|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_ABC_ligand_binding-like |
cd06346 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-397 |
3.32e-85 |
|
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: 262.50 E-value: 3.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAASGMSL 118
Cdd:cd06346 3 GALLPLTGPLASLGPPMLAAAELAVEEINAAGGVLGKKV-ELVVEDSQTDPTAAVDAARKLVDVeGVPAIVGAASSGVTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLE 198
Cdd:cd06346 82 AVASVAVPNGVVQISPSSTSPALTTLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVNNDYGQGLADAFKKAFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 199 ERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIGPDRIgvYGADGLRSeelPSLVAPG 277
Cdd:cd06346 162 ALGGTVTASVPYEPGQTSYRAELAQAAAGGPDALVLIGYpEDGATILREALELGLDFTPW--IGTDGLKS---DDLVEAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 278 QPERLSGMKGTAPASAENEQYvkdlKEFAPKLKE------LQFAPQVFDCATTIALAaekaesddprdyvkemngitkdg 351
Cdd:cd06346 237 GAEALEGMLGTAPGSPGSPAY----EAFAAAYKAeygddpGPFAANAYDAVMLLALA----------------------- 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1752498383 352 ekcnsfaackelladgrdidYEGVSGPLNFTDKGEPgQATIEVYGY 397
Cdd:cd06346 290 --------------------YEGASGPIDFDENGDV-AGPYEIWKV 314
|
|
| PBP1_ABC_LIVBP-like |
cd06342 |
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ... |
40-395 |
1.16e-52 |
|
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: 178.87 E-value: 1.16e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAAGVDAIVGAAASGMSLA 119
Cdd:cd06342 3 GVAGPLTGPNAALGQDIRNGAELAVDEINAKGGGLGFKI-ELVAQDDACDPAQAVAAAQKLVADGVVAVIGHYNSGAAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 120 FIDRVTGAGVVQCSGSNTAPTFTDyEDDGFYFRTVPSDALQGPILADVVRDDGH-DRVALVARADDYGRGLMEATRKTLE 198
Cdd:cd06342 82 AAPIYAEAGIPMISPSATNPKLTE-QGYKNFFRVVGTDDQQGPAAADYAAKTLKaKRVAVIHDGTAYGKGLADAFKKALK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 199 ERGLTVTLAETYDPKATNFDQVAQQIENSRPDaAVVIA--FEEGAQILQGMIESGIgpdRIGVYGADGLRSEELPSLVAP 276
Cdd:cd06342 161 ALGGTVVGREGITPGTTDFSALLTKIKAANPD-AVYFGgyYPEAGLLLRQLREAGL---KAPFMGGDGIVSPDFIKAAGD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 277 GQperlSGMKGTAPASAENEqyVKDLKEFAPKLKE------LQFAPQVFDCATTIALAAEKAESDDPRDYVKEMngitkd 350
Cdd:cd06342 237 AA----EGVYATTPGAPPEK--LPAAKAFLKAYKAkfgeppGAYAAYAYDAAQVLLAAIEKAGSTDRAAVAAAL------ 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1752498383 351 gekcnsfaackelladgRDIDYEGVSGPLNFTDKGEPGQATIEVY 395
Cdd:cd06342 305 -----------------RATDFDGVTGTISFDAKGDLTGPAFTVY 332
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
34-408 |
3.99e-52 |
|
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: 177.05 E-value: 3.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 34 DGELQFGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAA 112
Cdd:COG0683 1 ADPIKIGVLLPLTGPYAALGQPIKNGAELAVEEINAAGGVLGRKI-ELVVEDDASDPDTAVAAARKlIDQDKVDAIVGPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 113 ASGMSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILAD-VVRDDGHDRVALVARADDYGRGLME 191
Cdd:COG0683 80 SSGVALAVAPVAEEAGVPLISPSATAPALTGPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDDYAYGQGLAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 192 ATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIgpdrigvygadglrseel 270
Cdd:COG0683 160 AFKAALKAAGGEVVGEEYYPPGTTDFSAQLTKIKAAGPDAVFLAGYgGDAALFIKQAREAGL------------------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 271 pslvapgqperlsgmkgTAPAsaeNEQYVKDLKEFAPKlKELQFAPQVFDCATTIALAAEKAESDDPRDYVKEMngitkd 350
Cdd:COG0683 222 -----------------KGPL---NKAFVKAYKAKYGR-EPSSYAAAGYDAALLLAEAIEKAGSTDREAVRDAL------ 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498383 351 gekcnsfaackelladgRDIDYEGVSGPLNFTDKGEPGQAtIEVYGYDDKGALQTLRT 408
Cdd:COG0683 275 -----------------EGLKFDGVTGPITFDPDGQGVQP-VYIVQVKADGKFVVVET 314
|
|
| PBP1_ABC_ligand_binding-like |
cd19984 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-326 |
6.12e-39 |
|
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: 141.59 E-value: 6.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSL 118
Cdd:cd19984 3 GVILPLTGDAASYGEDMKNGIELAVEEINAAGGINGKKI-ELIYEDSKCDPKKAVSAANKlINVDKVKAIIGGVCSSETL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDYEDdgFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLE 198
Cdd:cd19984 82 AIAPIAEQNKVVLISPGASSPEITKAGD--YIFRNYPSDAYQGKVLAEFAYNKLYKKVAILYENNDYGVGLKDVFKKEFE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 199 ERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIgpdRIGVYGADGLRSEELPSlVAPG 277
Cdd:cd19984 160 ELGGKIVASESFEQGETDFRTQLTKIKAANPDAIFLPGYpKEGGLILKQAKELGI---KAPILGSDGFEDPELLE-IAGE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1752498383 278 QPErlsGMKGTAPASAENEQYVKDLKEFAPKLKE----LQFAPQVFDCATTIA 326
Cdd:cd19984 236 AAE---GVIFTYPAFDDSSEKKQKFFFYRYKEKYgkepDIYAALAYDAVMILA 285
|
|
| PBP1_ABC_LivK_ligand_binding-like |
cd06347 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
39-387 |
2.23e-38 |
|
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: 141.14 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMS 117
Cdd:cd06347 2 IGVIGPLTGEAAAYGQPALNGAELAVDEINAAGGILGKKI-ELIVYDNKSDPTEAANAAQKlIDEDKVVAIIGPVTSSIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 118 LAFIDRVTGAGVVQCSGSNTAPTFTDYEDdgFYFRTVPSDALQGPILADVVRDD-GHDRVA-LVARADDYGRGLMEATRK 195
Cdd:cd06347 81 LAAAPIAQKAKIPMITPSATNPLVTKGGD--YIFRACFTDPFQGAALAKFAYEElGAKKAAvLYDVSSDYSKGLAKAFKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 196 TLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGI-GPdrigVYGADGLRSEELPSL 273
Cdd:cd06347 159 AFEKLGGEIVAEETYTSGDTDFSAQLTKIKAANPDVIFLPGYyEEAALIIKQARELGItAP----ILGGDGWDSPELLEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 274 VapgqPERLSGMKGTAPASAENEQyvKDLKEFAPKLKELQ------FAPQVFDCATTIALAAEKAESDDPRDYVKEMNGI 347
Cdd:cd06347 235 G----GDAVEGVYFTTHFSPDDPS--PEVQEFVKAYKAKYgeppnaFAALGYDAVMLLADAIKRAGSTDPEAIRDALAKT 308
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1752498383 348 TkdgekcnsfaackelladgrdiDYEGVSGPLNFTDKGEP 387
Cdd:cd06347 309 K----------------------DFEGVTGTITFDPNGNP 326
|
|
| PBP1_ABC_ligand_binding-like |
cd19980 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-395 |
3.49e-37 |
|
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: 137.74 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLA-AGVDAIVGAAASGMSL 118
Cdd:cd19980 3 GVIAPLSGPVAALGQQVLNGAKLAVEEINAKGGVLGRKL-ELVVEDDKCPPAEGVAAAKKLITdDKVPAIIGAWCSSVTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDyEDDGFYFRTVPSDALQGPILADVVRDDG-HDRVALVARADDYGRGLMEATRKTL 197
Cdd:cd19980 82 AVMPVAERAKVPLVVEISSAPKITE-GGNPYVFRLNPTNSMLAKAFAKYLADKGkPKKVAFLAENDDYGRGAAEAFKKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 198 EERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIgpdRIGVYGADGLRSEELPsLVAP 276
Cdd:cd19980 161 KAKGVKVVATEYFDQGQTDFTTQLTKLKAANPDAIFVVAEtEDGALILKQARELGL---KQQLVGTGGTTSPDLI-KLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 277 GQPERLSGMKGTAPASAE------NEQYVKDLKEFAPKlkelqFAPQVFDCATTIALAAEKAESDDPRdyvkemngitkd 350
Cdd:cd19980 237 DAAEGVYGASIYAPTADNpankafVAAYKKKYGEPPDK-----FAALGYDAVMVIAEAIKKAGSTDPE------------ 299
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1752498383 351 gekcnsfAACKELLadgRDIDYEGVSGPLNFTDKgepGQATIEVY 395
Cdd:cd19980 300 -------KIRAAAL---KKVDYKGPGGTIKFDEK---GQAHKNVV 331
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
39-326 |
2.10e-36 |
|
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: 134.76 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLA-AGVDAIVGAAASGMS 117
Cdd:cd06268 2 IGVVVPLTGPYADYGEEILRGVALAVEEINAAGGINGRKL-ELVIADDQGDPETAVAVARKLVDdDKVLAVVGHYSSSVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 118 LAFIDRVTGAGVVQCSGSNTAPTFTDYEDDgFYFRTVPSDALQGPILADVVRDDGHD-RVALVARADDYGRGLMEATRKT 196
Cdd:cd06268 81 LAAAPIYQEAGIPLISPGSTAPELTEGGGP-YVFRTVPSDAMQAAALADYLAKKLKGkKVAILYDDYDYGKSLADAFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 197 LEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIgpdRIGVYGADGLRSEELPSLVa 275
Cdd:cd06268 160 LKALGGEIVAEEDFPLGTTDFSAQLTKIKAAGPDVLFLAGYgADAANALKQARELGL---KLPILGGDGLYSPELLKLG- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1752498383 276 pgqPERLSGMKGTAP--ASAENEQYVKDLKEFAPKLKEL--QFAPQVFDCATTIA 326
Cdd:cd06268 236 ---GEAAEGVVVAVPwhPDSPDPPKQAFVKAYKKKYGGPpsWRAATAYDATQALA 287
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
36-351 |
8.70e-36 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 134.32 E-value: 8.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 36 ELQFGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAAS 114
Cdd:pfam13458 1 PIKIGVLTPLSGPYASSGKSSRAGARAAIEEINAAGGVNGRKI-ELVVADDQGDPDVAAAAARRlVDQDGVDAIVGGVSS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 115 GMSLAFIDRVTGAGVVqcsgSNTAPTFTDYEDDGFYFRTVPSDALQGPILAD-VVRDDGHDRVALVARADDYGRGLMEAT 193
Cdd:pfam13458 80 AVALAVAEVLAKKGVP----VIGPAALTGEKCSPYVFSLGPTYSAQATALGRyLAKELGGKKVALIGADYAFGRALAAAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 194 RKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDA-AVVIAFEEGAQILQGMIESGIGPDRIGVYGADGlrseELPS 272
Cdd:pfam13458 156 KAAAKAAGGEVVGEVRYPLGTTDFSSQVLQIKASGADAvLLANAGADTVNLLKQAREAGLDAKGIKLVGLGG----DEPD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 273 LVAPGqPERLSGMKGTAP-----ASAENEQYVKDLKEFAPKLKELQFAPQVFDCATTIALAAEKAESDDPRDYVKEMNGI 347
Cdd:pfam13458 232 LKALG-GDAAEGVYATVPffpdlDNPATRAFVAAFAAKYGEAPPTQFAAGGYIAADLLLAALEAAGSPTREAVIAALRAL 310
|
....
