|
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 ... |
71-416 |
1.43e-89 |
|
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: 274.83 E-value: 1.43e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMC--PNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVS 147
Cdd:cd06346 2 IGALLPLTGPLASLGPPMLAAAELAVEEINAAGgvLGKKVELVVEDSQTDPTAAVDAARKLVDVeGVPAIVGAASSGVTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLL--GIPGDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESN 225
Cdd:cd06346 82 AVASVAVPNGVVQISPSSTSPALttLEDKGYVFRTAPSDALQGVVLAQLAAERGFKKVAVIYVNNDYGQGLADAFKKAFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYDPDpkaFPTAVPEAIRKLSGalgqpGSDAaIIFVTFEDDGIAAIQAAASDPvLSKVRWIGTDGIAySD 305
Cdd:cd06346 162 ALGGTVTASVPYEPG---QTSYRAELAQAAAG-----GPDA-LVLIGYPEDGATILREALELG-LDFTPWIGTDGLK-SD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 306 ALIKQVGKEmAAAKMLGTIAAPDPNdPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIacqlgtddsdkvkatleqw 385
Cdd:cd06346 231 DLVEAAGAE-ALEGMLGTAPGSPGS-PAYEAFAAAYKAEYGDDPGPFAANAYDAVMLLALA------------------- 289
|
330 340 350
....*....|....*....|....*....|.
gi 18161589 386 grqgtYQGVTGKVYLDEAGDRAyPNYVIWGV 416
Cdd:cd06346 290 -----YEGASGPIDFDENGDVA-GPYEIWKV 314
|
|
| ANF_receptor |
pfam01094 |
Receptor family ligand binding region; This family includes extracellular ligand binding ... |
88-416 |
1.90e-71 |
|
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: 229.19 E-value: 1.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 88 VKNAVELAVEDANKM---CPNIKFELLVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSGEVSAVKSFADQNKIIIFSPS 164
Cdd:pfam01094 2 VLLAVRLAVEDINADpglLPGTKLEYIILDTCCDPSLALAAALDLLKGEVVAIIGPSCSSVASAVASLANEWKVPLISYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 165 STSPLLGIPGDWVY--RIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKLGINIVASQGYDPdpk 242
Cdd:pfam01094 82 STSPALSDLNRYPTflRTTPSDTSQADAIVDILKHFGWKRVALIYSDDDYGESGLQALEDALRERGIRVAYKAVIPP--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 243 afPTAVPEAIRKLSGALGQpGSDAAIIFVTFEDdgIAAI-QAAASDPVLSK-VRWIGTDGIAYSDALIKQVGKEMAAAkm 320
Cdd:pfam01094 159 --AQDDDEIARKLLKEVKS-RARVIVVCCSSET--ARRLlKAARELGMMGEgYVWIATDGLTTSLVILNPSTLEAAGG-- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 321 LGTIAAPDPNDPKYQEFKQR-------YKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKV----------KATLE 383
Cdd:pfam01094 232 VLGFRLHPPDSPEFSEFFWEklsdekeLYENLGGLPVSYGALAYDAVYLLAHALHNLLRDDKPGRacgalgpwngGQKLL 311
|
330 340 350
....*....|....*....|....*....|...
