|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_mGluR_groupIII |
cd06376 |
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ... |
11-479 |
0e+00 |
|
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain of the group III metabotropic glutamate receptor, a family which contains mGlu4R, mGluR6R, mGluR7, and mGluR8; all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.
Pssm-ID: 380599 [Multi-domain] Cd Length: 467 Bit Score: 1003.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 11 IRIEGDVTLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTF 90
Cdd:cd06376 1 IRVEGDITLGGLFPVHARGLAGVPCGEIKKEKGIHRLEAMLYALDQINSDPDLLPNVTLGARILDTCSRDTYALEQSLTF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 91 VQALIQKDTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPD 170
Cdd:cd06376 81 VQALIQKDTSDVRCTNGDPPVFVKPEKVVGVIGASASSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 171 SFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGLCIAQSVRIPQERkdRTIDFDRIIKQLLDTPNSRA 250
Cdd:cd06376 161 SFQAQAMVDIVKALGWNYVSTLASEGNYGEKGVESFVQISREAGGVCIAQSEKIPRER--RTGDFDKIIKRLLETPNARA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 251 VVIFANDEDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLENNRRNV 330
Cdd:cd06376 239 VVIFADEDDIRRVLAAAKRANKTGHFLWVGSDSWGAKISPVLQQEDVAEGAITILPKRASIEGFDAYFTSRTLENNRRNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 331 WFAEYWEENFNCKLTISGSKKEDTDRKCTGQERIGKDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCADYRGVCPEMEQ 410
Cdd:cd06376 319 WFAEFWEENFNCKLTSSGSKKEDTLRKCTGQERIGRDSGYEQEGKVQFVVDAVYAMAHALHNMNKDLCPGYRGLCPEMEP 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2E4Z_A 411 AGGKKLLKYIRHVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTTNPGYRLIGQWTDELQLNIEDMQW 479
Cdd:cd06376 399 AGGKKLLKYIRNVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNGSNYGYRLIGQWTDELQLNIEDMQW 467
|
|
| PBP1_mGluR |
cd06362 |
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ... |
15-474 |
0e+00 |
|
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of the metabotropic glutamate receptors (mGluR), which are members of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses. mGluRs bind to glutamate and function as an excitatory neurotransmitter; they are involved in learning, memory, anxiety, and the perception of pain. Eight subtypes of mGluRs have been cloned so far, and are classified into three groups according to their sequence similarities, transduction mechanisms, and pharmacological profiles. Group I is composed of mGlu1R and mGlu5R that both stimulate PLC hydrolysis. Group II includes mGlu2R and mGlu3R, which inhibit adenylyl cyclase, as do mGlu4R, mGlu6R, mGlu7R, and mGlu8R, which form group III.
Pssm-ID: 380585 [Multi-domain] Cd Length: 460 Bit Score: 669.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 15 GDVTLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQAL 94
Cdd:cd06362 1 GDINLGGLFPVHERSSSGECCGEIREERGIQRLEAMLFAIDEINSRPDLLPNITLGFVILDDCSSDTTALEQALHFIRDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 95 IQKDTSDVRCTNGEPPV----FVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPD 170
Cdd:cd06362 81 LLSQESAGFCQCSDDPPnldeSFQFYDVVGVIGAESSSVSIQVANLLRLFKIPQISYASTSDELSDKERYPYFLRTVPSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 171 SFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAgGLCIAQSVRIPQERkdRTIDFDRIIKQLLDTPNSRA 250
Cdd:cd06362 161 SFQAKAIVDILLHFNWTYVSVVYSEGSYGEEGYKAFKKLARKA-GICIAESERISQDS--DEKDYDDVIQKLLQKKNARV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 251 VVIFANDEDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLENNRRNV 330
Cdd:cd06362 238 VVLFADQEDIRGLLRAAKRLGASGRFIWLGSDGWGTNIDDLKGNEDVALGALTVQPYSEEVPRFDDYFKSLTPSNNTRNP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 331 WFAEYWEENFNCKLTISGSKKEDTDrkctgQERIGKDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCADYRGVC-PEME 409
Cdd:cd06362 318 WFREFWQELFQCSFRPSRENSCNDD-----KLLINKSEGYKQESKVSFVIDAVYAFAHALHKMHKDLCPGDTGLCqDLMK 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
2E4Z_A 410 QAGGKKLLKYIRHVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTTNPGYRLIGQW---TDELQLNI 474
Cdd:cd06362 393 CIDGSELLEYLLNVSFTGEAGGEIRFDENGDGPGRYDIMNFQRNNDGSYEYVRVGVWdqyTQKLSLND 460
|
|
| PBP1_mGluR_groupII |
cd06375 |
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ... |
11-472 |
0e+00 |
|
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain of the group II metabotropic glutamate receptor, a family that contains mGlu2R and mGlu3R, all of which inhibit adenylyl cyclase. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes
Pssm-ID: 380598 [Multi-domain] Cd Length: 462 Bit Score: 529.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 11 IRIEGDVTLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTF 90
Cdd:cd06375 1 IKLEGDLVLGGLFPVHEKGEGMEECGRINEDRGIQRLEAMLFAIDRINRDPHLLPGVRLGVHILDTCSRDTYALEQSLEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 91 VQALIQK-DTSDVRCTNGEPPVFVK--PEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVV 167
Cdd:cd06375 81 VRASLTKvDDSEYMCPDDGSYAIQEdsPLPIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 168 PPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQiskEAG--GLCIAQSVRIPQERKDRTidFDRIIKQLLDT 245
Cdd:cd06375 161 PPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQ---EARlrNICIATAEKVGRSADRKS--FDGVIRELLQK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 246 PNSRAVVIFANDEDIKQILAAAKRADqvGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLEN 325
Cdd:cd06375 236 PNARVVVLFTRSDDARELLAAAKRLN--ASFTWVASDGWGAQESIVKGSEDVAEGAITLELASHPIPDFDRYFQSLTPYN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 326 NRRNVWFAEYWEENFNCKLTISGSKKEDTDrkctgQERIGKDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCADYRGVC 405
Cdd:cd06375 314 NHRNPWFRDFWEQKFQCSLQNKSQAASVSD-----KHLSIDSSNYEQESKIMFVVNAVYAMAHALHNMQRTLCPNTTRLC 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2E4Z_A 406 PEMEQAGGKKLLK-YIRHVNF-----NGSAGTPVMFNKNGDAPGRYDIFQYQTTNTTNP-GYRLIGQWTDELQL 472
Cdd:cd06375 389 DAMRSLDGKKLYKdYLLNVSFtapfpPADAGSEVKFDAFGDGLGRYNIFNYQRAGGSYGyRYKGVGKWANSLDL 462
|
|
| PBP1_ABC_transporter_GPCR_C-like |
cd04509 |
Family C of G-protein coupled receptors and their close homologs, the type 1 ... |
18-311 |
4.08e-175 |
|
Family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems; This CD includes members of the family C of G-protein coupled receptors and their close homologs, the type 1 periplasmic-binding proteins of ATP-binding cassette transporter-like systems. The family C GPCR includes glutamate/glycine-gated ion channels such as the NMDA receptor, G-protein-coupled receptors, metabotropic glutamate, GABA-B, calcium sensing, pheromone receptors, and atrial natriuretic peptide-guanylate cyclase receptors. The glutamate receptors that form cation-selective ion channels, iGluR, can be classified into three different subgroups according to their binding-affinity for the agonists NMDA (N-methyl-D-asparate), AMPA (alpha-amino-3-dihydro-5-methyl-3-oxo-4-isoxazolepropionic acid), and kainate. L-glutamate is a major neurotransmitter in the brain of vertebrates and acts through either mGluRs or iGluRs. mGluRs subunits possess seven transmembrane segments and a large N-terminal extracellular domain. ABC-type leucine-isoleucine-valine binding protein (LIVBP) is a bacterial periplasmic binding protein that has homology with the amino-terminal domain of the glutamate-receptor ion channels (iGluRs). The extracellular regions of iGluRs are made of two PBP-like domains in tandem, a LIVBP-like domain that constitutes the N terminus (included in this model) followed by a domain related to lysine-arginine-ornithine-binding protein (LAOBP) that belongs to the type 2 periplasmic binding fold protein superfamily. The uncharacterized periplasmic components of various ABC-type transport systems are also included in this family.
Pssm-ID: 380490 Cd Length: 306 Bit Score: 494.52 E-value: 4.08e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 18 TLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQALIQK 97
Cdd:cd04509 1 KVGVLFAVHGKGPSGVPCGDIVAQYGIQRFEAMEQALDDINADPNLLPNNTLGIVIYDDCCDPKQALEQSNKFVNDLIQK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 98 DTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAM 177
Cdd:cd04509 81 DTSDVRCTNGEPPVFVKPEGIKGVIGHLCSSVTIPVSNILELFGIPQITYAATAPELSDDRGYQLFLRVVPLDSDQAPAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 178 VDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEaGGLCIAQSVRIPQERKdrTIDFDRIIKQLLDTPNSRAVVIFAND 257
Cdd:cd04509 161 ADIVKEKVWQYVSIVHDEGQYGEGGARAFQDGLKK-GGLCIAFSDGITAGEK--TKDFDRLVARLKKENNIRFVVYFGYH 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
2E4Z_A 258 EDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATV 311
Cdd:cd04509 238 PEMGQILRAARRAGLVGKFQFMGSDGWANVSLSLNIAEESAEGLITIKPKVWFV 291
|
|
| PBP1_mGluR_groupI |
cd06374 |
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ... |
10-476 |
5.68e-172 |
|
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of the group I metabotropic glutamate receptor, a family containing mGlu1R and mGlu5R, all of which stimulate phospholipase C (PLC) hydrolysis. The metabotropic glutamate receptor is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into intracellular responses. The mGluRs are classified into three groups which comprise eight subtypes.
