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Conserved domains on  [gi|160298215|ref|NP_032194|]
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glutamate receptor ionotropic, kainate 5 isoform 1 precursor [Mus musculus]

Protein Classification

PBP1_iGluR_Kainate_KA1_2 and Periplasmic_Binding_Protein_Type_2 domain-containing protein( domain architecture ID 10157301)

PBP1_iGluR_Kainate_KA1_2 and Periplasmic_Binding_Protein_Type_2 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
23-401 0e+00

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: 765.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  23 SLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPAS 102
Cdd:cd06394    1 SLRMAAILDDQTVCGRGERLALALAREQINSIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 103 ASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFL 182
Cdd:cd06394   81 ASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDISLAVSRILKSFNYPSASLICAKAECLLRLEELVRQFL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 183 ISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSS 262
Cdd:cd06394  161 ISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 263 NILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPH 342
Cdd:cd06394  241 NILGFSMFNTSHPFYLEFVRSLNMSWRENCDASTYPGPALSSALMFDAVHVVVSAVRELNRSQEIGVKPLSCTSAQIWQH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 160298215 343 GTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNA 401
Cdd:cd06394  321 GTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNA 379
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
414-784 0e+00

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.


The actual alignment was detected with superfamily member cd13724:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 333  Bit Score: 572.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 493
Cdd:cd13724    1 NTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWY 573
Cdd:cd13724   81 DLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 NPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPralstrcvsgvwwaftliiissytanlaafltvqrmevPVE 653
Cdd:cd13724  161 SPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAP--------------------------------------PIE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLN 733
Cdd:cd13724  203 SVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRN 282
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 734 CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE 784
Cdd:cd13724  283 CNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWE 333
 
Name Accession Description Interval E-value
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
23-401 0e+00

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: 765.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  23 SLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPAS 102
Cdd:cd06394    1 SLRMAAILDDQTVCGRGERLALALAREQINSIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 103 ASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFL 182
Cdd:cd06394   81 ASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDISLAVSRILKSFNYPSASLICAKAECLLRLEELVRQFL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 183 ISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSS 262
Cdd:cd06394  161 ISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 263 NILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPH 342
Cdd:cd06394  241 NILGFSMFNTSHPFYLEFVRSLNMSWRENCDASTYPGPALSSALMFDAVHVVVSAVRELNRSQEIGVKPLSCTSAQIWQH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 160298215 343 GTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNA 401
Cdd:cd06394  321 GTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNA 379
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
414-784 0e+00

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: 572.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 493
Cdd:cd13724    1 NTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWY 573
Cdd:cd13724   81 DLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 NPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPralstrcvsgvwwaftliiissytanlaafltvqrmevPVE 653
Cdd:cd13724  161 SPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAP--------------------------------------PIE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLN 733
Cdd:cd13724  203 SVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRN 282
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 734 CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE 784
Cdd:cd13724  283 CNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWE 333
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
543-814 4.38e-101

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: 317.33  E-value: 4.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  543 SPAVWLFMLLAYLAVSCVLFLAARLSPYEWYNPHPCLrarphilENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSG 622
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPLETE-------ENRFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  623 VWWAFTLIIISSYTANLAAFLTVQRMEVPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFV 702
Cdd:pfam00060  74 VWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  703 KSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKW 782
Cdd:pfam00060 154 ALNEEGVALVRNGIYAYALLSENYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKW 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 160298215  783 WEG-GRCPKEEDHRAK-GLGMENIGGIFVVLICG 814
Cdd:pfam00060 234 WPKsGECDSKSSASSSsQLGLKSFAGLFLILGIG 267
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
651-785 2.53e-55

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: 187.50  E-value: 2.53e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215   651 PVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMqsKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHR 730
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYM--KSPEVFVKSYAEGVQRVRVSNYAFIMESPYLDYEL 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 160298215   731 RLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEG 785
Cdd:smart00079  79 SRNCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
40-379 1.83e-50

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: 181.81  E-value: 1.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215   40 ERLALALAREQINGIIEVPAKARVEVDIfelqRDSQYETTDTM--CQILPKG-VVSVLGPSSSPASAsTVSHICGEKEIP 116
Cdd:pfam01094   2 VLLAVRLAVEDINADPGLLPGTKLEYII----LDTCCDPSLALaaALDLLKGeVVAIIGPSCSSVAS-AVASLANEWKVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  117 HIKVG---PEETPRLQYLRFasVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAE-CLLRLEELV-----RGFLISKET 187
Cdd:pfam01094  77 LISYGstsPALSDLNRYPTF--LRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDyGESGLQALEdalreRGIRVAYKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  188 LSVRMLDDSRDPTPLLKEIRDdKVSTIIIDANASISHLVLRKASELGMTSAFYKYILT---TMDFPILHLDGIvEDSSNI 264
Cdd:pfam01094 155 VIPPAQDDDEIARKLLKEVKS-RARVIVVCCSSETARRLLKAARELGMMGEGYVWIATdglTTSLVILNPSTL-EAAGGV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  265 LGFSMFNTSHPFYPEFVRSLNMSWRENCEaSTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVkplACTSANIWPHGT 344
Cdd:pfam01094 233 LGFRLHPPDSPEFSEFFWEKLSDEKELYE-NLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGR---ACGALGPWNGGQ 308
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 160298215  345 SLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILE 379
Cdd:pfam01094 309 KLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILN 343
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
432-526 3.43e-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: 66.93  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNERFEGFCVDMLRELAELLrfryrlrlvedGLygAPEP-NGSWTGMVGELINRKADLAVAAFTITAEREKVI 510
Cdd:COG0834   10 PPFSFRDEDGKLVGFDVDLARAIAKRL-----------GL--KVEFvPVPWDRLIPALQSGKVDLIIAGMTITPEREKQV 76
                         90
                 ....*....|....*.
gi 160298215 511 DFSKPFMTLGISILYR 526
Cdd:COG0834   77 DFSDPYYTSGQVLLVR 92
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
408-526 1.72e-05

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 47.41  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 408 LSQTLANKTLVVTtiLENPYvmrrP--NFQALSGneRFEGFCVDMLRELAEllrfryrlrlvEDGLYGAPEPNgSWTGMV 485
Cdd:PRK11260  34 LNKVKERGTLLVG--LEGTY----PpfSFQGEDG--KLTGFEVEFAEALAK-----------HLGVKASLKPT-KWDGML 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 160298215 486 GELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYR 526
Cdd:PRK11260  94 ASLDSKRIDVVINQVTISDERKKKYDFSTPYTVSGIQALVK 134
 
Name Accession Description Interval E-value
PBP1_iGluR_Kainate_KA1_2 cd06394
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the KA1 and KA2 ...
23-401 0e+00

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: 765.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  23 SLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPAS 102
Cdd:cd06394    1 SLRMAAILDDQTVCGRGERLALALAREQINSIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 103 ASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFL 182
Cdd:cd06394   81 ASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDISLAVSRILKSFNYPSASLICAKAECLLRLEELVRQFL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 183 ISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSS 262
Cdd:cd06394  161 ISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLILKKASELGMTSAFYKYILTTMDFPLLHLDGIVDDQS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 263 NILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPH 342
Cdd:cd06394  241 NILGFSMFNTSHPFYLEFVRSLNMSWRENCDASTYPGPALSSALMFDAVHVVVSAVRELNRSQEIGVKPLSCTSAQIWQH 320
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 160298215 343 GTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNA 401
Cdd:cd06394  321 GTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNA 379
PBP2_iGluR_kainate_KA1 cd13724
The ligand-binding domain of the kainate subtype KA1 of ionotropic glutamate receptors, a ...
414-784 0e+00

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: 572.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 493
Cdd:cd13724    1 NTTLVVTTILENPYLMLKGNHQEMEGNDRYEGFCVDMLKELAEILRFNYKIRLVGDGVYGVPEANGTWTGMVGELIARKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWY 573
Cdd:cd13724   81 DLAVAGLTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPGVWLFMLLAYLAVSCVLFLVARLTPYEWY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 NPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPralstrcvsgvwwaftliiissytanlaafltvqrmevPVE 653
Cdd:cd13724  161 SPHPCAQGRCNLLVNQYSLGNSLWFPVGGFMQQGSTIAP--------------------------------------PIE 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLN 733
Cdd:cd13724  203 SVDDLADQTAIEYGTIHGGSSMTFFQNSRYQTYQRMWNYMYSKQPSVFVKSTEEGIARVLNSNYAFLLESTMNEYYRQRN 282
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 734 CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE 784
Cdd:cd13724  283 CNLTQIGGLLDTKGYGIGMPVGSVFRDEFDLAILQLQENNRLEILKRKWWE 333
PBP2_iGluR_Kainate_GluR7 cd13723
GluR7 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
414-783 2.10e-170

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: 501.91  E-value: 2.10e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 493
Cdd:cd13723    1 NRSLIVTTVLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWY 573
Cdd:cd13723   81 DLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 NPHPClRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPVE 653
Cdd:cd13723  161 DAHPC-NPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPID 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKqPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLN 733
Cdd:cd13723  240 SADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSK-PSALVKNNEEGIQRALTADYALLMESTTIEYVTQRN 318
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 160298215 734 CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 783
Cdd:cd13723  319 CNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWW 368
PBP2_iGluR_kainate_KA2 cd13725
The ligand-binding domain of the kainate subtype KA2 of ionotropic glutamate receptors, a ...
414-784 7.33e-148

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: 438.76  E-value: 7.33e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 493
Cdd:cd13725    1 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRVhmgrkpgyfsfldpfspavwlfmllaylavscvlflaarlspyewy 573
Cdd:cd13725   81 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRV---------------------------------------------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 nphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmEVPVE 653
Cdd:cd13725  115 ---------------------------------------------------------------------------HMPVE 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLN 733
Cdd:cd13725  120 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLN 199
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 734 CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE 784
Cdd:cd13725  200 CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE 250
PBP2_iGluR_Kainate cd13714
Kainate receptor of the type 2 periplasmic-binding fold superfamily; This group contains ...
414-784 5.91e-137