gi 18161589 384 QWGRQGTYQGVTGKVYLDEAGDRAYPNYVIWGV 416
Cdd:pfam01094 312 RYLKNVNFTGLTGNVQFDENGDRINPDYDILNL 344
|
|
| PBP1_ABC_LIVBP-like |
cd06342 |
type 1 periplasmic ligand-binding domain of ABC (Atpase Binding Cassette)-type active ... |
71-416 |
1.25e-66 |
|
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: 216.24 E-value: 1.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANK--MCPNIKFELLVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSGEVSA 148
Cdd:cd06342 2 IGVAGPLTGPNAALGQDIRNGAELAVDEINAkgGGLGFKIELVAQDDACDPAQAVAAAQKLVADGVVAVIGHYNSGAAIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 149 VKSFADQNKIIIFSPSSTSPLLGIPGDW-VYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNAITNESNK 226
Cdd:cd06342 82 AAPIYAEAGIPMISPSATNPKLTEQGYKnFFRVVGTDDQQGPAAADyAAKTLKAKRVAVIHDGTAYGKGLADAFKKALKA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 227 LGINIVASQGYDPDPKAFpTAVPEAIRKlsgalgqpgSDAAIIFVTFEDDGIAAIQAAASDpVLSKVRWIGTDGIaYSDA 306
Cdd:cd06342 162 LGGTVVGREGITPGTTDF-SALLTKIKA---------ANPDAVYFGGYYPEAGLLLRQLRE-AGLKAPFMGGDGI-VSPD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 307 LIKQVGKemAAAKMLGTIAAPDPND-PKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKVKATLeqw 385
Cdd:cd06342 230 FIKAAGD--AAEGVYATTPGAPPEKlPAAKAFLKAYKAKFGEPPGAYAAYAYDAAQVLLAAIEKAGSTDRAAVAAAL--- 304
|
330 340 350
....*....|....*....|....*....|.
gi 18161589 386 gRQGTYQGVTGKVYLDEAGDRAYPNYVIWGV 416
Cdd:cd06342 305 -RATDFDGVTGTISFDAKGDLTGPAFTVYQV 334
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
66-427 |
2.56e-60 |
|
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: 199.39 E-value: 2.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 66 KKTVYIGAALPLTGGSQSYGIGVKNAVELAVEDANKMC--PNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMT 142
Cdd:COG0683 1 ADPIKIGVLLPLTGPYAALGQPIKNGAELAVEEINAAGgvLGRKIELVVEDDASDPDTAVAAARKLIDQdKVDAIVGPLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 143 SGEVSAVKSFADQNKIIIFSPSSTSPLL--GIPGDWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNA 219
Cdd:COG0683 81 SGVALAVAPVAEEAGVPLISPSATAPALtgPECSPYVFRTAPSDAQQAEALADyLAKKLGAKKVALLYDDYAYGQGLAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 220 ITNESNKLGINIVASQGYDPDPKAFpTAVPEAIRKlSGAlgqpgsdAAIIFVTFEDDGIAAIqaaasdpvlskvrwigtd 299
Cdd:COG0683 161 FKAALKAAGGEVVGEEYYPPGTTDF-SAQLTKIKA-AGP-------DAVFLAGYGGDAALFI------------------ 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 300 giaysdalikqvgKEMAAAKMLGTIAapdpndpkyQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKVK 379
Cdd:COG0683 214 -------------KQAREAGLKGPLN---------KAFVKAYKAKYGREPSSYAAAGYDAALLLAEAIEKAGSTDREAVR 271
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 18161589 380 ATLEqwgrQGTYQGVTGKVYLDEAGDRAYPNYViwGVALEGGQPKYVD 427
Cdd:COG0683 272 DALE----GLKFDGVTGPITFDPDGQGVQPVYI--VQVKADGKFVVVE 313
|
|
| PBP1_ABC_ligand_binding-like |
cd19984 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-363 |
4.21e-60 |
|
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: 198.21 E-value: 4.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNI--KFELLVEDTGTNPQQALQKVQTL-YAKGARLIVGPMTSGEVS 147
Cdd:cd19984 2 IGVILPLTGDAASYGEDMKNGIELAVEEINAAGGINgkKIELIYEDSKCDPKKAVSAANKLiNVDKVKAIIGGVCSSETL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKL 227
Cdd:cd19984 82 AIAPIAEQNKVVLISPGASSPEITKAGDYIFRNYPSDAYQGKVLAEFAYNKLYKKVAILYENNDYGVGLKDVFKKEFEEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 228 GINIVASQGYDPDPKAFPTavpeAIRKLSGAlgqpgsDAAIIFVTFEDDGIAAI--QAAASDpvlSKVRWIGTDGIaYSD 305