gi 1752498383 348 TKDG 351
Cdd:pfam13458 311 PYDG 314
|
|
| ANF_receptor |
pfam01094 |
Receptor family ligand binding region; This family includes extracellular ligand binding ... |
58-399 |
9.56e-35 |
|
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: 131.74 E-value: 9.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 58 ESLKFAIQKINDAGGVLGKAVPNVVSSDEAGQEAVAAQSADRVLAAGVDAIVGAAASGMSLAFIDRVTGAGVVQCSGSNT 137
Cdd:pfam01094 4 LAVRLAVEDINADPGLLPGTKLEYIILDTCCDPSLALAAALDLLKGEVVAIIGPSCSSVASAVASLANEWKVPLISYGST 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 138 APTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLTVTLAETYDPkATNF 217
Cdd:pfam01094 84 SPALSDLNRYPTFLRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPP-AQDD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 218 DQVAQQIE---NSRPDAAVVIA-FEEGAQILQGMIESGIGPDRIGVYGADGLrSEELPSLVAPGQpERLSGMKGTAPASA 293
Cdd:pfam01094 163 DEIARKLLkevKSRARVIVVCCsSETARRLLKAARELGMMGEGYVWIATDGL-TTSLVILNPSTL-EAAGGVLGFRLHPP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 294 ENEQYVK-------DLKEFAPKLKELQFAPQV--FDCATTIALAAEKAESDDPRDYVKEMNGITKDGEKcnsfaackeLL 364
Cdd:pfam01094 241 DSPEFSEffweklsDEKELYENLGGLPVSYGAlaYDAVYLLAHALHNLLRDDKPGRACGALGPWNGGQK---------LL 311
|
330 340 350
....*....|....*....|....*....|....*
gi 1752498383 365 ADGRDIDYEGVSGPLNFTDKGEPGQATIEVYGYDD 399
Cdd:pfam01094 312 RYLKNVNFTGLTGNVQFDENGDRINPDYDILNLNG 346
|
|
| PBP1_ABC_HAAT-like |
cd06349 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
39-387 |
4.33e-34 |
|
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: 129.61 E-value: 4.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVPNVVSSDEA-GQEAVA-AQ---SADRVlaagvDAIVGAAA 113
Cdd:cd06349 2 IGVSGPLTGDNAEYGQQFKNGVELAVDEINAAGGVNGRKLELVVYDDQGdPKEAVNiAQkfvSDDKV-----VAVIGDFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 114 SGMSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDdgFYFRTVPSDALQGPILAD-VVRDDGHDRVALVARADDYGRGLMEA 192
Cdd:cd06349 77 SSCSMAAAPIYEEAGLVQISPTASHPDFTKGGD--YVFRNSPTQAVEAPFLADyAVKKLGAKKIAIIYLNTDWGVSAADA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 193 TRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIGPDrigVYGADGLRSEELP 271
Cdd:cd06349 155 FKKAAKALGGEIVATEAYLPGTKDFSAQITKIKNANPDAIYLAAYyNDAALIAKQARQLGWDVQ---IFGSSSLYSPEFI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 272 SLVApgqpERLSGMKGTAPASAENEQyvKDLKEFAPKLKEL------QFAPQVFDCATTIALAAEKAESDDprdyvkemn 345
Cdd:cd06349 232 ELAG----DAAEGVYLSSPFFPESPD--PEVKEFVKAYKAKygedpdDFAARAYDAVNILAEAIEKAGTDR--------- 296
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1752498383 346 gitkdgekcnsfAACKELLADGrdIDYEGVSGPLNFTDKGEP 387
Cdd:cd06349 297 ------------EAIRDALANI--KDFSGLTGTITFDENGDV 324
|
|
| PBP1_ABC_HAAT-like |
cd19988 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-326 |
7.15e-33 |
|
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: 125.47 E-value: 7.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAAG-VDAIVGAAASGMSL 118
Cdd:cd19988 3 GVFGPLSGDAAPYGQAMLQGAELAVEEINAAGGILGIPI-ELVVEDDEGLPAASVSAAKKLIYQDkVWAIIGSINSSCTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTD--YEddgFYFRTVPSDALQGPILAD-VVRDDGHDRVALVARADDYGRGLMEATRK 195
Cdd:cd19988 82 AAIRVALKAGVPQINPGSSAPTITEsgNP---WVFRCTPDDRQQAYALVDyAFEKLKVTKIAVLYVNDDYGRGGIDAFKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 196 TLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIA-FEEGAQILQGMIESGIgpdRIGVYGADGLRSEELPSLv 274
Cdd:cd19988 159 AAKKYGIEVVVEESYNRGDKDFSPQLEKIKDSGAQAIVMWGqYTEGALIAKQARELGL---KQPLFGSDGLVTPKFIEL- 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1752498383 275 APGQPErlsGMKGTAPASAEN--EQYVKDLKEFAPKLKEL--QFAPQVFDCATTIA 326
Cdd:cd19988 235 AGDAAE---GAIATTPFLPDSddPKVSAFVEKYKKRYGEEpdVFAAQAYDAMNILA 287
|
|
| PBP1_ABC_RPA1789-like |
cd06333 |
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ... |
40-347 |
6.11e-29 |
|
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: 115.72 E-value: 6.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLA-AGVDAIVGAAASGMSL 118
Cdd:cd06333 3 GAILSLTGPAASLGIPERNAVELLVEQINAAGGINGRKL-ELIVYDDESDPTKAVTNARKLIEeDKVDAIIGPSTTGESL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTdyEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLE 198
Cdd:cd06333 82 AVAPIAEEAKVPLISLAGAAAIVE--PVRKWVFKTPQSDSLVAEAILDYMKKKGIKKVALLGDSDAYGQSGRAALKKLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 199 ERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAFEEGAQILQ-GMIESGIGPDRIGVYG-------------ADG 264
Cdd:cd06333 160 EYGIEIVADERFARTDTDMTAQLTKIRAAKPDAVLVWASGPPAALVAkNLRQLGYKGPIYQSHGaanqdfiklagkaAEG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 265 LRSEELPSLVAPGQPErlsgmkgTAPASAENEQYVKDLKEfapKLKEL--QFAPQVFDCATTIALAAEKAESDDP---RD 339
Cdd:cd06333 240 VILPAGKLLVADQLPD-------SDPQKKVLLEFVKAYEA---KYGEGpsTFAGHAYDALLLLVEAIEPAGGTDRaalRD 309
|
....*...
gi 1752498383 340 YVKEMNGI 347
Cdd:cd06333 310 ALENTKGL 317
|
|
| PBP1_ABC_ligand_binding-like |
cd06335 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
40-348 |
3.92e-28 |
|
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: 113.47 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVPNVVSSDEAgQEAVAAQSADR-VLAAGVDAIVGAAASGMSL 118
Cdd:cd06335 3 GVIGPLTGPSAELGESARRGVELAVEEINAAGGILGRKIELVERDDEA-NPTKAVQNAQElIDKEKVVAIIGPTNSGVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDY--EDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKT 196
Cdd:cd06335 82 ATIPILQEAKIPLIIPVATGTAITKPpaKPRNYIFRVAASDTLQADFLVDYAVKKGFKKIAILHDTTGYGQGGLKDVEAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 197 LEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMiesgigpDRIG----VYGADGLRSEELP 271
Cdd:cd06335 162 LKKRGITPVATESFKIGDTDMTPQLLKAKDAGADVILVYGLgPDLAQILKAM-------EKLGwkvpLVGSWGLSMPNFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 272 SLVAPGQPERLSGM-----KGTAPASAENEQYVKDLKEfaPKLKELQFAPQVFDCATTIALAAEKAESDDPRDYVKEMNG 346
Cdd:cd06335 235 ELAGPLAEGTIMTQtfiedYLTPRAKKFIDAYKKKYGT--DRIPSPVSAAQGYDAVYLLAAAIKQAGSTDGKKIRAALEN 312
|
..
