|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_GABAb_receptor |
cd06366 |
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ... |
176-574 |
0e+00 |
|
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: 626.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 176 YIGALFPMSG--GWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKI-ILMPGCS 252
Cdd:cd06366 1 YIGGLFPLSGskGWWGGAGILPAAEMALEHINNRSDILPGYNLELIWNDTQCDPGLGLKALYDLLYTPPPKVmLLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 253 SVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLE 332
Cdd:cd06366 81 SVTEPVAEASKYWNLVQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 333 ERVKEAGIEITFRQSFFS-DPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDP 411
Cdd:cd06366 161 ELLEEANITIVATESFSSeDPTDQLENLKEKDARIIIGLFYEDAARKVFCEAYKLGMYGPKYVWILPGWYDDNWWDVPDN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 412 SINCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKrhPEETGGFQEAPLAYDAIWALALALNKTSG 491
Cdd:cd06366 241 DVNCTPEQMLEALEGHFSTELLPLNPDNTKTISGLTAQEFLKEYLERLS--NSNYTGSPYAPFAYDAVWAIALALNKTIE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 492 GGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTD 571
Cdd:cd06366 319 KLAEYNKTLEDFTYNDKEMADLFLEAMNSTSFEGVSGPVSFDSKGDRLGTVDIEQLQGGSYVKVGLYDPNADSLLLLNES 398
|
....*
gi 2462493251 572 --KWI 574
Cdd:cd06366 399 siVWP 403
|
|
| PBP1_glutamate_receptors-like |
cd06269 |
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ... |
176-568 |
1.04e-126 |
|
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: 375.22 E-value: 1.04e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 176 YIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06269 1 TIGALLPVHDYLESGAKVLPAFELALSDVNSRPDLLPKTTLGLAIRDSECNPTQALLSACDLLAAAKVVAILGPGCSASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERV 335
Cdd:cd06269 81 APVANLARHWDIPVLSYGATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEELF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 336 KEAGIEITFRQSFFS----DPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWfkiydp 411
Cdd:cd06269 161 QEKGGLITSRQSFDEnkddDLTKLLRNLRDTEARVIILLASPDTARSLMLEAKRLDMTSKDYVWFVIDGEASSS------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 412 siNCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQefveKLTKRLKRHPEETGGFQEAPLAYDAIWAlalalnktsg 491
Cdd:cd06269 235 --DEHGDEARQAAEGAITVTLIFPVVKEFLKFSMELKL----KSSKRKQGLNEEYELNNFAAFFYDAVLA---------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 492 gggrsgvrledfnynnqtitdqiyramnsssfegvsghvvfdasgSRMAWTLIEQLQ---GGSYKKIGYYDStKDDLSWS 568
Cdd:cd06269 299 ---------------------------------------------DRPGQFSIINLQyteAGDYRKVGTWDS-EGGLNMS 332
|
|
| ANF_receptor |
pfam01094 |
Receptor family ligand binding region; This family includes extracellular ligand binding ... |
192-549 |
2.32e-82 |
|
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: 261.55 E-value: 2.32e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 192 ACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELlYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLS 271
Cdd:pfam01094 1 LVLLAVRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDL-LKGEVVAIIGPSCSSVASAVASLANEWKVPLIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 272 YGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSF--- 348
Cdd:pfam01094 80 YGSTSPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIppa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 349 --FSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDPSInctvdemtEAVEG 426
Cdd:pfam01094 160 qdDDEIARKLLKEVKSRARVIVVCCSSETARRLLKAARELGMMGEGYVWIATDGLTTSLVILNPSTL--------EAAGG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 427 HITTEIVMLNPANTrsisnmtsQEFVEKLTKRLKRHPEETGGFQEAP--LAYDAIWALALALNKTSGGGGRSGVRLEDFN 504
Cdd:pfam01094 232 VLGFRLHPPDSPEF--------SEFFWEKLSDEKELYENLGGLPVSYgaLAYDAVYLLAHALHNLLRDDKPGRACGALGP 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462493251 505 YNNqtiTDQIYRAMNSSSFEGVSGHVVFDASGSRM-AWTLIEQLQG 549
Cdd:pfam01094 304 WNG---GQKLLRYLKNVNFTGLTGNVQFDENGDRInPDYDILNLNG 346
|
|
| PBP1_NPR_GC-like |
cd06352 |
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ... |
177-561 |
2.45e-41 |
|
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: 153.67 E-value: 2.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGG--WPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSV 254
Cdd:cd06352 2 VGVLAPSNSQslPVGYARSAPAIDIAIERINSEGLLLPGFNFEFTYRDSCCDESEAVGAAADLIYKRNVDVFIGPACSAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 255 STLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRThpSATLHNPTRV--KLFEKWGWKKIATIQQTTEVF-TSTLDDL 331
Cdd:cd06352 82 ADAVGRLATYWNIPIITWGAVSASFLDKSRYPTLTRT--SPNSLSLAEAllALLKQFNWKRAAIIYSDDDSKcFSIANDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 332 EERV-KEAGIEITFRQSFFSDPAVPVKN-LKRQD--ARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIG------WY 401
Cdd:cd06352 160 EDALnQEDNLTISYYEFVEVNSDSDYSSiLQEAKkrARIIVLCFDSETVRQFMLAAHDLGMTNGEYVFIFIElfkdgfGG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 402 ADNWFKIYDPSINCTVDEMTEAVeghItteIVMLNPANTRSISNmtsqeFVEKLTKRLKRHP-------EETGGFQeAPL 474
Cdd:cd06352 240 NSTDGWERNDGRDEDAKQAYESL---L---VISLSRPSNPEYDN-----FSKEVKARAKEPPfycydasEEEVSPY-AAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 475 AYDAIWALALALNKTSGgggrsgvrlEDFNYNNQTitdQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQ--GGSY 552
Cdd:cd06352 308 LYDAVYLYALALNETLA---------EGGNYRNGT---AIAQRMWNRTFQGITGPVTIDSNGDRDPDYALLDLDpsTGKF 375
|
....*....
gi 2462493251 553 KKIGYYDST 561
Cdd:cd06352 376 VVVLTYDGT 384
|
|
| PBP1_SAP_GC-like |
cd06370 |
Ligand-binding domain of membrane bound guanylyl cyclases; Ligand-binding domain of membrane ... |
196-558 |
6.89e-37 |
|
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: 141.61 E-value: 6.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 196 AVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIIlMPGCS-SVSTLVAEAarmWNLIVLSYGS 274
Cdd:cd06370 25 AITLAVDDVNNDPNLLPGHTLSFVWNDTRCDELLSIRAMTELWKRGVSAFI-GPGCTcATEARLAAA---FNLPMISYKC 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 275 SSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSfFSDPAV 354
Cdd:cd06370 101 ADPEVSDKSLYPTFARTIPPDSQISKSVIALLKHFNWNKVSIVYENETKWSKIADTIKELLELNNIEINHEEY-FPDPYP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 355 P-----------VKNLKrQDARIIVGLFYETEARKVFCEVYKERLFGKK-YVwfLIGWYAD-NWFKIYDPSINCTVDEMT 421
Cdd:cd06370 180 YttshgnpfdkiVEETK-EKTRIYVFLGDYSLLREFMYYAEDLGLLDNGdYV--VIGVELDqYDVDDPAKYPNFLSGDYT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 422 -----EAVEGHITTEIVMLNPANTRSIsnmtsQEFVEKLTKRLKRHP-----EETGGFQ-----EAPLAYDAIWALALAL 486
Cdd:cd06370 257 kndtkEALEAFRSVLIVTPSPPTNPEY-----EKFTKKVKEYNKLPPfnfpnPEGIEKTkevpiYAAYLYDAVMLYARAL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 487 NKTSGGGgrsgvrlEDfNYNNQTITDQIYRamnsSSFEGVSGHVVF-----DASG--SRMAWTLIEQLQGGSY--KKIGY 557
Cdd:cd06370 332 NETLAEG-------GD-PRDGTAIISKIRN----RTYESIQGFDVYidengDAEGnyTLLALKPNKGTNDGSYglHPVGT 399
|
.
gi 2462493251 558 Y 558
Cdd:cd06370 400 F 400
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
175-555 |
5.96e-33 |
|
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: 128.51 E-value: 5.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 175 VYIGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSS 253
Cdd:COG0683 4 IKIGVLLPLTGPYaALGQPIKNGAELAVEEINAAGGVL-GRKIELVVEDDASDPDTAVAAARKLIDQDKVDAIVGPLSSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 254 VSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLDDLE 332
Cdd:COG0683 83 VALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDDYAYGQGLAAAFK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 333 ERVKEAGIEITFRQSFF---SDPAVPVKNLKRQDARIIvglfyetearkvfcevykerlfgkkyvwFLIGWYADnwfkiy 409
Cdd:COG0683 163 AALKAAGGEVVGEEYYPpgtTDFSAQLTKIKAAGPDAV----------------------------FLAGYGGD------ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 410 dpsincTVDEMTEAVEGHITTEIVmlnpantrsisnmtsQEFVEKLTKRLKRHPEetggfQEAPLAYDAIWALALALNKT 489
Cdd:COG0683 209 ------AALFIKQAREAGLKGPLN---------------KAFVKAYKAKYGREPS-----SYAAAGYDAALLLAEAIEKA 262
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462493251 490 sggggrsgvrledfnynNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQ-GGSYKKI 555
Cdd:COG0683 263 -----------------GSTDREAVRDALEGLKFDGVTGPITFDPDGQGVQPVYIVQVKaDGKFVVV 312
|
|
| PBP1_GABAb_receptor_plant |
cd19990 |
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ... |
177-560 |
4.40e-30 |
|
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: 121.57 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGgwPGGQACQPAVEMALEDVNSRRDIlPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVST 256
Cdd:cd19990 2 IGAILDLNS--RVGKEAKVAIEMAVSDFNSDSSS-YGTKLVLHVRDSKGDPLQAASAALDLIKNKKVEAIIGPQTSEEAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 257 LVAEAARMWNLIVLSYGSSSPALSNRQrFPTFFRTHPSATLHnptrVK----LFEKWGWKKIATIQQTTEVFTSTLDDLE 332
Cdd:cd19990 79 FVAELGNKAQVPIISFSATSPTLSSLR-WPFFIRMTHNDSSQ----MKaiaaIVQSYGWRRVVLIYEDDDYGSGIIPYLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 333 ERVKEAGIEITFRQSFfsdPAVPVKN--------LKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADN 404
Cdd:cd19990 154 DALQEVGSRIEYRVAL---PPSSPEDsieeelikLKSMQSRVFVVHMSSLLASRLFQEAKKLGMMEKGYVWIVTDGITNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 405 wFKIYDPSInctvdemTEAVEGHITTeivmlnpantRSISNMtSQEFVEKLTKRLKRHPEETGGFQEAPL------AYDA 478
Cdd:cd19990 231 -LDSLDSST-------ISSMQGVIGI----------KTYIPE-SSEFQDFKARFRKKFRSEYPEEENAEPniyalrAYDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 479 IWALALALNKtsggggrsgvrledFNYNNQTITDQIYR-----AMNSSSFEGVSGHVVFDASgsrmawtlieQLQ----- 548
Cdd:cd19990 292 IWALAHAVEK--------------LNSSGGNISVSDSGkklleEILSTKFKGLSGEVQFVDG----------QLApppaf 347
|
410
....*....|....*...
gi 2462493251 549 ------GGSYKKIGYYDS 560
Cdd:cd19990 348 eivnviGKGYRELGFWSP 365
|
|
| PBP1_ABC_ligand_binding-like |
cd06336 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
177-488 |
9.80e-25 |
|
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 group 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 (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.