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: 410.39  E-value: 5.91e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEP-NGSWTGMVGELINRK 492
Cdd:cd13714    1 NKTLIVTTILEEPYVMLKESAKPLTGNDRFEGFCIDLLKELAKILGFNYTIRLVPDGKYGSYDPeTGEWNGMVRELIDGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMgrkpgyfsfldpfspavwlfmllaylavscvlflaarlspyew 572
Cdd:cd13714   81 ADLAVADLTITYERESVVDFTKPFMNLGISILYRKPT------------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 573 ynphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmevPV 652
Cdd:cd13714  118 ------------------------------------------------------------------------------PI 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 653 ESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRL 732
Cdd:cd13714  120 ESADDLAKQTKIKYGTLRGGSTMTFFRDSNISTYQKMWNFMMSAKPSVFVKSNEEGVARVLKGKYAFLMESTSIEYVTQR 199
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 160298215 733 NCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE 784
Cdd:cd13714  200 NCNLTQIGGLLDSKGYGIATPKGSPYRDKLSLAILKLQEKGKLEMLKNKWWK 251
PBP1_iGluR_non_NMDA-like cd06368
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ...
25-401 2.52e-112

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: 349.74  E-value: 2.52e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  25 RMAAILDDqtVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGpSSSPASAS 104
Cdd:cd06368    1 KIGAIFNE--VNDAHERAAFRYAVERLNTNIVKLAYFRITYSIEAIDSNSHFDATDKACDLLEKGVVAIVG-PSSSDSNN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 105 TVSHICGEKEIPHIKVGPEETPRLQylrFASVSLYPSNEdVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFLIS 184
Cdd:cd06368   78 ALQSICDALDVPHITVHDDPRLSKS---QYSLSLYPRNQ-LSQAVSDLLKYWRWKRFVLVYDDDDRLRRLQELLEAARFS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 185 KETLSVRMLDDS---RDPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPIL-HLDGIVED 260
Cdd:cd06368  154 KRFVSVRKVDLDyktLDETPLLKRKDCSLFSRILIDLSPEKAYTFLLQALEMGMTIELYHYFLTTMDLSLLlDLELFRYN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 261 SSNILGFSMFNTsHPFYPEFVRSLNMSWRENCE----ASTYPGPALSAALMFDAVHVVVSAVRElnrsqeigvkplacts 336
Cdd:cd06368  234 HANITGFQLVDN-NSMYKEDINRLAFNWSRFRQhikiESNLRGPPYEAALMFDAVLLLADAFRR---------------- 296
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160298215 337 aniwphgtslmnylrmveydglTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNA 401
Cdd:cd06368  297 ----------------------TGDLRFNGTGLRSNFTLRILELGYGGLRKIGFWDSNTRLAMNL 339
PBP2_iGluR_AMPA cd13715
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
414-788 1.32e-102

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: 321.23  E-value: 1.32e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNF--QALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEP-NGSWTGMVGELIN 490
Cdd:cd13715    1 NRTYIVTTILEEPYVMMKKNHegEPLEGNERYEGYCVDLADEIAKHLGIKYELRIVKDGKYGARDAdTGIWNGMVGELVR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 491 RKADLAVAAFTITAEREKVIDFSKPFMTLGISIlyrvhMGRKPgyfsfldpfspavwlfmllaylavscvlflaarlspy 570
Cdd:cd13715   81 GEADIAIAPLTITLVRERVIDFSKPFMSLGISI-----MIKKP------------------------------------- 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 571 ewynphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmeV 650
Cdd:cd13715  119 -------------------------------------------------------------------------------V 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 651 PVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMNEY 728
Cdd:cd13715  120 PIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYDKMWEYMNSAEPSVFVRTTDEGIARVRKSkgKYAYLLESTMNEY 199
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160298215 729 -HRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW-EGGRC 788
Cdd:cd13715  200 iNQRKPCDTMKVGGNLDSKGYGIATPKGSPLRNPLNLAVLKLKENGELDKLKNKWWyDKGEC 261
Lig_chan pfam00060
Ligand-gated ion channel; This family includes the four transmembrane regions of the ...
543-814 4.38e-101

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: 317.33  E-value: 4.38e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  543 SPAVWLFMLLAYLAVSCVLFLAARLSPYEWYNPHPCLrarphilENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSG 622
Cdd:pfam00060   1 SLEVWLGILVAFLIVGVVLFLLERFSPYEWRGPLETE-------ENRFTLSNSLWFSFGALVQQGHRENPRSLSGRIVVG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  623 VWWAFTLIIISSYTANLAAFLTVQRMEVPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFV 702
Cdd:pfam00060  74 VWWFFALILLSSYTANLAAFLTVERMQSPIQSLEDLAKQTKIEYGTVRGSSTYLFFRNSKIPSYKRMWEYMESAKPSVKD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  703 KSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKW 782
Cdd:pfam00060 154 ALNEEGVALVRNGIYAYALLSENYYLFQRECCDTMIVGETFATGGYGIATPKGSPLTDLLSLAILELEESGELDKLEKKW 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 160298215  783 WEG-GRCPKEEDHRAK-GLGMENIGGIFVVLICG 814
Cdd:pfam00060 234 WPKsGECDSKSSASSSsQLGLKSFAGLFLILGIG 267
PBP2_iGluR_non_NMDA_like cd13685
The ligand-binding domain of non-NMDA (N-methyl-D-aspartate) type ionotropic glutamate ...
414-784 7.34e-100

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: 313.35  E-value: 7.34e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNfqALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 493
Cdd:cd13685    1 NKTLRVTTILEPPFVMKKRD--SLSGNPRFEGYCIDLLEELAKILGFDYEIYLVPDGKYGSRDENGNWNGMIGELVRGEA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRvhmgrKPgyfsfldpfspavwlfmllaylavscvlflaarlspyewy 573
Cdd:cd13685   79 DIAVAPLTITAEREEVVDFTKPFMDTGISILMR-----KP---------------------------------------- 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 nphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmeVPVE 653
Cdd:cd13685  114 ----------------------------------------------------------------------------TPIE 117
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRM--WNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMNEYH 729
Cdd:cd13685  118 SLEDLAKQSKIEYGTLKGSSTFTFFKNSKNPEYRRYeyTKIMSAMSPSVLVASAAEGVQRVRESngGYAFIGEATSIDYE 197
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 160298215 730 RRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWE 784
Cdd:cd13685  198 VLRNCDLTKVGEVFSEKGYGIAVQQGSPLRDELSLAILELQESGELEKLKEKWWN 252
PBP2_iGluR_Kainate_GluR6 cd13721
GluR6 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
414-783 2.35e-91

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: 290.77  E-value: 2.35e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGA-PEPNGSWTGMVGELINRK 492
Cdd:cd13721    1 NRSLIVTTILEEPYVLFKKSDKPLYGNDRFEGYCIDLLRELSTILGFTYEIRLVEDGKYGAqDDVNGQWNGMVRELIDHK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISILYRvhmgrKPGyfsfldpfspavwlfmllaylavscvlflaarlspyew 572
Cdd:cd13721   81 ADLAVAPLAITYVREKVIDFSKPFMTLGISILYR-----KGT-------------------------------------- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 573 ynphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmevPV 652
Cdd:cd13721  118 ------------------------------------------------------------------------------PI 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 653 ESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRL 732
Cdd:cd13721  120 DSADDLAKQTKIEYGAVEDGATMTFFKKSKISTYDKMWAFMSSRRQSVLVKSNEEGIQRVLTSDYAFLMESTTIEFVTQR 199
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 733 NCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 783
Cdd:cd13721  200 NCNLTQIGGLIDSKGYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWW 250
PBP2_iGluR_putative cd13717
The ligand-binding domain of putative ionotropic glutamate receptors, a member of the type 2 ...
419-783 1.77e-88

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


Pssm-ID: 270435 [Multi-domain]  Cd Length: 360  Bit Score: 287.27  E-value: 1.77e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 419 VTTILENPYVMRRPNfqalsGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLAVA 498
Cdd:cd13717    6 IGTVESPPFVYRDRD-----GSPIWEGYCIDLIEEISEILNFDYEIVEPEDGKFGTMDENGEWNGLIGDLVRKEADIALA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 499 AFTITAEREKVIDFSKPFMTL-GISIlyrvhMGRKP----GYFSFLDPFSPAVWlfmllaylavscvlflaarlspyewy 573
Cdd:cd13717   81 ALSVMAEREEVVDFTVPYYDLvGITI-----LMKKPerptSLFKFLTVLELEVW-------------------------- 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 nphpclrarphileNQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPVE 653
Cdd:cd13717  130 --------------REFTLKESLWFCLTSLTPQGGGEAPKNLSGRLLVATWWLFVFIIIASYTANLAAFLTVSRLQTPVE 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRY----------------------------------QTYQRMWNYMQSkqpS 699
Cdd:cd13717  196 SLDDLARQYKIQYTVVKNSSTHTYFERMKNaedtlyemwkdmslndslspveraklavwdypvsEKYTKIYQAMQE---A 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 700 VFVKSTEEGIARVLNS---RYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLE 776
Cdd:cd13717  273 GLVANAEEGVKRVREStsaGFAFIGDATDIKYEILTNCDLQEVGEEFSRKPYAIAVQQGSPLKDELNYAILELQNDRFLE 352

                 ....*..
gi 160298215 777 ILKRKWW 783
Cdd:cd13717  353 KLKAKWW 359
PBP2_iGluR_Kainate_GluR5 cd13722
GluR5 subtype of kainate receptor, type 2 periplasmic-binding fold superfamily; This group ...
414-783 3.05e-87

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: 280.01  E-value: 3.05e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKA 493
Cdd:cd13722    1 NRTLIVTTILEEPYVMYRKSDKPLYGNDRFEGYCLDLLKELSNILGFLYDVKLVPDGKYGAQNDKGEWNGMVKELIDHRA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRvhmgrKPGyfsfldpfspavwlfmllaylavscvlflaarlspyewy 573
Cdd:cd13722   81 DLAVAPLTITYVREKVIDFSKPFMTLGISILYR-----KGT--------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 nphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmevPVE 653
Cdd:cd13722  117 -----------------------------------------------------------------------------PID 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 SADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLN 733
Cdd:cd13722  120 SADDLAKQTKIEYGAVRDGSTMTFFKKSKISTYEKMWAFMSSRQQTALVKNSDEGIQRVLTTDYALLMESTSIEYVTQRN 199
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 160298215 734 CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 783
Cdd:cd13722  200 CNLTQIGGLIDSKGYGVGTPIGSPYRDKITIAILQLQEEGKLHMMKEKWW 249
PBP2_iGluR_AMPA_GluR1 cd13729
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
414-788 1.03e-81