gi 1752498383 347 IT 348
Cdd:cd06335 313 LK 314
|
|
| PBP1_ABC_HAAT-like |
cd06344 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
58-387 |
3.40e-27 |
|
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: 110.39 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 58 ESLKFAIQKINDAGGVLGKAVPNVVSSDEA----GQeAVAAQSADRvlaAGVDAIVGAAASGMSLAFIDRVTGAGVVQCS 133
Cdd:cd06344 19 EGVELAVEEINAAGGVLGRKIRLVEYDDEAsvdkGL-AIAQRFADN---PDVVAVIGHRSSYVAIPASIIYERAGLLMLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 134 GSNTAPTFTDYeddGF-Y-FRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLTVTLAETYD 211
Cdd:cd06344 95 PGATAPKLTQH---GFkYiFRNIPSDEDIARQLARYAARQGYKRIVIYYDDDSYGKGLANAFEEEARELGITIVDRRSYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 212 PKATNFDQVAQQIENSRPDAAVVIA--FEEGAQILQGMIESGIgpdRIGVYGADGLRSEELPSLVapGQperlSGMKGTA 289
Cdd:cd06344 172 SDEEDFRRLLSKWKALDFFDAIFLAgsMPEGAEFIKQARELGI---KVPIIGGDGLDSPELIEIA--GK----AAEGVVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 290 PAS----AENEQYVKDLKEFAPKLKEL--QFAPQVFDCATTIALAAEKAESDDPRDyvkemngitkdgekcnsfaackeL 363
Cdd:cd06344 243 ATVfdpdDPRPEVRAFVEAFRKKYGREpdVWAAQGYDAVKLLAEAIEKAGSTVPAK-----------------------I 299
|
330 340
....*....|....*....|....*
gi 1752498383 364 LADGRDI-DYEGVSGPLNFTDKGEP 387
Cdd:cd06344 300 ASALRFLeNWEGVTGTYSFDANGDV 324
|
|
| PBP1_ABC_HAAT-like |
cd19986 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-258 |
6.74e-27 |
|
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: 108.87 E-value: 6.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAAG-VDAIVGAAASGMSL 118
Cdd:cd19986 3 GVVAPLTGPAALNGEYQKNGAQLALEEINAAGGVLGRPL-ELVVEDDQGTNTGAVNAVNKLISDDkVVAVIGPHYSTQVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGsNTAPTFTDYEDDgFYFRTVPSDALQGPILADVVRDD-GHDRVALVARADDYGRGLMEATRKTL 197
Cdd:cd19986 82 AVSPLVKEAKIPVITG-GTSPKLTEQGNP-YMFRIRPSDSVSAKALAKYAVEElGAKKIAILYDNDDFGTGGADVVTAAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498383 198 EERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAFE-EGAQILQGMIESGIGPDRIG 258
Cdd:cd19986 160 KALGLEPVAVESYNTGDKDFTAQLLKLKNSGADVIIAWGHDaEAALIARQIRQLGLDVPVIG 221
|
|
| PBP1_ABC_ligand_binding-like |
cd06340 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
40-337 |
2.91e-23 |
|
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: 99.94 E-value: 2.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGV--LGKAVPNVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAASGM 116
Cdd:cd06340 3 GVLYPLSGPLALIGQEAKRGAELAVDEINAAGGIksLGGAKIELVVADTQSDPEVAASEAERLITQeGVVAIIGAYSSSV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 117 SLAfIDRVT-GAGVVQCSGSNTAPTFTDyedDGF--YFRTVPSDALQGPILADVVRD----DGHD--RVALVARADDYGR 187
Cdd:cd06340 83 TLA-ASQVAeRYGVPFVTASAVADEITE---RGFkyVFRTAPTASQFAEDAVDFLKElakkKGKKikKVAIIYEDSAFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 188 GLMEATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDaaVVIA---FEEGAQILQGMIESGIGPDRIGVYGADG 264
Cdd:cd06340 159 SVAKGLKKAAKKAGLEVVLDEPYPAGATDLSSEVLKLKAAKPD--VVFAtsyTNDAILLLRTMKELGFKPKAIIGVGGGY 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752498383 265 LRSEELPSLvapgqPERLSGMKGTAPASAENEQYVKDLKEFAPKLKEL------QFAPQVFDCATTIALAAEKAESDDP 337
Cdd:cd06340 237 SDPEFLKAL-----GKDAEGVFSVVPWSPDLAKKKPGAKEVNERYKKKygedmtGHAARAYTAAWVLADALERAGSTDP 310
|
|
| PBP1_ABC_ligand_binding-like |
cd06338 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
39-348 |
1.13e-22 |
|
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: 98.04 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVL--GKAVP-NVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAAS 114
Cdd:cd06338 2 IGASLSLTGPFAGEGKAQKRGYELWVEDVNAAGGVKggGKKRPvELVYYDDQSDPATAVRLYEKLITEdKVDLLLGPYSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 115 GMSLA---FIDRvtgAGVVQCSGSNTAPTFtdYEDDGFY-FRTVPSDALQGPILADVVRDDGH--DRVALVARADDYGRG 188
Cdd:cd06338 82 GLTLAaapVAEK---YGIPMIAGGAASDSI--FERGYKYvFGVLPPASDYAKGLLDLLAELGPkpKTVAIVYEDDPFGKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 189 LMEATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIA-FEEGAQILQGMIESGIGPDRIGVYGADGLRS 267
Cdd:cd06338 157 VAEGAREAAKKAGLEVVYDESYPPGTTDFSPLLTKVKAANPDILLVGGyPPDAITLVRQMKELGYNPKAFFLTVGPAFPA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 268 --EELPSL----VAPGQPERLSGMKGTapasAENEQYVKDLKEFAPKLKELQfAPQVFDCATTIALAAEKAESDDP---R 338
Cdd:cd06338 237 frEALGKDaegvLGPSQWEPSLPYKVF----PGAKEFVKAYKEKFGEEPSYH-AAAAYAAGQVLQQAIEKAGSLDPekvR 311
|
330
....*....|
gi 1752498383 339 DYVKEMNGIT 348
Cdd:cd06338 312 DALASLDFDT 321
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
34-400 |
1.39e-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: 380566 [Multi-domain] Cd Length: 355 Bit Score: 98.02 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 34 DGELQFGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAA 112
Cdd:cd06343 4 DDEIKIGTSLPLSGPAAAYGKPVRAGAAAYFDEVNAAGGINGRKI-ELIVEDDGYDPARAVAAVRKlVEQDKVFAIVGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 113 ASGMSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFyFRTVPSDALQGPILAD-VVRDDGHDRVALVARADDYGRGLME 191
Cdd:cd06343 83 GTPTNLAVRPYLNEAGVPQLFPATGASALSPPPKPYT-FGVQPSYEDEGRILADyIVETLPAAKVAVLYQNDDFGKDGLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 192 ATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIGPDRIGVYGADGlrseel 270
Cdd:cd06343 162 GLKEALKAYGLEVVAEETYEPGDTDFSSQVLKLKAAGADVVVLGTLpKEAAAALKEAAKLGWKPTFLGSSVSAD------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 271 PSLVAPGQPERLSGMKGTA----PASAENE---QYVKDLKEFAPKLKELQFAPQVFDCATTIALAAEKAESDDPRD-YVK 342
Cdd:cd06343 236 PTTLAKAGGDAAEGVYSASylkdPTDADDPavkEFREAYKKYFPDDPPNAYALYGYAAAQVFVEALKRAGKDLTREgLIK 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498383 343 EMNGItkdgekcnsfaackelladgRDIDYEGVSGPLNFTDKGEPGQATIEVYGYDDK 400
Cdd:cd06343 316 ALESL--------------------KDFDDGGPGPPVTFSPDDHRGIESMYLVQVDGG 353
|
|
| PBP1_ABC_ligand_binding-like |
cd06345 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
59-386 |
6.49e-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: 96.18 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 59 SLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSLAFIDR---------VTGAg 128
Cdd:cd06345 19 GAELAVEEINAAGGILGRKV-ELVVADTQGKPEDGVAAAERlITEDKVDAIVGGFRSEVVLAAMEVaaeykvpfiVTGA- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 129 vvqCSGSNTAPTFTDYEDDGFYFRTVPSDALQG-----PILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLT 203
Cdd:cd06345 97 ---ASPAITKKVKKDYEKYKYVFRVGPNNSYLGatvaeFLKDLLVEKLGFKKVAILAEDAAWGRGIAEALKKLLPEAGLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 204 VTLAETYDPKATNFDQVAQQIENSRPDAAVVI-AFEEGAQILQGMIESGIgpdRIGVYGADGlrseelpSLVAPGQPERL 282
Cdd:cd06345 174 VVGVERFPTGTTDFTPILSKIKASGADVIVTIfSGPGGILLVKQWAELGV---PAPLVGINV-------PAQDPEFWENT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 283 SGM-------KGTAPASAENEQYVKDLKEFAPKLKELQ--FAPQVFDCATTIALAAEKAESDDPRDYVKEMNgitkdgek 353
Cdd:cd06345 244 GGAgeyeitlAFAAPKAKVTPKTKPFVDAYKKKYGEAPnyTAYTAYDAIYILAEAIERAGSTDPDALVKALE-------- 315
|
330 340 350
....*....|....*....|....*....|...
gi 1752498383 354 cnsfaackelladgrDIDYEGVSGPLNFTDKGE 386
Cdd:cd06345 316 ---------------KTDYEGVRGRIKFDKKDE 333
|
|
| PBP1_ABC_HAAT-like |
cd19981 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-270 |
1.18e-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 or peptides; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type active transport systems that are predicted to be involved in the uptake of amino acids or peptides. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, its ligand specificity has not been determined experimentally.
Pssm-ID: 380636 [Multi-domain] Cd Length: 297 Bit Score: 94.28 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAASGMSL 118
Cdd:cd19981 3 GFFAPLTGPAAADGKSALHGAELAVEQINAAGGINGKKV-ELVVYDDQASPKQAVNIAQKLIEQdKVVAVVSGSYSGPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDYEDdgFYFRTVPSDALQGPILADVVRDDGH-DRVALVARADDYGRGLMEATRKTL 197
Cdd:cd19981 82 AAAPIFQEAKVPMVSAYAVHPDITKAGD--YVFRVAFLGPVQGRAGAEYAVKDLGaKKVAILTIDNDFGKSLAAGFKEEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1752498383 198 EERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIA-FEEGAQILQGMIESGIgpdRIGVYGADGLRSEEL 270
Cdd:cd19981 160 KKLGAEIVSEYAYALGDRDFRPILTKIKSANPDAIYASGyYAEAAPIVKQARELGI---KVPIIGQEGYDSPKF 230
|
|
| PBP1_ABC_HAAT-like |
cd19983 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-236 |
1.29e-21 |
|
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: 94.19 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVPNVVSSDeaGQEAVAAQSADRVLAA-GVDAIVGAAASGMSL 118
Cdd:cd19983 3 GFVGGLTGRYSDLGVQGRNGAQLAVEEINAAGGINGRPVELIIRDD--QQDPEAAKAADRELIAgGVVAIIGHMTSAMTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDyEDDGFyFRTVPSDALQGPILADVVRDDGH-DRVALV----ARAddYGRGLMEAT 193
Cdd:cd19983 81 AVLPVINEAKVLMISPTVSTPELSG-KDDYF-FRVTPTTRESAQALARYAYNRGGlRRVAVIydlsNRA--YSESWLDNF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752498383 194 RKTLEERGLTVTLAETYDPKA-TNFDQVAQQIENSRPDAAVVIA 236
Cdd:cd19983 157 RSEFEALGGRIVAEIPFSSGAdVDFSDLARRLLASKPDGLLLVA 200
|
|
| PBP1_AmiC-like |
cd06331 |
type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system ... |
40-351 |
2.14e-21 |
|
type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF); This group includes the type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system for short-chain and urea (FmdDEF), found in bacteria and Archaea. AmiC controls expression of the amidase operon by a ligand-triggered conformational switch. In the absence of ligand or presence of butyramide (repressor), AmiC (the ligand sensor and negative regulator) adopts an open conformation and inhibits the transcription antitermination function of AmiR by direct protein-protein interaction. In the presence of inducing ligands such as acetamide, AmiC adopts a closed conformation which disrupts a silencing AmiC-AmiR complex and the expression of amidase and other genes of the operon is induced. FmdDEF is predicted to be an ATP-dependent transporter and closely resembles the periplasmic binding protein and the two transmembrane proteins present in various hydrophobic amino acid-binding transport systems.