Pssm-ID: 380597 [Multi-domain] Cd Length: 474 Bit Score: 493.01 E-value: 5.68e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 10 SIRIEGDVTLGGLFPVHAKGP----SGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALE 85
Cdd:cd06374 3 VARMPGDIIIGALFPVHHQPPlkkvFSRKCGEIREQYGIQRVEAMFRTLDKINKDPNLLPNITLGIEIRDSCWYSPVALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 86 QSLTFVQ-ALIQKDTSDVRCTNGEPPVFVKPEK---VVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYD 161
Cdd:cd06374 83 QSIEFIRdSVASVEDEKDTQNTPDPTPLSPPENrkpIVGVIGPGSSSVTIQVQNLLQLFHIPQIGYSATSIDLSDKSLYK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 162 FFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAgGLCIAQSVRIPQerKDRTIDFDRIIKQ 241
Cdd:cd06374 163 YFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEE-GICIAHSDKIYS--NAGEEEFDRLLRK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 242 LLDTPN-SRAVVIFANDEDIKQILAAAKRADQVGHFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTS 320
Cdd:cd06374 240 LMNTPNkARVVVCFCEGETVRGLLKAMRRLNATGHFLLIGSDGWADRKDVVEGYEDEAAGGITIKIHSPEVESFDEYYFN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 321 RTLENNRRNVWFAEYWEENFNCKLTISGSKKEDTDRKCTGQERIgkDSNYEQEGKVQFVIDAVYAMAHALHHMNKDLCAD 400
Cdd:cd06374 320 LKPETNSRNPWFREFWQHRFDCRLPGHPDENPYFKKCCTGEESL--LGNYVQDSKLGFVINAIYAMAHALHRMQEDLCGG 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2E4Z_A 401 YR-GVCPEMEQAGGKKLLKYIRHVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTTNPGYRLIGQWtDELQLNIED 476
Cdd:cd06374 398 YSvGLCPAMLPINGSLLLDYLLNVSFVGVSGDTIMFDENGDPPGRYDIMNFQKTGEGSYDYVQVGSW-KNGSLKMDD 473
|
|
| PBP1_GPCR_family_C-like |
cd06350 |
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ... |
18-476 |
2.29e-135 |
|
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate; categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (m; Ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory transmission on the cellular surface through initial binding of glutamate and are categorized into ionotropic glutamate receptors (iGluRs) and metabotropic glutamate receptors (mGluRs). The metabotropic glutamate receptors (mGluR) are key receptors in the modulation of excitatory synaptic transmission in the central nervous system. The mGluRs are coupled to G proteins and are thus distinct from the iGluRs which internally contain ligand-gated ion channels. The mGluR structure is divided into three regions: the extracellular region, the seven-spanning transmembrane region and the cytoplasmic region. The extracellular region is further divided into the ligand-binding domain (LBD) and the cysteine-rich domain. The LBD has sequence similarity to the LIVBP, which is a bacterial periplasmic protein (PBP), as well as to the extracellular region of both iGluR and the gamma-aminobutyric acid (GABA)b receptor. iGluRs are divided into three main subtypes based on pharmacological profile: NMDA, AMPA, and kainate receptors. All family C GPCRs have a large extracellular N terminus that contain a domain with homology to bacterial periplasmic amino acid-binding proteins.
Pssm-ID: 380573 Cd Length: 350 Bit Score: 395.13 E-value: 2.29e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 18 TLGGLFPVHAKGPSGVPCGDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVqaliqk 97
Cdd:cd06350 1 IIGGLFPVHYRDDADFCCCGILNPRGVQLVEAMIYAIEEINNDSSLLPNVTLGYDIRDTCSSSSVALESSLEFL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 98 DTSDVRCTNGEPPVFVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAM 177
Cdd:cd06350 75 LDNGIKLLANSNGQNIGPPNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAKAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 178 VDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAgGLCIAQSVRIPQERKDRtiDFDRIIKQLLDTPNSRAVVIFAND 257
Cdd:cd06350 155 ADLLKHFNWNYVSTVYSDDDYGRSGIEAFEREAKER-GICIAQTIVIPENSTED--EIKRIIDKLKSSPNAKVVVLFLTE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 258 EDIKQILAAAKRADQVGhFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTSrtlennrrnvwfaeywe 337
Cdd:cd06350 232 SDARELLKEAKRRNLTG-FTWIGSDGWGDSLVILEGYEDVLGGAIGVVPRSKEIPGFDDYLKS----------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 338 enfnckltisgskkedtdrkctgqerigkdsnyeqegKVQFVIDAVYAMahalhhmnkdlcadyrgvcpemeqaggkkll 417
Cdd:cd06350 294 -------------------------------------YAPYVIDAVYAT------------------------------- 305
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 418 kyirhvnfngsagtpVMFNKNGDAPGRYDIFQYQTTNTTNPGYRLIGQWTD-ELQLNIED 476
Cdd:cd06350 306 ---------------VKFDENGDGNGGYDIVNLQRTGTGNYEYVEVGTWDSnSGGLSLNS 350
|
|
| PBP1_glutamate_receptors-like |
cd06269 |
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ... |
18-474 |
4.98e-114 |
|
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as natriuretic peptide receptors (NPRs), and N-terminal leucine/isoleucine/valine-binding protein (LIVBP)-like domain of ionotropic glutamate rece; This CD represents the ligand-binding domain of the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases such as the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the ionotropic glutamate receptors, all of which are structurally similar and related to the periplasmic-binding fold type 1 family. The family C GPCRs consists of metabotropic glutamate receptor (mGluR), a calcium-sensing receptor (CaSR), gamma-aminobutyric acid receptor (GABAbR), the promiscuous L-alpha-amino acid receptor GPR6A, families of taste and pheromone receptors, and orphan receptors. Truncated splicing variants of the orphan receptors are not included in this CD. The family C GPCRs are activated by endogenous agonists such as amino acids, ions, and sugar based molecules. Their amino terminal ligand-binding region is homologous to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). The ionotropic glutamate receptors (iGluRs) have an integral ion channel and are subdivided into three major groups based on their pharmacology and structural similarities: NMDA receptors, AMPA receptors, and kainate receptors. The family of membrane bound guanylyl cyclases is further divided into three subfamilies: the ANP receptor (GC-A)/C-type natriuretic peptide receptor (GC-B), the heat-stable enterotoxin receptor (GC-C)/sensory organ specific membrane GCs such as retinal receptors (GC-E, GC-F), and olfactory receptors (GC-D and GC-G).
Pssm-ID: 380493 [Multi-domain] Cd Length: 332 Bit Score: 339.78 E-value: 4.98e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 18 TLGGLFPVHAKgpsgvpcgdikRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQAliqk 97
Cdd:cd06269 1 TIGALLPVHDY-----------LESGAKVLPAFELALSDVNSRPDLLPKTTLGLAIRDSECNPTQALLSACDLLAA---- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 98 dtsdvrctngeppvfvkpEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAM 177
Cdd:cd06269 66 ------------------AKVVAILGPGCSASAAPVANLARHWDIPVLSYGATAPGLSDKSRYAYFLRTVPPDSKQADAM 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 178 VDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGlCIAQSVRIPQErkdRTIDFDRIIKQLLDTPNsRAVVIFAND 257
Cdd:cd06269 128 LALVRRLGWNKVVLIYSDDEYGEFGLEGLEELFQEKGG-LITSRQSFDEN---KDDDLTKLLRNLRDTEA-RVIILLASP 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 258 EDIKQILAAAKRADQVG-HFLWVGSDSWGSKIN-PLHQHEDIAEGAITIQPKRATVEGFDAYFTSRTLennrrnvwfaey 335
Cdd:cd06269 203 DTARSLMLEAKRLDMTSkDYVWFVIDGEASSSDeHGDEARQAAEGAITVTLIFPVVKEFLKFSMELKL------------ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 336 weenfnckltisgskkedtdrkCTGQERIGKDSNYEQEGKVQFVIDAVYAmahalhhmnkdlcadyrgvcpemeqaggkk 415
Cdd:cd06269 271 ----------------------KSSKRKQGLNEEYELNNFAAFFYDAVLA------------------------------ 298
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
2E4Z_A 416 llkyirhvnfngsagtpvmfnkngDAPGRYDIFQYQTTNttNPGYRLIGQWTDELQLNI 474
Cdd:cd06269 299 ------------------------DRPGQFSIINLQYTE--AGDYRKVGTWDSEGGLNM 331
|
|
| ANF_receptor |
pfam01094 |
Receptor family ligand binding region; This family includes extracellular ligand binding ... |
45-453 |
5.81e-100 |
|
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: 304.31 E-value: 5.81e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 45 HRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQAliqkdtsdvrctngeppvfvkpeKVVGVIGA 124
Cdd:pfam01094 1 LVLLAVRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKG-----------------------EVVAIIGP 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 125 SGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVE 204
Cdd:pfam01094 58 SCSSVASAVASLANEWKVPLISYGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 205 SFTQISKEAgGLCIAQSVRIPQERkdrtiDFDRIIKQLLDTPNS--RAVVIFANDEDIKQILAAAKRADQVGH-FLWVGS 281
Cdd:pfam01094 138 ALEDALRER-GIRVAYKAVIPPAQ-----DDDEIARKLLKEVKSraRVIVVCCSSETARRLLKAARELGMMGEgYVWIAT 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 282 DSWGSKINPLHQ-HEDIAEGAITIQPKRATVEGFDAYFtsrtlennrrnvwfaeyWEENFNCKltisgskkedtdrkctg 360
Cdd:pfam01094 212 DGLTTSLVILNPsTLEAAGGVLGFRLHPPDSPEFSEFF-----------------WEKLSDEK----------------- 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 361 qerigkdSNYEQEGKVQFV-----IDAVYAMAHALHHMNKDLCADYRGVCPEMeQAGGKKLLKYIRHVNFNGSAGTpVMF 435
Cdd:pfam01094 258 -------ELYENLGGLPVSygalaYDAVYLLAHALHNLLRDDKPGRACGALGP-WNGGQKLLRYLKNVNFTGLTGN-VQF 328
|
410
....*....|....*....