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: 265.35  E-value: 1.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNG-SWTGMVGELINRK 492
Cdd:cd13729    1 NRTYIVTTILESPYVMLKKNHEQFEGNDRYEGYCVELAAEIAKHVGYSYKLEIVSDGKYGARDPETkMWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISIlyrvhMGRKPgyfsfldpfspavwlfmllaylavscvlflaarlspyew 572
Cdd:cd13729   81 ADVAVAPLTITLVREEVIDFSKPFMSLGISI-----MIKKP--------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 573 ynphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmEVPV 652
Cdd:cd13729  117 ----------------------------------------------------------------------------TSPI 120
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 653 ESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMNEY-H 729
Cdd:cd13729  121 ESAEDLAKQTEIAYGTLDAGSTKEFFRRSKIAVFEKMWSYMKSADPSVFVKTTDEGVMRVRKSkgKYAYLLESTMNEYiE 200
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 730 RRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW-EGGRC 788
Cdd:cd13729  201 QRKPCDTMKVGGNLDSKGYGIATPKGSALRNPVNLAVLKLNEQGLLDKLKNKWWyDKGEC 260
PBP2_iGluR_AMPA_GluR4 cd13727
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
414-788 3.63e-76

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: 250.34  E-value: 3.63e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGS-WTGMVGELINRK 492
Cdd:cd13727    1 NRTVVVTTIMESPYVMYKKNHEMFEGNDKFEGYCVDLASEIAKHIGIKYKIAIVPDGKYGARDPETKiWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISIlyrvhMGRKPgyfsfldpfspavwlfmllaylavscvlflaarlspyew 572
Cdd:cd13727   81 AEIAVAPLTITLVREEVIDFSKPFMSLGISI-----MIKKP--------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 573 ynphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmeVPV 652
Cdd:cd13727  117 -----------------------------------------------------------------------------QPI 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 653 ESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMNEY-H 729
Cdd:cd13727  120 ESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMKSAEPSVFTRTTAEGVARVRKSkgKFAFLLESTMNEYiE 199
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 730 RRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW-EGGRC 788
Cdd:cd13727  200 QRKPCDTMKVGGNLDSKGYGVATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWyDKGEC 259
PBP2_iGluR_AMPA_GluR2 cd13726
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
414-788 1.70e-73

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: 243.01  E-value: 1.70e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGS-WTGMVGELINRK 492
Cdd:cd13726    1 NKTVVVTTILESPYVMMKKNHEMLEGNERYEGYCVDLAAEIAKHCGFKYKLTIVGDGKYGARDADTKiWNGMVGELVYGK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISIlyrvhMGRKPgyfsfldpfspavwlfmllaylavscvlflaarlspyew 572
Cdd:cd13726   81 ADIAIAPLTITLVREEVIDFSKPFMSLGISI-----MIKKG--------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 573 ynphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmeVPV 652
Cdd:cd13726  117 -----------------------------------------------------------------------------TPI 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 653 ESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMNEY-H 729
Cdd:cd13726  120 ESAEDLSKQTEIAYGTLDSGSTKEFFRRSKIAVFDKMWTYMRSAEPSVFVRTTAEGVARVRKSkgKYAYLLESTMNEYiE 199
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 730 RRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW-EGGRC 788
Cdd:cd13726  200 QRKPCDTMKVGGNLDSKGYGIATPKGSSLGNAVNLAVLKLNEQGLLDKLKNKWWyDKGEC 259
PBP2_iGluR_AMPA_GluR3 cd13728
The ligand-binding domain of the AMPA (alpha-amino-3-hydroxyl-5-methyl-4-isoxazolepropionic ...
414-788 1.96e-71

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: 237.28  E-value: 1.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 414 NKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEP-NGSWTGMVGELINRK 492
Cdd:cd13728    1 NRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPeTKIWNGMVGELVYGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISIlyrvhMGRKPgyfsfldpfspavwlfmllaylavscvlflaarlspyew 572
Cdd:cd13728   81 ADIAVAPLTITLVREEVIDFSKPFMSLGISI-----MIKKP--------------------------------------- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 573 ynphpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmeVPV 652
Cdd:cd13728  117 -----------------------------------------------------------------------------QPI 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 653 ESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNS--RYAFLLESTMNEY-H 729
Cdd:cd13728  120 ESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSkgKFAFLLESTMNEYiE 199
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 730 RRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW-EGGRC 788
Cdd:cd13728  200 QRKPCDTMKVGGNLDSKGYGVATPKGSALGNAVNLAVLKLNEQGLLDKLKNKWWyDKGEC 259
PBP2_iGluR_ligand_binding cd00998
The ligand-binding domain of ionotropic glutamate receptor family, a member of the periplasmic ...
415-783 4.34e-60

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: 205.30  E-value: 4.34e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 415 KTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEpNGSWTGMVGELINRKAD 494
Cdd:cd00998    1 KTLKVVVPLEPPFVMFVTGSNAVTGNGRFEGYCIDLLKELSQSLGFTYEYYLVPDGKFGAPV-NGSWNGMVGEVVRGEAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 495 LAVAAFTITAEREKVIDFSKPFMTLGISILyrvhmgrkpgyfsfldpfspavwlfmllaylavscvlflaarlspyewyn 574
Cdd:cd00998   80 LAVGPITITSERSVVIDFTQPFMTSGIGIM-------------------------------------------------- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 575 phpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmeVPVES 654
Cdd:cd00998  110 ---------------------------------------------------------------------------IPIRS 114
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 655 ADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMqsKQPSVFVKSTEEGIARVLNSR-YAFLLESTMNEYH-RRL 732
Cdd:cd00998  115 IDDLKRQTDIEFGTVENSFTETFLRSSGIYPFYKTWMYS--EARVVFVNNIAEGIERVRKGKvYAFIWDRPYLEYYaRQD 192
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 733 NCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 783
Cdd:cd00998  193 PCKLIKTGGGFGSIGYGFALPKNSPLTNDLSTAILKLVESGVLQKLKNKWL 243
PBP1_iGluR_Kainate cd06382
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ...
25-397 7.38e-58

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: 202.45  E-value: 7.38e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  25 RMAAILDDQtvcGRGERLALALAREQINgIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPASAs 104
Cdd:cd06382    1 RIGGIFDED---DEDLEIAFKYAVDRIN-RERTLPNTKLVPDIERVPRDDSFEASKKVCELLEEGVAAIFGPSSPSSSD- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 105 TVSHICGEKEIPHIKVGPEETPRLQylRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFLIS 184
Cdd:cd06382   76 IVQSICDALEIPHIETRWDPKESNR--DTFTINLYPDPDALSKAYADLVKSLNWKSFTILYEDDEGLIRLQELLKLPKPK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 185 KETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNI 264
Cdd:cd06382  154 DIPITVRQLDPGDDYRPVLKEIKKSGETRIILDCSPDRLVDVLKQAQQVGMLTEYYHYILTNLDLHTLDLEPFKYSGANI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 265 LGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYPGP-ALSAALMFDAVHVVVSAVRElnrsqeigvkplactsaniwphg 343
Cdd:cd06382  234 TGFRLVDPENPEVKNVLKDWSKREKEGFNKDIGPGQiTTETALMYDAVNLFANALKE----------------------- 290
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 160298215 344 tslmnylrmveydGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTL 397
Cdd:cd06382  291 -------------GLTGPIKFDEEGQRTDFKLDILELTEGGLVKVGTWNPTDGL 331
PBPe smart00079
Eukaryotic homologues of bacterial periplasmic substrate binding proteins; Prokaryotic ...
651-785 2.53e-55

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: 187.50  E-value: 2.53e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215   651 PVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMqsKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHR 730
Cdd:smart00079   1 PITSVEDLAKQTKIEYGTQDGSSTLAFFKRSGNPEYSRMWPYM--KSPEVFVKSYAEGVQRVRVSNYAFIMESPYLDYEL 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 160298215   731 RLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEG 785
Cdd:smart00079  79 SRNCDLMTVGEEFGRKGYGIAFPKGSPLRDDLSRAILKLSESGELEKLRNKWWKD 133
Lig_chan-Glu_bd pfam10613
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
415-527 5.00e-52

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: 177.33  E-value: 5.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  415 KTLVVTTILENPYVMRRPNfqaLSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAP-EPNGSWTGMVGELINRKA 493
Cdd:pfam10613   1 KTLIVTTILEPPFVMLKEN---LEGNDRYEGFCIDLLKELAEILGFKYEIRLVPDGKYGSLdPTTGEWNGMIGELIDGKA 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 160298215  494 DLAVAAFTITAEREKVIDFSKPFMTLGISILYRV 527
Cdd:pfam10613  78 DLAVAPLTITSEREKVVDFTKPFMTLGISILMKK 111
ANF_receptor pfam01094
Receptor family ligand binding region; This family includes extracellular ligand binding ...
40-379 1.83e-50

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: 181.81  E-value: 1.83e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215   40 ERLALALAREQINGIIEVPAKARVEVDIfelqRDSQYETTDTM--CQILPKG-VVSVLGPSSSPASAsTVSHICGEKEIP 116
Cdd:pfam01094   2 VLLAVRLAVEDINADPGLLPGTKLEYII----LDTCCDPSLALaaALDLLKGeVVAIIGPSCSSVAS-AVASLANEWKVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  117 HIKVG---PEETPRLQYLRFasVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAE-CLLRLEELV-----RGFLISKET 187
Cdd:pfam01094  77 LISYGstsPALSDLNRYPTF--LRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDyGESGLQALEdalreRGIRVAYKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  188 LSVRMLDDSRDPTPLLKEIRDdKVSTIIIDANASISHLVLRKASELGMTSAFYKYILT---TMDFPILHLDGIvEDSSNI 264
Cdd:pfam01094 155 VIPPAQDDDEIARKLLKEVKS-RARVIVVCCSSETARRLLKAARELGMMGEGYVWIATdglTTSLVILNPSTL-EAAGGV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  265 LGFSMFNTSHPFYPEFVRSLNMSWRENCEaSTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVkplACTSANIWPHGT 344
Cdd:pfam01094 233 LGFRLHPPDSPEFSEFFWEKLSDEKELYE-NLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGR---ACGALGPWNGGQ 308
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 160298215  345 SLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILE 379
Cdd:pfam01094 309 KLLRYLKNVNFTGLTGNVQFDENGDRINPDYDILN 343
PBP2_iGluR_delta_1 cd13730
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-1, a member of the ...
416-783 1.73e-43