Pssm-ID: 380554 [Multi-domain] Cd Length: 333 Bit Score: 94.21 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSL 118
Cdd:cd06331 3 GLLTPLSGPASVYGRAIANGAELAVEEINAAGGVLGRPV-ELVVEDDASDPATAVAAARRlIQQDKVDAIVGPITSATRN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCsgsntapTFTDYE-----DDGFYFRTVPSDALQgPILADVVRDDGhDRVALVarADDY--GRGLME 191
Cdd:cd06331 82 AVAPVAERAKVPLL-------YPTFYEggecsPYLFCFGEVPNQQLD-PLIPWLMEEYG-KKFYLI--GSDYvwPRTMND 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 192 ATRKTLEERGLTVtLAETYDP-KATNFDQVAQQIENSRPDaaVVIAF---EEGAQILQGMIESGIgpDRIGVYGADGLRS 267
Cdd:cd06331 151 AARRVIEAHGGEV-VGEEYLPlGTTDFSSVIEKIKASGAD--VVLSTlvgADAVTFLKQFAAAGL--RRKVRIAALLFDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 268 EELPSLvapgQPERLSGMKGTAPA-----SAENEQYVKDLKEFAPKLKELQ--FAPQVFDCATTIALAAEKAESDDPRDY 340
Cdd:cd06331 226 NTLAGL----GAEAAEGIYSVLSYfqsldTPENKAFVAAYRKKFGEDAPPItsLSEAAYEAVHLYAAAVEKAGSTDPEAV 301
|
330
....*....|.
gi 1752498383 341 VKEMNGITKDG 351
Cdd:cd06331 302 IAALPGVSFDG 312
|
|
| PBP1_GPCR_family_C-like |
cd06350 |
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ... |
56-307 |
4.64e-20 |
|
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: 90.43 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 56 QIESLKFAIQKINDAGGVLgkavPNV----------VSSDEAGQEAV-----------AAQSADRVLAAGVDAIVGAAAS 114
Cdd:cd06350 29 LVEAMIYAIEEINNDSSLL----PNVtlgydirdtcSSSSVALESSLeflldngikllANSNGQNIGPPNIVAVIGAASS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 115 GMSLAfIDRVTGA-GVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEAT 193
Cdd:cd06350 105 SVSIA-VANLLGLfKIPQISYASTSPELSDKIRYPYFLRTVPSDTLQAKAIADLLKHFNWNYVSTVYSDDDYGRSGIEAF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 194 RKTLEERGLTVTLAE--TYDPKATNFDQVAQQIEnSRPDAAVVIAFEEGAQILQGMIESG---------IGPDRigvYGA 262
Cdd:cd06350 184 EREAKERGICIAQTIviPENSTEDEIKRIIDKLK-SSPNAKVVVLFLTESDARELLKEAKrrnltgftwIGSDG---WGD 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1752498383 263 DGLRSEELPSLVApgqperlsGMKGTAPASAENEQYVKDLKEFAP 307
Cdd:cd06350 260 SLVILEGYEDVLG--------GAIGVVPRSKEIPGFDDYLKSYAP 296
|
|
| PBP1_ABC_HAAT-like |
cd19985 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-258 |
6.15e-20 |
|
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: 89.64 E-value: 6.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVPNVVSsDEAGQEAVAAQSADRVLAAGVDAIVGAAASGMSLA 119
Cdd:cd19985 3 AVVGPMSGKSASKGKSMLRGAELYIDQINAAGGINGKKVKLDVF-DDQNDPDAARKAAQIIVSDKALAVIGHYYSSASIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 120 FIDRVTGAGVVQCSGSNTAPTFTdyEDDGFYFRTVPSDALQGPILADVVRDD-GHDRVALVARADDYGRGLMEATRKTLE 198
Cdd:cd19985 82 AGKIYKKAGIPAITPSATADAVT--RDNPWYFRVIFNDSLQGRFLANYAKKVlKKDKVSIIYEEDSYGKSLASVFEATAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498383 199 ERGLTVTLAETYDPKATNFDQVAQQIENSRPDA-----AVVIAF--EEGAQILQGMIESG-----IGPDRIG 258
Cdd:cd19985 160 ALGLKVLKKWSFDTDSSQLDQNLDQIVDELKKApdepgVIFLAThaDEGAKLIKKLRDAGlkapiIGPDSLA 231
|
|
| PBP1_SBP-like |
cd19989 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
40-237 |
4.10e-19 |
|
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: 86.95 E-value: 4.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSL 118
Cdd:cd19989 3 GVLTPLSGPYAALGEEARRGAQLAVEEINAAGGILGRPV-ELVVEDTEGKPATAVQKARKlVEQDGVDFLTGAVSSAVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVArAD-DYGRGLMEATRKTL 197
Cdd:cd19989 82 AVAPKAAELKVPYLVTVAADDELTGENCNRYTFRVNTSDRMIARALAPWLAENGGKKWYIVY-ADyAWGQSSAEAFKEAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1752498383 198 EERGLTVtLAETYDP-KATNFDQVAQQIENSRPDAAVVIAF 237
Cdd:cd19989 161 EELGGEV-VGTLFAPlGTTDFSSYITQISDSGADGLLLALA 200
|
|
| PBP1_As_SBP-like |
cd06330 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
40-351 |
4.98e-19 |
|
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: 87.62 E-value: 4.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSL 118
Cdd:cd06330 3 GVITPLSGAAAVYGEPARNGAELAVEEINAAGGILGRKI-ELVVRDDKGKPDEAVRAARElVLQEGVDFLIGTISSGVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 A---FIDRVTGAGVVQCSGSN--TAPTFTDYeddgfYFRTVPSDALQGPILADVVRDDGHD--RVALVARADDYGRGLME 191
Cdd:cd06330 82 AvapVAEELKVLFIATDAATDrlTEENFNPY-----VFRTSPNTYMDAVAAALYAAKKPPDvkRWAGIGPDYEYGRDSWA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 192 ATRKTLEERGLTVTLAETYDPK--ATNFDQVAQQIENSRPDAAVV-------IAFeegaqILQGmieSGIGP-DRIGVYG 261
Cdd:cd06330 157 AFKAALKKLKPDVEVVGELWPKlgATDYTAYITALLAAKPDGVFSslwggdlVTF-----VKQA---KPYGLfDKTKVVS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 262 ADGLRSEELPSLVAPGQPERLSGMKG--TAPASAENEQYVKDLKEfapKLKEL--QFAPQVFDCATTIALAAEKAESDDP 337
Cdd:cd06330 229 GLGGGSEVLQALGKEMPEGLIGGGRYpfGWPDTPLNKAFVEAYRA---KYGEYptYWAYEAYAAVMALKAAIEKAGSTDT 305
|
330
....*....|....
gi 1752498383 338 RDYVKEMNGITKDG 351
Cdd:cd06330 306 DKVIAALEGLTFDT 319
|
|
| PBP1_SBP-like |
cd06328 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
40-353 |
1.54e-16 |
|
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); Periplasmic substrate-binding domain of active transport proteins found in gram-negative and gram-positive bacteria. 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: 380551 [Multi-domain] Cd Length: 336 Bit Score: 80.04 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGG-VLGKAVpNVVSSDEAGQEAVAAQSADRVLA-AGVDAIVGAAASGMS 117
Cdd:cd06328 3 GVITSLTGPLAAYGKQTERGFELGLEYATDGTMeVDGRKI-EVIVKDDQGDPDTAKAAATELIGdDGVDILVGTVSSAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 118 LAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPS---DALQGPILADvvrDDGHDRVALVARADDYGRGLMEATR 194
Cdd:cd06328 82 LALAPVAEQNKKILIVGPAAADSITGENWNKYTFRTSRNswqDAIAGAKALA---DPLGKSVAFLAQDYAFGQDGVAAFK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 195 KTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVI-AFEEGAQILQGMIESGIgPDRIGVY--GADglrseeLP 271
Cdd:cd06328 159 KALEAKGGKIVGEELVPVTTTDFTPYLQRILDAKPDVLFVAwAGTGALTLWQQLADQGV-LDDIKVVtgGPD------IA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 272 SLVAPGqpERLSGMKG------TAPASAENEQYVKDLKEFAPKLKELqFAPQVFDCATTIALAAEKAESD-DPRDYVKEM 344
Cdd:cd06328 232 TLAALG--DALPGIEGltyyyyGLPKNPVNDWLVKAHKERYNAPPDL-FTAGGFAAAQAVVRALEKAGGDtDVEKLIAAL 308
|
....*....