2E4Z_A 436 NKNGDAP-GRYDIFQYQTT 453
Cdd:pfam01094 329 DENGDRInPDYDILNLNGS 347
|
|
| PBP1_CaSR |
cd06364 |
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ... |
19-479 |
1.56e-96 |
|
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the CaSR calcium-sensing receptor, which is a member of the family C receptors within the G-protein coupled receptor superfamily. CaSR provides feedback control of extracellular calcium homeostasis by responding sensitively to acute fluctuations in extracellular ionized Ca2+ concentration. This ligand-binding domain has homology to the bacterial leucine-isoleucine-valine binding protein (LIVBP) and a leucine binding protein (LBP). CaSR is widely expressed in mammalian tissues and is active in tissues that are not directly involved in extracellular calcium homeostasis. Moreover, CaSR responds to aromatic, aliphatic, and polar amino acids, but not to positively charged or branched chain amino acids, which suggests that changes in plasma amino acid levels are likely to modulate whole body calcium metabolism. Additionally, the family C GPCRs includes at least two receptors with broad-spectrum amino acid-sensing properties: GPRC6A which recognizes basic and various aliphatic amino acids, its gold-fish homolog the 5.24 chemoreceptor, and a specific taste receptor (T1R) which responds to aliphatic, polar, charged, and branched amino acids, but not to aromatic amino acids.
Pssm-ID: 380587 [Multi-domain] Cd Length: 473 Bit Score: 299.94 E-value: 1.56e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 19 LGGLFPVHAKGPSGVPCGDIKREN---------GIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLT 89
Cdd:cd06364 2 IGGLFPIHFRPVSPDPDFTTEPHSpecegfnfrGFRWAQTMIFAIEEINNSPDLLPNITLGYRIYDSCATISKALRAALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 90 FVqALIQKDTSDVRCtNGEPPVfvkpekvVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPP 169
Cdd:cd06364 82 LV-NGQEETNLDERC-SGGPPV-------AAVIGESGSTLSIAVARTLGLFYIPQVSYFASCACLSDKKQFPSFLRTIPS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 170 DSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGlCIAQSVRIP----QERKDRTIDfdrIIKqlldT 245
Cdd:cd06364 153 DYYQSRALAQLVKHFGWTWVGAIASDDDYGRNGIKAFLEEAEKLGI-CIAFSETIPrtysQEKILRIVE---VIK----K 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 246 PNSRAVVIFANDEDIKQILAAAKRADQVGhFLWVGSDSWGSKINPLH-QHEDIAEGAITIQPKRATVEGFDAYFTSRTLE 324
Cdd:cd06364 225 STAKVIVVFSSEGDLEPLIKELVRQNITG-RQWIASEAWITSSLLATpEYFPVLGGTIGFAIRRGEIPGLKEFLLRVHPS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 325 NNRRNVWFAEYWEENFNCKLTISGSK-KEDTDRK-CTGQERIGKDSN-----------YEqegkvqfVIDAVYAMAHALH 391
Cdd:cd06364 304 KSPSNPFVKEFWEETFNCSLSSSSKSnSSSSSRPpCTGSENLENVQNpytdvsqlrisYN-------VYKAVYAIAHALH 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 392 HM----------NKDLCADYRGVCPemeqaggKKLLKYIRHVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTTNPGYR 461
Cdd:cd06364 377 DLlqcepgkgpfSNGSCADIKKVEP-------WQLLYYLKHVNFTTKFGEEVYFDENGDPVASYDIINWQLSDDGTIQFV 449
|
490 500
....*....|....*....|....
2E4Z_A 462 LIGQWT------DELQLNIEDMQW 479
Cdd:cd06364 450 TVGYYDasapsgEELVINESKILW 473
|
|
| PBP1_pheromone_receptor |
cd06365 |
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ... |
19-479 |
2.96e-76 |
|
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily; Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptor, the GABAb receptor, the calcium-sensing receptor (CaSR), the T1R taste receptor, and a small group of uncharacterized orphan receptors.
Pssm-ID: 380588 [Multi-domain] Cd Length: 464 Bit Score: 247.17 E-value: 2.96e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 19 LGGLFPVHA----------KGPSGVPCGDIKRENgIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSL 88
Cdd:cd06365 2 IGGVFPIHTfsegkkkdfkEPPSPLLCFRFSIKY-YQHLLAFLFAIEEINKNPDLLPNITLGFHIYDSCSSERLALESSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 89 TFvqaliqkdtsdvrcTNGEPPVF-----VKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFF 163
Cdd:cd06365 81 SI--------------LSGNSEPIpnyscREQRKLVAFIGDLSSSTSVAMARILGLYKYPQISYGAFDPLLSDKVQFPSF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 164 SRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGlCIAQSVRIPQERKDRTID--FDRIIKQ 241
Cdd:cd06365 147 YRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDDDYGEQFSQDLKKEMEKNGI-CVAFVEKIPTNSSLKRIIkyINQIIKS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 242 lldtpNSRAVVIFANDEDIKQILAAAKraDQVG-HFLWVGSDSWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAYFTS 320
Cdd:cd06365 226 -----SANVIIIYGDTDSLLELLFRLW--EQLVtGKVWITTSQWDISTLPFEFYLNLFNGTLGFSQHSGEIPGFKEFLQS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 321 RTLENNRRNVWFAEYWEENFNCKLtISGSKKEDTDRKCTGQERIGKDSNYEQE--GKVQFVIDAVYAMAHALHHM----- 393
Cdd:cd06365 299 VHPSKYPEDIFLKTLWESYFNCKW-PDQNCKSLQNCCGNESLETLDVHSFDMTmsRLSYNVYNAVYAVAHALHEMllcqp 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 394 --NKDLCADYRGVCPemeqaggKKLLKYIRHVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTTNPGYRLIGQW----- 466
Cdd:cd06365 378 ktGPGNCSDRRNFQP-------WQLHHYLKKVQFTNPAGDEVNFDEKGDLPTKYDILNWQIFPNGTGTKVKVGTFdpsap 450
|
490
....*....|....
2E4Z_A 467 -TDELQLNIEDMQW 479
Cdd:cd06365 451 sGQQLIINDSMIEW 464
|
|
| PBP1_taste_receptor |
cd06363 |
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ... |
12-479 |
4.78e-67 |
|
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste receptor. The T1R is a member of the family C receptors within the G-protein coupled receptor superfamily, which also includes the metabotropic glutamate receptors, GABAb receptors, the calcium-sensing receptor (CaSR), the V2R pheromone receptors, and a small group of uncharacterized orphan receptors.
Pssm-ID: 380586 [Multi-domain] Cd Length: 418 Bit Score: 221.80 E-value: 4.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 12 RIEGDVTLGGLFPVHA---------KGPSGVPCgDIKRENGIHRLEAMLYALDQINSDPNLLPNVTLGARILDTCSrDTY 82
Cdd:cd06363 2 RLPGDYLLGGLFPLHEltstlphrpPEPTDCSC-DRFNLHGYHLAQAMRFAVEEINNSSDLLPGVTLGYEIFDTCS-DAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 83 ALEQSLTFvqaLIQKDTSDVR--C--TNGEPpvfvkpeKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDR 158
Cdd:cd06363 80 NFRPTLSF---LSQNGSHDIEvqCnyTNYQP-------RVVAVIGPDSSELALTTAKLLGFFLMPQISYGASSEELSNKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 159 RYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFtqiSKEAG--GLCIAQSVRIPQERkDRTIDFD 236
Cdd:cd06363 150 LYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLF---SEKAAntGICVAYQGLIPTDT-DPKPKYQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 237 RIIKQLLDTpNSRAVVIFANDEDIKQILAAAKRaDQVGHFLWVGSDSWGskINP-LHQHEDIAEG----AITIQpkRATV 311
Cdd:cd06363 226 DILKKINQT-KVNVVVVFAPKQAAKAFFEEVIR-QNLTGKVWIASEAWS--LNDtVTSLPGIQSIgtvlGFAIQ--TGTL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 312 EGFDAYftsrtlennrrnvwfaEYWeENFNckltisgskkedtdrkctgqerigkdsnyeqegkvqfVIDAVYAMAHALH 391
Cdd:cd06363 300 PGFQEF----------------IYA-FAFS-------------------------------------VYAAVYAVAHALH 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 392 HM---NKDLCADYRGVCPEMeqaggkkLLKYIRHVNFNGSaGTPVMFNKNGDAPGRYDIFQYQTTNTTnPGYRLIGQW-T 467
Cdd:cd06363 326 NLlgcNSGACPKGRVVYPWQ-------LLEELKKVNFTLL-NQTIRFDENGDPNFGYDIVQWIWNNSS-WTFEVVGSYsT 396
|
490
....*....|....
2E4Z_A 468 DELQLNIED--MQW 479
Cdd:cd06363 397 YPIQLTINEskIKW 410
|
|
| PBP1_GPC6A-like |
cd06361 |
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ... |
19-454 |
8.18e-48 |
|
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor; This family includes the ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a broad-spectrum amino acid-sensing receptor, and its fish homolog, the 5.24 chemoreceptor. GPRC6A is a member of the family C of G-protein-coupled receptors that transduce extracellular signals into G-protein activation and ultimately into cellular responses.