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: 158.58  E-value: 1.73e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 416 TLVVTTILENPYVMRRPNFqaLSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADL 495
Cdd:cd13730    3 TLKVVTVLEEPFVMVAENI--LGQPKRYKGFSIDVLDALAKALGFKYEIYQAPDGKYGHQLHNTSWNGMIGELISKRADL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 496 AVAAFTITAEREKVIDFSKPFMTLGISILYrvhmgRKPGyfsfldpfspavwlfmllaylavscvlflaarlspyewynp 575
Cdd:cd13730   81 AISAITITPERESVVDFSKRYMDYSVGILI-----KKPE----------------------------------------- 114
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 576 hpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmevPVESA 655
Cdd:cd13730  115 ---------------------------------------------------------------------------PIRTF 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 656 DDLADQTNIEYGTIHAGSTMTFFQNS------RYQTYQRMWNYMQSKQPS-VFVKSTEEGIARVLNSRYAFLLESTMNEY 728
Cdd:cd13730  120 QDLSKQVEMSYGTVRDSAVYEYFRAKgtnpleQDSTFAELWRTISKNGGAdNCVSSPSEGIRKAKKGNYAFLWDVAVVEY 199
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 160298215 729 HRRLN--CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 783
Cdd:cd13730  200 AALTDddCSVTVIGNSISSKGYGIALQHGSPYRDLFSQRILELQDTGDLDVLKQKWW 256
PBP2_iGluR_delta_like cd13716
The ligand-binding domain of the delta family of ionotropic glutamate receptors, a member of ...
416-783 2.58e-41

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: 152.69  E-value: 2.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 416 TLVVTTILENPYVMRRPNFqaLSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADL 495
Cdd:cd13716    3 VLRVVTVLEEPFVMVSENV--LGKPKKYQGFSIDVLDALANYLGFKYEIYVAPDHKYGSQQEDGTWNGLIGELVFKRADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 496 AVAAFTITAEREKVIDFSKPFMTLGISILYrvhmgRKPgyfsfldpfspavwlfmllaylavscvlflaarlspyewynp 575
Cdd:cd13716   81 GISALTITPERENVVDFTTRYMDYSVGVLL-----RKA------------------------------------------ 113
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 576 hpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmeVPVESA 655
Cdd:cd13716  114 --------------------------------------------------------------------------ESIQSL 119
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 656 DDLADQTNIEYGTIHAGSTMTFFQNS------RYQTYQRMW-NYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEY 728
Cdd:cd13716  120 QDLSKQTDIPYGTVLDSAVYEYVRSKgtnpfeRDSMYSQMWrMINRSNGSENNVSESSEGIRKVKYGNYAFVWDAAVLEY 199
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 160298215 729 hRRLN---CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 783
Cdd:cd13716  200 -VAINdddCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 256
PBP2_iGluR_NMDA cd13687
The ligand-binding domain of the NMDA (N-methyl-D-aspartate) subtype of ionotropic glutamate ...
417-782 3.03e-38

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: 143.16  E-value: 3.03e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 417 LVVTTILENPYVMRRPNfqalsgnerfEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEP--NGSWTGMVGELINRKAD 494
Cdd:cd13687    4 LKVVTLEEAPFVYVKCC----------YGFCIDLLKKLAEDVNFTYDLYLVTDGKFGTVNKsiNGEWNGMIGELVSGRAD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 495 LAVAAFTITAEREKVIDFSKPFMTLGISIlyrvhMGRKPGYFSFL-DPfspavwlfmllaylavscvlflaaRLSpyewy 573
Cdd:cd13687   74 MAVASLTINPERSEVIDFSKPFKYTGITI-----LVKKRNELSGInDP------------------------RLR----- 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 574 NPHPCLRarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmevpve 653
Cdd:cd13687  120 NPSPPFR------------------------------------------------------------------------- 126
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 654 saddladqtnieYGTIHAGSTMTFFQNSRYQTYQRMWNYMQskqpsvfvKSTEEGIARVLNSRY-AFLLESTMNEYHRR- 731
Cdd:cd13687  127 ------------FGTVPNSSTERYFRRQVELMHRYMEKYNY--------ETVEEAIQALKNGKLdAFIWDSAVLEYEASq 186
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 160298215 732 -LNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKW 782
Cdd:cd13687  187 dEGCKLVTVGSLFARSGYGIGLQKNSPWKRNVSLAILQFHESGFMEELDKKW 238
PBP1_iGluR_AMPA cd06380
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ...
62-391 8.71e-37

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: 143.19  E-value: 8.71e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  62 RVEVDIfeLQRDSqYETTDTMCQILPKGVVSVLGPSSSPASAsTVSHICGEKEIPHIKVGPEETPRLQYLRFAsVSLYPS 141
Cdd:cd06380   38 TERIDI--TNADS-FSVSRAICSQLSRGVFAIFGSSDASSLN-TIQSYSDTFHMPYITPSFPKNEPSDSNPFE-LSLRPS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 142 NED--VSLAVSRILKSFNYPSASlicakAECLLRLEELVRgFLISKETLSV--RMLDDSRDPTPLLKEIRD----DKVST 213
Cdd:cd06380  113 YIEaiVDLIRHYGWKKVVYLYDS-----DEGLLRLQQLYD-YLKEKSNISVrvRRVRNVNDAYEFLRTLREldreKEDKR 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 214 IIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFYpefvRSLNMSWRENCE 293
Cdd:cd06380  187 IVLDLSSERYQKILEQIVEDGMNRRNYHYLLANLDFLDLDLERFLHGGVNITGFQLVDTNNKTV----KDFLQRWKKLDP 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 294 AsTYPGPALS-----AALMFDAVHVVVSAVREL---NRSQEI----------GVKPLACTSANIWP--HGTSLMNYLRMV 353
Cdd:cd06380  263 R-EYPGAGTDtipyeAALAVDAVLVIAEAFQSLlrqNDDIFRftfhgelynnGSKGIDCDPNPPLPweHGKAIMKALKKV 341
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 160298215 354 EYDGLTGRVEFNSKGQRTNYTLRILE-KSRQGHREIGVW 391
Cdd:cd06380  342 RFEGLTGNVQFDDFGQRKNYTLDVIElTSNRGLRKIGTW 380
PBP2_iGluR_delta_2 cd13731
The ligand-binding domain of an orphan ionotropic glutamate receptor delta-2, a member of the ...
417-783 3.92e-32

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


Pssm-ID: 270449 [Multi-domain]  Cd Length: 257  Bit Score: 125.91  E-value: 3.92e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 417 LVVTTILENPYVMRRPNfqALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLA 496
Cdd:cd13731    4 LRVVTVLEEPFVMVSEN--VLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 497 VAAFTITAEREKVIDFSKPFMTLGISILYRvhmgrkpgyfsfldpfspavwlfmllaylavscvlflaarlspyewynph 576
Cdd:cd13731   82 ISALTITPDRENVVDFTTRYMDYSVGVLLR-------------------------------------------------- 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 577 pclrarphilenqytlgnslwfpvggfmqqgseimpRALStrcvsgvwwaftliiissytanlaafltvqrmevpVESAD 656
Cdd:cd13731  112 ------------------------------------RAES-----------------------------------IQSLQ 120
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 657 DLADQTNIEYGTIHAGST--------MTFFQnsRYQTYQRMW-NYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNE 727
Cdd:cd13731  121 DLSKQTDIPYGTVLDSAVyehvrmkgLNPFE--RDSMYSQMWrMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLE 198
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 160298215 728 Y--HRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWW 783
Cdd:cd13731  199 YvaINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQNGDMDILKHKWW 256
PBP2_iGluR_NMDA_Nr1 cd13719
The ligand-binding domain of the NR1 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
415-789 9.40e-29

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: 116.69  E-value: 9.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 415 KTLVVTTILENPYVMRRP----------------NFQALSGNERF---EGFCVDMLRELAELLRFRYRLRLVEDGLYGAP 475
Cdd:cd13719    2 THLKIVTIHEEPFVYVRPtpsdgtcreeftvncpNFNISGRPTVPfccYGYCIDLLIKLARKMNFTYELHLVADGQFGTQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 476 EP-NGS----WTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYrvhmgRKPGYFSFLDPfspavwlfm 550
Cdd:cd13719   82 ERvNNSnkkeWNGMMGELVSGRADMIVAPLTINPERAQYIEFSKPFKYQGLTILV-----KKEIRLTGIND--------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 551 llaylavscvlflaARLSpyewyNPhpclrarphilenqytlgnslwfpvggfmqqgseimpralstrcvsgvwwaftli 630
Cdd:cd13719  148 --------------PRLR-----NP------------------------------------------------------- 153
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 631 iissytanlaafltvqrMEvpvesaddladqtNIEYGTIHAGSTMTFFQnsRYQTYQRMWNYMQSKQpsvfVKSTEEGIA 710
Cdd:cd13719  154 -----------------SE-------------KFIYATVKGSSVDMYFR--RQVELSTMYRHMEKHN----YETAEEAIQ 197
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 711 RVLNSR-YAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEGGRCP 789
Cdd:cd13719  198 AVRDGKlHAFIWDSSRLEFEASQDCDLVTAGELFGRSGYGIGLQKNSPWTDNVSLAILKMHESGFMEDLDKTWIRYQECE 277
PBP2_iGluR_NMDA_Nr2 cd13718
The ligand-binding domain of the NR2 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
445-785 4.94e-23

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: 100.10  E-value: 4.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 445 GFCVDMLRELAELLRFRYRLRLVEDGLYGAPEpNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISIl 524
Cdd:cd13718   58 GFCIDILKKLAKDVGFTYDLYLVTNGKHGKKI-NGVWNGMIGEVVYKRADMAVGSLTINEERSEVVDFSVPFVETGISV- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 525 yrvhMGRKPGYFSFL-DPfspavwlfmllaylavscvlflaaRL-SPYEWYNPhpclrarphilenqytlgnslwfpvgg 602
Cdd:cd13718  136 ----MVARSNQVSGLsDK------------------------KFqRPHDQSPP--------------------------- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 603 fmqqgseimpralstrcvsgvwwaftliiissytanlaafltvqrmevpvesaddladqtnIEYGTIHAGSTMtffQNSR 682
Cdd:cd13718  161 -------------------------------------------------------------FRFGTVPNGSTE---RNIR 176
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 683 yQTYQRMWNYM-QSKQPSVfvkstEEGIARVLNSRY-AFLLESTMNEY--HRRLNCNLTQIGG--LLDTKGYGIGMPLGS 756
Cdd:cd13718  177 -NNYPEMHQYMrKYNQKGV-----EDALVSLKTGKLdAFIYDAAVLNYmaGQDEGCKLVTIGSgkWFAMTGYGIALQKNS 250
                        330       340
                 ....*....|....*....|....*....
gi 160298215 757 PFRDEITLAILQLQENNRLEILKRKWWEG 785
Cdd:cd13718  251 KWKRPFDLALLQFRGDGELERLERLWLTG 279
PBP1_iGluR_AMPA_GluR3 cd06387
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR3 subunit ...
41-391 3.95e-22