Pssm-ID: 380559 [Multi-domain] Cd Length: 345 Bit Score: 105.39 E-value: 9.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGG---WpgGQACQPAVEMALEDVNSRRDILPD---YELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPG 250
Cdd:cd06336 2 IGFLGPLSGPaaaW--GLPMLRGLELAADEINAAGGIKVGgkkYKVEVVSYDDKYTPAEAVAAARRLVSQDGVKFIFGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 251 CSSVSTLVAEAARMWNLIVLSYGSSSPALSnrQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLD 329
Cdd:cd06336 80 GSAIAAAVQPVTERNKVLLLTAAFSDPILG--PDNPLLFRIPPTPYEYAPPFIKwLKKNGPIKTVALIAPNDATGKDWAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 330 DLEERVKEAGIEITFRQSF------FSDPAVPVKNLKrQDArIIVGLFYETEARKVFcevyKE-RLFGKKYVWFLIGWya 402
Cdd:cd06336 158 AFVAAWKAAGGEVVAEEFYdrgttdFYPVLTKILALK-PDA-LDLGGSSPGPAGLII----KQaRELGFKGPFVSEGG-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 403 dnwfkiydpsinCTVDEM-----TEAVEGhitteIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEEtggfqEAPLAYD 477
Cdd:cd06336 230 ------------AKADEIlkevgGEAAEG-----FIGVLPADDDPIASPGAKAFVERYKKKYGEPPNS-----ESALFYD 287
|
330
....*....|.
gi 2462493251 478 AIWALALALNK 488
Cdd:cd06336 288 AAYILVKAMEK 298
|
|
| PBP1_ABC_LIVBP-like |
cd06342 |
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ... |
177-538 |
6.96e-24 |
|
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: 102.99 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILPdYELKLIHHDSKCDPGQATKYLYELLyNDPIKIILMPGCSSVS 255
Cdd:cd06342 2 IGVAGPLTGPNaALGQDIRNGAELAVDEINAKGGGLG-FKIELVAQDDACDPAQAVAAAQKLV-ADGVVAVIGHYNSGAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSnRQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTeVFTSTL-DDLEE 333
Cdd:cd06342 80 IAAAPIYAEAGIPMISPSATNPKLT-EQGYKNFFRVVGTDDQQGPAAADyAAKTLKAKRVAVIHDGT-AYGKGLaDAFKK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 334 RVKEAGIEITFRQSF------FSDPAVPVKNLKrQDArIIVGLFYE------TEARKVFcevYKERLFGkkyvwfligwy 401
Cdd:cd06342 158 ALKALGGTVVGREGItpgttdFSALLTKIKAAN-PDA-VYFGGYYPeaglllRQLREAG---LKAPFMG----------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 402 ADNwfkIYDPSInctVDEMTEAVEGhitteIVMLNPANTRSiSNMTSQEFVEKLTkrlKRHPEETGGFqeAPLAYDAIWA 481
Cdd:cd06342 222 GDG---IVSPDF---IKAAGDAAEG-----VYATTPGAPPE-KLPAAKAFLKAYK---AKFGEPPGAY--AAYAYDAAQV 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462493251 482 LALALNKTsggggrsgvrledfnynNQTITDQIYRAMNSSSFEGVSGHVVFDASGSR 538
Cdd:cd06342 285 LLAAIEKA-----------------GSTDRAAVAAALRATDFDGVTGTISFDAKGDL 324
|
|
| PBP1_mGluR |
cd06362 |
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ... |
177-566 |
1.02e-23 |
|
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: 104.30 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPM----SGGWPGGQ-----ACQP--AVEMALEDVNSRRDILPDYEL-------------------KLIHHDSKCD 226
Cdd:cd06362 5 LGGLFPVhersSSGECCGEireerGIQRleAMLFAIDEINSRPDLLPNITLgfvilddcssdttaleqalHFIRDSLLSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 227 PGQATK-------YLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHN 299
Cdd:cd06362 85 ESAGFCqcsddppNLDESFQFYDVVGVIGAESSSVSIQVANLLRLFKIPQISYASTSDELSDKERYPYFLRTVPSDSFQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 300 PTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVP-----VKNLKRQ-DARIIVgLFYE 373
Cdd:cd06362 165 KAIVDILLHFNWTYVSVVYSEGSYGEEGYKAFKKLARKAGICIAESERISQDSDEKdyddvIQKLLQKkNARVVV-LFAD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 374 TE-ARKVFcEVYKERLFGKKYVWflIGwyADNWFKIYDPsinctVDEMTEAVEGHITTE------------IVMLNP-AN 439
Cdd:cd06362 244 QEdIRGLL-RAAKRLGASGRFIW--LG--SDGWGTNIDD-----LKGNEDVALGALTVQpyseevprfddyFKSLTPsNN 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 440 TRSI------SNMTSQEFVEKLTKRLKRHPE---ETGGF-QEAPLA--YDAIWALALALNKTSGGGGRSGVRLEDfnYNN 507
Cdd:cd06362 314 TRNPwfrefwQELFQCSFRPSRENSCNDDKLlinKSEGYkQESKVSfvIDAVYAFAHALHKMHKDLCPGDTGLCQ--DLM 391
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462493251 508 QTI-TDQIYRAMNSSSFEGVSGHVV-FDASGSRMAWTLIEQLQ---GGSY--KKIGYYDSTKDDLS 566
Cdd:cd06362 392 KCIdGSELLEYLLNVSFTGEAGGEIrFDENGDGPGRYDIMNFQrnnDGSYeyVRVGVWDQYTQKLS 457
|
|
| PBP1_ABC_ligand_binding-like |
cd19984 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
177-348 |
1.52e-23 |
|
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: 101.14 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGWPG-GQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd19984 2 IGVILPLTGDAASyGEDMKNGIELAVEEINAAGGIN-GKKIELIYEDSKCDPKKAVSAANKLINVDKVKAIIGGVCSSET 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNRQRFptFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEvFTSTL-DDLEER 334
Cdd:cd19984 81 LAIAPIAEQNKVVLISPGASSPEITKAGDY--IFRNYPSDAYQGKVLAEFAYNKLYKKVAILYENND-YGVGLkDVFKKE 157
|
170
....*....|....
gi 2462493251 335 VKEAGIEITFRQSF 348
Cdd:cd19984 158 FEELGGKIVASESF 171
|
|
| PBP1_ABC_ligand_binding-like |
cd06346 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
177-540 |
3.01e-23 |
|
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: 100.72 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06346 2 IGALLPLTGPLaSLGPPMLAAAELAVEEINAAGGVL-GKKVELVVEDSQTDPTAAVDAARKLVDVEGVPAIVGAASSGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERV 335
Cdd:cd06346 81 LAVASVAVPNGVVQISPSSTSPALTTLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVNNDYGQGLADAFKKAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 336 KEAGIEITFRQSFfsDPAVP-----VKNLKRQDARIIVGLFYETEARKVFCEVYkeRLFGKKYVWFLIGWYADNWFKIyd 410
Cdd:cd06346 161 EALGGTVTASVPY--EPGQTsyraeLAQAAAGGPDALVLIGYPEDGATILREAL--ELGLDFTPWIGTDGLKSDDLVE-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 411 psinctvDEMTEAVEGHITTEivmlnPAntrSISNMTSQEFVEKLTKRlkrHPEETGGFqeAPLAYDAIWALALAlnkts 490
Cdd:cd06346 235 -------AAGAEALEGMLGTA-----PG---SPGSPAYEAFAAAYKAE---YGDDPGPF--AANAYDAVMLLALA----- 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2462493251 491 ggggrsgvrledfnynnqtitdqiyramnsssFEGVSGHVVFDASGSRMA 540
Cdd:cd06346 290 --------------------------------YEGASGPIDFDENGDVAG 307
|
|
| PBP1_ABC_ligand_binding-like |
cd06345 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
177-550 |
1.22e-22 |
|
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: 99.65 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSggWPGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVST 256
Cdd:cd06345 2 IGVLGPLS--APAGEAMERGAELAVEEINAAGGIL-GRKVELVVADTQGKPEDGVAAAERLITEDKVDAIVGGFRSEVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 257 LVAE-AARMwNLIVLSYGSSSPAL-----SNRQRFPTFFRTHP-----SATLHNPTRVKLFEKWGWKKIATIQQTTEVFT 325
Cdd:cd06345 79 AAMEvAAEY-KVPFIVTGAASPAItkkvkKDYEKYKYVFRVGPnnsylGATVAEFLKDLLVEKLGFKKVAILAEDAAWGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 326 STLDDLEERVKEAGIEITFRQSF------FSDPAVPVKNLKrqdARIIVGLFYETEArkvfcevykeRLFGKKyvWFLIG 399
Cdd:cd06345 158 GIAEALKKLLPEAGLEVVGVERFptgttdFTPILSKIKASG---ADVIVTIFSGPGG----------ILLVKQ--WAELG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 400 WyADNWFKIYDPSINctvDEMTEAVEGHITTEIvMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFqeaplAYDAI 479
Cdd:cd06345 223 V-PAPLVGINVPAQD---PEFWENTGGAGEYEI-TLAFAAPKAKVTPKTKPFVDAYKKKYGEAPNYTAYT-----AYDAI 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 480 WALALALNKTsggggrsgvrledfnynNQTITDQIYRAMNSSSFEGVSGHVVFDA---------SGSRMAWTLIEQLQGG 550
Cdd:cd06345 293 YILAEAIERA-----------------GSTDPDALVKALEKTDYEGVRGRIKFDKkdeyphdvkYGPGYVTGLIFQWQDG 355
|
|
| PBP1_ABC_ligand_binding-like |
cd06340 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
177-488 |
1.73e-21 |
|
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: 96.09 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDI--LPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILmpGC-- 251
Cdd:cd06340 2 IGVLYPLSGPLaLIGQEAKRGAELAVDEINAAGGIksLGGAKIELVVADTQSDPEVAASEAERLITQEGVVAII--GAys 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 252 SSVS---TLVAEAAR--MWNLIvlsygSSSPALSNRQrFPTFFRTHPSATLHNPTRVKLFEKW------GWKKIATIQQT 320
Cdd:cd06340 80 SSVTlaaSQVAERYGvpFVTAS-----AVADEITERG-FKYVFRTAPTASQFAEDAVDFLKELakkkgkKIKKVAIIYED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 321 TEVFTSTLDDLEERVKEAGIEITFRQSF---FSDPAVPVKNLKRQDARIIVGLFYETEArKVFCEVYKERLFGKKYVWFL 397
Cdd:cd06340 154 SAFGTSVAKGLKKAAKKAGLEVVLDEPYpagATDLSSEVLKLKAAKPDVVFATSYTNDA-ILLLRTMKELGFKPKAIIGV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 398 IGWYADNWFkiydpsinctVDEMTEAVEGHITTeivmlNPANTRSISNM-TSQEFVEKLTKRLKRHPEETGGFqeaplAY 476
Cdd:cd06340 233 GGGYSDPEF----------LKALGKDAEGVFSV-----VPWSPDLAKKKpGAKEVNERYKKKYGEDMTGHAAR-----AY 292
|
330
....*....|..