Pssm-ID: 380584 [Multi-domain] Cd Length: 401 Bit Score: 170.24 E-value: 8.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 19 LGGLFPVHAKGPSgVPCGDIKRE---------NGIHRLEAMLYALDQINSDPnLLPNVTLGARILDTCSRDTYALEQSLT 89
Cdd:cd06361 2 IGGLFPIHEKVLD-LHDRPTKPQifictgfdlRGFLQSLAMIHAIEMINNST-LLPGIKLGYEIYDTCSDVTKALQATLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 90 FVQALiqkDTSD--VRCTNGEPPVFVKpekvvGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVV 167
Cdd:cd06361 80 LLSKF---NSSNelLECDYTDYVPPVK-----AVIGASYSEISIAVARLLNLQLIPQISYESSAPILSDKLRFPSFLRTV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 168 PPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISkEAGGLCIAQSVRIPQERKDRTIDFDriIKQLLDT-- 245
Cdd:cd06361 152 PSDFHQTKAMAKLISHFGWNWVGIIYTDDDYGRSALESFIIQA-EAENVCIAFKEVLPAYLSDPTMNVR--INDTIQTiq 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 246 --PNSRAVVIFANDEDIKQILAAAKRADQvgHFLWVGSDSWgSKINPLHQHEDIAE-GAIT-IQPKRATVEGFDAYFtsR 321
Cdd:cd06361 229 ssSQVNVVVLFLKPSLVKKLFKEVIERNI--SKIWIASDNW-STAREILKMPNINKvGKILgFTFKSGNISSFHNYL--K 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 322 TLENNRrnvwfaeyweenfnckltisgskkedtdrkctgqerigkdsnyeqegkVQFvidAVYAMAHALHhmnkDLCADY 401
Cdd:cd06361 304 NLLIYS------------------------------------------------IQL---AVTAIANALR----KLCCER 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
2E4Z_A 402 RGVCPEMEQAGgkKLLKYIRHVNFNgSAGTPVMFNKNGDAPGRYDIFQYQTTN 454
Cdd:cd06361 329 GCQDPTAFQPW--ELLKELKKVTFT-DDGETYHFDANGDLNTGYDLILWKEDN 378
|
|
| PBP1_GABAb_receptor |
cd06366 |
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ... |
18-479 |
1.07e-37 |
|
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: 142.77 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 18 TLGGLFPVHakgpsgvpcGDIKRENGIHRLEAMLYALDQINSDPNLLPNvtlgarildtcsrdtYALEqsltfvqaLIQK 97
Cdd:cd06366 1 YIGGLFPLS---------GSKGWWGGAGILPAAEMALEHINNRSDILPG---------------YNLE--------LIWN 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 98 DTsdvRCTNGEP-PVFV----KPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSF 172
Cdd:cd06366 49 DT---QCDPGLGlKALYdllyTPPPKVMLLGPGCSSVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 173 QAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGLCIAqsvripqERKDRTIDFDRIIKQLLDTpNSRAVV 252
Cdd:cd06366 126 FNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLEELLEEANITIVA-------TESFSSEDPTDQLENLKEK-DARIII 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 253 IFANDEDIKQILAAAKRADQVGH----FL--WVGSDSWGSKINPLHQhediaegaiTIQPKRATVEGfdaYFTSRTLENN 326
Cdd:cd06366 198 GLFYEDAARKVFCEAYKLGMYGPkyvwILpgWYDDNWWDVPDNDVNC---------TPEQMLEALEG---HFSTELLPLN 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 327 RRNvwfaeyweenfncKLTISGSKKEDTDRKCtgQERIGKdSNYEQEGKVQFVIDAVYAMAHALHH-------MNKDLcA 399
Cdd:cd06366 266 PDN-------------TKTISGLTAQEFLKEY--LERLSN-SNYTGSPYAPFAYDAVWAIALALNKtieklaeYNKTL-E 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 400 DYRGVCPEMeqagGKKLLKYIRHVNFNGSAGtPVMFNKNGDAPGRYDIFQYQttnttNPGYRLIGQW---TDELQLNIED 476
Cdd:cd06366 329 DFTYNDKEM----ADLFLEAMNSTSFEGVSG-PVSFDSKGDRLGTVDIEQLQ-----GGSYVKVGLYdpnADSLLLLNES 398
|
....
2E4Z_A 477 -MQW 479
Cdd:cd06366 399 sIVW 402
|
|
| PBP1_ABC_ligand_binding-like |
cd06346 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
116-450 |
2.22e-28 |
|
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: 380569 [Multi-domain] Cd Length: 314 Bit Score: 114.58 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASE 195
Cdd:cd06346 66 EGVPAIVGAASSGVTLAVASVAVPNGVVQISPSSTSPALTTLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVN 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 196 GSYGEKGVESFTQISKEAGGLcIAQSVRIPQERKdrtiDFDRIIKQLLDTpNSRAVVIFANDEDIKQILAAAKRADQVGH 275
Cdd:cd06346 146 NDYGQGLADAFKKAFEALGGT-VTASVPYEPGQT----SYRAELAQAAAG-GPDALVLIGYPEDGATILREALELGLDFT 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 276 fLWVGSDswGSKINPLHQ--HEDIAEGAITIQPKRATVEGFDAyftsrtlennrrnvwFAEYWEENFNckltisgskked 353
Cdd:cd06346 220 -PWIGTD--GLKSDDLVEaaGAEALEGMLGTAPGSPGSPAYEA---------------FAAAYKAEYG------------ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 354 tdrkctGQERIGKDSNYeqegkvqfviDAVYAMAHAlhhmnkdlcadYRGVcpemeqAGgkkllkyirhvnfngsagtPV 433
Cdd:cd06346 270 ------DDPGPFAANAY----------DAVMLLALA-----------YEGA------SG-------------------PI 297
|
330
....*....|....*..
2E4Z_A 434 MFNKNGDAPGRYDIFQY 450
Cdd:cd06346 298 DFDENGDVAGPYEIWKV 314
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
36-291 |
8.77e-24 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 100.81 E-value: 8.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 36 GDIKREN-GIHRLEAMLYALDQINsdpnllpnvtLGARILDTCSRDTYALEQSLTFVQaliqkdtsdvrctngeppvfvk 114
Cdd:cd01391 9 LHQIREQfGIQRVEAIFHTADKLG----------ASVEIRDSCWHGSVALEQSIEFIR---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 115 pEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLAS 194
Cdd:cd01391 57 -DNIAGVIGPGSSSVAIVIQNLAQLFDIPQLALDATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 195 EGS-YGEKGVESFTQISKEAgGLCIAQSVRIPQERKDRTidFDRIIKQLLDTPNSRAVVIFaNDEDIKQILAAAKRADQV 273
Cdd:cd01391 136 EGLnSGELRMAGFKELAKQE-GICIVASDKADWNAGEKG--FDRALRKLREGLKARVIVCA-NDMTARGVLSAMRRLGLV 211
|
250 260
....*....|....*....|....*.
2E4Z_A 274 GHFLWVGSDSW--------GSKINPL 291
Cdd:cd01391 212 GDVSVIGSDGWadrdevgyEVEANGL 237
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
14-451 |
7.36e-23 |
|
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 440447 [Multi-domain] Cd Length: 314 Bit Score: 98.85 E-value: 7.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 14 EGDVTLGGLFPVhaKGPSGVPcgdikrenGIHRLEAMLYALDQINSDPNLLpNVTLGARILDtcsrDTYALEQSLTFVQA 93
Cdd:COG0683 1 ADPIKIGVLLPL--TGPYAAL--------GQPIKNGAELAVEEINAAGGVL-GRKIELVVED----DASDPDTAVAAARK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 94 LIQKDtsdvrctngeppvfvkpeKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQ 173
Cdd:COG0683 66 LIDQD------------------KVDAIVGPLSSGVALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQ 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 174 AQAMVD-IVKALGWNYVSTLASEGSYGEKGVESFTQISKEAGGLcIAQSVRIPQErkdrTIDFDRIIKQLLDTpNSRAVV 252
Cdd:COG0683 128 AEALADyLAKKLGAKKVALLYDDYAYGQGLAAAFKAALKAAGGE-VVGEEYYPPG----TTDFSAQLTKIKAA-GPDAVF 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 253 IFANDEDIKQILAAAKRADqvghflwvgsdsWGSKINplhqhediaegaitiqpkRATVEGFDAYFtsrtleNNRRNVWF 332
Cdd:COG0683 202 LAGYGGDAALFIKQAREAG------------LKGPLN------------------KAFVKAYKAKY------GREPSSYA 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 333 AEYWeenfnckltisgskkedtdrkctgqerigkdsnyeqegkvqfviDAVYAMAHAlhhmnkdlcadyrgvcpeMEQAG 412
Cdd:COG0683 246 AAGY--------------------------------------------DAALLLAEA------------------IEKAG 263
|
410 420 430 440
....*....|....*....|....*....|....*....|..
2E4Z_A 413 ---GKKLLKYIRHVNFNGSAGtPVMFNKNGDAPGRYDIFQYQ 451
Cdd:COG0683 264 stdREAVRDALEGLKFDGVTG-PITFDPDGQGVQPVYIVQVK 304
|
|
| PBP1_GABAb_receptor_plant |
cd19990 |
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ... |
112-467 |
3.04e-20 |
|
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: 92.29 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 112 FVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRrYDFFSRVVPPDSFQAQAMVDIVKALGWNYVST 191
Cdd:cd19990 59 LIKNKKVEAIIGPQTSEEASFVAELGNKAQVPIISFSATSPTLSSLR-WPFFIRMTHNDSSQMKAIAAIVQSYGWRRVVL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 192 LASEGSYGEkgvESFTQISKE--AGGLCIAQSVRIPQerkdrTIDFDRIIKQL--LDTPNSRAVVIFANDEDIKQILAAA 267
Cdd:cd19990 138 IYEDDDYGS---GIIPYLSDAlqEVGSRIEYRVALPP-----SSPEDSIEEELikLKSMQSRVFVVHMSSLLASRLFQEA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 268 KRADQVGH-FLWVGSDSWGSKINPLHQHeDIA--EGAITIQPKratvegfdaYFTSRTLENnrrnvwFAEYWEENFNckl 344
Cdd:cd19990 210 KKLGMMEKgYVWIVTDGITNLLDSLDSS-TISsmQGVIGIKTY---------IPESSEFQD------FKARFRKKFR--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 345 tisgskkedtdrkctgqerigkdSNYEQEGKVQFVI------DAVYAMAHALHHMNKDlcadyrgVCPEMEQAGGKKLLK 418
Cdd:cd19990 271 -----------------------SEYPEEENAEPNIyalrayDAIWALAHAVEKLNSS-------GGNISVSDSGKKLLE 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
2E4Z_A 419 YIRHVNFNGSAGtPVMFNKNGDAPG-RYDIfqyqtTNTTNPGYRLIGQWT 467
Cdd:cd19990 321 EILSTKFKGLSG-EVQFVDGQLAPPpAFEI-----VNVIGKGYRELGFWS 364
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
47-306 |
4.55e-20 |
|
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.