gi 1752498383 345 NGITKDGEK 353
Cdd:cd06328 309 EGLTFETPK 317
|
|
| PBP1_ABC_ligand_binding-like |
cd06336 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
39-344 |
2.91e-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 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: 79.20 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVL--GKAVP-NVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAAS 114
Cdd:cd06336 2 IGFLGPLSGPAAAWGLPMLRGLELAADEINAAGGIKvgGKKYKvEVVSYDDKYTPAEAVAAARRlVSQDGVKFIFGPGGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 115 GMSLAFIDRVTGAGVVQCSGSNTAPTFT-DYEddgFYFRTVPSDALQGPILADVVRD-DGHDRVALVARADDYGRGLMEA 192
Cdd:cd06336 82 AIAAAVQPVTERNKVLLLTAAFSDPILGpDNP---LLFRIPPTPYEYAPPFIKWLKKnGPIKTVALIAPNDATGKDWAAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 193 TRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAFEEG--AQILQGMIESGI-GPdrigVYGADGLRSEE 269
Cdd:cd06336 159 FVAAWKAAGGEVVAEEFYDRGTTDFYPVLTKILALKPDALDLGGSSPGpaGLIIKQARELGFkGP----FVSEGGAKADE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 270 LPSLVApgqPERLSGMKGTAPASAENEQ--YVKDL-KEFAPKLKELQ--FAPQVFDCATTIALAAEKAESDDPRDYVKEM 344
Cdd:cd06336 235 ILKEVG---GEAAEGFIGVLPADDDPIAspGAKAFvERYKKKYGEPPnsESALFYDAAYILVKAMEKAGTVDDTKKIRAA 311
|
|
| PRK15404 |
PRK15404 |
high-affinity branched-chain amino acid ABC transporter substrate-binding protein; |
5-208 |
3.75e-16 |
|
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
Pssm-ID: 237959 [Multi-domain] Cd Length: 369 Bit Score: 79.29 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 5 IRRSAIFASAAALVIAvcgttGTAQAEpgdgELQFGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVPNVVSS 84
Cdd:PRK15404 3 SKGKTLLAGCIALALS-----HAALAD----DIKIAIVGPMSGPVAQYGDMEFTGARQAIEDINAKGGIKGDKLEGVEYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 85 DEAG-QEAVAAqsADRVLAAGVDAIVGAAASGMSLAFIDRVTGAGVVQCSGSNTAPTFTD--YEddgFYFRTVPSDALQG 161
Cdd:PRK15404 74 DACDpKQAVAV--ANKVVNDGIKYVIGHLCSSSTQPASDIYEDEGILMITPAATAPELTArgYQ---LIFRTIGLDSDQG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1752498383 162 PI----LADVVRDdghDRVALVARADDYGRGLMEATRKTLEERGLTVTLAE 208
Cdd:PRK15404 149 PTaakyILEKVKP---KRIAVLHDKQQYGEGLARSVKDGLKKAGANVVFFE 196
|
|
| PBP1_ABC_HAAT-like |
cd06348 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
40-391 |
4.61e-16 |
|
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: 78.81 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAG--QEAVAAQsadRVLAA--GVDAIVGAAASG 115
Cdd:cd06348 3 GVALSLTGPGALYGQSQKNGAQLAVEEINAAGGVGGVKI-ELIVEDTAGdpEQAINAF---QKLINqdKVLAILGPTLSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 116 MSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDdgFYFR-TVPSDALQGPILADVVRDDGHDRVALV-ARADDYGRGLMEAT 193
Cdd:cd06348 79 EAFAADPIAQQAKVPVVGISNTAPGITDIGP--YIFRnSLPEDKVIPPTVKAAKKKYGIKKVAVLyDQDDAFTVSGTKVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 194 RKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIA-FEEGAQILQGMIESGI-GPdrigVYGADGLRSEELP 271
Cdd:cd06348 157 PAALKKNGVEVLDTETFQTGDTDFSAQLTKIKALNPDAIVISAlAQEGALIVKQARELGLkGP----IVGGNGFNSPDLI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 272 SLV----------APGQPERlsgmkgtapASAENEQYVKDLKEFAPKLKElQFAPQVFDCATTIALAAEKAESDDPRDYV 341
Cdd:cd06348 233 KLAgkaaegvivgSAWSPDN---------PDPKNQAFVAAYKEKYGKEPD-QFAAQAYDAAYILAEAIKKAGSTTDRADL 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1752498383 342 K-EMNGITKDGekcnsfaackelladgrdiDYEGVSGPLNFTDKGEPGQAT 391
Cdd:cd06348 303 RdALARILIAK-------------------DFEGPLGPFSFDADRDGIQPP 334
|
|
| PBP1_SBP-like |
cd06329 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
38-351 |
7.95e-15 |
|
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: 75.00 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 38 QFGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAAGVDAIVGAAASGMS 117
Cdd:cd06329 1 KIAFIDPLSGPFASVGEIYLKGLQFAIEEINAGGGLLGRKI-ELVPFDNKGSPQEALIQLKKAIDQGIRFVLQGNSSAVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 118 LAFID-------RVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGH-DRVALVARADDYGRGL 189
Cdd:cd06329 80 GALIDaiekhnqRNPDKRVLFLNYGAEAPELTGAKCSFWHFRFDANADMKMAALADYMKKDGSiKKVYLINQDYSFGRDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 190 MEATRKTLEERGLTVTLA-ETYDP--KATNFDQVAQQIENSRPDAavVIAFEEGA---QILQGMIESGIGPdRIGVYGAD 263
Cdd:cd06329 160 AAAAKKNLKKKRPDIEIVgEDLHPlgKVKDFSPYIAKIKASGADT--VITGNWGNdltLLMKAARDSGLKA-PFYTYYAD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 264 GlrseelpslvaPGQPERLS-GMKGT---------APASAENEQYVKDLKefapklKELQFAPQVFDCATTIAL-----A 328
Cdd:cd06329 237 G-----------PGAPAAIGeAGVGRlvavaywhpNPKTPELEKFAEAFR------AKYGRYPDFNIGRTYMGVemlaaA 299
|
330 340
....*....|....*....|...
gi 1752498383 329 AEKAESDDPRDYVKEMNGITKDG 351
Cdd:cd06329 300 IKKAGSTDPEKVAKALEGLSFDT 322
|
|
| PBP1_ABC_transporter_GPCR_C-like |
cd04509 |
Family C of G-protein coupled receptors and their close homologs, the type 1 ... |
53-258 |
1.01e-14 |
|
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: 74.26 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 53 GPPQIESLKFAIQKINDAGGVLGKAVPNVVSSDEAGQEAVAAQSADRVLAA-----------------------GVDAIV 109
Cdd:cd04509 26 GIQRFEAMEQALDDINADPNLLPNNTLGIVIYDDCCDPKQALEQSNKFVNDliqkdtsdvrctngeppvfvkpeGIKGVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 110 GAAASGMSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGL 189
Cdd:cd04509 106 GHLCSSVTIPVSNILELFGIPQITYAATAPELSDDRGYQLFLRVVPLDSDQAPAMADIVKEKVWQYVSIVHDEGQYGEGG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 190 MEATRKTLEERGLTVTLAE--TYDPKATNFDQVAQQIENsRPDAAVVIAFEEG---AQILQGMIESG-------IGPDRI 257
Cdd:cd04509 186 ARAFQDGLKKGGLCIAFSDgiTAGEKTKDFDRLVARLKK-ENNIRFVVYFGYHpemGQILRAARRAGlvgkfqfMGSDGW 264
|
.
gi 1752498383 258 G 258
Cdd:cd04509 265 A 265
|
|
| PBP1_ABC_ligand_binding-like |
cd06326 |
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ... |
39-236 |
5.57e-13 |
|
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the 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); its ligand specificity has not been determined experimentally, however.
Pssm-ID: 380549 [Multi-domain] Cd Length: 339 Bit Score: 69.49 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAASGMS 117
Cdd:cd06326 3 IGQSAPLSGPLAELGREYLAGAKAYFDQVNAAGGINGRKI-RLVTLDDGYDPARTVENTRQLIEQdKVVALFGYVGTANV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 118 LAFIDRVTGAGVVQ---CSGSNTAPTFTDyeddGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATR 194
Cdd:cd06326 82 EAVLPLLEEAGVPLvgpLTGADSLREPGN----PYVFHVRASYADEVEKIVRHLATLGLKRIAVVYQDDPFGKEGLAAAE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1752498383 195 KTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIA 236
Cdd:cd06326 158 AALAARGLEPVATAAVARNAADVAAAAAALAAAKPQAVVLIA 199
|
|
| PBP1_mGluR_groupI |
cd06374 |
ligand binding domain of the group I metabotropic glutamate receptor; Ligand binding domain of ... |
135-248 |
1.75e-12 |
|
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: 68.52 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 135 SNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLTVTLAETYDPKA 214
Cdd:cd06374 149 SATSIDLSDKSLYKYFLRVVPSDYLQARAMLDIVKRYNWTYVSTVHTEGNYGESGIEAFKELAAEEGICIAHSDKIYSNA 228
|
90 100 110
....*....|....*....|....*....|....*.
gi 1752498383 215 TN--FDQVAQQIENSRPDAAVVIAFEEGAqILQGMI 248
Cdd:cd06374 229 GEeeFDRLLRKLMNTPNKARVVVCFCEGE-TVRGLL 263
|
|
| PBP1_RPA0668_benzoate-like |
cd20014 |
type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the ... |
40-349 |
2.34e-12 |
|
type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the active transport of lignin-derived benzoate derivative compounds, and its close homologs; This group includes RPA0668 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0668 is the periplasmic binding-protein component of an ABC system that is involved in the active transport of lignin-derived benzoate derivative compounds. 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: 380667 [Multi-domain] Cd Length: 346 Bit Score: 67.65 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINdaGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLA-AGVDAIVGAAASGMSL 118
Cdd:cd20014 3 GLLLPYSGVYAALGEDIRNGFQLYLDEHG--GKLGGRPI-ELVKEDDEADPDVALQKARKLIEqDKVDVLVGPVSSGVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVarADDY--GRGLMEATRKT 196
Cdd:cd20014 80 AIRDVVEQAKVPLIVANAGANALTRAACSPYIFRTSFSNWQLGYALGKYAAENVGKTVVTI--ASDYaaGREVVAGFKEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 197 LEERGLTVtLAETYDP--KATNFDQVAQQIENSRPDAavVIAF---EEGAQILQGMIESGIgPDRIGVYGADGLRSEElp 271
Cdd:cd20014 158 FEAAGGKV-VGEIWTPlgTTTDFSPYLTQIAASGPDA--VYAFfagADAVRFVKQYAEFGL-KGKIPLYGPGFLTDED-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 272 slVAPGQPERLSGMKGTAP-----ASAENEQYVKDLKEFAPKLKELqFAPQVFDCATTIALAAEKAESD-DPRDYVKEMN 345
Cdd:cd20014 232 --VLPALGEAAEGIITVLHyaptlDNPANRAFVAAYQAKYGRLPDV-YAVQGYDAAQVIDAALEAVGGDtSDKDILAAAL 308
|
....
gi 1752498383 346 GITK 349
Cdd:cd20014 309 ELGS 312
|
|
| PBP1_ABC_ligand_binding-like |
cd19982 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
40-254 |
2.99e-12 |
|
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: 66.92 E-value: 2.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSL 118
Cdd:cd19982 3 GAILSLTGPFAPFGEMFKNGYEMALEEINAAGGIKGKKL-ELVIEDDQSKPQTALAAAEKlVSQDKVPLIVGGYSSGITL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 ---AFIDRVTGAGVVQCSGSNTApTFTDYEddgFYFRT-VPSDALQGPILaDVVRDDGHDR-VALVARADDYGRGLMEAT 193
Cdd:cd19982 82 pvaAVAERQKIPLLVPTAADDDI-TKPGYK---YVFRLnPPASIYAKALF-DFFKELVKPKtIAILYENTAFGTSVAKAA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752498383 194 RKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF-EEGAQILQGMIESGIGP 254
Cdd:cd19982 157 RRFAKKRGIEVVADESYDKGATDFKPLLNKVKAANPDVVYMVSYlNDAILLMRQAKELGLNP 218
|
|
| PBP1_CaSR |
cd06364 |
ligand-binding domain of the CaSR calcium-sensing receptor, a member of the family C receptors ... |
57-237 |
6.65e-12 |
|
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: 6.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 57 IESLKFAIQKIN----------------DAGGVLGKAVPNVVSSdEAGQEAVAAQSADRVlAAGVDAIVGAAASGMSLAf 120
Cdd:cd06364 39 AQTMIFAIEEINnspdllpnitlgyriyDSCATISKALRAALAL-VNGQEETNLDERCSG-GPPVAAVIGESGSTLSIA- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 121 IDRVTGA-GVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEE 199
Cdd:cd06364 116 VARTLGLfYIPQVSYFASCACLSDKKQFPSFLRTIPSDYYQSRALAQLVKHFGWTWVGAIASDDDYGRNGIKAFLEEAEK 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1752498383 200 RGLTVTLAETYdPKATN---FDQVAQQIENSRpdAAVVIAF 237
Cdd:cd06364 196 LGICIAFSETI-PRTYSqekILRIVEVIKKST--AKVIVVF 233
|
|
| PBP1_glutamate_receptors-like |
cd06269 |
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ... |
40-241 |
7.98e-11 |
|
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: 62.82 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYlGPPQIESLKFAIQKINDAGGVLGKAVPNVVSSDEAGQEAVAAQSA-DRVLAAGVDAIVGAAASgMSL 118
Cdd:cd06269 3 GALLPVHDYLES-GAKVLPAFELALSDVNSRPDLLPKTTLGLAIRDSECNPTQALLSAcDLLAAAKVVAILGPGCS-ASA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGA-GVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTL 197
Cdd:cd06269 81 APVANLARHwDIPVLSYGATAPGLSDKSRYAYFLRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEELF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1752498383 198 EERGLTVTLAETYDPKAT-NFDQVAQQIENSRPDAAVVIAFEEGA 241
Cdd:cd06269 161 QEKGGLITSRQSFDENKDdDLTKLLRNLRDTEARVIILLASPDTA 205
|
|
| PBP1_ABC_ligand_binding-like |
cd19978 |
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ... |
37-236 |
1.51e-10 |
|
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in the uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the 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); its ligand specificity has not been determined experimentally, however.