gi 2462493251 477 DAIWALALALNK 488
Cdd:cd06340 293 TAAWVLADALER 304
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
177-483 |
1.83e-21 |
|
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: 95.09 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGWPG-GQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06268 2 IGVVVPLTGPYADyGEEILRGVALAVEEINAAGGIN-GRKLELVIADDQGDPETAVAVARKLVDDDKVLAVVGHYSSSVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNrQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLDDLEER 334
Cdd:cd06268 81 LAAAPIYQEAGIPLISPGSTAPELTE-GGGPYVFRTVPSDAMQAAALADyLAKKLKGKKVAILYDDYDYGKSLADAFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 335 VKEAGIEITFRQSF---FSDPAVPVKNLKRQDARIIVGLFYETEARKVFcEVYKErlFGKKYVWF-LIGWYADNWFKIYD 410
Cdd:cd06268 160 LKALGGEIVAEEDFplgTTDFSAQLTKIKAAGPDVLFLAGYGADAANAL-KQARE--LGLKLPILgGDGLYSPELLKLGG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462493251 411 psinctvdemtEAVEGHITTeiVMLNPANTRSisnmTSQEFVEKLTKRLKRHPeetggFQEAPLAYDAIWALA 483
Cdd:cd06268 237 -----------EAAEGVVVA--VPWHPDSPDP----PKQAFVKAYKKKYGGPP-----SWRAATAYDATQALA 287
|
|
| PBP1_ABC_LivK_ligand_binding-like |
cd06347 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
177-536 |
2.88e-21 |
|
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: 95.30 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILPdYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06347 2 IGVIGPLTGEAaAYGQPALNGAELAVDEINAAGGILG-KKIELIVYDNKSDPTEAANAAQKLIDEDKVVAIIGPVTSSIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPAL-SNRqrfPTFFRTHPSatlhNPTRVK-----LFEKWGWKKIATIQQTTEVFTSTLD 329
Cdd:cd06347 81 LAAAPIAQKAKIPMITPSATNPLVtKGG---DYIFRACFT----DPFQGAalakfAYEELGAKKAAVLYDVSSDYSKGLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 330 DL-EERVKEAGIEITFRQSFFS---DPAVPVKNLKRQDARII--------VGLFYeTEARKVfceVYKERLFGkkyvwfl 397
Cdd:cd06347 154 KAfKEAFEKLGGEIVAEETYTSgdtDFSAQLTKIKAANPDVIflpgyyeeAALII-KQAREL---GITAPILG------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 398 igwyADNWfkiYDPSINcTVDEmtEAVEGHI-TTEIVMLNPantrsisNMTSQEFVEKLTkrlKRHPEETGGFqeAPLAY 476
Cdd:cd06347 223 ----GDGW---DSPELL-ELGG--DAVEGVYfTTHFSPDDP-------SPEVQEFVKAYK---AKYGEPPNAF--AALGY 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 477 DAIWALALALNKTSGGggrsgvrledfnyNNQTITDQIyraMNSSSFEGVSGHVVFDASG 536
Cdd:cd06347 281 DAVMLLADAIKRAGST-------------DPEAIRDAL---AKTKDFEGVTGTITFDPNG 324
|
|
| PBP1_ABC_transporter_GPCR_C-like |
cd04509 |
Family C of G-protein coupled receptors and their close homologs, the type 1 ... |
177-386 |
7.26e-21 |
|
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: 93.52 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGWPGGQACQP-----------AVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQA----TKYLYELLYND 241
Cdd:cd04509 2 VGVLFAVHGKGPSGVPCGDivaqygiqrfeAMEQALDDINADPNLLPNNTLGIVIYDDCCDPKQAleqsNKFVNDLIQKD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 242 ------------------PIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRV 303
Cdd:cd04509 82 tsdvrctngeppvfvkpeGIKGVIGHLCSSVTIPVSNILELFGIPQITYAATAPELSDDRGYQLFLRVVPLDSDQAPAMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 304 KLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITfrqsfFSDpAVPVKNLKRQDARIIVGLFYETEARKVFCEV 383
Cdd:cd04509 162 DIVKEKVWQYVSIVHDEGQYGEGGARAFQDGLKKGGLCIA-----FSD-GITAGEKTKDFDRLVARLKKENNIRFVVYFG 235
|
...
gi 2462493251 384 YKE 386
Cdd:cd04509 236 YHP 238
|
|
| PBP1_ABC_ligand_binding-like |
cd19980 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
177-536 |
1.94e-19 |
|
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: 89.59 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRrDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd19980 2 IGVIAPLSGPVaALGQQVLNGAKLAVEEINAK-GGVLGRKLELVVEDDKCPPAEGVAAAKKLITDDKVPAIIGAWCSSVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNrQRFPTFFRTHPSatlhNPTRVKLFEKW-----GWKKIATIQQTTEVFTSTLDD 330
Cdd:cd19980 81 LAVMPVAERAKVPLVVEISSAPKITE-GGNPYVFRLNPT----NSMLAKAFAKYladkgKPKKVAFLAENDDYGRGAAEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 331 LEERVKEAGIEITFRQSF------FSDPAVPVKNLKrQDARIIVGlfyETEARKVFCEVYKErlFGKKYVWF-LIGWYAD 403
Cdd:cd19980 156 FKKALKAKGVKVVATEYFdqgqtdFTTQLTKLKAAN-PDAIFVVA---ETEDGALILKQARE--LGLKQQLVgTGGTTSP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 404 NWFKIYDpsinctvdemtEAVEGHITTEIvmlnPANTrsISNMTSQEFVEKLTKRLKRHPEetggfQEAPLAYDAIWALA 483
Cdd:cd19980 230 DLIKLAG-----------DAAEGVYGASI----YAPT--ADNPANKAFVAAYKKKYGEPPD-----KFAALGYDAVMVIA 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2462493251 484 LALNKTsggggrsgvrledfnynnQTITDQ--IYRAMNSSSFEGVSGHVVFDASG 536
Cdd:cd19980 288 EAIKKA------------------GSTDPEkiRAAALKKVDYKGPGGTIKFDEKG 324
|
|
| PBP1_ABC_ligand_binding-like |
cd06338 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
177-550 |
1.92e-18 |
|
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); however, their ligand specificity has not been determined experimentally.
Pssm-ID: 380561 [Multi-domain] Cd Length: 347 Bit Score: 86.87 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILPD---YELKLIHHDSKCDPGQATKyLYE-LLYNDpiKI-ILMPG 250
Cdd:cd06338 2 IGASLSLTGPFaGEGKAQKRGYELWVEDVNAAGGVKGGgkkRPVELVYYDDQSDPATAVR-LYEkLITED--KVdLLLGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 251 CSSVSTL----VAEAARMwnlIVLSYGSSSPALSNRQrFPTFFRTHPSATLHNPTRVKLFEKWGW--KKIATIQQTTEVF 324
Cdd:cd06338 79 YSSGLTLaaapVAEKYGI---PMIAGGAASDSIFERG-YKYVFGVLPPASDYAKGLLDLLAELGPkpKTVAIVYEDDPFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 325 TSTLDDLEERVKEAGIEITFRQSF---FSDPAVPVKNLKRQDARIIVGLFYETEARKvFCEVYKERLFGKKYVWFLIGwy 401
Cdd:cd06338 155 KEVAEGAREAAKKAGLEVVYDESYppgTTDFSPLLTKVKAANPDILLVGGYPPDAIT-LVRQMKELGYNPKAFFLTVG-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 402 adnwfkiydPSINCTVDEMTEAVEGhITTEIVMlNPANTRSIsNMTSQEFVEKLTKRLKRHPEETggfqeAPLAYDAIWA 481
Cdd:cd06338 232 ---------PAFPAFREALGKDAEG-VLGPSQW-EPSLPYKV-FPGAKEFVKAYKEKFGEEPSYH-----AAAAYAAGQV 294
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462493251 482 LALALNKTsggggrsgvrledfnynnQTITDQ-IYRAMNSSSFEGVSGHVVFDASGSRMAW-TLIEQLQGG 550
Cdd:cd06338 295 LQQAIEKA------------------GSLDPEkVRDALASLDFDTVYGPIKFDETGLQIGKpMVVVQWQGG 347
|
|
| PBP1_GPCR_family_C-like |
cd06350 |
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ... |
176-406 |
3.64e-18 |
|
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: 86.20 E-value: 3.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 176 YIGALFPMSGGWPGGQACQP-----------AVEMALEDVNSRRDILPDYELKLIHHDSkCD-PGQATKYLYELLYN--- 240
Cdd:cd06350 1 IIGGLFPVHYRDDADFCCCGilnprgvqlveAMIYAIEEINNDSSLLPNVTLGYDIRDT-CSsSSVALESSLEFLLDngi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 241 -----------DPIKIILM--PGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFE 307
Cdd:cd06350 80 kllansngqniGPPNIVAVigAASSSVSIAVANLLGLFKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAKAIADLLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 308 KWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSD------PAVpVKNLKRQD-ARIIVgLF-YETEARKV 379
Cdd:cd06350 160 HFNWNYVSTVYSDDDYGRSGIEAFEREAKERGICIAQTIVIPENstedeiKRI-IDKLKSSPnAKVVV-LFlTESDAREL 237
|
250 260
....*....|....*....|....*..