Pssm-ID: 380492 [Multi-domain] Cd Length: 298 Bit Score: 90.46 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 47 LEAMLYALDQINSDPNLLpNVTLGARILDtcsrDTYALEQSLTFVQALIQKDtsdvrctngeppvfvkpeKVVGVIGASG 126
Cdd:cd06268 20 LRGVALAVEEINAAGGIN-GRKLELVIAD----DQGDPETAVAVARKLVDDD------------------KVLAVVGHYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 127 SSVSIMVANILRLFQIPQISYASTAPELSDDrRYDFFSRVVPPDSFQAQAMVD-IVKALGWNYVSTLASEGSYGEKGVES 205
Cdd:cd06268 77 SSVTLAAAPIYQEAGIPLISPGSTAPELTEG-GGPYVFRTVPSDAMQAAALADyLAKKLKGKKVAILYDDYDYGKSLADA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 206 FTQISKEAGGLcIAQSVRIPQErkdrTIDFDRIIKQLLDTpNSRAVVIFANDEDIKQILAAAKRADqvGHFLWVGSDSWG 285
Cdd:cd06268 156 FKKALKALGGE-IVAEEDFPLG----TTDFSAQLTKIKAA-GPDVLFLAGYGADAANALKQARELG--LKLPILGGDGLY 227
|
250 260
....*....|....*....|.
2E4Z_A 286 SKINpLHQHEDIAEGAITIQP 306
Cdd:cd06268 228 SPEL-LKLGGEAAEGVVVAVP 247
|
|
| PBP1_SAP_GC-like |
cd06370 |
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ... |
49-459 |
1.47e-18 |
|
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane bound guanylyl cyclases (GCs), which are known to be activated by sperm-activating peptides (SAPs), such as speract or resact. These ligand peptides are released by a range of invertebrates to stimulate the metabolism and motility of spermatozoa and are also potent chemoattractants. These GCs contain a single transmembrane segment, an extracellular ligand binding domain, and intracellular protein kinase-like and cyclase catalytic domains. GCs of insect and nematodes, which exhibit high sequence similarity to the speract receptor are also included in this model.
Pssm-ID: 380593 [Multi-domain] Cd Length: 400 Bit Score: 87.69 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 49 AMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQsltfvqaliqkdTSDVRCtngeppvfvkpEKVVGVIGASGS- 127
Cdd:cd06370 25 AITLAVDDVNNDPNLLPGHTLSFVWNDTRCDELLSIRA------------MTELWK-----------RGVSAFIGPGCTc 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 128 SVSIMVANILRLfqiPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFT 207
Cdd:cd06370 82 ATEARLAAAFNL---PMISYKCADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKWSKIADTIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 208 QISkEAGGLCIAQSVRIPQE---RKDRTIDFDRIIKQLLDTpnSRAVVIFANDEDIKQILAAAKRAD--QVGHFLWVGSD 282
Cdd:cd06370 159 ELL-ELNNIEINHEEYFPDPypyTTSHGNPFDKIVEETKEK--TRIYVFLGDYSLLREFMYYAEDLGllDNGDYVVIGVE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 283 ----------------SWGSKINPLHQHEDIAEGAITIQPKRATVEGFDAyFTSRTLENNRRnvwfaeyweENFNcklti 346
Cdd:cd06370 236 ldqydvddpakypnflSGDYTKNDTKEALEAFRSVLIVTPSPPTNPEYEK-FTKKVKEYNKL---------PPFN----- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 347 sgskkedtdrkctgqerigkDSNYEQEGKVQFVI-------DAVYAMAHALHhmnkdlcadyrgvcpEMEQAG-----GK 414
Cdd:cd06370 301 --------------------FPNPEGIEKTKEVPiyaaylyDAVMLYARALN---------------ETLAEGgdprdGT 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
2E4Z_A 415 KLLKYIRHVNFNGSAGTPVMFNKNGDAPGRYDIFQYQTTNTTNPG 459
Cdd:cd06370 346 AIISKIRNRTYESIQGFDVYIDENGDAEGNYTLLALKPNKGTNDG 390
|
|
| PBP1_ABC_ligand_binding-like |
cd19984 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
116-307 |
1.41e-17 |
|
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: 380639 [Multi-domain] Cd Length: 296 Bit Score: 83.04 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDrrYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASE 195
Cdd:cd19984 66 DKVKAIIGGVCSSETLAIAPIAEQNKVVLISPGASSPEITKA--GDYIFRNYPSDAYQGKVLAEFAYNKLYKKVAILYEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 196 GSYGEKGVESFTQISKEAGGLcIAQSVRIPQERKD-RTIdfdrI--IKQLldtpNSRAVVIFANDEDIKQILaaaKRADQ 272
Cdd:cd19984 144 NDYGVGLKDVFKKEFEELGGK-IVASESFEQGETDfRTQ----LtkIKAA----NPDAIFLPGYPKEGGLIL---KQAKE 211
|
170 180 190
....*....|....*....|....*....|....*.
2E4Z_A 273 VG-HFLWVGSDSWGSKiNPLHQHEDIAEGAITIQPK 307
Cdd:cd19984 212 LGiKAPILGSDGFEDP-ELLEIAGEAAEGVIFTYPA 246
|
|
| PBP1_NPR_GC-like |
cd06352 |
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ... |
49-457 |
2.13e-16 |
|
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: 80.86 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 49 AMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLTFVQAliqkdtsdvrctngeppvfvkpEKVVGVIGASGSS 128
Cdd:cd06352 23 AIDIAIERINSEGLLLPGFNFEFTYRDSCCDESEAVGAAADLIYK----------------------RNVDVFIGPACSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 129 VSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGV-ESFT 207
Cdd:cd06352 81 AADAVGRLATYWNIPIITWGAVSASFLDKSRYPTLTRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDDSKCFSIaNDLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 208 QISKEAGGLCIAQsvrIPQERKDRTIDFDRIIKQLLDtpNSRAVVIFANDEDIKQILAAAKRADQV-GHFLWVGSDSW-- 284
Cdd:cd06352 161 DALNQEDNLTISY---YEFVEVNSDSDYSSILQEAKK--RARIIVLCFDSETVRQFMLAAHDLGMTnGEYVFIFIELFkd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 285 GSKINPLHQHE----------DIAEGAITIQPKRATVEGFDAYftsrtlennRRNVWfAEYWEENFNCkltisgskkedt 354
Cdd:cd06352 236 GFGGNSTDGWErndgrdedakQAYESLLVISLSRPSNPEYDNF---------SKEVK-ARAKEPPFYC------------ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 355 drkctgqerigKDSNYEQegKVQFVI---DAVYAMAHALHHMNKDLcADYRgvcpemeqaGGKKLLKYIRHVNFNGSAGt 431
Cdd:cd06352 294 -----------YDASEEE--VSPYAAalyDAVYLYALALNETLAEG-GNYR---------NGTAIAQRMWNRTFQGITG- 349
|
410 420
....*....|....*....|....*..
2E4Z_A 432 PVMFNKNGDapgRYDIFQ-YQTTNTTN 457
Cdd:cd06352 350 PVTIDSNGD---RDPDYAlLDLDPSTG 373
|
|
| PBP1_ABC_LIVBP-like |
cd06342 |
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ... |
116-450 |
7.71e-15 |
|
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine); This subgroup includes the type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active transport systems that are involved in the transport of all three branched chain aliphatic amino acids (leucine, isoleucine and valine). This subgroup also includes a leucine-specific binding protein (or LivK), which is very similar in sequence and structure to leucine-isoleucine-valine binding protein (LIVBP). ABC-type active transport systems are transmembrane proteins that function in the transport of diverse sets of substrates across extra- and intracellular membranes, including carbohydrates, amino acids, inorganic ions, dipeptides and oligopeptides, metabolic products, lipids and sterols, and heme, to name a few.
Pssm-ID: 380565 [Multi-domain] Cd Length: 334 Bit Score: 75.64 E-value: 7.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSdDRRYDFFSRVVPPDSFQAQAMVD-IVKALGWNYVSTLAS 194
Cdd:cd06342 65 DGVVAVIGHYNSGAAIAAAPIYAEAGIPMISPSATNPKLT-EQGYKNFFRVVGTDDQQGPAAADyAAKTLKAKRVAVIHD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 195 EGSYGEKGVESFTQISKEAGGLCIAQ-SVRipqerkDRTIDFDRIIKQLLDtpnSRAVVIF--ANDEDIKQILAAAKRAD 271
Cdd:cd06342 144 GTAYGKGLADAFKKALKALGGTVVGReGIT------PGTTDFSALLTKIKA---ANPDAVYfgGYYPEAGLLLRQLREAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 272 qvGHFLWVGSDswGSKiNPlhqheDIAEGAitiqpkRATVEGfdAYFTSRTLENNRRNVWFAeyWEENFnckltisgskk 351
Cdd:cd06342 215 --LKAPFMGGD--GIV-SP-----DFIKAA------GDAAEG--VYATTPGAPPEKLPAAKA--FLKAY----------- 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 352 edtdrkctgQERIGKD-SNYeqegkVQFVIDAVYAMAHAlhhmnkdlcadyrgvcpeMEQAGG---KKLLKYIRHVNFNG 427
Cdd:cd06342 264 ---------KAKFGEPpGAY-----AAYAYDAAQVLLAA------------------IEKAGStdrAAVAAALRATDFDG 311
|
330 340
....*....|....*....|....