Pssm-ID: 380633 [Multi-domain] Cd Length: 341 Bit Score: 62.21 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 37 LQFGYVLPETGQLAYLGppqiESLKF----AIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVL-AAGVDAIVGA 111
Cdd:cd19978 1 IRLGMSAALSGPAAELG----NEMKRgieaAFNEVNAQGGVNGRKI-KLIALDDGYEPDRTVKNTKKLIeEDKVFALIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 112 AASGMSLAFIDRVTGAGVV---QCSGsntAPTFTDYEDDG-FYFRtvPSDALQGPILAD-VVRDDGHDRVALVARADDYG 186
Cdd:cd19978 76 VGTPTALAALPLANEKKIPlfgPFTG---AEFLRTPFLPYvFNLR--ASYADETEALVDyLVKTLGPKRIAIFYQNDAFG 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752498383 187 RGLMEATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIA 236
Cdd:cd19978 151 LAGLEGAKKALKKRGLTPVAEGSYTRNTLDVEEALAKILKAKPEAIILVG 200
|
|
| PBP1_FmdD-like |
cd06355 |
periplasmic component (FmdD) of an active transport system for short-chain amides and urea ... |
46-351 |
2.77e-10 |
|
periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF); This group includes the periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF), found in Methylophilus methylotrophus, and its homologs from other bacteria. FmdD, a type 1 periplasmic binding protein, is induced by short-chain amides and urea and repressed by excess ammonia, while FmdE and FmdF are hydrophobic transmembrane proteins. FmdDEF is predicted to be an ATP-dependent transporter and closely resembles the periplasmic binding protein and the two transmembrane proteins present in various hydrophobic amino acid-binding transport systems.
Pssm-ID: 380578 [Multi-domain] Cd Length: 347 Bit Score: 61.44 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 46 TGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVPNVVsSDEAGQEAVAAQSADRVL-AAGVDAIVGAAASGMSLAFIDRV 124
Cdd:cd06355 9 SGTMAISERPLVDATLLAIDEINAAGGLLGRKIEPVI-EDGASDWPTFAEKAEKLItQDKVAVIFGCWTSASRKAVLPVI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 125 TGAGV-----VQCSGSNTAPtftdyedDGFYFRTVPSdalQGPILA-DVVRDDGHDRVALVARADDYGRGLMEATRKTLE 198
Cdd:cd06355 88 EKYNGllfypVQYEGLEQSP-------NIVYTGATPN---QQILPAiDWLLENLGKRFFLVGSDYVFPRTANKIIRDQLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 199 ERGLTVtLAETYDP-KATNFDQVAQQIENSRPDaAVV--------IAFeegaqiLQGMIESGIGPDRIGVYGADgLRSEE 269
Cdd:cd06355 158 ALGGEV-VGEEYVPlGGTDFDAIVAKIKAFKPD-VIVntlngdsnIAF------FKQLAAAGITASDLPVLSFS-VSEAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 270 LPSLvapgQPERLSGMKGTAP-----ASAENEQYVKDLKEFAPKlKELQFAPQVfdcATTIAL-----AAEKAESDDPRD 339
Cdd:cd06355 229 LRAI----GPEELAGHYAAWNyfqslDTPENQAFVEAFKAKYGA-DRVTSDPME---AAYLGVylwaqAVEKAGSFDPDA 300
|
330
....*....|..
gi 1752498383 340 YVKEMNGITKDG 351
Cdd:cd06355 301 VRAALKGQSFEA 312
|
|
| PBP1_mGluR |
cd06362 |
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ... |
105-245 |
6.61e-10 |
|
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: 60.77 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 105 VDAIVGAAASGMSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADD 184
Cdd:cd06362 108 VVGVIGAESSSVSIQVANLLRLFKIPQISYASTSDELSDKERYPYFLRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGS 187
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752498383 185 YGRGLMEATRKTLEERGLTVTLAE--TYDPKATNFDQVAQQIENsRPDAAVVIAFEEGAQILQ 245
Cdd:cd06362 188 YGEEGYKAFKKLARKAGICIAESEriSQDSDEKDYDDVIQKLLQ-KKNARVVVLFADQEDIRG 249
|
|
| PBP1_GPC6A-like |
cd06361 |
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ... |
105-252 |
2.03e-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: 58.92 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 105 VDAIVGAAASGMSLAfIDRVTGAGVV-QCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARAD 183
Cdd:cd06361 102 VKAVIGASYSEISIA-VARLLNLQLIpQISYESSAPILSDKLRFPSFLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDD 180
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498383 184 DYGRGLMEATRKTLEERGLTVTLAETY-----DP-KATNFDQVAQQIENSrPDAAVVIAFEEGAQI---LQGMIESGI 252
Cdd:cd06361 181 DYGRSALESFIIQAEAENVCIAFKEVLpaylsDPtMNVRINDTIQTIQSS-SQVNVVVLFLKPSLVkklFKEVIERNI 257
|
|
| PBP1_ABC_ligand_binding-like |
cd06341 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
40-309 |
8.31e-09 |
|
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: 380564 [Multi-domain] Cd Length: 340 Bit Score: 56.93 E-value: 8.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAaSGMSL 118
Cdd:cd06341 3 GLIYPDTGPGAASFSAARAGAEARFGLANAAGGINGRKV-EYVWCDDQSDPATNLQAARQlVEDEKVFALVGSS-SAASG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALqgpILADVVRDDGHDRVALV-----ARADDYGRGLMEAT 193
Cdd:cd06341 81 SANDYLAQAGIPVVGGAGVSVWCFRNMFSNFFSLGGGGSTT---TYGQYAAALGGTKAAVVvtdipAASQQLAQQLAASL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 194 RKTleerGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAFEEG-AQILQGMiesgigpDRIGVYGADGLRSEELPS 272
Cdd:cd06341 158 RAA----GVEVVGTAPYAAAAPDYTAVAQAAKAAGADAVVGVLDPDVaARVLKAA-------RAQGLDLKVALSPSGYDP 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1752498383 273 LVAPGQPERLSGMKGTAPA------SAENEQYVKDLKEFAPKL 309
Cdd:cd06341 227 SVLAAYGAALAGVSVASTFlpfeadTPAVKAYRAAMAKYAPEL 269
|
|
| PBP1_AmiC |
cd06357 |
periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding ... |
45-350 |
9.14e-09 |
|
periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding fold protein family; This group includes the periplasmic binding domain of amidase (AmiC) that belongs to the type 1 periplasmic binding fold protein family. AmiC controls expression of the amidase operon by the ligand-triggered conformational switch. In the absence of ligand or presence of butyramide (repressor), AmiC (the ligand sensor and negative regulator) adopts an open conformation and inhibits the transcription antitermination function of AmiR by direct protein-protein interaction. In the presence of inducing ligands such as acetamide, AmiC adopts a closed conformation which disrupts a silencing AmiC-AmiR complex and the expression of amidase and other genes of the operon are induced.
Pssm-ID: 380580 [Multi-domain] Cd Length: 357 Bit Score: 56.82 E-value: 9.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 45 ETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSLAFIDR 123
Cdd:cd06357 8 QTGVTAIIEQSMLNGALLAIEEINAAGGVNGRPI-EPVVYDPASDPDRYRELAERlLLEDGVRHIFGCYTSASRKAVLPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 124 VTGAGVVQCSgsntaPTFtdYEddGF-------YFRTVPSDALQGpiLADVVRDDGHDRVALVARADDYGRGLMEATRKT 196
Cdd:cd06357 87 VERHNALLWY-----PTP--YE--GFeyspnviYTGAVPNQHLLP--LARYLLAHFGKRVFLVGSNYVYPWESNRVAREL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 197 LEERGLTVtLAETYDP-KATNFDQVAQQIENSRPDA---AVV----IAFeegaqiLQGMIESGIGPDRIGVygADGLRSE 268
Cdd:cd06357 156 IEASGGEV-VGERYVPlGDTDFAEIIEEIKSLKPDVvfsTLVgdsiYAF------YRAYAEAGLDPADMPI--ASLTTSE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 269 elPSLVAPGqPERLSGMKGTAP-----ASAENEQYVKDLKEFAPKLKELQ-FAPQVFDCATTIALAAEKAESDDPRDYVK 342
Cdd:cd06357 227 --AEVAAIG-AEAAAGHYTSAPyfqsiDTPENRAFVEAYRARFGDDAVTSaVAEAAYFQVHLLARAIERAGSDDPEAIRA 303
|
....*...
gi 1752498383 343 EMNGITKD 350
Cdd:cd06357 304 ALYGQEFD 311
|
|
| PBP1_GABAb_receptor |
cd06366 |
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ... |
130-393 |
3.81e-08 |
|
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: 54.94 E-value: 3.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 130 VQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLTVTLAET 209
Cdd:cd06366 96 VQLSYAATSPALSDRKRYPYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAEDLEELLEEANITIVATES 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 210 YdpkaTNFDqVAQQIEN-SRPDAAVVIAF---EEGAQIL-----QGMiesgIGPDR----IGVY-------GADGLR--S 267
Cdd:cd06366 176 F----SSED-PTDQLENlKEKDARIIIGLfyeDAARKVFceaykLGM----YGPKYvwilPGWYddnwwdvPDNDVNctP 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 268 EEL-----------PSLVAPGQPERLSGMkgTApasaenEQYVKDLKEFAPKLKEL--QFAPQVFDCATTIALAAEKAES 334
Cdd:cd06366 247 EQMlealeghfsteLLPLNPDNTKTISGL--TA------QEFLKEYLERLSNSNYTgsPYAPFAYDAVWAIALALNKTIE 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 335 DDPRdYVKEMNGITKDgekcNSFAAcKELLADGRDIDYEGVSGPLNFTDKGEP-GQATIE 393
Cdd:cd06366 319 KLAE-YNKTLEDFTYN----DKEMA-DLFLEAMNSTSFEGVSGPVSFDSKGDRlGTVDIE 372
|
|
| PBP1_SBP-like |
cd19987 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
39-262 |
5.41e-08 |
|
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: 380642 [Multi-domain] Cd Length: 353 Bit Score: 54.26 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAG------------GVLGKAVpNVVSSDEAGQEAVAAQSADRVLA-AGV 105
Cdd:cd19987 2 IGLNVPLSGPYAPQGEDQRRGFELAVDHLNNGGglvdkdsrlsgdGILGKKV-ELVTADTETKADTAVDNAKRLIEqDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 106 DAIVGAAASGMSLAFIDRVTGAGVVQ---CSGSNtAPTFTDYEDDGF--YFRTVPSDALQGPILADVVrddGHDRVALVA 180
Cdd:cd19987 81 VMITGGSSSAVAVAAQKLAQKEGVLYfagLSHSN-DTTGKDCHRYGFreCFNAHMSAKALAPYLVEKF---GKDRKYFYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 181 RAD-DYGRGLMEATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAF----------------EEGAQI 243
Cdd:cd19987 157 TADyTWGHSTEQSMREYTEAHGWKTVGNPATPLGETDFSAALLNAADSGADVLVLVLFgrdmvnalkqakqfglLKKMDI 236
|
250 260
....*....|....*....|....