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: 99.71  E-value: 3.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  41 RLALALAREQINgIIEVPAKARVEVDifELQRDSQYETTDTMCQILPKGVVSVLGPSSSPASAsTVSHICGEKEIPHIkv 120
Cdd:cd06387   18 RFAVQLYNTNQN-TTEKPFHLNYHVD--HLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMN-TLTSFCGALHTSFI-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 121 gpeeTPRlqylrfasvslYPSNEDVSLaVSRILKSFNYPSASLICA-KAECLLRLEELVRGFLISKETL----------S 189
Cdd:cd06387   92 ----TPS-----------FPTDADVQF-VIQMRPALKGAILSLLAHyKWEKFVYLYDTERGFSILQAIMeaavqnnwqvT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 190 VRMLDDSRDPTP---LLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILG 266
Cdd:cd06387  156 ARSVGNIKDVQEfrrIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 267 FSMFNTSHPFYPEFV-RSLNMSWRENCEASTYPgPALSAALMFDAVHVVVSAVRELNRSQ-EIGVKPLA--CTS--ANIW 340
Cdd:cd06387  236 FQIVNNENPMVQQFLqRWVRLDEREFPEAKNAP-LKYTSALTHDAILVIAEAFRYLRRQRvDVSRRGSAgdCLAnpAVPW 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 341 PHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 391
Cdd:cd06387  315 SQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKPSGSRKAGYW 365
PBP2_iGluR_NMDA_Nr3 cd13720
The ligand-binding domain of the NR3 subunit of ionotropic NMDA (N-methyl-D-aspartate) ...
419-783 1.06e-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: 96.46  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 419 VTTILENPYVMRR----------------------PNFQALSGNERFE-------------GFCVDMLRELAELLRFRYR 463
Cdd:cd13720    6 VVTLLEHPFVFTRevdeeglcpagqlcldpmtndsSTLDALFSSLHSSndtvpikfrkccyGYCIDLLEKLAEDLGFDFD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 464 LRLVEDGLYGaPEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILyrvhmgrkpgyfsfldpfs 543
Cdd:cd13720   86 LYIVGDGKYG-AWRNGRWTGLVGDLLSGRAHMAVTSFSINSARSQVIDFTSPFFSTSLGIL------------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 544 pavwlfmllaylavscvlflaarlspyewynphpclrARPHilenqytlgnslwfpvggfmQQGSEIMPRALSTRCVSgv 623
Cdd:cd13720  146 -------------------------------------VRTR--------------------DELSGIHDPKLHHPSQG-- 166
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 624 wwaftliiissytanlaafltvQRmevpvesaddladqtnieYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSkqpsvfvk 703
Cdd:cd13720  167 ----------------------FR------------------FGTVRESSAEYYVKKSFPEMHEHMRRYSLP-------- 198
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 704 STEEGIARVLNSRY---AFLLESTMNEYHRRLN--CNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEIL 778
Cdd:cd13720  199 NTPEGVEYLKNDPEkldAFIMDKALLDYEVSIDadCKLLTVGKPFAIEGYGIGLPQNSPLTSNISELISQYKSNGFMDLL 278

                 ....*
gi 160298215 779 KRKWW 783
Cdd:cd13720  279 HDKWY 283
PBP1_iGluR_AMPA_GluR1 cd06390
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ...
202-391 1.25e-20

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: 95.01  E-value: 1.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 202 LLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFypefV 281
Cdd:cd06390  163 LFQDLDKKKERLVVVDCESERLNAILGQIVKLEKNGIGYHYILANLGFMDIDLTKFKESGANVTGFQLVNYTDTI----P 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 282 RSLNMSWREN----CEASTYPGPALSAALMFDAVHVVVSAVRELnRSQEIGVKPLA----CTS--ANIWPHGTSLMNYLR 351
Cdd:cd06390  239 ARIMQQWKNSdsrdLPRVDWKRPKYTSALTYDGVKVMAEAFQSL-RRQRIDISRRGnagdCLAnpAVPWGQGIDIQRALQ 317
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 160298215 352 MVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 391
Cdd:cd06390  318 QVRFEGLTGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYW 357
Lig_chan-Glu_bd smart00918
Ligated ion channel L-glutamate- and glycine-binding site; This region, sometimes called the ...
426-489 6.13e-20

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: 84.22  E-value: 6.13e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 160298215   426 PYVMRRPNfqALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELI 489
Cdd:smart00918   1 PYVMLKES--PDGGNDRFEGYCIDLLKELAKKLGFTYEIILVPDGKYGARLPNGSWNGMVGELV 62
PBP1_iGluR_AMPA_GluR2 cd06389
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ...
192-391 2.75e-17

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: 85.07  E-value: 2.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 192 MLDDSRDPT--PLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSM 269
Cdd:cd06389  156 INNDKKDETyrSLFQDLELKKERRVILDCERDKVNDIVDQVITIGKHVKGYHYIIANLGFTDGDLLKIQFGGANVSGFQI 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 270 FNTSHPFYPEFVRSlnmsWrENCEASTYPGP-----ALSAALMFDAVHVVVSAVRELnRSQEIGVKPLA----CTS--AN 338
Cdd:cd06389  236 VDYDDSLVSKFIER----W-STLEEKEYPGAhtttiKYTSALTYDAVQVMTEAFRNL-RKQRIEISRRGnagdCLAnpAV 309
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 160298215 339 IWPHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 391
Cdd:cd06389  310 PWGQGVEIERALKQVQVEGLSGNIKFDQNGKRINYTINIMELKTNGPRKIGYW 362
PBP1_iGluR_AMPA_GluR4 cd06388
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR4 subunit ...
202-391 1.99e-16

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: 82.38  E-value: 1.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 202 LLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFypefV 281
Cdd:cd06388  170 LLEDLDRRQEKKFVIDCEIERLQNILEQIVSVGKHVKGYHYIIANLGFKDISLERFMHGGANVTGFQLVDFNTPM----V 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 282 RSLNMSWREnCEASTYPG----PALSAALMFDAVHVVVSAVRELNR-----SQEIGVKPLACTSANIWPHGTSLMNYLRM 352
Cdd:cd06388  246 TKLMQRWKK-LDQREYPGsetpPKYTSALTYDGVLVMAETFRNLRRqkidiSRRGNAGDCLANPAAPWGQGIDMERTLKQ 324
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 160298215 353 VEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVW 391
Cdd:cd06388  325 VRIQGLTGNVQFDHYGRRVNYTMDVFELKSTGPRKVGYW 363
PBP2_peptides_like cd13530
Peptide-binding protein and related homologs; type 2 periplasmic binding protein fold; This ...
416-524 2.56e-13

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: 69.97  E-value: 2.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 416 TLVVTTilENPYvmrrPNFQALSGNERFEGFCVDMLRELAELLrfryrlrlvedGLygAPEP-NGSWTGMVGELINRKAD 494
Cdd:cd13530    1 TLRVGT--DADY----PPFEYIDKNGKLVGFDVDLANAIAKRL-----------GV--KVEFvDTDFDGLIPALQSGKID 61
                         90       100       110
                 ....*....|....*....|....*....|
gi 160298215 495 LAVAAFTITAEREKVIDFSKPFMTLGISIL 524
Cdd:cd13530   62 VAISGMTITPERAKVVDFSDPYYYTGQVLV 91
PBP2_GluR0 cd00997
Bacterial GluR0 ligand-binding domain; the type 2 periplasmic binding protein fold; Glutamate ...
415-528 1.55e-12

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: 67.75  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 415 KTLVVTTILENPYVMrrpnfqalSGNERFEGFCVDMLRELAELLRFRYRLRLVEdglygapepngSWTGMVGELINRKAD 494
Cdd:cd00997    3 QTLTVATVPRPPFVF--------YNDGELTGFSIDLWRAIAERLGWETEYVRVD-----------SVSALLAAVAEGEAD 63
                         90       100       110
                 ....*....|....*....|....*....|....
gi 160298215 495 LAVAAFTITAEREKVIDFSKPFMTLGISILYRVH 528
Cdd:cd00997   64 IAIAAISITAEREAEFDFSQPIFESGLQILVPNT 97
HisJ COG0834
ABC-type amino acid transport/signal transduction system, periplasmic component/domain [Amino ...
432-526 3.43e-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: 66.93  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNERFEGFCVDMLRELAELLrfryrlrlvedGLygAPEP-NGSWTGMVGELINRKADLAVAAFTITAEREKVI 510
Cdd:COG0834   10 PPFSFRDEDGKLVGFDVDLARAIAKRL-----------GL--KVEFvPVPWDRLIPALQSGKVDLIIAGMTITPEREKQV 76
                         90
                 ....*....|....*.
gi 160298215 511 DFSKPFMTLGISILYR 526
Cdd:COG0834   77 DFSDPYYTSGQVLLVR 92
SBP_bac_3 pfam00497
Bacterial extracellular solute-binding proteins, family 3; This is a sensor domain found in ...
433-526 5.87e-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: 66.16  E-value: 5.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  433 NFQALSGNerFEGFCVDMLRELAELlrfryrlrlvedgLYGAPEP-NGSWTGMVGELINRKADLAVAAFTITAEREKVID 511
Cdd:pfam00497  13 EYVDENGK--LVGFDVDLAKAIAKR-------------LGVKVEFvPVSWDGLIPALQSGKVDLIIAGMTITPERAKQVD 77
                          90
                  ....*....|....*
gi 160298215  512 FSKPFMTLGISILYR 526
Cdd:pfam00497  78 FSDPYYYSGQVILVR 92
PBP1_iGluR_NMDA_NR1 cd06379
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ...
78-372 6.39e-11