Cdd:cd19984 162 GGKIVASESFEQGETDFRT----QLTKIKAA------NPDAIFLPGYPKEGGLIlkQAKELG---IKAPILGSDGF-EDP 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18161589 306 ALIKQVGKemAAAKMLGTIAAPDP-NDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMML 363
Cdd:cd19984 228 ELLEIAGE--AAEGVIFTYPAFDDsSEKKQKFFFYRYKEKYGKEPDIYAALAYDAVMIL 284
|
|
| PBP1_ABC_transporter_LIVBP-like |
cd06268 |
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ... |
71-363 |
2.93e-54 |
|
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: 182.91 E-value: 2.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVS 147
Cdd:cd06268 2 IGVVVPLTGPYADYGEEILRGVALAVEEINAAggINGRKLELVIADDQGDPETAVAVARKLVDDdKVLAVVGHYSSSVTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGI-PGDWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNAITNESN 225
Cdd:cd06268 82 AAAPIYQEAGIPLISPGSTAPELTEgGGPYVFRTVPSDAMQAAALADyLAKKLKGKKVAILYDDYDYGKSLADAFKKALK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYDPDPKAFPTAVPEAIRKlsgalgqpGSDaAIIFVTFEDDGIAAIQAAASDPVlsKVRWIGTDGiAYSD 305
Cdd:cd06268 162 ALGGEIVAEEDFPLGTTDFSAQLTKIKAA--------GPD-VLFLAGYGADAANALKQARELGL--KLPILGGDG-LYSP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 18161589 306 ALIKQVGKemAAAKMLGTIA-APDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMML 363
Cdd:cd06268 230 ELLKLGGE--AAEGVVVAVPwHPDSPDPPKQAFVKAYKKKYGGPPSWRAATAYDATQAL 286
|
|
| PBP1_ABC_LivK_ligand_binding-like |
cd06347 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-405 |
2.36e-53 |
|
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: 181.59 E-value: 2.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVS 147
Cdd:cd06347 2 IGVIGPLTGEAAAYGQPALNGAELAVDEINAAggILGKKIELIVYDNKSDPTEAANAAQKLIDEdKVVAIIGPVTSSIAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADL-LKTLGVKRAVIIY-RNDAWGVGLRNAITNESN 225
Cdd:cd06347 82 AAAPIAQKAKIPMITPSATNPLVTKGGDYIFRACFTDPFQGAALAKFaYEELGAKKAAVLYdVSSDYSKGLAKAFKEAFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYDPDPKAFpTAVPEAIRKlsgalgqpgSDAAIIFVT--FEDDGIAAIQAAASDPvlsKVRWIGTDGiAY 303
Cdd:cd06347 162 KLGGEIVAEETYTSGDTDF-SAQLTKIKA---------ANPDVIFLPgyYEEAALIIKQARELGI---TAPILGGDG-WD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 304 SDALIkqvgkEMAAAKMLGTI----AAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKVK 379
Cdd:cd06347 228 SPELL-----ELGGDAVEGVYftthFSPDDPSPEVQEFVKAYKAKYGEPPNAFAALGYDAVMLLADAIKRAGSTDPEAIR 302
|
330 340
....*....|....*....|....*.
gi 18161589 380 ATLEQwgrQGTYQGVTGKVYLDEAGD 405
Cdd:cd06347 303 DALAK---TKDFEGVTGTITFDPNGN 325
|
|
| PBP1_ABC_HAAT-like |
cd06349 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
70-413 |
3.47e-46 |
|
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: 162.74 E-value: 3.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQAlqkvqtlyAKGARLIV--------- 138
Cdd:cd06349 1 KIGVSGPLTGDNAEYGQQFKNGVELAVDEINAAggVNGRKLELVVYDDQGDPKEA--------VNIAQKFVsddkvvavi 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 139 GPMTSGEVSAVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLL-KTLGVKRAVIIYRNDAWGVGLR 217
Cdd:cd06349 73 GDFSSSCSMAAAPIYEEAGLVQISPTASHPDFTKGGDYVFRNSPTQAVEAPFLADYAvKKLGAKKIAIIYLNTDWGVSAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 218 NAITNESNKLGINIVASQGYDPDPKAFpTAVpeaIRKLSGAlgqpGSDAAIIFVTFEDDGIAAIQAAASDpvlSKVRWIG 297
Cdd:cd06349 153 DAFKKAAKALGGEIVATEAYLPGTKDF-SAQ---ITKIKNA----NPDAIYLAAYYNDAALIAKQARQLG---WDVQIFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 298 TDGiAYSDALIKQVGkEMAAAKMLGTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDdsdk 377
Cdd:cd06349 222 SSS-LYSPEFIELAG-DAAEGVYLSSPFFPESPDPEVKEFVKAYKAKYGEDPDDFAARAYDAVNILAEAIEKAGTD---- 295
|
330 340 350
....*....|....*....|....*....|....*..