gi 2462493251 380 FCEVYKERLfgKKYVWflIGwyADNWF 406
Cdd:cd06350 238 LKEAKRRNL--TGFTW--IG--SDGWG 258
|
|
| PBP1_ABC_HAAT-like |
cd06349 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
176-552 |
2.73e-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 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: 83.39 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 176 YIGALFPMSGGWPG-GQACQPAVEMALEDVNSRRDILPdYELKLIHHDSKCDPGQATKyLYELLYNDPiKIILMPG-CSS 253
Cdd:cd06349 1 KIGVSGPLTGDNAEyGQQFKNGVELAVDEINAAGGVNG-RKLELVVYDDQGDPKEAVN-IAQKFVSDD-KVVAVIGdFSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 254 VSTLVA----EAARMwnlIVLSYGSSSPALSnrQRFPTFFRTHPSATLHNPTRVKL-FEKWGWKKIATIQQTTEVFTSTL 328
Cdd:cd06349 78 SCSMAAapiyEEAGL---VQISPTASHPDFT--KGGDYVFRNSPTQAVEAPFLADYaVKKLGAKKIAIIYLNTDWGVSAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 329 DDLEERVKEAGIEITFRQSF------FSDPAVPVKNLKrQDArIIVGLFYETEArkVFCEVYKErlFGKKYVWFLIGwya 402
Cdd:cd06349 153 DAFKKAAKALGGEIVATEAYlpgtkdFSAQITKIKNAN-PDA-IYLAAYYNDAA--LIAKQARQ--LGWDVQIFGSS--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 403 dnwfkiydpsiNCTVDEMTE----AVEGHITTeiVMLNPANTRsiSNMtsQEFVEKLTkrlKRHPEETGGFqeAPLAYDA 478
Cdd:cd06349 224 -----------SLYSPEFIElagdAAEGVYLS--SPFFPESPD--PEV--KEFVKAYK---AKYGEDPDDF--AARAYDA 281
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462493251 479 IWALALALNKTSGGGgrsgvrledfnynnQTITDQIyraMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSY 552
Cdd:cd06349 282 VNILAEAIEKAGTDR--------------EAIRDAL---ANIKDFSGLTGTITFDENGDVLKSLTILVVKDGKF 338
|
|
| PBP1_ABC_ligand_binding-like |
cd06335 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
177-488 |
1.05e-16 |
|
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: 81.89 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSV- 254
Cdd:cd06335 2 IGVIGPLTGPSaELGESARRGVELAVEEINAAGGIL-GRKIELVERDDEANPTKAVQNAQELIDKEKVVAIIGPTNSGVa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 255 --STLVAEAARMWNLIVLSYGSSSPALSNRQrFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLE 332
Cdd:cd06335 81 laTIPILQEAKIPLIIPVATGTAITKPPAKP-RNYIFRVAASDTLQADFLVDYAVKKGFKKIAILHDTTGYGQGGLKDVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 333 ERVKEAGIEITFRQSFfsDPAVP-----VKNLKRQDARIIVGLFYETEARKVFcevyK--ERLfgkKYVWFLIG-WYAD- 403
Cdd:cd06335 160 AALKKRGITPVATESF--KIGDTdmtpqLLKAKDAGADVILVYGLGPDLAQIL----KamEKL---GWKVPLVGsWGLSm 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 404 -NWFKIYDPsinctvdemteAVEGHITTEIVMLNPANTRsisnmtSQEFVEKLTKRLKRHPEETggFQEAPLAYDAIWAL 482
Cdd:cd06335 231 pNFIELAGP-----------LAEGTIMTQTFIEDYLTPR------AKKFIDAYKKKYGTDRIPS--PVSAAQGYDAVYLL 291
|
....*.
gi 2462493251 483 ALALNK 488
Cdd:cd06335 292 AAAIKQ 297
|
|
| PBP1_As_SBP-like |
cd06330 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
177-534 |
1.30e-16 |
|
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: 81.45 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGgwPG---GQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSS 253
Cdd:cd06330 2 IGVITPLSG--AAavyGEPARNGAELAVEEINAAGGIL-GRKIELVVRDDKGKPDEAVRAARELVLQEGVDFLIGTISSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 254 VSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEK--WGWKKIATI-------QQTTEVF 324
Cdd:cd06330 79 VALAVAPVAEELKVLFIATDAATDRLTEENFNPYVFRTSPNTYMDAVAAALYAAKkpPDVKRWAGIgpdyeygRDSWAAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 325 TSTLddleervKEAGIEITF-RQSFF----SDPAVPVKNLKRQDARIIV------------------GLFyetEARKVFC 381
Cdd:cd06330 159 KAAL-------KKLKPDVEVvGELWPklgaTDYTAYITALLAAKPDGVFsslwggdlvtfvkqakpyGLF---DKTKVVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 382 ----EVYKERLFGKKY--VWFLIGWYADNWFKiydpsinctvdemteaveghitteivmlNPANtrsisnmtsQEFVEKL 455
Cdd:cd06330 229 glggGSEVLQALGKEMpeGLIGGGRYPFGWPD----------------------------TPLN---------KAFVEAY 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462493251 456 TKRLKRHPeetggFQEAPLAYDAIWALALALNKTsggggrsgvrledfnynNQTITDQIYRAMNSSSFEGVSGHVVFDA 534
Cdd:cd06330 272 RAKYGEYP-----TYWAYEAYAAVMALKAAIEKA-----------------GSTDTDKVIAALEGLTFDTPGGKITIRA 328
|
|
| PBP1_NPR-like |
cd06373 |
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ... |
194-540 |
1.91e-16 |
|
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of natriuretic peptide receptor (NPR) family which consists of three different subtypes: type A natriuretic peptide receptor (NPR-A, or GC-A), type B natriuretic peptide receptors (NPR-B, or GC-B), and type C natriuretic peptide receptor (NPR-C). There are three types of natriuretic peptide (NP) ligands specific to the receptors: atrial NP (ANP), brain or B-type NP (BNP), and C-type NP (CNP). The NP family is thought to have arisen through gene duplication during evolution and plays an essential role in cardiovascular and body fluid homeostasis. ANP and BNP bind mainly to NPR-A, while CNP binds specifically to NPR-B. Both NPR-A and NPR-B have guanylyl cyclase catalytic activity and produces intracellular secondary messenger cGMP in response to peptide-ligand binding. Consequently, the NPR-A activation results in vasodilation and inhibition of vascular smooth muscle cell proliferation. NPR-C acts as the receptor for all the three members of NP family, and functions as a clearance receptor. Unlike NPR-A and -B, NPR-C lacks an intracellular guanylyl cyclase domain and is thought to exert biological actions by sequestration of released natriuretic peptides and/or inhibition of adenylyl cyclase.
Pssm-ID: 380596 [Multi-domain] Cd Length: 394 Bit Score: 81.55 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 194 QPAVEMALEDVnSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYG 273
Cdd:cd06373 20 LPAIELALRRV-ERRGFLPGWRFQVHYRDTKCSDTLAPLAAVDLYCAKKVDVFLGPVCEYALAPVARYAGHWNVPVLTAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 274 SSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQ---TTEVFTS----TLDDLEERVKEA--GIEITF 344
Cdd:cd06373 99 GLAAGFDDKTEYPLLTRMGGSYVKLGEFVLTLLRHFGWRRVALLYHdnlRRKAGNSncyfTLEGIFNALTGErdSIHKSF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 345 RQsfFSDPAVPVKNLKRQ---DARIIVgLFYETEA-RKVFCEVYKERLFGKKYVWFLI-----------GWYADNwfkiy 409
Cdd:cd06373 179 DE--FDETKDDFEILLKRvsnSARIVI-LCASPDTvREIMLAAHELGMINGEYVFFNIdlfsssskgarPWYREN----- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 410 DpsincTVDEMTEAVEGHITTEIVMLNPANtrsisnmtSQEFvEKLTKRLKR-----------HPEE----TGGFQEAPL 474
Cdd:cd06373 251 D-----TDERNEKARKAYRALLTVTLRRPD--------SPEY-RNFSEEVKErakekynyftyGDEEvnsfVGAFHDAVL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462493251 475 AYdaiwalALALNKTSGgggrsgvrlEDFNYNNQTItdqIYRAMNSSSFEGVSGHVVFDASGSRMA 540
Cdd:cd06373 317 LY------ALALNETLA---------EGGSPRNGTE---ITERMWNRTFEGITGNVSIDANGDRNA 364
|
|
| PBP1_ABC_HAAT-like |
cd19988 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
176-483 |
1.29e-15 |
|
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: 77.70 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 176 YIGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSV 254
Cdd:cd19988 1 KIGVFGPLSGDAaPYGQAMLQGAELAVEEINAAGGIL-GIPIELVVEDDEGLPAASVSAAKKLIYQDKVWAIIGSINSSC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 255 STLVAEAARMWNLIVLSYGSSSPALSNrQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLDDLEE 333
Cdd:cd19988 80 TLAAIRVALKAGVPQINPGSSAPTITE-SGNPWVFRCTPDDRQQAYALVDyAFEKLKVTKIAVLYVNDDYGRGGIDAFKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 334 RVKEAGIEITFRQSFFSDPavpvKNLKRQDARIivglfYETEARKVFcevykerlfgkkyVWfliGWYADNWF---KIYD 410
Cdd:cd19988 159 AAKKYGIEVVVEESYNRGD----KDFSPQLEKI-----KDSGAQAIV-------------MW---GQYTEGALiakQARE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 411 PSINCTV---DEMT---------EAVEGHITTeiVMLNPANTrsisNMTSQEFVEKLTKRLKRHPEetggfQEAPLAYDA 478
Cdd:cd19988 214 LGLKQPLfgsDGLVtpkfielagDAAEGAIAT--TPFLPDSD----DPKVSAFVEKYKKRYGEEPD-----VFAAQAYDA 282
|
....*
gi 2462493251 479 IWALA 483
Cdd:cd19988 283 MNILA 287
|
|
| PBP1_GC_G-like |
cd06372 |
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding ... |
196-539 |
7.25e-15 |
|
Ligand-binding domain of membrane guanylyl cyclase G; This group includes the ligand-binding domain of membrane guanylyl cyclase G (GC-G) which is a sperm surface receptor and might function, similar to its sea urchin counterpart, in the early signaling event that regulates the Ca2+ influx/efflux and subsequent motility response in sperm. GC-G appears to be a pseudogene in human. Furthermore, in contrast to the other orphan receptor GCs, GC-G has a broad tissue distribution in rat, including lung, intestine, kidney, and skeletal muscle.