gi 1752498383 244 L-----QGMIESGIGPDRIGVYGA 262
Cdd:cd19987 237 VvplltAFMAESVGPEIMEGVLGT 260
|
|
| PBP1_NHase |
cd06358 |
type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively ... |
40-237 |
6.19e-08 |
|
type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides; This group includes the type 1 periplasmic-binding protein of the nitrile hydratase (NHase) system that selectively converts nitriles to corresponding amides, which are subsequently converted by amidases to yield free carboxylic acids and ammonia. NHases from bacteria and fungi have been purified and characterized. In Rhodococcus sp., the nitrile hydratase operon consists of six genes encoding NHase regulator 2, NHase regulator 1, amidase, NHase alpha subunit, NHase beta subunit, and NHase activator. The operon produces a constitutive hydratase that has a broad substrate spectrum: aliphatic and aromatic nitriles, mononitriles and dinitriles, hydroxynitriles and amino-nitriles, and a constitutive amidase of equally low substrate specificity. NHases are metalloenzymes containing either cobalt or iron, and therefore can be classified into two subgroups: ferric NHases and cobalt NHases.
Pssm-ID: 380581 [Multi-domain] Cd Length: 333 Bit Score: 54.13 E-value: 6.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAAG-VDAIVGAAASGMSL 118
Cdd:cd06358 3 GLLIPLSGPAGLWGPSCEACAELAAAEINAAGGILGREV-ELVLIDAGGPPAEVAAAARRLVDDGaVDAIVGMHTSAVRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AfIDRVTGAGV------VQCSGSNTAPTFTDYEddgfyfrtVPSDALQGPI--LADVVRDdghDRVALVarADDY--GRG 188
Cdd:cd06358 82 A-LANAVGGRVpyvytpLYEGGERTPGVYAIGE--------TPEEQLRPALrwLADERRV---RRWFLV--GNDYvwPRA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1752498383 189 LMEATRKTLEERGLTVTlAETYDP-KATNFDQVAQQIENSRPDaAVVIAF 237
Cdd:cd06358 148 SHAAARRYIARLGGEVV-GERFVPlGEDDFERVLARIRASRPD-AVLISL 195
|
|
| PBP1_Nba-like |
cd06359 |
type 1 periplasmic binding component of active transport systems predicted to be involved in ... |
40-389 |
1.27e-07 |
|
type 1 periplasmic binding component of active transport systems predicted to be involved in 2-nitrobenzoic acid degradation pathway; This group includes the type 1 periplasmic binding component of active transport systems that are predicted to be involved in 2-nitrobenzoic acid degradation pathway; their substrate specificities are not well characterized.
Pssm-ID: 380582 [Multi-domain] Cd Length: 333 Bit Score: 53.03 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 40 GYVLPETGQLAYLGPPQIESLKFAIQKIndaGGVLGKAVPNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMSL 118
Cdd:cd06359 3 GFITTLSGPAAVLGQDMRDGFNLALEQL---GGKLGGLPVEVVVEDDQLKPDVAKQAAERlIERDKVDFVTGIIFSNVML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSgSNTAPtfTDYEDDG----FYFRTVPSDAlQGPILADVVRDDGHDRVALVarADDY--GRGLMEA 192
Cdd:cd06359 80 AVVKPVVDSKVFYIS-ANAGP--SDLAGKGcnpnFFVTSWQNDQ-LHEAAGKYANDKGYKRVYLL--APNYqaGKDALAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 193 TRKTLEerGLTVTlaETYDP-KATNFDQVAQQIENSRPDAavVIAFEEGA---QILQGMIESGIGpDRIGVYGAdgLRSE 268
Cdd:cd06359 154 FKRTYK--GEVVG--EIYTPlGQLDFSAELAQIRAAKPDA--VFAFYPGGmgvNFVKQYAQAGLK-KKIPLYTV--GTLD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 269 ELPSLvaPGQPERLSGMKGTAPASA-----ENEQYVKDlkeFAPKLKEL--QFAPQVFDCATTIALAaekaesddprdyV 341
Cdd:cd06359 225 DEDLL--PAMGDAALGVLSVSQWSPdldnpENKRFVAA---FRKKYGRPpsNYAAQGYDAALLIDAA------------V 287
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1752498383 342 KEMNGITKDGEKcnsfaackeLLADGRDIDYEGVSGPLNFTDKGEPGQ 389
Cdd:cd06359 288 KAVGGDLSDKDA---------LRAALRKADFKSVRGAFRFNNNQFPIQ 326
|
|
| PBP1_amide_urea_BP-like |
cd06356 |
periplasmic component (FmdD) of an active transport system for short-chain amides and urea ... |
39-351 |
1.35e-07 |
|
periplasmic component (FmdD) of an active transport system for short-chain amides and urea (FmdDEF); This group includes the type 1 periplasmic-binding proteins that are predicted to have a function similar to that of an active transport system for short chain amides and/or urea in bacteria and Archaea, by sequence comparison and phylogenetic analysis.
Pssm-ID: 380579 [Multi-domain] Cd Length: 334 Bit Score: 53.07 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADR-VLAAGVDAIVGAAASGMS 117
Cdd:cd06356 2 IGSIFDLSGGLNIYGKPMVHAMKLAVEEINAAGGLLGRQI-ELVAYDTQSDMQKYTQYAQQlILRDKVDVVFGGITSASR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 118 LAF---IDRvtgagvvqcsgsNTAPTF--TDYED---DGFYFRTVPSDALQGPILADVVRDDGHDRVALVArAD-DYGRG 188
Cdd:cd06356 81 EAIrpiLRR------------NKILYFynTQYEGgvcDKNTFCTGSTPEQQVSPLIEWAIKKYGKKVYIIA-ADyNFGQI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 189 LMEATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDaAVVIAFEEGAQI--LQGMIESGIgPDRIG----VYGA 262
Cdd:cd06356 148 SADWVKKYAKKNGGEVVGEEFFPLDVTDFGPTIQKIQAAKPD-FVVSLLVGGNHIsfYRQWAAAGL-KKKIPivstVFGA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 263 DG----LRSEELPSL-VAPGQPERLSgmkgtapaSAENEQYVKDLKEFAPKLKEL-QFAPQVFDCATTIALAAEKAESDD 336
Cdd:cd06356 226 GNehkvLSPPELEGMyVSYSYFEELD--------TPANKAFVAKWRAKYGDEPYInQEAVGVYNAVYLWAEAVEKAGSTE 297
|
330
....*....|....*.
gi 1752498383 337 PRDYVKEM-NGITKDG 351
Cdd:cd06356 298 REAVIAALeSGISFDG 313
|
|
| PBP1_ABC_ligand_binding-like |
cd19979 |
amino acid amide ABC transporter substrate binding protein haat family; This subgroup includes ... |
63-251 |
1.48e-07 |
|
amino acid amide ABC transporter substrate binding protein haat family; 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: 380634 [Multi-domain] Cd Length: 350 Bit Score: 53.00 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 63 AIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAAG-VDAIVGAAASGMSLAFIDRVTGAGVVQCSGSNTAPTF 141
Cdd:cd19979 26 AIDEINAAGGLLGRKL-ELVAKDHRGNPARGVDNLREFAADPdVLAVFGGLHSPVLLAELDFIHELKIPYLVPWAAATPI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 142 TDYE-DDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLTVTLAETYDPKATNFDQV 220
Cdd:cd19979 105 TRNGySPNYIFRLSVDDSLAGPFLVEYALKKGCKRPALLLENTGWGRSNLKAMTKALAKKGLQPVGVEWFNWGDTDAKPQ 184
|
170 180 190
....*....|....*....|....*....|..
gi 1752498383 221 AQQIENSRPDAAVVIAFE-EGAQILQGMIESG 251
Cdd:cd19979 185 LRALKAAGADAILLVANApEGAAIVKALAALP 216
|
|
| PBP1_mGluR_groupIII |
cd06376 |
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ... |
105-237 |
5.42e-07 |
|
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: 51.34 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 105 VDAIVGAAASGMSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARADD 184
Cdd:cd06376 108 VVGVIGASASSVSIMVANILRLFQIPQISYASTAPELSDDRRYDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGN 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1752498383 185 YGRGLMEATRKTLEERGlTVTLAET----YDPKATNFDQVAQQIENSrPDAAVVIAF 237
Cdd:cd06376 188 YGEKGVESFVQISREAG-GVCIAQSekipRERRTGDFDKIIKRLLET-PNARAVVIF 242
|
|
| PBP1_YraM_LppC_lipoprotein-like |
cd06339 |
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup ... |
43-224 |
6.03e-07 |
|
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup includes periplasmic binding component of lipoprotein LppC, an immunodominant antigen, whose molecular function is not characterized. Members of this subgroup are predicted to be involved in transport of lipid compounds, and they are sequence similar to the family of ABC-type hydrophobic amino acid transporters (HAAT).