gi 18161589 378 vKATLEQWGRQGT-YQGVTGKVYLDEAGDRAYPNYVI 413
Cdd:cd06349 296 -REAIRDALANIKdFSGLTGTITFDENGDVLKSLTIL 331
|
|
| PBP1_ABC_HAAT-like |
cd06348 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-413 |
1.11e-45 |
|
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: 161.63 E-value: 1.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMC--PNIKFELLVEDTGTNPQQALQKVQTLYAKGARL-IVGPMTSGEVS 147
Cdd:cd06348 2 IGVALSLTGPGALYGQSQKNGAQLAVEEINAAGgvGGVKIELIVEDTAGDPEQAINAFQKLINQDKVLaILGPTLSSEAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPllGIP--GDWVYRI-VPTDFAQAAAIADLLKTLGVKRAVIIY-RNDAWGVGLRNAITNE 223
Cdd:cd06348 82 AADPIAQQAKVPVVGISNTAP--GITdiGPYIFRNsLPEDKVIPPTVKAAKKKYGIKKVAVLYdQDDAFTVSGTKVFPAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 224 SNKLGINIVASQGY---DPDPKAFPTAV----PEAIrkLSGALGQpgsDAAIIFVTFEDDGIaaiqaaasdpvlsKVRWI 296
Cdd:cd06348 160 LKKNGVEVLDTETFqtgDTDFSAQLTKIkalnPDAI--VISALAQ---EGALIVKQARELGL-------------KGPIV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 297 GTDGIaYSDALIKQVGKemAAAkmlGTIAA----PDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLG- 371
Cdd:cd06348 222 GGNGF-NSPDLIKLAGK--AAE---GVIVGsawsPDNPDPKNQAFVAAYKEKYGKEPDQFAAQAYDAAYILAEAIKKAGs 295
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 18161589 372 TDDSDKVKATLEQWGRQGTYQGVTGKVYLDEAGDRAYPNYVI 413
Cdd:cd06348 296 TTDRADLRDALARILIAKDFEGPLGPFSFDADRDGIQPPVVL 337
|
|
| PBP1_ABC_RPA1789-like |
cd06333 |
type 1 periplasmic binding-protein component (CouP) of an ABC system (CouPSTU; RPA1789, ... |
71-396 |
6.33e-45 |
|
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: 159.64 E-value: 6.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMcPNI---KFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEV 146
Cdd:cd06333 2 IGAILSLTGPAASLGIPERNAVELLVEQINAA-GGIngrKLELIVYDDESDPTKAVTNARKLIEEdKVDAIIGPSTTGES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 147 SAVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNK 226
Cdd:cd06333 81 LAVAPIAEEAKVPLISLAGAAAIVEPVRKWVFKTPQSDSLVAEAILDYMKKKGIKKVALLGDSDAYGQSGRAALKKLAPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 227 LGINIVASQGYDPDPKAFPTAV-------PEAIrkLSGALGQPgsdAAIIFVTFEDDGIaaiqaaasdpvlsKVRWIGTD 299
Cdd:cd06333 161 YGIEIVADERFARTDTDMTAQLtkiraakPDAV--LVWASGPP---AALVAKNLRQLGY-------------KGPIYQSH 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 300 GIAySDALIKQVGK-----EMAAAKML--GTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGT 372
Cdd:cd06333 223 GAA-NQDFIKLAGKaaegvILPAGKLLvaDQLPDSDPQKKVLLEFVKAYEAKYGEGPSTFAGHAYDALLLLVEAIEPAGG 301
|
330 340
....*....|....*....|....
gi 18161589 373 DDSDKVKATLEQwgrQGTYQGVTG 396
Cdd:cd06333 302 TDRAALRDALEN---TKGLVGVTG 322
|
|
| Peripla_BP_6 |
pfam13458 |
Periplasmic binding protein; This family includes a diverse range of periplasmic binding ... |
68-413 |
1.23e-44 |
|
Periplasmic binding protein; This family includes a diverse range of periplasmic binding proteins.