Pssm-ID: 380595 [Multi-domain] Cd Length: 390 Bit Score: 76.76 E-value: 7.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 196 AVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSS 275
Cdd:cd06372 22 AIQLAVDKVNSEPSLLGNYSLDFVYTDCGCNAKESLGAFIDQVQKENISALFGPACPEAAEVTGLLASEWNIPMFGFVGQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 276 SPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEvfTSTLDDLEERVK------EAGIEITFRQSF- 348
Cdd:cd06372 102 SPKLDDRDVYDTYVKLVPPLQRIGEVLVKTLQFFGWTHVAMFGGSSA--TSTWDKVDELWKsvenqlKFNFNVTAKVKYd 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 349 FSDPAVPVKNLKRQD--ARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADN-WFKIYDPSINCTVDEMTEAVe 425
Cdd:cd06372 180 TSNPDLLQENLRYISsvARVIVLICSSEDARSILLEAEKLGLMDGEYVFFLLQQFEDSfWKEVLNDEKNQVFLKAYEMV- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 426 ghitteiVMLNPantRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLA------YDAIWALALALNKTSGGGgrsgvr 499
Cdd:cd06372 259 -------FLIAQ---SSYGTYGYSDFRKQVHQKLRRAPFYSSISSEDQVSpysaylHDAVLLYAMGLKEMLKDG------ 322
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462493251 500 lEDFnYNNQTITDQIyRAMNSSSFEGVSGHVVFDASGSRM 539
Cdd:cd06372 323 -KDP-RDGRALLQTL-RGYNQTTFYGITGLVYLDVQGERH 359
|
|
| PBP1_ABC_RPA1789-like |
cd06333 |
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ... |
177-348 |
9.06e-15 |
|
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: 75.66 E-value: 9.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06333 2 IGAILSLTGPAaSLGIPERNAVELLVEQINAAGGIN-GRKLELIVYDDESDPTKAVTNARKLIEEDKVDAIIGPSTTGES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNRQRFptFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERV 335
Cdd:cd06333 81 LAVAPIAEEAKVPLISLAGAAAIVEPVRKW--VFKTPQSDSLVAEAILDYMKKKGIKKVALLGDSDAYGQSGRAALKKLA 158
|
170
....*....|...
gi 2462493251 336 KEAGIEITFRQSF 348
Cdd:cd06333 159 PEYGIEIVADERF 171
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
175-539 |
2.09e-14 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 74.62 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 175 VYIGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSS 253
Cdd:pfam13458 2 IKIGVLTPLSGPYaSSGKSSRAGARAAIEEINAAGGVN-GRKIELVVADDQGDPDVAAAAARRLVDQDGVDAIVGGVSSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 254 VSTLVAEAARMWNLIVLsygsSSPALSNRQRFPTFFRTHPS-ATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLE 332
Cdd:pfam13458 81 VALAVAEVLAKKGVPVI----GPAALTGEKCSPYVFSLGPTySAQATALGRYLAKELGGKKVALIGADYAFGRALAAAAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 333 ERVKEAGIEI--TFRQSFF-SDPAVPVKNLKRQDARIIVGLFYETEARKvFCEVYKER-LFGKKYVwfLIGW-YADNWFK 407
Cdd:pfam13458 157 AAAKAAGGEVvgEVRYPLGtTDFSSQVLQIKASGADAVLLANAGADTVN-LLKQAREAgLDAKGIK--LVGLgGDEPDLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 408 IYDPsinctvdemtEAVEGHITTEIVMLNPANTRsisnmtSQEFVEKLTkrlKRHPEETGGfQEAPLAYDAIWALALALN 487
Cdd:pfam13458 234 ALGG----------DAAEGVYATVPFFPDLDNPA------TRAFVAAFA---AKYGEAPPT-QFAAGGYIAADLLLAALE 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2462493251 488 KTsggggrsgvrledfnynnQTIT-DQIYRAMNSSSFEGVSGHVVFDASGSRM 539
Cdd:pfam13458 294 AA------------------GSPTrEAVIAALRALPYDGPFGPVGFRAEDHQA 328
|
|
| PBP1_ABC_HAAT-like |
cd06344 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
197-536 |
3.22e-14 |
|
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: 74.18 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 197 VEMALEDVNSRRDILPdYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVST---LVAEAARmwnLIVLSYG 273
Cdd:cd06344 21 VELAVEEINAAGGVLG-RKIRLVEYDDEASVDKGLAIAQRFADNPDVVAVIGHRSSYVAIpasIIYERAG---LLMLSPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 274 SSSPALSNrQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPA 353
Cdd:cd06344 97 ATAPKLTQ-HGFKYIFRNIPSDEDIARQLARYAARQGYKRIVIYYDDDSYGKGLANAFEEEARELGITIVDRRSYSSDEE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 354 ------VPVKNLKRQDARIIVGLFYET-----EARKVFCEVykeRLFGKKyvwfliGWYADNWFKIYDpsinctvdemtE 422
Cdd:cd06344 176 dfrrllSKWKALDFFDAIFLAGSMPEGaefikQARELGIKV---PIIGGD------GLDSPELIEIAG-----------K 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 423 AVEGHITTEIVmlNPANTRSIsnmtSQEFVEKLTKRLKRHPEetggfQEAPLAYDAIWALALALNKTSGGggrsgvrled 502
Cdd:cd06344 236 AAEGVVVATVF--DPDDPRPE----VRAFVEAFRKKYGREPD-----VWAAQGYDAVKLLAEAIEKAGST---------- 294
|
330 340 350
....*....|....*....|....*....|....
gi 2462493251 503 fnynNQTITDQIYRAMNssSFEGVSGHVVFDASG 536
Cdd:cd06344 295 ----VPAKIASALRFLE--NWEGVTGTYSFDANG 322
|
|
| PBP1_ABC_HAAT-like |
cd19986 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
176-483 |
3.87e-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 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: 73.43 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 176 YIGALFPMSGGWPG-GQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSS- 253
Cdd:cd19986 1 KIGVVAPLTGPAALnGEYQKNGAQLALEEINAAGGVL-GRPLELVVEDDQGTNTGAVNAVNKLISDDKVVAVIGPHYSTq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 254 ---VSTLVAEAArmwnlIVLSYGSSSPALSNrQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLD 329
Cdd:cd19986 80 vlaVSPLVKEAK-----IPVITGGTSPKLTE-QGNPYMFRIRPSDSVSAKALAKyAVEELGAKKIAILYDNDDFGTGGAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 330 DLEERVKEAGIEITFRQSFFS---DPAVPVKNLKRQDARIIVGLFYETEARKVF---------CEVYKERLFGKKYVWFL 397
Cdd:cd19986 154 VVTAALKALGLEPVAVESYNTgdkDFTAQLLKLKNSGADVIIAWGHDAEAALIArqirqlgldVPVIGSSSFATPTVLLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 398 IGWYADNWFKIYDpsinCTVDEMTEAVeghitteivmlnpantrsisnmtsQEFVEKLTKRLKRHPEETGGfqeapLAYD 477
Cdd:cd19986 234 AGEALEGIYSVTD----FVPSDPDPKV------------------------QAFVKKYKAKYGEDPDLYSA-----WYYD 280
|
....*.
gi 2462493251 478 AIWALA 483
Cdd:cd19986 281 AMYLLA 286
|
|
| PBP1_ABC_HAAT-like |
cd06348 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
177-536 |
5.50e-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 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: 73.42 E-value: 5.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGG---WpgGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSS 253
Cdd:cd06348 2 IGVALSLTGPgalY--GQSQKNGAQLAVEEINAAGGVG-GVKIELIVEDTAGDPEQAINAFQKLINQDKVLAILGPTLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 254 ---VSTLVAEAARMwnlIVLSYGSSSPALSnrQRFPTFFRTHPSATLHNPTRVKLF-EKWGWKKIATIQQTTEVFTST-L 328
Cdd:cd06348 79 eafAADPIAQQAKV---PVVGISNTAPGIT--DIGPYIFRNSLPEDKVIPPTVKAAkKKYGIKKVAVLYDQDDAFTVSgT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 329 DDLEERVKEAGIEITFRQSF------FSDPAVPVKNLKrQDARIIVGLFYE-----TEARKVfceVYKERLFGKkyvwfl 397
Cdd:cd06348 154 KVFPAALKKNGVEVLDTETFqtgdtdFSAQLTKIKALN-PDAIVISALAQEgalivKQAREL---GLKGPIVGG------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 398 IGWYADNWFKIYDPsinctvdemteAVEGHITTeiVMLNPANTrsisNMTSQEFVEKLTKRLKRHPEetggfQEAPLAYD 477
Cdd:cd06348 224 NGFNSPDLIKLAGK-----------AAEGVIVG--SAWSPDNP----DPKNQAFVAAYKEKYGKEPD-----QFAAQAYD 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462493251 478 AIWALALALNKTSGGGGRsgvrledfnynnQTITDQIYRAMNSSSFEGVSGHVVFDASG 536
Cdd:cd06348 282 AAYILAEAIKKAGSTTDR------------ADLRDALARILIAKDFEGPLGPFSFDADR 328
|
|
| PBP1_taste_receptor |
cd06363 |
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ... |
196-395 |
1.22e-12 |
|
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: 70.03 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 196 AVEMALEDVNSRRDILPD----YELklihHDSkCDPGQATKYLYELL----------YNDPIKI------ILMPGcSSVS 255
Cdd:cd06363 47 AMRFAVEEINNSSDLLPGvtlgYEI----FDT-CSDAVNFRPTLSFLsqngshdievQCNYTNYqprvvaVIGPD-SSEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLI-VLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEER 334
Cdd:cd06363 121 ALTTAKLLGFFLMpQISYGASSEELSNKLLYPSFLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEK 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462493251 335 VKEAGIEITFRQSF-FSDPAVP-----VKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKkyVW 395
Cdd:cd06363 201 AANTGICVAYQGLIpTDTDPKPkyqdiLKKINQTKVNVVVVFAPKQAAKAFFEEVIRQNLTGK--VW 265
|
|
| PBP1_aromatic_compounds-like |
cd06332 |
type 1 periplasmic binding proteins of active transport systems predicted to be involved in ... |
177-489 |
6.55e-12 |
|
type 1 periplasmic binding proteins of active transport systems predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes; This group includes the type 1 periplasmic binding proteins of active transport systems that are predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes; their substrate specificities are not well characterized, however. Members also exhibit close similarity to active transport systems for short chain amides and/or urea found in bacteria and archaea.