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


Pssm-ID: 380602  Cd Length: 364  Bit Score: 65.05  E-value: 6.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215  78 TTDTMC-QILPKGVVSVL---GPSSSPASASTVSHICGEKEIPHIKVGPEETP------RLQYLRfaSVSLYPSNEDVSL 147
Cdd:cd06379   51 TALSVCeDLIASQVYAVIvshPPTPSDLSPTSVSYTAGFYRIPVIGISARDSAfsdkniHVSFLR--TVPPYSHQADVWA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 148 AvsrILKSFNYPSASLICAK---AECLL-RLEELVRGFLISKEtLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASIS 223
Cdd:cd06379  129 E---MLRHFEWKQVIVIHSDdqdGRALLgRLETLAETKDIKIE-KVIEFEPGEKNFTSLLEEMKELQSRVILLYASEDDA 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 224 HLVLRKASELGMTSAFYKYILTtmdfpilhldgivE---DSSNIlgfsmfntshpfyPEFVRSLNMSWRENCEAStypgp 300
Cdd:cd06379  205 EIIFRDAAMLNMTGAGYVWIVT-------------EqalAASNV-------------PDGVLGLQLIHGKNESAH----- 253
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160298215 301 alsaalMFDAVHVVVSAVRELNRSQEIGVK-PLACT-SANIWPHGTSLMNYLRMVEY-DGLTGRVEFNSKGQRTN 372
Cdd:cd06379  254 ------IRDSVSVVAQAIRELFRSSENITDpPVDCRdDTNIWKSGQKFFRVLKSVKLsDGRTGRVEFNDKGDRIG 322
PBP2_Arg_Lys_His cd13624
Substrate binding domain of the arginine-, lysine-, histidine-binding protein ArtJ; the type 2 ...
416-526 1.41e-09

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: 59.05  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 416 TLVVTTilENPYvmrrPNFQALSGNERFEGFCVDMLRELAEllrfryrlrlvEDGLygapEP---NGSWTGMVGELINRK 492
Cdd:cd13624    1 TLVVGT--DATF----PPFEFVDENGKIVGFDIDLIKAIAK-----------EAGF----EVefkNMAFDGLIPALQSGK 59
                         90       100       110
                 ....*....|....*....|....*....|....
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISILYR 526
Cdd:cd13624   60 IDIIISGMTITEERKKSVDFSDPYYEAGQAIVVR 93
PBPb smart00062
Bacterial periplasmic substrate-binding proteins; bacterial proteins, eukaryotic ones are in ...
439-526 1.65e-08

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


Pssm-ID: 214497 [Multi-domain]  Cd Length: 219  Bit Score: 56.18  E-value: 1.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215   439 GNERFEGFCVDMLRELAELLRFRYRLRLVedglygapepngSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMT 518
Cdd:smart00062  18 EDGELTGFDVDLAKAIAKELGLKVEFVEV------------SFDSLLTALKSGKIDVVAAGMTITPERAKQVDFSDPYYR 85

                   ....*...
gi 160298215   519 LGISILYR 526
Cdd:smart00062  86 SGQVILVR 93
PBP1_GABAb_receptor_plant cd19990
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ...
214-391 6.21e-08

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


Pssm-ID: 380645 [Multi-domain]  Cd Length: 373  Bit Score: 56.08  E-value: 6.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 214 IIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHldgiVEDSSNIlgFSM-----FNTSHPFYPEFvRSLNMSW 288
Cdd:cd19990  193 FVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNLLD----SLDSSTI--SSMqgvigIKTYIPESSEF-QDFKARF 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 289 RENCEAST----YPGPALSAALMFDAVHVVVSAVRELNRSqeigvkplaCTSANIWPHGTSLMNYLRMVEYDGLTGRVEF 364
Cdd:cd19990  266 RKKFRSEYpeeeNAEPNIYALRAYDAIWALAHAVEKLNSS---------GGNISVSDSGKKLLEEILSTKFKGLSGEVQF 336
                        170       180
                 ....*....|....*....|....*..
gi 160298215 365 NSKGQRTNYTLRILEKSRQGHREIGVW 391
Cdd:cd19990  337 VDGQLAPPPAFEIVNVIGKGYRELGFW 363
PBP2_Arg_3 cd13622
Substrate binding domain of an arginine 3rd transport system; the type 2 periplasmic binding ...
415-518 1.39e-06

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: 50.38  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 415 KTLVV-TTILENPYVMRrpnfqalSGNERFEGFCVDMLRELAELLRfryrlrlvEDGLYGAPEPNGswtgMVGELINRKA 493
Cdd:cd13622    2 KPLIVgVGKFNPPFEMQ-------GTNNELFGFDIDLMNEICKRIQ--------RTCQYKPMRFDD----LLAALNNGKV 62
                         90       100
                 ....*....|....*....|....*
gi 160298215 494 DLAVAAFTITAEREKVIDFSKPFMT 518
Cdd:cd13622   63 DVAISSISITPERSKNFIFSLPYLL 87
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
479-518 1.58e-06

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


Pssm-ID: 270346 [Multi-domain]  Cd Length: 219  Bit Score: 50.16  E-value: 1.58e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 160298215 479 GSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMT 518
Cdd:cd13628   47 YDFNGLIPALASGQADLALAGITPTPERKKVVDFSEPYYE 86
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
432-526 1.91e-06

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: 49.97  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNERfEGFCVDMLRELAELLRFRYRLRLVEdglygapepngsWTGMVGELINRKADLAVAAFTITAEREKVID 511
Cdd:cd00994   11 VPFEFKQDGKY-VGFDIDLWEAIAKEAGFKYELQPMD------------FKGIIPALQTGRIDIAIAGITITEERKKVVD 77
                         90
                 ....*....|....*
gi 160298215 512 FSKPFMTLGISILYR 526
Cdd:cd00994   78 FSDPYYDSGLAVMVK 92
PBP2_Cysteine cd13694
Substrate binding domain of ABC cysteine transporter; the type 2 periplasmic binding protein ...
432-521 2.19e-06

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


Pssm-ID: 270412 [Multi-domain]  Cd Length: 229  Bit Score: 50.04  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNERFEGFCVDMLRELAELLRfryrlrlvedGLYGAPEpngsWTGM-----VGELINRKADLAVAAFTITAER 506
Cdd:cd13694   19 PPFGYVDENGKFQGFDIDLAKQIAKDLF----------GSGVKVE----FVLVeaanrVPYLTSGKVDLILANFTVTPER 84
                         90
                 ....*....|....*..
gi 160298215 507 EKVIDFSKPFM--TLGI 521
Cdd:cd13694   85 AEVVDFANPYMkvALGV 101
PBP2_Dsm1740 cd13629
Amino acid-binding domain of the type 2 periplasmic binding fold superfamily; This subfamily ...
445-526 2.90e-06

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


Pssm-ID: 270347 [Multi-domain]  Cd Length: 221  Bit Score: 49.49  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 445 GFCVDMLRELAELLrfryrlrlvedglyGAP-EP-NGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGIS 522
Cdd:cd13629   24 GFDVDLAKALAKDL--------------GVKvEFvNTAWDGLIPALQTGKFDLIISGMTITPERNLKVNFSNPYLVSGQT 89

                 ....
gi 160298215 523 ILYR 526
Cdd:cd13629   90 LLVN 93
PBP1_NPR_GC-like cd06352
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ...
144-381 4.17e-06

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: 50.05  E-value: 4.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 144 DVSLAVSRILKSFNYPSASLICAKAE--CLLRLEELVRGFL-ISKETLSVRMLDDSRDPTP---LLKEIRddKVSTIII- 216
Cdd:cd06352  124 SLAEALLALLKQFNWKRAAIIYSDDDskCFSIANDLEDALNqEDNLTISYYEFVEVNSDSDyssILQEAK--KRARIIVl 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 217 --DANaSISHLVLRkASELGMTSAFYKYIL-----TTMDFPILHL----DGIVEDS----SNILGFSMFNTSHPFYPEF- 280
Cdd:cd06352  202 cfDSE-TVRQFMLA-AHDLGMTNGEYVFIFielfkDGFGGNSTDGwernDGRDEDAkqayESLLVISLSRPSNPEYDNFs 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 281 --VRSLNMSWRENCEASTYPGPALSAALMFDAVHVVVSAvreLNRSQEIGVKPlactsaniwPHGTSLMNYLRMVEYDGL 358
Cdd:cd06352  280 keVKARAKEPPFYCYDASEEEVSPYAAALYDAVYLYALA---LNETLAEGGNY---------RNGTAIAQRMWNRTFQGI 347
                        250       260
                 ....*....|....*....|....
gi 160298215 359 TGRVEFNSKGQR-TNYTLRILEKS 381
Cdd:cd06352  348 TGPVTIDSNGDRdPDYALLDLDPS 371
PBP2_Peb1a_like cd13691
Substrate binding domain of an ABC aspartate/glutamate transporter; the type 2 ...
442-526 5.15e-06

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: 48.60  E-value: 5.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 442 RFEGFCVDMLRELAELlrfryrlrlvedGLYGAPEPNGSWTGMVGELI-NRKADLAVAAFTITAEREKVIDFSKPFMTLG 520
Cdd:cd13691   30 KYEGMEVDLARKLAKK------------GDGVKVEFTPVTAKTRGPLLdNGDVDAVIATFTITPERKKSYDFSTPYYTDA 97

                 ....*.
gi 160298215 521 ISILYR 526
Cdd:cd13691   98 IGVLVE 103
PBP2_GluB cd13690
Substrate binding domain of ABC glutamate transporter; the type 2 periplasmic binding protein ...
432-526 5.66e-06

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: 48.80  E-value: 5.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNE-RFEGFCVDMLRELAELLrfryrlrlvedglyGAPEPNGSWTGMVGE-----LINRKADLAVAAFTITAE 505
Cdd:cd13690   19 PGFSLRNPTTgEFEGFDVDIARAVARAI--------------GGDEPKVEFREVTSAerealLQNGTVDLVVATYSITPE 84
                         90       100
                 ....*....|....*....|.
gi 160298215 506 REKVIDFSKPFMTLGISILYR 526
Cdd:cd13690   85 RRKQVDFAGPYYTAGQRLLVR 105
PBP2_HisK cd13704
The periplasmic sensor domain of histidine kinase receptors; the type 2 periplasmic binding ...
432-526 6.30e-06

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: 48.35  E-value: 6.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNERFEGFCVDMLRELAEllrfryrlrlvEDGLygapepN-----GSWTGMVGELINRKADLAVAAFtITAER 506
Cdd:cd13704   13 PPYEFLDENGNPTGFNVDLLRAIAE-----------EMGL------KveirlGPWSEVLQALENGEIDVLIGMA-YSEER 74
                         90       100
                 ....*....|....*....|
gi 160298215 507 EKVIDFSKPFMTLGISILYR 526
Cdd:cd13704   75 AKLFDFSDPYLEVSVSIFVR 94
PBP2_OccT_like cd13699
Substrate binding domain of ABC-type octopine transporter-like; the type 2 periplasmic-binding ...
480-521 1.22e-05

