----KAKYGEPPNAF----AALGYDAVMLLADA----------IKRAGS- 295
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1890342996 338 gdclanpavpwSQGIDIERAL-KMVQVQGMTGNIQFD 373
Cdd:cd06347   296 -----------TDPEAIRDALaKTKDFEGVTGTITFD 321
PBP2_SMa0082_like cd01072
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ...
452-541 7.70e-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: 39.17  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890342996 452 EGYCVDLAYEIAKHVRIKYKLSIVGDGkygARDPEtkiwngmvgeLVYGRADIAVAPLTITLVREEVIDFSKPFMSLGIS 531
Cdd:cd01072    36 QGYDVDVAKLLAKDLGVKLELVPVTGA---NRIPY----------LQTGKVDMLIASLGITPERAKVVDFSQPYAAFYLG 102
                          90
                  ....*....|
gi 1890342996 532 IMIKKPQKSK 541
Cdd:cd01072   103 VYGPKDAKVK 112
 
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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