Pssm-ID: 380555 [Multi-domain] Cd Length: 336 Bit Score: 66.85 E-value: 6.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRrdiLPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06332 2 IGLLAPLTGPFaALGEDMVRGFELALEEVGGE---VAGRKVELVVEDDAGDPDTAVTKARKLVEQDKVDVLIGPLSGDEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSAT-LHNPTRVKLFEKWGWKKIATIQQT-----------TEV 323
Cdd:cd06332 79 LAVAPYAKEPGVPFINPVAGADDLTQRAKAPNFFRTSFTGSqWSAPLGDYAYKELGYKKVATIGSDyafgyeqaagfKRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 324 FTstlddleervkEAGIEITfrQSFF-----SDPAVPVKNLKRqDARIIVGLFYETEARKvFCEVYKErlFGKKYVWFLI 398
Cdd:cd06332 159 FE-----------AAGGEVV--QEIWvplgtTDFSPYIAQIPS-ADDAVFAFLGGADAVR-FLKQYRE--FGLKDKIPLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 399 GWYadnwfkiydpsinCTVDE-----MTEAVEGHITTEIV---MLNPANtrsisnmtsQEFVEKLTKRLKRHPeetGGFQ 470
Cdd:cd06332 222 GGG-------------TTVDEsvlpaMGDAALGIISASHYaegLDNPEN---------KKFVAAYKKKFGKLP---SLYA 276
|
330
....*....|....*....
gi 2462493251 471 EAplAYDAIWALALALNKT 489
Cdd:cd06332 277 AG--GYDGAQAILEALEAV 293
|
|
| PBP1_CaSR |
cd06364 |
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ... |
177-394 |
1.30e-11 |
|
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: 66.90 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW----------PGGQAC--------QPAVEM--ALEDVNSRRDILPDYELKLIHHDSkCD---PG-QATK 232
Cdd:cd06364 2 IGGLFPIHFRPvspdpdfttePHSPECegfnfrgfRWAQTMifAIEEINNSPDLLPNITLGYRIYDS-CAtisKAlRAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 233 YL---YELLYND-------PIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTR 302
Cdd:cd06364 81 ALvngQEETNLDercsggpPVAAVIGESGSTLSIAVARTLGLFYIPQVSYFASCACLSDKKQFPSFLRTIPSDYYQSRAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 303 VKLFEKWGWKKIATIQqttevftsTLDD--------LEERVKEAGIEITFRQSFFSDPAVP-----VKNLKRQDARIIVG 369
Cdd:cd06364 161 AQLVKHFGWTWVGAIA--------SDDDygrngikaFLEEAEKLGICIAFSETIPRTYSQEkilriVEVIKKSTAKVIVV 232
|
250 260
....*....|....*....|....*
gi 2462493251 370 LFYETEARKVFCEVYKERLFGKKYV 394
Cdd:cd06364 233 FSSEGDLEPLIKELVRQNITGRQWI 257
|
|
| PBP1_NPR_C |
cd06386 |
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C ... |
194-558 |
2.64e-11 |
|
ligand-binding domain of type C natriuretic peptide receptor; Ligand-binding domain of type C natriuretic peptide receptor (NPR-C). NPR-C is found in atrial, mesentery, placenta, lung, kidney, venous tissue, aortic smooth muscle, and aortic endothelial cells. The affinity of NPR-C for natriuretic peptides is ANP>CNP>BNP. The extracellular domain of NPR-C is about 30% identical to NPR-A and NPR-B. However, unlike the cyclase-linked receptors, it contains only 37 intracellular amino acids and no guanylyl cyclase activity. Major function of NPR-C is to clear natriuretic peptides from the circulation or extracellular surroundings through constitutive receptor-mediated internalization and degradation.
Pssm-ID: 380609 [Multi-domain] Cd Length: 391 Bit Score: 65.65 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 194 QPAVEMALEDVNSRRDILPDYELKLIHHDSKCDpGQATKYLYELLYNDPIK--IILMPGCSSVSTLVAEAARMWNLIVLS 271
Cdd:cd06386 23 RPAIEYALRSVEGNGLLPPGTRFNVAYEDSDCG-NRALFSLVDRVAQKRAKpdLILGPVCEYAAAPVARLASHWNLPMLS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 272 YGSSSPALSNRQR-FPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQttevftstlDDLEER---VKEAGIEITFRQS 347
Cdd:cd06386 102 AGALAAGFSHKDSeYSHLTRVAPAYAKMGEMFLALFRHHHWSRAFLVYS---------DDKLERncyFTLEGVHEVFQEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 348 FFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCE-----------VYKERLFGKKYVWFLI-----GWYADNWFKIYDp 411
Cdd:cd06386 173 GLHTSIYSFDETKDLDLEEIVRNIQASERVVIMCAssdtirsimlvAHRHGMTNGDYAFFNIelfnsSSYGNGSWKRGD- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 412 sinctvDEMTEAVEGHITTEIVMLnpanTRSIsnmtSQEFvEKLTKRLKRHPEETG------------GFQEAPLAYdai 479
Cdd:cd06386 252 ------KHDFEAKQAYSSLQTVTL----LRTV----KPEF-EKFSMEVKSSVQKQGlndedyvnmfveGFHDAILLY--- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 480 walALALNKTSGgggrsgvrledfNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSR------MAWTLIEqlqGGSYK 553
Cdd:cd06386 314 ---ALALHEVLR------------NGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRygdfsvIAMTDVE---AGTQE 375
|
....*
gi 2462493251 554 KIGYY 558
Cdd:cd06386 376 VIGDY 380
|
|
| PBP1_SBP-like |
cd19989 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
177-342 |
1.29e-10 |
|
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: 62.68 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd19989 2 IGVLTPLSGPYaALGEEARRGAQLAVEEINAAGGIL-GRPVELVVEDTEGKPATAVQKARKLVEQDGVDFLTGAVSSAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSatlhNPTRVKLFEKW----GWKKIATIQQTTEVFTSTLDDL 331
Cdd:cd19989 81 LAVAPKAAELKVPYLVTVAADDELTGENCNRYTFRVNTS----DRMIARALAPWlaenGGKKWYIVYADYAWGQSSAEAF 156
|
170
....*....|.
gi 2462493251 332 EERVKEAGIEI 342
Cdd:cd19989 157 KEAIEELGGEV 167
|
|
| PBP1_NPR_B |
cd06384 |
ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B ... |
187-568 |
3.57e-10 |
|
ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B natriuretic peptide receptor (NPR-B). NPR-B is one of three known single membrane-spanning natriuretic peptide receptors that have been identified. Natriuretic peptides are family of structurally related but genetically distinct hormones/paracrine factors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. Like NPR-A (or GC-A), NPR-B (or GC-B) is a transmembrane guanylyl cyclase, an enzyme that catalyzes the synthesis of cGMP. NPR-B is the predominant natriuretic peptide receptor in the brain. The rank of order activation of NPR-B by natriuretic peptides is CNP>>ANP>BNP. Homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux.
Pssm-ID: 380607 [Multi-domain] Cd Length: 399 Bit Score: 62.18 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 187 WPggqACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDpGQATKYLYEL------LYNDPiKIILMPGCSSVSTLVAE 260
Cdd:cd06384 17 WP---RVFPALRMAVDALQRKGKLLRGYTVNLLFHSSELQ-GACSEYVAPLmavdlkLYHDP-DVLFGPGCVYPAASVGR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 261 AARMWNLIVLSYGSSSPALS-NRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIqqtteVFTST-LDDLEERVKEA 338
Cdd:cd06384 92 FASHWRLPLITAGAVAFGFSsKDEHYRTTVRTGPSAPKLGEFVSHLHSHFNWTSRAAL-----LYHDLkTDDRPYYFIIE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 339 GIEITFRQSFFSDPAVPVKNLKRQDARIIVGlFYETEARKVF-C-----------EVYKERLFGKKYVWFLIGWYADNWF 406
Cdd:cd06384 167 GVFLALDGENLTVEHVPYDDQENGDPREAIH-FIKANGRIVYiCgplemlheimlQAQRENLTNGDYVFFYLDVFGESLR 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 407 -KIYDPSINCTVDEMTEAVEGHITTEIVMlnpaNTRSISNMTSQEFVEKLTKRLKrhpEETGGFQEAPLA-------YDA 478
Cdd:cd06384 246 dDDTRPAEKPSSDIQWQDLREAFKTVLVI----TYKEPDNPEYQEFQRELIARAK---QEFGVQLNPSLMnliagcfYDG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 479 IWALALALNKTSGgggrsgvrlEDFNYNNQTitdQIYRAMNSSSFEGVSGHVVFDASGSR----MAWTLIEqLQGGSYKK 554
Cdd:cd06384 319 VLLYAQALNETLR---------EGGSQKDGL---NIVEKMQDRRFWGVTGLVSMDKNNDRdtdfNLWAMTD-HESGQYEV 385
|
410
....*....|....
gi 2462493251 555 IGYYDSTKDDLSWS 568
Cdd:cd06384 386 VAHYNGAEKQIVWT 399
|
|
| PBP1_GPC6A-like |
cd06361 |
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ... |
233-357 |
1.39e-09 |
|
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: 60.46 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 233 YLYELLYND------PIKIILMPGCSSVSTLVAeaaRMWNLIV---LSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRV 303
Cdd:cd06361 86 SSNELLECDytdyvpPVKAVIGASYSEISIAVA---RLLNLQLipqISYESSAPILSDKLRFPSFLRTVPSDFHQTKAMA 162
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462493251 304 KLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQ---SFFSDPAVPVK 357
Cdd:cd06361 163 KLISHFGWNWVGIIYTDDDYGRSALESFIIQAEAENVCIAFKEvlpAYLSDPTMNVR 219
|
|
| Sushi |
pfam00084 |
Sushi repeat (SCR repeat); |
112-162 |
8.86e-09 |
|
Sushi repeat (SCR repeat);
Pssm-ID: 459664 [Multi-domain] Cd Length: 56 Bit Score: 51.73 E-value: 8.86e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2462493251 112 LENGKVflTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQ-GQWSTPKPHC 162
Cdd:pfam00084 7 IPNGKV--SATKNEYNYGASVSYECDPGYRLVGSPTITCQEdGTWSPPFPEC 56
|
|
| PBP1_mGluR_groupIII |
cd06376 |
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ... |
177-429 |
9.42e-09 |
|
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: 57.89 E-value: 9.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGWPGGQAC-----------QPAVEMALEDVNSRRDILPDYEL-----------------------KLIHHD 222
Cdd:cd06376 9 LGGLFPVHARGLAGVPCgeikkekgihrLEAMLYALDQINSDPDLLPNVTLgarildtcsrdtyaleqsltfvqALIQKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 223 S---KCDPGQATkylyelLYNDPIKIILMPGC--SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATL 297
Cdd:cd06376 89 TsdvRCTNGDPP------VFVKPEKVVGVIGAsaSSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 298 HNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAG-------IEITFRQSFFSDPAVPVKNLKRQDARIIVGL 370
Cdd:cd06376 163 QAQAMVDIVKALGWNYVSTLASEGNYGEKGVESFVQISREAGgvciaqsEKIPRERRTGDFDKIIKRLLETPNARAVVIF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462493251 371 FYETEARKVFCEVYKERLFGkKYVWflIGwyADNWFKIYDPsinctVDEMTEAVEGHIT 429
Cdd:cd06376 243 ADEDDIRRVLAAAKRANKTG-HFLW--VG--SDSWGAKISP-----VLQQEDVAEGAIT 291
|
|
| PBP1_ABC_ligand_binding-like |
cd19982 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
177-348 |
1.49e-08 |
|
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: 56.52 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPgQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd19982 2 IGAILSLTGPFaPFGEMFKNGYEMALEEINAAGGIK-GKKLELVIEDDQSKP-QTALAAAEKLVSQDKVPLIVGGYSSGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TL----VAEAARMWNLIVlsygSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGW-KKIATIQQTTEVFTSTLDD 330
Cdd:cd19982 80 TLpvaaVAERQKIPLLVP----TAADDDITKPGYKYVFRLNPPASIYAKALFDFFKELVKpKTIAILYENTAFGTSVAKA 155
|
170
....*....|....*...