2E4Z_A 428 SAGtPVMFNKNGD-APGRYDIFQY 450
Cdd:cd06342 312 VTG-TISFDAKGDlTGPAFTVYQV 334
|
|
| PBP1_ABC_LivK_ligand_binding-like |
cd06347 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
43-286 |
7.75e-14 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380570 [Multi-domain] Cd Length: 334 Bit Score: 72.58 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 43 GIHRLEAMLYALDQINSDPNLLP-NVTLgaRILDTCSRDTyaleQSLTFVQALIQKDtsdvrctngeppvfvkpeKVVGV 121
Cdd:cd06347 16 GQPALNGAELAVDEINAAGGILGkKIEL--IVYDNKSDPT----EAANAAQKLIDED------------------KVVAI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 122 IGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFfsRVVPPDSFQAQAMVD-IVKALGWNYVSTLASEGS-YG 199
Cdd:cd06347 72 IGPVTSSIALAAAPIAQKAKIPMITPSATNPLVTKGGDYIF--RACFTDPFQGAALAKfAYEELGAKKAAVLYDVSSdYS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 200 EKGVESFTQISKEAGGLCIAQsvripQERKDRTIDFDRIIKQLLdtpNSRAVVIF--ANDEDIKQILAAAKRADQVGHFL 277
Cdd:cd06347 150 KGLAKAFKEAFEKLGGEIVAE-----ETYTSGDTDFSAQLTKIK---AANPDVIFlpGYYEEAALIIKQARELGITAPIL 221
|
....*....
2E4Z_A 278 wvGSDSWGS 286
Cdd:cd06347 222 --GGDGWDS 228
|
|
| PBP1_ABC_ligand_binding-like |
cd19980 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
42-338 |
1.38e-13 |
|
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: 71.87 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 42 NGIHRLEAMLYALDQINSDPNLLpnvtlgARILDTCSRDT-YALEQSLTFVQALIQKDtsdvrctngeppvfvkpeKVVG 120
Cdd:cd19980 15 LGQQVLNGAKLAVEEINAKGGVL------GRKLELVVEDDkCPPAEGVAAAKKLITDD------------------KVPA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 121 VIGASGSSVSIMVANILRLFQIPQISYASTAPELSdDRRYDFFSRVVPPDSFQAQAMVD-IVKALGWNYVSTLASEGSYG 199
Cdd:cd19980 71 IIGAWCSSVTLAVMPVAERAKVPLVVEISSAPKIT-EGGNPYVFRLNPTNSMLAKAFAKyLADKGKPKKVAFLAENDDYG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 200 EKGVESFTQISKEAGGLCIAqsvripQERKDR-TIDFDRIIKQLLDTpNSRAVVIFANDEDIKQILaaaKRADQVGHFL- 277
Cdd:cd19980 150 RGAAEAFKKALKAKGVKVVA------TEYFDQgQTDFTTQLTKLKAA-NPDAIFVVAETEDGALIL---KQARELGLKQq 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
2E4Z_A 278 WVGSDSWGSKiNPLHQHEDIAEGAITIqpkratvegfDAYF-TSRTLENNRRNVWFAEYWEE 338
Cdd:cd19980 220 LVGTGGTTSP-DLIKLAGDAAEGVYGA----------SIYApTADNPANKAFVAAYKKKYGE 270
|
|
| PBP1_ABC_RPA1789-like |
cd06333 |
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ... |
43-214 |
2.92e-12 |
|
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, RPA1791-1793), involved in active transport of lignin-derived aromatic substrates, and its close homologs; This group includes RPA1789 (CouP) from Rhodopseudomonas palustris and its close homologs in other bacteria. RPA1789 (CouP) is the periplasmic binding-protein component of an ABC system (CouPSTU; RPA1789, RPA1791-1793) that is involved in the active transport of lignin-derived aromatic substrates. Members of this group has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP).
Pssm-ID: 380556 [Multi-domain] Cd Length: 342 Bit Score: 67.96 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 43 GIHRLEAMLYALDQINSDPNLLP-NVTLgaRILDTCSRDTyaleQSLTFVQALIQKDtsdvrctngeppvfvkpeKVVGV 121
Cdd:cd06333 16 GIPERNAVELLVEQINAAGGINGrKLEL--IVYDDESDPT----KAVTNARKLIEED------------------KVDAI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 122 IGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFfsRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEK 201
Cdd:cd06333 72 IGPSTTGESLAVAPIAEEAKVPLISLAGAAAIVEPVRKWVF--KTPQSDSLVAEAILDYMKKKGIKKVALLGDSDAYGQS 149
|
170
....*....|...
2E4Z_A 202 GVESFTQISKEAG 214
Cdd:cd06333 150 GRAALKKLAPEYG 162
|
|
| PBP1_ABC_HAAT-like |
cd19985 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
116-287 |
2.09e-11 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides; 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 the uptake of hydrophobic amino acids or peptides. 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: 380640 [Multi-domain] Cd Length: 321 Bit Score: 64.99 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFfsRVVPPDSFQAQAMVD-IVKALGWNYVSTLAS 194
Cdd:cd19985 65 DKALAVIGHYYSSASIAAGKIYKKAGIPAITPSATADAVTRDNPWYF--RVIFNDSLQGRFLANyAKKVLKKDKVSIIYE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 195 EGSYGEKGVESFTQISKEAgGLCIAQSVRIPQERKDRTIDFDRIIKQLLDTPNSRAVVIFA--NDEDIKqILAAAKRADq 272
Cdd:cd19985 143 EDSYGKSLASVFEATARAL-GLKVLKKWSFDTDSSQLDQNLDQIVDELKKAPDEPGVIFLAthADEGAK-LIKKLRDAG- 219
|
170
....*....|....*
2E4Z_A 273 VGHFLwVGSDSWGSK 287
Cdd:cd19985 220 LKAPI-IGPDSLASE 233
|
|
| PBP1_ABC_ligand_binding-like |
cd06335 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
49-214 |
5.41e-11 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport 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 transport of amino acids, peptides, or inorganic ions. Members of this group are sequence-similar to members of the family of ABC-type hydrophobic amino acid transporters, such as leucine-isoleucine-valine binding protein (LIVBP); however their ligand specificity has not been determined experimentally.
Pssm-ID: 380558 [Multi-domain] Cd Length: 348 Bit Score: 64.17 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 49 AMLYALDQINSDPNLLpnvtlGARI-LDTcsRDTYA-LEQSLTFVQALIQKdtsdvrctngeppvfvkpEKVVGVIGASG 126
Cdd:cd06335 22 GVELAVEEINAAGGIL-----GRKIeLVE--RDDEAnPTKAVQNAQELIDK------------------EKVVAIIGPTN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 127 SSVSIMVANILRLFQIPQISYASTAPELSDDRRYDF---FsRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGV 203
Cdd:cd06335 77 SGVALATIPILQEAKIPLIIPVATGTAITKPPAKPRnyiF-RVAASDTLQADFLVDYAVKKGFKKIAILHDTTGYGQGGL 155
|
170
....*....|.
2E4Z_A 204 ESFTQISKEAG 214
Cdd:cd06335 156 KDVEAALKKRG 166
|
|
| PBP1_ABC_HAAT-like |
cd06344 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
117-270 |
9.96e-10 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides; 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 the uptake of hydrophobic amino acids or peptides. 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: 380567 [Multi-domain] Cd Length: 332 Bit Score: 59.93 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 117 KVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDR-RYDFfsRVVPPDSFQAQAMVDIVKALGWNYVSTLASE 195
Cdd:cd06344 65 DVVAVIGHRSSYVAIPASIIYERAGLLMLSPGATAPKLTQHGfKYIF--RNIPSDEDIARQLARYAARQGYKRIVIYYDD 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2E4Z_A 196 GSYGEKGVESFTQISKEAGGLCIAQSVRIPQERkdrtiDFDRIIKQLLDTPNSRAVVIFANDEDIKQILAAAKRA 270
Cdd:cd06344 143 DSYGKGLANAFEEEARELGITIVDRRSYSSDEE-----DFRRLLSKWKALDFFDAIFLAGSMPEGAEFIKQAREL 212
|
|
| PBP1_iGluR_AMPA |
cd06380 |
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ... |
19-472 |
1.51e-09 |
|
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: 59.60 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 19 LGGLFPVhakgpsgvpcgdikRENGIHRleAMLYALDQINSDPNLLPNVTLGARILDTCSRDTYALEQSLtfvqaliqkd 98
Cdd:cd06380 2 IGAIFDS--------------GEDQVQT--AFRYAIDRHNSNNNNRFRLFPLTERIDITNADSFSVSRAI---------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 99 tsdvrCTNGEPPVFVkpekVVGviGASGSSVSIMVAnILRLFQIPQISYASTAPELSDDRRYDFFSRvvpPDSfqAQAMV 178
Cdd:cd06380 56 -----CSQLSRGVFA----IFG--SSDASSLNTIQS-YSDTFHMPYITPSFPKNEPSDSNPFELSLR---PSY--IEAIV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 179 DIVKALGWN---YVstlasegsY-GEKGVESFTQI---SKEAGGLCI-AQSVRIPQErkdrTIDFDRIIKQLLDTPNSRA 250
Cdd:cd06380 119 DLIRHYGWKkvvYL--------YdSDEGLLRLQQLydyLKEKSNISVrVRRVRNVND----AYEFLRTLRELDREKEDKR 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 251 VVIFANDEDIKQILAAAKRADQVG---HFLWVGSDswgskINPLHQhEDIAEGAITIqpkraTveGFdayftsRTLENNR 327
Cdd:cd06380 187 IVLDLSSERYQKILEQIVEDGMNRrnyHYLLANLD-----FLDLDL-ERFLHGGVNI-----T--GF------QLVDTNN 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 328 RNVW-FAEYWEENFNckltisgskkedtdrkcTGQERIGKDS-NYEqegkVQFVIDAVYAMAHALHHM---NKDLCADYR 402
Cdd:cd06380 248 KTVKdFLQRWKKLDP-----------------REYPGAGTDTiPYE----AALAVDAVLVIAEAFQSLlrqNDDIFRFTF 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 403 GV-----------C---PEMEQAGGKKLLKYIRHVNFNGSAGtPVMFNKNGdapGR--YDIFQYQTTNTTNPgyRLIGQW 466
Cdd:cd06380 307 HGelynngskgidCdpnPPLPWEHGKAIMKALKKVRFEGLTG-NVQFDDFG---QRknYTLDVIELTSNRGL--RKIGTW 380
|
....*.