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


Pssm-ID: 270417 [Multi-domain]  Cd Length: 211  Bit Score: 47.37  E-value: 1.22e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 160298215 480 SWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPF---------MTLGI 521
Cdd:cd13699   49 DWDGMIPALNAGKFDVIMDAMSITAERKKVIDFSTPYaatpnsfavVTIGV 99
PBP2_HisJ_LAO_like cd01001
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporters and ...
415-540 1.50e-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: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 415 KTLVVTTilENPYvmrrPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVedglygapepngSWTGMVGELINRKAD 494
Cdd:cd01001    2 DTLRIGT--EGDY----PPFNFLDADGKLVGFDIDLANALCKRMKVKCEIVTQ------------PWDGLIPALKAGKYD 63
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 160298215 495 LAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLD 540
Cdd:cd01001   64 AIIASMSITDKRRQQIDFTDPYYRTPSRFVARKDSPITDTTPAKLK 109
PRK11260 PRK11260
cystine ABC transporter substrate-binding protein;
408-526 1.72e-05

cystine ABC transporter substrate-binding protein;


Pssm-ID: 183061 [Multi-domain]  Cd Length: 266  Bit Score: 47.41  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 408 LSQTLANKTLVVTtiLENPYvmrrP--NFQALSGneRFEGFCVDMLRELAEllrfryrlrlvEDGLYGAPEPNgSWTGMV 485
Cdd:PRK11260  34 LNKVKERGTLLVG--LEGTY----PpfSFQGEDG--KLTGFEVEFAEALAK-----------HLGVKASLKPT-KWDGML 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 160298215 486 GELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYR 526
Cdd:PRK11260  94 ASLDSKRIDVVINQVTISDERKKKYDFSTPYTVSGIQALVK 134
PBP1_iGluR_N_LIVBP-like cd06351
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NMDA, AMPA, ...
203-397 1.87e-05

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: 48.11  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 203 LKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFYPEFVR 282
Cdd:cd06351  188 LQSIRMVLEVRPAYFERNFAWHAITQNEVEISSQSDNAHIMFMNPMAYDILLETVYRDRLGLTRTTYNLNENPMVQQFIQ 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 283 SLNMS-WRENCEASTYPgPALSAALMFDAVHVVVSAVRElnrsqeigvkplactsaniwphgtslmnylrmveydglTGR 361
Cdd:cd06351  268 RWVRLdEREFPEAKNAE-LQLSSAFYFDLALRSALAFKE--------------------------------------TGY 308
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 160298215 362 VEFNSKGQRTNYTLRILE-KSRQGHREIGVWYSNRTL 397
Cdd:cd06351  309 GTFDLQSTQPFNGHSFMKfEMDINVRKIRGWSEYESV 345
PBP2_FliY cd13712
Substrate binding domain of an Escherichia coli ABC transporter; the type 2 periplasmic ...
433-526 2.16e-05

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: 46.61  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 433 NFQALSGneRFEGFCVDMLRELAELLRFRYRLRLVEdglygapepngsWTGMVGELINRKADLAVAAFTITAEREKVIDF 512
Cdd:cd13712   14 NFKDETG--QLTGFEVDVAKALAAKLGVKPEFVTTE------------WSGILAGLQAGKYDVIINQVGITPERQKKFDF 79
                         90
                 ....*....|....
gi 160298215 513 SKPFMTLGISILYR 526
Cdd:cd13712   80 SQPYTYSGIQLIVR 93
PBP2_Cystine_like_1 cd13713
Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 ...
444-526 2.19e-05

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: 46.51  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 444 EGFCVDMLRELAELlrfryrlrlvedgLYGAPEP-NGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGIS 522
Cdd:cd13713   23 VGFDVDVAKAIAKR-------------LGVKVEPvTTAWDGIIAGLWAGRYDIIIGSMTITEERLKVVDFSNPYYYSGAQ 89

                 ....
gi 160298215 523 ILYR 526
Cdd:cd13713   90 IFVR 93
GluR_Plant cd13686
Plant glutamate receptor domain; the type 2 periplasmic binding protein fold; This subfamily ...
428-524 2.57e-05

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


Pssm-ID: 270404 [Multi-domain]  Cd Length: 232  Bit Score: 46.74  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 428 VMRRPNfqalSGNERFEGFCVDM----LRELAellrfryrlrlvedglYGAP------EPNGSWTGMVGELINRKADLAV 497
Cdd:cd13686   19 VTRDPI----TNSTSVTGFCIDVfeaaVKRLP----------------YAVPyefipfNDAGSYDDLVYQVYLKKFDAAV 78
                         90       100
                 ....*....|....*....|....*..
gi 160298215 498 AAFTITAEREKVIDFSKPFMTLGISIL 524
Cdd:cd13686   79 GDITITANRSLYVDFTLPYTESGLVMV 105
glnH PRK09495
glutamine ABC transporter periplasmic protein; Reviewed
397-524 4.91e-05

glutamine ABC transporter periplasmic protein; Reviewed


Pssm-ID: 236540 [Multi-domain]  Cd Length: 247  Bit Score: 45.89  E-value: 4.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 397 LAMNATTLDINLSQTLANKTLVVTTilENPYVmrrPnFQALSGNeRFEGFCVDMLRELAEllrfryrlrlvEDGLYGAPE 476
Cdd:PRK09495   7 VSLAALTLAFAVSSHAADKKLVVAT--DTAFV---P-FEFKQGD-KYVGFDIDLWAAIAK-----------ELKLDYTLK 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 160298215 477 PNgSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISIL 524
Cdd:PRK09495  69 PM-DFSGIIPALQTKNVDLALAGITITDERKKAIDFSDGYYKSGLLVM 115
PBP1_ABC_ligand_binding-like cd19980
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ...
198-369 5.05e-05

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: 380635 [Multi-domain]  Cd Length: 334  Bit Score: 46.45  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 198 DPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYI-LTTMDFPILH---LDGIVedssnilgfsmfnTS 273
Cdd:cd19980  179 DFTTQLTKLKAANPDAIFVVAETEDGALILKQARELGLKQQLVGTGgTTSPDLIKLAgdaAEGVY-------------GA 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 274 HPFYPEFVRSLNMSWRENCEASTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLActsaniwphgtslmnyLRMV 353
Cdd:cd19980  246 SIYAPTADNPANKAFVAAYKKKYGEPPDKFAALGYDAVMVIAEAIKKAGSTDPEKIRAAA----------------LKKV 309
                        170
                 ....*....|....*.
gi 160298215 354 EYDGLTGRVEFNSKGQ 369
Cdd:cd19980  310 DYKGPGGTIKFDEKGQ 325
PBP2_BsGlnH cd13689
Substrate binding domain of ABC glutamine transporter from Bacillus subtilis; the type 2 ...
487-526 5.05e-05

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: 45.69  E-value: 5.05e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 160298215 487 ELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYR 526
Cdd:cd13689   63 ELQNGRVDLVAANLTYTPERAEQIDFSDPYFVTGQKLLVK 102
PBP2_mlr5654_like cd13702
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
481-518 6.84e-05

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


Pssm-ID: 270420 [Multi-domain]  Cd Length: 223  Bit Score: 45.39  E-value: 6.84e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 160298215 481 WTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMT 518
Cdd:cd13702   50 WDGIIPALQAKKFDAIIASMSITPERKKQVDFTDPYYT 87
PBP2_GltI_DEBP cd13688
Substrate-binding domain of ABC aspartate-glutamate transporter; the type 2 periplasmic ...
434-526 7.01e-05

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: 45.32  E-value: 7.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 434 FQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYgapePNGSWTGMvgELI-NRKADLAVAAFTITAEREKVIDF 512
Cdd:cd13688   21 FSYLDDNGKPVGYSVDLCNAIADALKKKLALPDLKVRYV----PVTPQDRI--PALtSGTIDLECGATTNTLERRKLVDF 94
                         90
                 ....*....|....
gi 160298215 513 SKPFMTLGISILYR 526
Cdd:cd13688   95 SIPIFVAGTRLLVR 108
PBP2_BvgS_HisK_like cd01007
The type 2 periplasmic ligand-binding protein domain of the sensor-kinase BvgS and histidine ...
432-523 8.13e-05

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


Pssm-ID: 270228 [Multi-domain]  Cd Length: 220  Bit Score: 44.83  E-value: 8.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNERFEGFCVDMLRELAELLrfryrlrlvedGLYGAPEPNGSWTGMVGELINRKADLaVAAFTITAEREKVID 511
Cdd:cd01007   13 PPFEFIDEGGEPQGIAADYLKLIAKKL-----------GLKFEYVPGDSWSELLEALKAGEIDL-LSSVSKTPEREKYLL 80
                         90
                 ....*....|..
gi 160298215 512 FSKPFMTLGISI 523
Cdd:cd01007   81 FTKPYLSSPLVI 92
PBP2_GltS cd13620
Substrate binding domain of glutamate or arginine ABC transporter, a member of the type 2 ...
483-526 8.33e-05

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: 45.02  E-value: 8.33e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 160298215 483 GMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYR 526
Cdd:cd13620   57 NLLASLQSGKVDMAISGMTPTPERKKSVDFSDVYYEAKQSLLVK 100
PBP2_Cystine_like cd13626
Substrate binding domain of cystine ABC transporters; the type 2 periplasmic binding protein ...
432-526 8.84e-05

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: 45.00  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 432 PNFQALSGNERFEGFCVDMLRELAELLrfryrlrlvedGLYGAPEPnGSWTGMVGELINRKADLAVAAFTITAEREKVID 511
Cdd:cd13626   11 PPFTFKDEDGKLTGFDVEVGREIAKRL-----------GLKVEFKA-TEWDGLLPGLNSGKFDVIANQVTITPEREEKYL 78
                         90
                 ....*....|....*
gi 160298215 512 FSKPFMTLGISILYR 526
Cdd:cd13626   79 FSDPYLVSGAQIIVK 93
PBP2_YxeM cd13709
Substrate binding domain of an ABC transporter YxeMNO; the type 2 periplasmic binding protein ...
440-532 9.32e-05