Pssm-ID: 380562 [Multi-domain] Cd Length: 331 Bit Score: 51.12 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 43 LPETGQLAYLGppqiESLKFAIQkinDAGGVLGKAVPNVVSSDEAGQEAvAAQSADRVLAAGVDAIVG----AAASgmsl 118
Cdd:cd06339 6 LPLSGPYAAAG----QAIRDGIE---LALFDAGGSRPELRVYDTGGPEG-AAAAYQQAVAEGADLIIGpllkSSVA---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 119 AFIDRVTGAGVVQCSGSNTAptfTDYEDDG-FYFRTVPSDalQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTL 197
Cdd:cd06339 74 ALAAAAQALGVPVLALNNDE---SATAGPGlFQFGLSPED--EARQAARYAVQQGLRRFAVLAPDNAYGQRVANAFREAW 148
|
170 180
....*....|....*....|....*..
gi 1752498383 198 EERGLTVTLAETYDPKATNFDQVAQQI 224
Cdd:cd06339 149 QALGGTVVAVESYDPDETDFSAAIRRL 175
|
|
| PBP1_GABAb_receptor_plant |
cd19990 |
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ... |
59-384 |
2.50e-06 |
|
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: 49.15 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 59 SLKFAIQKINDAGGVLG-KAVPNVVSSdeAGQEAVAAQSADRVL-AAGVDAIVGAAASGMSLAFIDRVTGAGVVQCSGSN 136
Cdd:cd19990 19 AIEMAVSDFNSDSSSYGtKLVLHVRDS--KGDPLQAASAALDLIkNKKVEAIIGPQTSEEASFVAELGNKAQVPIISFSA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 137 TAPTFTDYEDDGFyFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLTVTLAETYDPKATN 216
Cdd:cd19990 97 TSPTLSSLRWPFF-IRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEVGSRIEYRVALPPSSPE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 217 fDQVAQQI-----ENSR-------PDAAVVIaFEEgAQILqGMIESG---IGPDRIGVYgadglrseeLPSLvapgQPER 281
Cdd:cd19990 176 -DSIEEELiklksMQSRvfvvhmsSLLASRL-FQE-AKKL-GMMEKGyvwIVTDGITNL---------LDSL----DSST 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 282 LSGMKG---TAPASAENEQYvkdlKEFAPKLK---------ELQFAPQVF-----DCATTIALAAEKAesddprdyvkem 344
Cdd:cd19990 239 ISSMQGvigIKTYIPESSEF----QDFKARFRkkfrseypeEENAEPNIYalrayDAIWALAHAVEKL------------ 302
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1752498383 345 ngiTKDGEKCNSFAACKELLADGRDIDYEGVSGPLNFTDK 384
Cdd:cd19990 303 ---NSSGGNISVSDSGKKLLEEILSTKFKGLSGEVQFVDG 339
|
|
| PBP1_mGluR_groupII |
cd06375 |
ligand binding domain of the group II metabotropic glutamate receptor; Ligand binding domain ... |
53-237 |
6.73e-06 |
|
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: 47.89 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 53 GPPQIESLKFAIQKIND-----AGGVLGKAVPNVVSSD----EAGQEAVAA--------------------QSADRVLAA 103
Cdd:cd06375 33 GIQRLEAMLFAIDRINRdphllPGVRLGVHILDTCSRDtyalEQSLEFVRAsltkvddseymcpddgsyaiQEDSPLPIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 104 GVdaiVGAAASGMSLAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHDRVALVARAD 183
Cdd:cd06375 113 GV---IGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEG 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1752498383 184 DYGRGLMEATRKTLEERGLTVTLAE----TYDPKAtnFDQVAQQIENsRPDAAVVIAF 237
Cdd:cd06375 190 DYGETGIEAFEQEARLRNICIATAEkvgrSADRKS--FDGVIRELLQ-KPNARVVVLF 244
|
|
| Peripla_BP_5 |
pfam13433 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
45-348 |
1.24e-05 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins.
Pssm-ID: 463875 [Multi-domain] Cd Length: 363 Bit Score: 46.82 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 45 ETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVPNVVsSDEAGQEAVAAQSADRVLAA-GVDAIVGAAASgmslafidr 123
Cdd:pfam13433 9 LTGTMAISERSLKDATLMAIEEINAAGGVLGRKIEPVV-VDPASDWPLFAEKARKLIDQdKVRVVFGCWTS--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 124 VTGAGVVQCSGSNTAPTF--TDYE-----DDGFYFRTVPSdalQGPI-LADVVRDDGHDRVALVARADDYGRGLMEATRK 195
Cdd:pfam13433 79 ASRKAVLPVFERHNGLLFypVQYEgfessRNIFYTGAAPN---QQAIpAVDYLLSELGKRFFLVGSDYVYPRTTNRILRA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 196 TLEERGLTVtLAETYDP-KATNFDQVAQQIENSRPDAAV-VIAFEEGAQILQGMIESGIGPDRIGVYgADGLRSEELPSL 273
Cdd:pfam13433 156 YLKAKGGEV-VGERYLPlGSSDWQSIVAKIKAAGPDVVFsTINGDSNVAFYRALRAAGITAEDIPVM-SFSVAEEELAGM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 274 vapgQPERLSGMKGTAP-----ASAENEQYVKDLKEFAPKlKELQFAPQvfdCATTIAL-----AAEKAESDDPRDYVKE 343
Cdd:pfam13433 234 ----GPEPLVGHLAAWNyfqslDTPENKAFVAAFKARYGD-DRVTNDPM---EAAYIGVhlwaqAVEKAGTDDPDAVRQA 305
|
....*
gi 1752498383 344 MNGIT 348
Cdd:pfam13433 306 MLGQE 310
|
|
| PBP1_ABC_ligand_binding-like |
cd06334 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
39-234 |
2.36e-05 |
|
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: 380557 [Multi-domain] Cd Length: 360 Bit Score: 46.08 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 39 FGYVLPETGQLAYLGPPQIESLKFAIQKINDAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAaSGMS 117
Cdd:cd06334 2 IGLLTDLTGPTADVGKPYAQGVRDYLNYVNEEGGINGVKI-ELEECDTGYKVPRAVACYKRLKAQdGVVAILGWG-TGDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 118 LAFIDRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQGPILADVVRDDGHD-----RVALVARADDYGRGLMEA 192
Cdd:cd06334 80 EALAPRVAKDKIPYISASYGRSLADDGKVFPYNFFVGATYSSQARALLKYIAQEWGGklkgpKVAFVYHDSPFGREPIPA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1752498383 193 TRKTLEERGLTVTLAETYDPKATnfDQVAQ--QIENSRPDAAVV 234
Cdd:cd06334 160 LKAYAKELGFEVVAEQVPSPGAL--DATAQwlRIRRAGPDYVII 201
|
|
| PBP1_SBP-like |
cd20378 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
38-351 |
6.42e-05 |
|
periplasmic substrate-binding domain of active transport proteins; Periplasmic substrate-binding domain of active transport proteins found in bacteria and Archaea. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.
Pssm-ID: 380668 [Multi-domain] Cd Length: 357 Bit Score: 44.64 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 38 QFGYVLPETGQLAYLGPPQIESLKFAIQKindAGGVLGKAVpNVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAASGM 116
Cdd:cd20378 1 TLGGLVSMSGAFAAAGKLADRGMRLAVEE---YGGALGRPL-KYITRDTEGKPGTGVRKVQEAIAQdGARFFIGGTLSSV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 117 SLAFIDRVTGAGVVQCSGSNT----------------APTFTDYEddgfyfRTVPSDALQGP-------ILADVVrddgh 173
Cdd:cd20378 77 ALAVSEEAEKAGGVYITSGGAdeitgsrcnrstfrwsVPTYGAIR------QTVRPVIKAMPkakrwytITPQYV----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 174 drvalvaraddYGRGLMEATRKTLEERGLTVTLAETYDPKATNFDQVAQQIENSRPDAAVVIAFeeGAQ---ILQGMIES 250
Cdd:cd20378 146 -----------FGESLLKNAKEVLKEKGIEHVGNSYHSLGEREFSGYLTKAMAARPDVLLILNF--GSQavdALRQAVSF 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 251 GIGPdRIGVYGADGLRSEELPSLvapgQPERLSGM--------KGTAPAsaeNEQYVKDLKEfapKLKELQ--FAPQVFD 320
Cdd:cd20378 213 GLKR-KMKILVAWSSGLDQFQEL----GPDICEGVyfgaqywhDVDTPA---NKALVKVYQA---KFKETPsyALAAGYA 281
|
330 340 350
....*....|....*....|....*....|.
gi 1752498383 321 CATTIALAAEKAESDDPRDYVKEMNGITKDG 351
Cdd:cd20378 282 CTRMLLDAIDKAGSTDPAAVIKALEGLKYDG 312
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
172-276 |
6.54e-04 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 40.01 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 172 GHDRVALVA----RADDYGRGLMEATRKTLEERGLTV--TLAETYDPKATNFDQVAQQIENSRPDAAVVIAFEEGAQILQ 245
Cdd:pfam13377 6 GHRRIALIGpegdRDDPYSDLRERGFREAARELGLDVepTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEVALGVLQ 85
|
90 100 110
....*....|....*....|....*....|..
gi 1752498383 246 GMIESGIG-PDRIGVYGADGlrsEELPSLVAP 276
Cdd:pfam13377 86 ALREAGLRvPEDLSVIGFDD---SPLAALVSP 114
|
|
| PBP1_SBP-like |
cd06327 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
53-237 |
9.19e-04 |
|
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs); Periplasmic substrate-binding domain of active transport proteins found in gram-negative, gram-positive 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: 380550 [Multi-domain] Cd Length: 336 Bit Score: 41.02 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 53 GPPQIESLKFAIqkiNDAGG-VLGKAVpNVVSSDEAGQEAVAAQSADRVLAA-GVDAIVGAAASGMSLAF---------I 121
Cdd:cd06327 17 GPGSVEAAKMAV---EDFGGkVLGRPI-EVVSADHQNKPDVASAIAREWYDRdGVDAIVDVPNSAVALAVqklakekkkI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 122 DRVTGAGVVQCSGSNTAPTFTDYEDDGFYFRTVPSDALQgpiladvvrDDGHDRVALVarADDY--GRGLMEATRKTLEE 199
Cdd:cd06327 93 AIVTGAGSSDLTGKACSPYGVHWAYDTYALARGTVKALV---------KQGGKSWFFI--TADYafGHSLEADATAAVKA 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1752498383 200 RGLTVTLAETYDPKATNFDQVAQQIENSRPDaavVIAF 237
Cdd:cd06327 162 AGGKVVGSVRHPLGTTDFSSFLLQAQASGAD---VIAL 196
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
81-204 |
3.33e-03 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 39.13 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 81 VVSSDEAGQEAVAAQSADRVLAAGVDAIVGAAASGMSLaFIDRVTGAGV-----VQCSGSNTAPTFTdyeddgfyfrtvP 155
Cdd:cd06285 32 VLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAP-DLQELAARGVpvvlvDRRIGDTALPSVT------------V 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1752498383 156 SDALQGPILADVVRDDGHDRVALVARADDY--GRGLMEATRKTLEERGLTV 204
Cdd:cd06285 99 DNELGGRLATRHLLELGHRRIAVVAGPLNAstGRDRLRGYRRALAEAGLPV 149
|
|
| PBP1_taste_receptor |
cd06363 |
ligand-binding domain of the T1R taste receptor; Ligand-binding domain of the T1R taste ... |
150-244 |
3.77e-03 |
|
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: 39.21 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752498383 150 YFRTVPSDALQGPILADVVRDDGHDRVALVARADDYGRGLMEATRKTLEERGLTVT---LAETYDPKATNFDQVAQQIEN 226
Cdd:cd06363 154 FLRTVPSDKYQVEAMVQLLQEFGWNWVAFLGSDDEYGQDGLQLFSEKAANTGICVAyqgLIPTDTDPKPKYQDILKKINQ 233
|
90
....*....|....*...
gi 1752498383 227 SRPDAAVVIAFEEGAQIL 244
Cdd:cd06363 234 TKVNVVVVFAPKQAAKAF 251
|
|
| |