2E4Z_A 467 TDELQL 472
Cdd:cd06380 381 SEGDGF 386
|
|
| PBP1_ABC_HAAT-like |
cd06349 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
112-274 |
6.22e-09 |
|
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 or peptides; 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 the uptake of amino acids or peptides. 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: 380572 [Multi-domain] Cd Length: 338 Bit Score: 57.58 E-value: 6.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 112 FVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDrrYDFFSRVVPPDSFQAQAMVD-IVKALGWNYVS 190
Cdd:cd06349 62 FVSDDKVVAVIGDFSSSCSMAAAPIYEEAGLVQISPTASHPDFTKG--GDYVFRNSPTQAVEAPFLADyAVKKLGAKKIA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 191 TLASEGSYGEKGVESFTQISKEAGGLCIAQSVRIPQERkdrtiDFDRIIKQLLDTpNSRAVVIFANDEDIKQIlaaAKRA 270
Cdd:cd06349 140 IIYLNTDWGVSAADAFKKAAKALGGEIVATEAYLPGTK-----DFSAQITKIKNA-NPDAIYLAAYYNDAALI---AKQA 210
|
....
2E4Z_A 271 DQVG 274
Cdd:cd06349 211 RQLG 214
|
|
| PBP1_ABC_HAAT-like |
cd19988 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
43-215 |
7.89e-09 |
|
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 or peptides; 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 the uptake of amino acids or peptides. 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: 380643 [Multi-domain] Cd Length: 302 Bit Score: 56.90 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 43 GIHRLEAMLYALDQINSdpnllPNVTLGARIlDTCSRDTYAL-EQSLTFVQALIQKDtsdvrctngeppvfvkpeKVVGV 121
Cdd:cd19988 16 GQAMLQGAELAVEEINA-----AGGILGIPI-ELVVEDDEGLpAASVSAAKKLIYQD------------------KVWAI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 122 IGASGSSVSIMVANILRLFQIPQISYASTAPELSdDRRYDFFSRVVPPDSFQAQAMVD-IVKALGWNYVSTLASEGSYGE 200
Cdd:cd19988 72 IGSINSSCTLAAIRVALKAGVPQINPGSSAPTIT-ESGNPWVFRCTPDDRQQAYALVDyAFEKLKVTKIAVLYVNDDYGR 150
|
170
....*....|....*
2E4Z_A 201 KGVESFTQISKEAGG 215
Cdd:cd19988 151 GGIDAFKDAAKKYGI 165
|
|
| PBP1_ABC_HAAT-like |
cd19986 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
116-287 |
4.25e-08 |
|
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 or peptides; 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 the uptake of amino acids or peptides. 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: 380641 [Multi-domain] Cd Length: 297 Bit Score: 54.56 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQIsYASTAPELSDdRRYDFFSRVVPPDSFQAQAMVD-IVKALGWNYVSTLAS 194
Cdd:cd19986 66 DKVVAVIGPHYSTQVLAVSPLVKEAKIPVI-TGGTSPKLTE-QGNPYMFRIRPSDSVSAKALAKyAVEELGAKKIAILYD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 195 EGSYGEKGVESFTQISKEAgGLCIAQSVRIPQERKDRTidfdriiKQLLDTPNSRA--VVIFANDEDIKQIlaaAKRADQ 272
Cdd:cd19986 144 NDDFGTGGADVVTAALKAL-GLEPVAVESYNTGDKDFT-------AQLLKLKNSGAdvIIAWGHDAEAALI---ARQIRQ 212
|
170
....*....|....*.
2E4Z_A 273 VG-HFLWVGSDSWGSK 287
Cdd:cd19986 213 LGlDVPVIGSSSFATP 228
|
|
| PBP1_ABC_HAAT-like |
cd19981 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
43-215 |
4.92e-08 |
|
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 or peptides; 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 the uptake of amino acids or peptides. 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: 380636 [Multi-domain] Cd Length: 297 Bit Score: 54.60 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 43 GIHRLEAMLYALDQINSdpnllpNVTLGARIL------DTCSRDtyaleQSLTFVQALIQKDtsdvrctngeppvfvkpe 116
Cdd:cd19981 16 GKSALHGAELAVEQINA------AGGINGKKVelvvydDQASPK-----QAVNIAQKLIEQD------------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 117 KVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSddRRYDFFSRVVPPDSFQAQAMVD-IVKALGWNYVSTLASE 195
Cdd:cd19981 67 KVVAVVSGSYSGPTRAAAPIFQEAKVPMVSAYAVHPDIT--KAGDYVFRVAFLGPVQGRAGAEyAVKDLGAKKVAILTID 144
|
170 180
....*....|....*....|
2E4Z_A 196 GSYGEKGVESFTQISKEAGG 215
Cdd:cd19981 145 NDFGKSLAAGFKEEAKKLGA 164
|
|
| PBP1_iGluR_Kainate |
cd06382 |
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ... |
49-274 |
1.74e-07 |
|
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: 53.00 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 49 AMLYALDQINSDpNLLPNVTLGARILDTCSRDTYALEQsltFVQALIQkdtsdvrctngeppvfvkpEKVVGVIGASGSS 128
Cdd:cd06382 16 AFKYAVDRINRE-RTLPNTKLVPDIERVPRDDSFEASK---KVCELLE-------------------EGVAAIFGPSSPS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 129 VSIMVANILRLFQIPQISYASTAPELSDDRrydfFSRVVPPDSFQ-AQAMVDIVKALGWNyvstlasegsygekgveSFT 207
Cdd:cd06382 73 SSDIVQSICDALEIPHIETRWDPKESNRDT----FTINLYPDPDAlSKAYADLVKSLNWK-----------------SFT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 208 QISKEAGGLCIAQSV-RIPQERKDRTidfdrIIKQLLDTPNSRAV------------VIFANDEDIKQILAAAKradQVG 274
Cdd:cd06382 132 ILYEDDEGLIRLQELlKLPKPKDIPI-----TVRQLDPGDDYRPVlkeikksgetriILDCSPDRLVDVLKQAQ---QVG 203
|
|
| PBP1_ABC_HAAT-like |
cd19983 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
116-259 |
5.97e-07 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems predicted to be involved in uptake of hydrophobic amino acids or peptides; 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 the uptake of hydrophobic amino acids or peptides. 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: 380638 [Multi-domain] Cd Length: 303 Bit Score: 51.05 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRryDFFSRVVPPDSFQAQAMVD-IVKALGwnyVSTLA- 193
Cdd:cd19983 65 GGVVAIIGHMTSAMTVAVLPVINEAKVLMISPTVSTPELSGKD--DYFFRVTPTTRESAQALARyAYNRGG---LRRVAv 139
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 194 ----SEGSYGEKGVESFTQISKEAGGLcIAQSVRIPQERKDrtiDFDRIIKQLLDTpNSRAVVIFANDED 259
Cdd:cd19983 140 iydlSNRAYSESWLDNFRSEFEALGGR-IVAEIPFSSGADV---DFSDLARRLLAS-KPDGLLLVASAVD 204
|
|
| PBP1_YraM_LppC_lipoprotein-like |
cd06339 |
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup ... |
47-284 |
7.81e-07 |
|
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup includes periplasmic binding component of lipoprotein LppC, an immunodominant antigen, whose molecular function is not characterized. Members of this subgroup are predicted to be involved in transport of lipid compounds, and they are sequence similar to the family of ABC-type hydrophobic amino acid transporters (HAAT).
Pssm-ID: 380562 [Multi-domain] Cd Length: 331 Bit Score: 51.12 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 47 LEAMLYALDQIN-SDPNLLPnvtlgarildtcsRDTYALEQSLTFVQALIQkdtsdvrctngeppvfvkpEKVVGVIG-A 124
Cdd:cd06339 20 RDGIELALFDAGgSRPELRV-------------YDTGGPEGAAAAYQQAVA-------------------EGADLIIGpL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 125 SGSSVSImVANILRLFQIPQISYASTAPELSDDRRYDFFsrvVPPDSfQAQAMVDIVKALGWNYVSTLASEGSYGEKGVE 204
Cdd:cd06339 68 LKSSVAA-LAAAAQALGVPVLALNNDESATAGPGLFQFG---LSPED-EARQAARYAVQQGLRRFAVLAPDNAYGQRVAN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 205 SFTQISKEAGGLcIAQSVRIPQERKdrtiDFDRIIKQLLDTPNSR---------------------AVVIFANDEDIKQI 263
Cdd:cd06339 143 AFREAWQALGGT-VVAVESYDPDET----DFSAAIRRLLGVDQSEarirqlgellefeprrrqdfdAIFLPAGPEQARLI 217
|
250 260
....*....|....*....|...
2E4Z_A 264 --LAAAKRADQVgHFLwvGSDSW 284
Cdd:cd06339 218 apQLAFYGAGDV-PLL--GTSLW 237
|
|
| PBP1_ABC_ligand_binding-like |
cd06340 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
116-184 |
2.59e-06 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport 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 transport 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, their ligand specificity has not been determined experimentally.