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: 45.03  E-value: 9.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 440 NERFEGFCVDMLRELAELLRfryrlrlvedglYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTL 519
Cdd:cd13709   19 NGKLKGFEVDVWNAIGKRTG------------YKVEFVTADFSGLFGMLDSGKVDTIANQITITPERQEKYDFSEPYVYD 86
                         90
                 ....*....|...
gi 160298215 520 GISILyrVHMGRK 532
Cdd:cd13709   87 GAQIV--VKKDNN 97
PBP2_ml15202_like cd13701
Substrate binding domain of ABC-type histidine/lysine/arginine/ornithine transporter-like; the ...
426-516 9.89e-05

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


Pssm-ID: 270419 [Multi-domain]  Cd Length: 227  Bit Score: 44.76  E-value: 9.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 426 PYvmrrPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVedglygapepngSWTGMVGELINRKADLAVAAFTITAE 505
Cdd:cd13701   12 PY----PPFTSKDASGKWSGWEIDLIDALCARLDARCEITPV------------AWDGIIPALQSGKIDMIWNSMSITDE 75
                         90
                 ....*....|.
gi 160298215 506 REKVIDFSKPF 516
Cdd:cd13701   76 RKKVIDFSDPY 86
PBP2_Cys_DEBP_like cd01000
Substrate-binding domain of cysteine- and aspartate/glutamate-binding proteins; the type 2 ...
488-524 1.41e-04

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


Pssm-ID: 270221 [Multi-domain]  Cd Length: 228  Bit Score: 44.22  E-value: 1.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 160298215 488 LINRKADLAVAAFTITAEREKVIDFSKPFMTLGISIL 524
Cdd:cd01000   66 LQSGKVDLIIATMTITPERAKEVDFSVPYYADGQGLL 102
PBP2_YfhD_N cd01009
The solute binding domain of YfhD proteins, a member of the type 2 periplasmic binding fold ...
439-518 1.98e-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: 43.74  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 439 GNERFEGFCVDMLRELAELLRfryrlrlVEdgLYGAPEPNgsWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMT 518
Cdd:cd01009   17 DRGGPRGFEYELAKAFADYLG-------VE--LEIVPADN--LEELLEALEEGKGDLAAAGLTITPERKKKVDFSFPYYY 85
PBP2_BvgS_D2 cd13707
The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 ...
440-518 3.06e-04

The second of the two tandem periplasmic domains of sensor-kinase BvgS; the type 2 peripasmic-binding fold protein; This group contains the second domain of the periplasmic solute-binding domains of BvgS and related proteins. BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS 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: 270425 [Multi-domain]  Cd Length: 221  Bit Score: 43.36  E-value: 3.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 160298215 440 NERFEGFCVDMLRELAELLrfryrlrlvedGLYGAPEPNGSWTGMVGELINRKADLAvAAFTITAEREKVIDFSKPFMT 518
Cdd:cd13707   21 NGQFRGISADLLELISLRT-----------GLRFEVVRASSPAEMIEALRSGEADMI-AALTPSPEREDFLLFTRPYLT 87
PBP2_SMa0082_like cd01072
The substrate-binding domain of putatuve amino acid transporter; the type 2 periplasmic ...
488-523 3.26e-04

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: 43.41  E-value: 3.26e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 160298215 488 LINRKADLAVAAFTITAEREKVIDFSKPFMTLGISI 523
Cdd:cd01072   68 LQTGKVDMLIASLGITPERAKVVDFSQPYAAFYLGV 103
PBP2_ArtJ_like cd13697
Putative substrate-binding domain of ABC arginine transporter; the type 2 periplasmic-binding ...
408-524 3.41e-04

Putative substrate-binding domain of ABC arginine transporter; the type 2 periplasmic-binding protein fold; The ArtJ 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: 270415 [Multi-domain]  Cd Length: 228  Bit Score: 43.29  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 408 LSQTLANKTLVVTTileNPYVmrrPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVedglygapepngSWTGMVGE 487
Cdd:cd13697    1 LDEILASKKLVVGV---NPNL---PPLGAYDDKNVIEGFDVDVAKKLADRLGVKLELVPV------------SSADRVPF 62
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 160298215 488 LINRKADLAVAAFTITAEREKVIDFSKPFMTLGISIL 524
Cdd:cd13697   63 LMAGKIDAVLGGLTRTPDRAKVIDFSDPVNTEVLGIL 99
PBP2_HisJ_LAO cd13703
Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; ...
480-516 9.82e-04

Substrate binding domain of ABC-type histidine- and lysine/arginine/ornithine transporters; the type 2 periplasmic-binding protein fold; This subgroup includes the periplasmic-binding proteins, HisJ and LAO, that serve as initial receptors in the ABC transport of histidine and lysine-arginine-ornithine amino acids. They are 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: 270421 [Multi-domain]  Cd Length: 229  Bit Score: 41.85  E-value: 9.82e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 160298215 480 SWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPF 516
Cdd:cd13703   49 DFDGLIPGLLARKFDAIISSMSITEERKKVVDFTDKY 85
PBP2_PheC cd01069
Cyclohexadienyl dehydratase, a member of the type 2 periplasmic binding fold protein ...
407-520 1.94e-03

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: 40.79  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 407 NLSQTLANKTLVV-TTILENPYVMRRPNFQalsgnerFEGFCVDMLRELAELLRFRYRLRLVedglygapepngSWTGMV 485
Cdd:cd01069    2 RLDKILERGVLRVgTTGDYKPFTYRDNQGQ-------YEGYDIDMAEALAKSLGVKVEFVPT------------SWPTLM 62
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 160298215 486 GELINRKADLAVAAFTITAEREKVIDFSKPFMTLG 520
Cdd:cd01069   63 DDLAADKFDIAMGGISITLERQRQAFFSAPYLRFG 97
PBP2_ArtJ cd00999
The solute binding domain of ArtJ protein, a member of the type 2 periplasmic binding fold ...
685-782 2.07e-03

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: 40.77  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 685 TYQRmwNYMQSkQPSVFVKS---TEEGIARVLNSRYAFlleSTMNEYHRRLNCNLTQIGGLLDT--------KGYGIGMP 753
Cdd:cd00999  120 TIQE--VFLRS-LPGVEVKSfqkTDDCLREVVLGRSDA---AVMDPTVAKVYLKSKDFPGKLATaftlpewgLGKALAVA 193
                         90       100       110
                 ....*....|....*....|....*....|
gi 160298215 754 LGSP-FRDEITLAILQLQENNRLEILKRKW 782
Cdd:cd00999  194 KDDPaLKEAVNKALDELKKEGELAALRKKW 223
PBP2_AA_binding_like_2 cd13627
Substrate-binding domain of putative amino acid-binding protein; the type 2 ...
480-516 2.62e-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: 270345 [Multi-domain]  Cd Length: 243  Bit Score: 40.46  E-value: 2.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 160298215 480 SWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPF 516
Cdd:cd13627   60 EWNGLIPALNSGDIDLIIAGMSKTPEREKTIDFSDPY 96
PBP2_Ala cd13628
Periplasmic substrate binding domain of ABC-type transporter specific to alanine; the type 2 ...
747-782 3.72e-03

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: 40.14  E-value: 3.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 160298215 747 GYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKW 782
Cdd:cd13628  184 GSAIAFPKGSPLRDDFNRWLKEMGDSGELELMVRRW 219
PBP2_GlnP cd13619
Glutamine-binding domain of ABC transporter, a member of the type 2 periplasmic binding fold ...
493-523 3.78e-03

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: 39.99  E-value: 3.78e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 160298215 493 ADLAVAAFTITAEREKVIDFSKPFMTLGISI 523
Cdd:cd13619   60 ADGVIAGMSITDERKKTFDFSDPYYDSGLVI 90
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
439-526 4.00e-03

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


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 40.82  E-value: 4.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 439 GNERFEGFCVDMLRELAELLRFRYRLRLVEDglygapepngsWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMT 518
Cdd:COG4623   38 YRGGPMGFEYELAKAFADYLGVKLEIIVPDN-----------LDELLPALNAGEGDIAAAGLTITPERKKQVRFSPPYYS 106

                 ....*...
gi 160298215 519 LGISILYR 526
Cdd:COG4623  107 VSQVLVYR 114
PBP1_GABAb_receptor cd06366
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ...
272-394 4.08e-03

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


Pssm-ID: 380589 [Multi-domain]  Cd Length: 404  Bit Score: 40.69  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 272 TSHPFYPEFVRSLNMswrENCEASTYpgpalsAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPHGTSLMNYLR 351
Cdd:cd06366  276 TAQEFLKEYLERLSN---SNYTGSPY------APFAYDAVWAIALALNKTIEKLAEYNKTLEDFTYNDKEMADLFLEAMN 346
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 160298215 352 MVEYDGLTGRVEFNSKGQRTnYTLRILEKSRQGHREIGVWYSN 394
Cdd:cd06366  347 STSFEGVSGPVSFDSKGDRL-GTVDIEQLQGGSYVKVGLYDPN 388
PBP2_Atu4678_like cd13696
The substrate binding domain of putative amino acid transporter; the type 2 periplasmic ...
408-526 4.24e-03

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: 39.67  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160298215 408 LSQTLANKTLVVTTILENPyvmrrP-NFQALSGNErfEGFCVDMLRELAELLRfryrlrlVEDGLYGAPEPNgswtgMVG 486
Cdd:cd13696    1 LDDILSSGKLRCGVCLDFP-----PfGFRDAAGNP--VGYDVDYAKDLAKALG-------VKPEIVETPSPN-----RIP 61
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 160298215 487 ELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYR 526
Cdd:cd13696   62 ALVSGRVDVVVANTTRTLERAKTVAFSIPYVVAGMVVLTR 101
PBP2_GlnH cd00994
Glutamine binding domain of ABC-type transporter; the type 2 periplasmic binding protein fold; ...
735-782 8.28e-03

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: 38.80  E-value: 8.28e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 160298215 735 NLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKW 782
Cdd:cd00994  169 KVKVVGEPLTGEQYGIAFPKGSELREKVNAALKTLKADGTYDEIYKKW 216
PBP2_MidA_like cd01004
Mimosine binding domain of ABC-type transporter MidA and similar proteins; the type 2 ...
478-524 9.45e-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: 38.76  E-value: 9.45e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 160298215 478 NGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSkPFMTLGISIL 524
Cdd:cd01004   47 NVSFDGLIPALQSGRYDIIMSGITDTPERAKQVDFV-DYMKDGLGVL 92
 
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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