gi 2462493251 331 LEERVKEAGIEITFRQSF 348
Cdd:cd19982 156 ARRFAKKRGIEVVADESY 173
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
177-368 |
2.28e-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, 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: 56.04 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSR-----RDIlpdyelKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPG 250
Cdd:cd06343 9 IGTSLPLSGPAaAYGKPVRAGAAAYFDEVNAAggingRKI------ELIVEDDGYDPARAVAAVRKLVEQDKVFAIVGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 251 CSSVSTLVAEAARMWNLIVLSYGSSSPALSNrQRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATIQQTTEVFTSTLD 329
Cdd:cd06343 83 GTPTNLAVRPYLNEAGVPQLFPATGASALSP-PPKPYTFGVQPSYEDEGRILADyIVETLPAAKVAVLYQNDDFGKDGLE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2462493251 330 DLEERVKEAGIEITFRQSF---FSDPAVPVKNLKRQDARIIV 368
Cdd:cd06343 162 GLKEALKAYGLEVVAEETYepgDTDFSSQVLKLKAAGADVVV 203
|
|
| CCP |
cd00033 |
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) ... |
111-163 |
2.36e-08 |
|
Complement control protein (CCP) modules (aka short consensus repeats SCRs or SUSHI repeats) have been identified in several proteins of the complement system; SUSHI repeats (short complement-like repeat, SCR) are abundant in complement control proteins. The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. Typically, 2 to 4 modules contribute to a binding site, implying that the orientation of the modules to each other is critical for function.
Pssm-ID: 153056 [Multi-domain] Cd Length: 57 Bit Score: 50.54 E-value: 2.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2462493251 111 TLENGKVFLTGGDLPAldGARVDFRCDPDFHLVGSSRSIC-SQGQWSTPKPHCQ 163
Cdd:cd00033 6 VPENGTVTGSKGSYSY--GSTVTYSCNEGYTLVGSSTITCtENGGWSPPPPTCE 57
|
|
| CCP |
smart00032 |
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat ... |
111-162 |
4.55e-08 |
|
Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR); The complement control protein (CCP) modules (also known as short consensus repeats SCRs or SUSHI repeats) contain approximately 60 amino acid residues and have been identified in several proteins of the complement system. A missense mutation in seventh CCP domain causes deficiency of the b subunit of factor XIII.
Pssm-ID: 214478 [Multi-domain] Cd Length: 56 Bit Score: 49.83 E-value: 4.55e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 2462493251 111 TLENGKVFLTGGDLPAldGARVDFRCDPDFHLVGSSRSIC-SQGQWSTPKPHC 162
Cdd:smart00032 6 DIENGTVTSSSGTYSY--GDTVTYSCDPGYTLIGSSTITClENGTWSPPPPTC 56
|
|
| PBP1_NPR_A |
cd06385 |
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A ... |
195-398 |
1.00e-07 |
|
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A natriuretic peptide receptor (NPR-A). NPR-A is one of three known single membrane-spanning natriuretic peptide receptors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. NPR-A is highly expressed in kidney, adrenal, terminal ileum, adipose, aortic, and lung tissues. The rank order of NPR-A activation by natriuretic peptides is ANP>BNP>>CNP. Single allele-inactivating mutations in the promoter of human NPR-A are associated with hypertension and heart failure.
Pssm-ID: 380608 [Multi-domain] Cd Length: 408 Bit Score: 54.44 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 195 PAVEMALEDVNSRRDILPDYELKLIHHDSK-----CDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIV 269
Cdd:cd06385 22 PAVELALERVNARPDLLPGWHVRTVLGSSEnkegvCSDSTAPLVAVDLKFEHHPAVFLGPGCVYTAAPVARFTAHWRVPL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 270 LSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATI--------------------QQTTEVFTSTLD 329
Cdd:cd06385 102 LTAGAPALGFGVKDEYALTTRTGPSHKKLGEFVARLHRRYGWERRALLvyadrkgddrpcffaveglyMQLRRRLNITVD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462493251 330 DLEERVKEAGIEITFRQSFfsdpavpvknlkRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLI 398
Cdd:cd06385 182 DLVFNEDEPLNYTELLRDI------------RQKGRVIYVCCSPDTFRKLMLQAWREGLCGEDYAFFYI 238
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
68-184 |
7.87e-07 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 50.81 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 68 IEYVCRGEREVVGPKVRKCLANGSWTDMDTPSR--CVRICSKSYLTLENGKvfLTGGDLPALDGARVDFRCDPDFHLVGS 145
Cdd:PHA02927 108 ITYSCNSGYQLIGESKSYCELGSTGSMVWNPEApiCESVKCQSPPSISNGR--HNGYEDFYTDGSVVTYSCNSGYSLIGN 185
|
90 100 110
....*....|....*....|....*....|....*....
gi 2462493251 146 SRSICSQGQWSTPkPHCQVNRTPHSERRAVYIGALFPMS 184
Cdd:PHA02927 186 SGVLCSGGEWSDP-PTCQIVKCPHPTISNGYLSSGFKRS 223
|
|
| PHA02927 |
PHA02927 |
secreted complement-binding protein; Provisional |
68-168 |
2.49e-06 |
|
secreted complement-binding protein; Provisional
Pssm-ID: 222943 [Multi-domain] Cd Length: 263 Bit Score: 49.27 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 68 IEYVCRG--EREVVGPKVRKCLANGsWTDMDtpsRCVRICSKSYLTLENGKVFLTGGDLpaldGARVDFRCDPDFHLVGS 145
Cdd:PHA02927 50 IEYLCLPgyRKQKMGPIYAKCTGTG-WTLFN---QCIKRRCPSPRDIDNGQLDIGGVDF----GSSITYSCNSGYQLIGE 121
|
90 100
....*....|....*....|....*...
gi 2462493251 146 SRSICSQGQ-----WSTPKPHCQVNRTP 168
Cdd:PHA02927 122 SKSYCELGStgsmvWNPEAPICESVKCQ 149
|
|
| PBP1_pheromone_receptor |
cd06365 |
Ligand-binding domain of the V2R pheromone receptor, a member of the family C receptors within ... |
200-401 |
4.67e-06 |
|
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: 49.18 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 200 ALEDVNSRRDILPD----YELklihHDSKCDPGQATKYLYELL---------YN---DPIKIILMPGCSSVSTLVaeaar 263
Cdd:cd06365 45 AIEEINKNPDLLPNitlgFHI----YDSCSSERLALESSLSILsgnsepipnYScreQRKLVAFIGDLSSSTSVA----- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 264 MWNLIVL------SYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKE 337
Cdd:cd06365 116 MARILGLykypqiSYGAFDPLLSDKVQFPSFYRTVPSDTSQSLAIVQLLKHFGWTWVGLIISDDDYGEQFSQDLKKEMEK 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462493251 338 AGIEITFRQSFFSDPAVP-----VKNLKRQDARIIVgLFYETEARKVF-CEVYKERLFGKkyVW-FLIGWY 401
Cdd:cd06365 196 NGICVAFVEKIPTNSSLKriikyINQIIKSSANVII-IYGDTDSLLELlFRLWEQLVTGK--VWiTTSQWD 263
|
|
| PBP1_ABC_HAAT-like |
cd19983 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
177-483 |
6.31e-06 |
|
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: 48.35 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSG-GWPGGQACQPAVEMALEDVNS------RRdilpdyeLKLIHHDSKCDPGQATKYLyELLYNDPIKIILMP 249
Cdd:cd19983 2 IGFVGGLTGrYSDLGVQGRNGAQLAVEEINAaggingRP-------VELIIRDDQQDPEAAKAAD-RELIAGGVVAIIGH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 250 GCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFptFFRTHPsaTLHNPTRV---KLFEKWGWKKIATIQQTT-EVFT 325
Cdd:cd19983 74 MTSAMTVAVLPVINEAKVLMISPTVSTPELSGKDDY--FFRVTP--TTRESAQAlarYAYNRGGLRRVAVIYDLSnRAYS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 326 ST-LDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQ------DARIIVglfyeteARKV----FCEvyKERLFGKKYV 394
Cdd:cd19983 150 ESwLDNFRSEFEALGGRIVAEIPFSSGADVDFSDLARRllaskpDGLLLV-------ASAVdtamLAQ--QIRKLGSKIP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 395 WFLIGWYAdnwfkiydpsincTVDEMTE---AVEGhitteiVMLNPANTRSISNMTSQEFVEKLTKRLKRHPeetgGFQe 471
Cdd:cd19983 221 LFSSAWAA-------------TEELLELggkAVEG------MLFSQAYDRNSSNPRYLAFKEAYEERFGREP----SFA- 276
|
330
....*....|..