Pssm-ID: 380563 [Multi-domain] Cd Length: 352 Bit Score: 49.48 E-value: 2.59e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDdRRYDFFSRVVPPDSFQAQAMVDIVKAL 184
Cdd:cd06340 69 EGVVAIIGAYSSSVTLAASQVAERYGVPFVTASAVADEITE-RGFKYVFRTAPTASQFAEDAVDFLKEL 136
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
116-306 |
2.79e-06 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 49.19 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDrryDFFSrVVPPDSFQAQAMVD-IVKALGWNYVSTLAS 194
Cdd:pfam13458 68 DGVDAIVGGVSSAVALAVAEVLAKKGVPVIGPAALTGEKCSP---YVFS-LGPTYSAQATALGRyLAKELGGKKVALIGA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 195 EGSYGEKGVESFTQISKEAGGLcIAQSVRIPQErkdrTIDFDRIIKQLLDtpnSRA-VVIFAND-EDIKQILAAAKRADq 272
Cdd:pfam13458 144 DYAFGRALAAAAKAAAKAAGGE-VVGEVRYPLG----TTDFSSQVLQIKA---SGAdAVLLANAgADTVNLLKQAREAG- 214
|
170 180 190
....*....|....*....|....*....|....*
2E4Z_A 273 vGHFLWVGSDSWGSKINPLHQ-HEDIAEGAITIQP 306
Cdd:pfam13458 215 -LDAKGIKLVGLGGDEPDLKAlGGDAAEGVYATVP 248
|
|
| PBP1_iGluR_NMDA_NR1 |
cd06379 |
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR1, an ... |
53-274 |
6.54e-06 |
|
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: 48.10 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 53 ALDQINSDPNLLPNVTLGArilDTCSRDTYALEQSLTFVQALIQKDTSDVrctngeppvfvkpekVVGVIGASGSSVSIM 132
Cdd:cd06379 21 AVNEVNAHSHLPRKITLNA---TSITLDPNPIRTALSVCEDLIASQVYAV---------------IVSHPPTPSDLSPTS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 133 VANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGSYGEKGVESFtqiske 212
Cdd:cd06379 83 VSYTAGFYRIPVIGISARDSAFSDKNIHVSFLRTVPPYSHQADVWAEMLRHFEWKQVIVIHSDDQDGRALLGRL------ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2E4Z_A 213 agglciaQSVRIPQERK-DRTIDFD----RIIKQLLDTPN--SRAVVIFANDEDIKQILAAAKRADQVG 274
Cdd:cd06379 157 -------ETLAETKDIKiEKVIEFEpgekNFTSLLEEMKElqSRVILLYASEDDAEIIFRDAAMLNMTG 218
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
112-317 |
2.30e-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: 380566 [Multi-domain] Cd Length: 355 Bit Score: 46.41 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 112 FVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSrVVPPDSFQAQAMVD-IVKALGWNYVS 190
Cdd:cd06343 69 LVEQDKVFAIVGGLGTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKPYTFG-VQPSYEDEGRILADyIVETLPAAKVA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 191 TLASEGSYGEKGVESFTQISKEAGglciAQSV-RIPQERKDrtIDFDRIIKQLLDTpNSRAVVIFANdedIKQILAAAKR 269
Cdd:cd06343 148 VLYQNDDFGKDGLEGLKEALKAYG----LEVVaEETYEPGD--TDFSSQVLKLKAA-GADVVVLGTL---PKEAAAALKE 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
2E4Z_A 270 ADQVG-HFLWVGSDSWGSKINPLHQHEDIAEGAITIQ----PKRATVEGFDAY 317
Cdd:cd06343 218 AAKLGwKPTFLGSSVSADPTTLAKAGGDAAEGVYSASylkdPTDADDPAVKEF 270
|
|
| PBP1_SBP-like |
cd19989 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
41-341 |
2.54e-05 |
|
periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380644 [Multi-domain] Cd Length: 299 Bit Score: 46.12 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 41 ENGIHRLEAMLYALDQINSDPNLL-PNVTLgaRILDTCSRDTYALEQsltfVQALIQKDTSDVrctngeppvfvkpekvv 119
Cdd:cd19989 14 ALGEEARRGAQLAVEEINAAGGILgRPVEL--VVEDTEGKPATAVQK----ARKLVEQDGVDF----------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 120 gVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDD--RRYDFfsRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGS 197
Cdd:cd19989 71 -LTGAVSSAVALAVAPKAAELKVPYLVTVAADDELTGEncNRYTF--RVNTSDRMIARALAPWLAENGGKKWYIVYADYA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 198 YGEKGVESFTQISKEAGGLcIAQSVRIPQErkdrTIDFDRIIKQLldtPNSRA----VVIFANDedikqILAAAKRADQV 273
Cdd:cd19989 148 WGQSSAEAFKEAIEELGGE-VVGTLFAPLG----TTDFSSYITQI---SDSGAdgllLALAGSD-----AVNFLKQAGQF 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2E4Z_A 274 G---HFLWVGSDSWGSKINpLHQHEDIAEGAITIqpkratvEGFDAYFTSrtlENNRRnvwFAEYWEENFN 341
Cdd:cd19989 215 GlgkKYKIVGGILSIEPLA-LPALGDAAEGVYGG-------VRYPPTLDT---PANRA---FVEAYEKEYG 271
|
|
| PBP1_ABC_HAAT-like |
cd06348 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
43-183 |
4.96e-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 or peptides; 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 the uptake of amino acids or peptides. 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: 380571 [Multi-domain] Cd Length: 342 Bit Score: 45.30 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 43 GIHRLEAMLYALDQINSDPNLLpNVTLGARILDTCSrdtyALEQSLTFVQALIQKDtsdvrctngeppvfvkpeKVVGVI 122
Cdd:cd06348 16 GQSQKNGAQLAVEEINAAGGVG-GVKIELIVEDTAG----DPEQAINAFQKLINQD------------------KVLAIL 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
2E4Z_A 123 GASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFfsRVVPPDSFQAQAMVDIVKA 183
Cdd:cd06348 73 GPTLSSEAFAADPIAQQAKVPVVGISNTAPGITDIGPYIF--RNSLPEDKVIPPTVKAAKK 131
|
|
| PBP1_ABC_ligand_binding-like |
cd06345 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
116-238 |
4.16e-04 |
|
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: 380568 [Multi-domain] Cd Length: 356 Bit Score: 42.64 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPEL-----SDDRRYDFFSRVVPPDSFQAQAMVD-----IVKALG 185
Cdd:cd06345 63 DKVDAIVGGFRSEVVLAAMEVAAEYKVPFIVTGAASPAItkkvkKDYEKYKYVFRVGPNNSYLGATVAEflkdlLVEKLG 142
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
2E4Z_A 186 WNYVSTLASEGSYGEKGVESFTQISKEAgGLCIAQSVRIPQERKDRTIDFDRI 238
Cdd:cd06345 143 FKKVAILAEDAAWGRGIAEALKKLLPEA-GLEVVGVERFPTGTTDFTPILSKI 194
|
|
| PBP1_As_SBP-like |
cd06330 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
116-214 |
4.72e-04 |
|
periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea that is predicted to be involved in the efflux of toxic compounds. Members of this subgroup include proteins from Herminiimonas arsenicoxydans, which is resistant to arsenic (As) and various heavy metals such as cadmium and zinc. Moreover, they show significant sequence similarity to the cluster of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa.
Pssm-ID: 380553 [Multi-domain] Cd Length: 342 Bit Score: 42.16 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 116 EKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNY--VSTLA 193
Cdd:cd06330 66 EGVDFLIGTISSGVALAVAPVAEELKVLFIATDAATDRLTEENFNPYVFRTSPNTYMDAVAAALYAAKKPPDVkrWAGIG 145
|
90 100
....*....|....*....|.
2E4Z_A 194 SEGSYGEKGVESFTQISKEAG 214
Cdd:cd06330 146 PDYEYGRDSWAAFKAALKKLK 166
|
|
| PBP1_ABC_ligand_binding-like |
cd19982 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
112-214 |
1.40e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport 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 transport 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, their ligand specificity has not been determined experimentally.
Pssm-ID: 380637 [Multi-domain] Cd Length: 302 Bit Score: 40.73 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 112 FVKPEKVVGVIGASGSSVSIMVANILRLFQIPQISYASTAPELSdDRRYDFFSRVVPPDSFQAQAMVDIVKALGW-NYVS 190
Cdd:cd19982 62 LVSQDKVPLIVGGYSSGITLPVAAVAERQKIPLLVPTAADDDIT-KPGYKYVFRLNPPASIYAKALFDFFKELVKpKTIA 140
|
90 100
....*....|....*....|....
2E4Z_A 191 TLASEGSYGEKGVESFTQISKEAG 214
Cdd:cd19982 141 ILYENTAFGTSVAKAARRFAKKRG 164
|
|
| PBP1_iGluR_non_NMDA-like |
cd06368 |
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the non-NMDA ... |
42-269 |
3.11e-03 |
|
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: 39.66 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 42 NGIHRLEAMLYALDQINSDPNLLPNVTLgarildtcsrdtyalEQSLTFVQALIQKDTSDVRCTngeppvfVKPEKVVGV 121
Cdd:cd06368 10 NDAHERAAFRYAVERLNTNIVKLAYFRI---------------TYSIEAIDSNSHFDATDKACD-------LLEKGVVAI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2E4Z_A 122 IGASGSSVSIMVANILRLFQIPQISyastaPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVsTLASEGSYGEK 201
Cdd:cd06368 68 VGPSSSDSNNALQSICDALDVPHIT-----VHDDPRLSKSQYSLSLYPRNQLSQAVSDLLKYWRWKRF-VLVYDDDDRLR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2E4Z_A 202 GVESFT---QISKEagglciaqSVRIPQERKD-RTIDFDRIIKQLLDTPNSRaVVIFANDEDIKQILAAAKR 269
Cdd:cd06368 142 RLQELLeaaRFSKR--------FVSVRKVDLDyKTLDETPLLKRKDCSLFSR-ILIDLSPEKAYTFLLQALE 204
|
|
| |