gi 2462493251 472 APLAYDAIWALA 483
Cdd:cd19983 277 AAYAYEAAMVLA 288
|
|
| PBP1_mGluR_groupI |
cd06374 |
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ... |
177-560 |
1.86e-05 |
|
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: 47.34 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGWPGGQA----CQPA--------VEMALEDV---NSRRDILPDYELKLIHHDSkC---------------- 225
Cdd:cd06374 12 IGALFPVHHQPPLKKVfsrkCGEIreqygiqrVEAMFRTLdkiNKDPNLLPNITLGIEIRDS-Cwyspvaleqsiefird 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 226 -----DPGQATKYLYELL------YNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPS 294
Cdd:cd06374 91 svasvEDEKDTQNTPDPTplsppeNRKPIVGVIGPGSSSVTIQVQNLLQLFHIPQIGYSATSIDLSDKSLYKYFLRVVPS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 295 ATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDpAVP------VKNLKRQD--ARI 366
Cdd:cd06374 171 DYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEEGICIAHSDKIYSN-AGEeefdrlLRKLMNTPnkARV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 367 IVglfyetearkVFCE------VYK--ERLFGKKYvWFLIGwyADNW-------------------FKIYDPSInctvde 419
Cdd:cd06374 250 VV----------CFCEgetvrgLLKamRRLNATGH-FLLIG--SDGWadrkdvvegyedeaaggitIKIHSPEV------ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 420 mtEAVEGHITTeivmLNP-ANTRsisNMTSQEFVE-KLTKRLKRHPEETGGF---------------QEAPLAY--DAIW 480
Cdd:cd06374 311 --ESFDEYYFN----LKPeTNSR---NPWFREFWQhRFDCRLPGHPDENPYFkkcctgeesllgnyvQDSKLGFviNAIY 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 481 ALALALNKTSggggrsgvrlEDFNYNNQ--------TITDQIYRA-MNSSSFEGVSGHVV-FDASGSRMAWTLIEQLQG- 549
Cdd:cd06374 382 AMAHALHRMQ----------EDLCGGYSvglcpamlPINGSLLLDyLLNVSFVGVSGDTImFDENGDPPGRYDIMNFQKt 451
|
490
....*....|....*
gi 2462493251 550 ----GSYKKIGYYDS 560
Cdd:cd06374 452 gegsYDYVQVGSWKN 466
|
|
| PBP1_iGluR_AMPA |
cd06380 |
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the AMPA receptor; ... |
177-560 |
6.27e-05 |
|
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: 45.73 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMsggwpGGQACQPAVEMALEDVNSRRDILPDYELKLIHHD-SKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06380 2 IGAIFDS-----GEDQVQTAFRYAIDRHNSNNNNRFRLFPLTERIDiTNADSFSVSRAICSQLSRGVFAIFGSSDASSLN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMwN--LIVLSYgsssPALSNRQRFPTFFRTHPSatlHNPTRVKLFEKWGWKKIA----------TIQQTTEv 323
Cdd:cd06380 77 TIQSYSDTF-HmpYITPSF----PKNEPSDSNPFELSLRPS---YIEAIVDLIRHYGWKKVVylydsdegllRLQQLYD- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 324 FTSTLDDLE---ERVKEAGIEITFRQSFFSdpavpvKNLKRQDARIIVGLfyETEA-RKVFCEVYKERLFGKKYVWFLIG 399
Cdd:cd06380 148 YLKEKSNISvrvRRVRNVNDAYEFLRTLRE------LDREKEDKRIVLDL--SSERyQKILEQIVEDGMNRRNYHYLLAN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 400 WYADNW----FKIYdpSINCT----VDEmteaveghitteivmlnpantrsiSNMTSQEFVEKLTKRLKRHPEETGGFQ- 470
Cdd:cd06380 220 LDFLDLdlerFLHG--GVNITgfqlVDT------------------------NNKTVKDFLQRWKKLDPREYPGAGTDTi 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 471 --EAPLAYDAIWALALALNKTS---GGGGRSGVRLEDFNYNNQTIT------------DQIYRAMNSSSFEGVSGHVVFD 533
Cdd:cd06380 274 pyEAALAVDAVLVIAEAFQSLLrqnDDIFRFTFHGELYNNGSKGIDcdpnpplpwehgKAIMKALKKVRFEGLTGNVQFD 353
|
410 420
....*....|....*....|....*....
gi 2462493251 534 ASGSRMAWTL--IEQLQGGSYKKIGYYDS 560
Cdd:cd06380 354 DFGQRKNYTLdvIELTSNRGLRKIGTWSE 382
|
|
| PBP1_mGluR_groupII |
cd06375 |
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ... |
252-317 |
8.37e-05 |
|
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: 45.20 E-value: 8.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462493251 252 SSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATI 317
Cdd:cd06375 120 SSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTV 185
|
|
| PBP1_SBP-like |
cd06329 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
182-319 |
4.17e-04 |
|
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); 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: 380552 [Multi-domain] Cd Length: 343 Bit Score: 42.65 E-value: 4.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 182 PMSGGW-PGGQACQPAVEMALEDVNSRRDILpDYELKLIHHDSKCDPGQATKYLYELLyNDPIKIILMPGCSSVSTLVAE 260
Cdd:cd06329 7 PLSGPFaSVGEIYLKGLQFAIEEINAGGGLL-GRKIELVPFDNKGSPQEALIQLKKAI-DQGIRFVLQGNSSAVAGALID 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462493251 261 AARMWNL-------IVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGW-KKIATIQQ 319
Cdd:cd06329 85 AIEKHNQrnpdkrvLFLNYGAEAPELTGAKCSFWHFRFDANADMKMAALADYMKKDGSiKKVYLINQ 151
|
|
| PRK15404 |
PRK15404 |
high-affinity branched-chain amino acid ABC transporter substrate-binding protein; |
177-344 |
5.59e-04 |
|
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
Pssm-ID: 237959 [Multi-domain] Cd Length: 369 Bit Score: 42.32 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGgwPGGQ---ACQPAVEMALEDVNSRRDILPDyELKLIHHDSKCDPGQATKYLYELLyNDPIKIILMPGCSS 253
Cdd:PRK15404 28 IAIVGPMSG--PVAQygdMEFTGARQAIEDINAKGGIKGD-KLEGVEYDDACDPKQAVAVANKVV-NDGIKYVIGHLCSS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 254 vSTLvaEAARMWN---LIVLSYGSSSPALSNRqRFPTFFRTHPSATLHNPTRVK-LFEKWGWKKIATI---QQTTE-VFT 325
Cdd:PRK15404 104 -STQ--PASDIYEdegILMITPAATAPELTAR-GYQLIFRTIGLDSDQGPTAAKyILEKVKPKRIAVLhdkQQYGEgLAR 179
|
170
....*....|....*....
gi 2462493251 326 STLDDLeervKEAGIEITF 344
Cdd:PRK15404 180 SVKDGL----KKAGANVVF 194
|
|
| PBP1_ABC_HAAT-like |
cd19985 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
176-478 |
7.89e-04 |
|
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: 41.88 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 176 YIGALFPMSG-GWPGGQACQPAVEMALEDVNSRRDIlPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKII--LMPGCS 252
Cdd:cd19985 1 HIAVVGPMSGkSASKGKSMLRGAELYIDQINAAGGI-NGKKVKLDVFDDQNDPDAARKAAQIIVSDKALAVIghYYSSAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 253 SVSTLVAEAARMwnlIVLSYGSSSPALSnrQRFPTFFRTHP-----SATLHNPTRvKLFEKwgwKKIATIqQTTEVFTST 327
Cdd:cd19985 80 IAAGKIYKKAGI---PAITPSATADAVT--RDNPWYFRVIFndslqGRFLANYAK-KVLKK---DKVSII-YEEDSYGKS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 328 LDD-LEERVKEAGIEITFRQSFFSDP----------AVPVKNLKRQDARIIVGLFYEtEARKVfceVYKERLFGKKYVwf 396
Cdd:cd19985 150 LASvFEATARALGLKVLKKWSFDTDSsqldqnldqiVDELKKAPDEPGVIFLATHAD-EGAKL---IKKLRDAGLKAP-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 397 LIGwyADNW-FKIYDPSINCTVDEMTEA---VEG-HITTEIVMlnpantrSISNMTSQEFVEKLTKRLKRHPEETGGFqe 471
Cdd:cd19985 224 IIG--PDSLaSESFAQGFAEYPEEKEEPgyyTDGiYATSPFIF-------DIANEKAQKFRDTYQKRYGEEPSWIAAF-- 292
|
....*..
gi 2462493251 472 aplAYDA 478
Cdd:cd19985 293 ---AYDA 296
|
|
| PBP1_iGluR_AMPA_GluR1 |
cd06390 |
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit ... |
514-574 |
1.99e-03 |
|
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit of the AMPA receptor; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR1 subunit of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor. The AMPA receptor is a member of the glutamate-receptor ion channels (iGluRs) which are the major mediators of excitatory synaptic transmission in the central nervous system. AMPA receptors are composed of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current. Furthermore, this N-terminal domain of the iGluRs has homology with LIVBP, a bacterial periplasmic binding protein, as well as with the structurally related glutamate-binding domain of the G-protein-coupled metabotropic receptors (mGluRs).
Pssm-ID: 380613 [Multi-domain] Cd Length: 367 Bit Score: 40.69 E-value: 1.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462493251 514 IYRAMNSSSFEGVSGHVVFDASGSRMAWTL-IEQLQGGSYKKIGYydstkddlsWSKTDKWI 574
Cdd:cd06390 312 IQRALQQVRFEGLTGNVQFNEKGRRTNYTLhVIEMKHDGIRKIGY---------WNEDDKLV 364
|
|
| PBP1_iGluR_AMPA_GluR2 |
cd06389 |
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit ... |
513-575 |
2.14e-03 |
|
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit of the AMPA receptor; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the GluR2 subunit of the AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor. The AMPA receptor is a member of the glutamate-receptor ion channels (iGluRs) which are the major mediators of excitatory synaptic transmission in the central nervous system. AMPA receptors are composed of four types of subunits (GluR1, GluR2, GluR3, and GluR4) which combine to form a tetramer and play an important role in mediating the rapid excitatory synaptic current. Furthermore, this N-terminal domain of the iGluRs has homology with LIVBP, a bacterial periplasmic binding protein, as well as with the structurally related glutamate-binding domain of the G-protein-coupled metabotropic receptors (mGluRs).
Pssm-ID: 380612 [Multi-domain] Cd Length: 372 Bit Score: 40.77 E-value: 2.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462493251 513 QIYRAMNSSSFEGVSGHVVFDASGSRMAWTL-IEQLQGGSYKKIGYydstkddlsWSKTDKWIV 575
Cdd:cd06389 316 EIERALKQVQVEGLSGNIKFDQNGKRINYTInIMELKTNGPRKIGY---------WSEVDKMVV 370
|
|
| PBP1_alkylbenzenes-like |
cd06360 |
type 1 periplasmic binding component of active transport systems predicted be involved in ... |
177-489 |
4.28e-03 |
|
type 1 periplasmic binding component of active transport systems predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; This group includes the type 1 periplasmic binding component of active transport systems that are predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; their substrate specificity is not well characterized, however.
Pssm-ID: 380583 [Multi-domain] Cd Length: 357 Bit Score: 39.59 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 177 IGALFPMSGGW-PGGQACQPAVEMALEDVNSRrdiLPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVS 255
Cdd:cd06360 2 IGVLLPLTGPLaVNGEDVRDGFELYFDEIGNQ---VAGRKIELIVEDDEGKPDVGLTKARKLVERDKVHVLAGIVSSAVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 256 TLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRT-HPSATLHNPTRVKLFEKWGWKKIATI-------QQTTEVFTST 327
Cdd:cd06360 79 YAVRDYVVEQKIPLVISNAGAAPLTQELASPYIFRTsFSNGQYDAPFGQYAYEKLGYRRIAVMasdyaagHEQAGAFART 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 328 LddleervKEAGIEITfrQSFF-----SDPAVPVKNLKRQDARIIVGLFYETEARKvFCEVYKErlFGKKYVWFLIGwya 402
Cdd:cd06360 159 F-------KQAGGKVV--QEIYpplgtADFAPYLARIQQDAADAVWAFFAGADAIR-FVKQYDE--YGLKGKLPLVG--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462493251 403 dnwfkiydpsINCTVDEMTEAVEGHITTEIVmlNPAN-TRSISNMTSQEFVEKLTKRLKRHPEetggfQEAPLAYDAIWA 481
Cdd:cd06360 224 ----------IGGLVDDAILPEQGDAALGIV--SYLHySAALDTPENKAFVQAYRKKYGRDPG-----LYAEGGYVAARA 286
|
....*...
gi 2462493251 482 LALALNKT 489
Cdd:cd06360 287 IAEALEAV 294
|
|
| |