Pssm-ID: 433225 [Multi-domain] Cd Length: 342 Bit Score: 158.98 E-value: 1.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 68 TVYIGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSG 144
Cdd:pfam13458 1 PIKIGVLTPLSGPYASSGKSSRAGARAAIEEINAAggVNGRKIELVVADDQGDPDVAAAAARRLVDQdGVDAIVGGVSSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 145 EVSAVKSFADQNKIIIFSPSSTSPllGIPGDWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNAITNE 223
Cdd:pfam13458 81 VALAVAEVLAKKGVPVIGPAALTG--EKCSPYVFSLGPTYSAQATALGRyLAKELGGKKVALIGADYAFGRALAAAAKAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 224 SNKLGINIVASQGYDPDPKAFPTAVPEAirKLSGAlgqpgsdAAIIFVTFEDDGIAAI-QAAASDPVLSKVRWIGTdgiA 302
Cdd:pfam13458 159 AKAAGGEVVGEVRYPLGTTDFSSQVLQI--KASGA-------DAVLLANAGADTVNLLkQAREAGLDAKGIKLVGL---G 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 303 YSDALIKQVGKEMAAAKMLGTIAAPDPNDPKYQEFKQRYKAKYGKDPV-AYDPYGYDAAMMLMQIACQLGTDDSDKVKAT 381
Cdd:pfam13458 227 GDEPDLKALGGDAAEGVYATVPFFPDLDNPATRAFVAAFAAKYGEAPPtQFAAGGYIAADLLLAALEAAGSPTREAVIAA 306
|
330 340 350
....*....|....*....|....*....|..
gi 18161589 382 LeqwgRQGTYQGVTGKVYLDEAGDRAYPNYVI 413
Cdd:pfam13458 307 L----RALPYDGPFGPVGFRAEDHQAVHCMYL 334
|
|
| PBP1_YraM_LppC_lipoprotein-like |
cd06339 |
periplasmic binding component of lipoprotein LppC, an immunodominant antigen; This subgroup ... |
71-404 |
1.53e-41 |
|
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: 150.11 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANkmcpNIKFELLVEDTGtNPQQALQKVQTLYAKGARLIVGPMTSGEVSAVK 150
Cdd:cd06339 2 IALLLPLSGPYAAAGQAIRDGIELALFDAG----GSRPELRVYDTG-GPEGAAAAYQQAVAEGADLIIGPLLKSSVAALA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 151 SFADQNKIIIFSPSSTSPLlgIPGDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKLGIN 230
Cdd:cd06339 77 AAAQALGVPVLALNNDESA--TAGPGLFQFGLSPEDEARQAARYAVQQGLRRFAVLAPDNAYGQRVANAFREAWQALGGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 231 IVASQGYDPDPKAFPTAV--------------PEAIRKLSGALGQPGSDAAIIFVTFEDDGIAAIQAAASDpvLSKVRWI 296
Cdd:cd06339 155 VVAVESYDPDETDFSAAIrrllgvdqsearirQLGELLEFEPRRRQDFDAIFLPAGPEQARLIAPQLAFYG--AGDVPLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 297 GTDGIaYSDALIKQVGKEMAAAkmlgTIAAPDPNDPKyQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIAcQLGTDDSd 376
Cdd:cd06339 233 GTSLW-YSGKLNLLRDPDLNGA----WFADPPWLLSP-RAFPLRYRLAYGWPPPRLAALGYDAYRLAARLA-RLGGGLT- 304
|
330 340
....*....|....*....|....*...
gi 18161589 377 kvkatleqwgRQGTYQGVTGKVYLDEAG 404
Cdd:cd06339 305 ----------PGAGFSGLTGLLRLDPDG 322
|
|
| PBP1_ABC_HAAT-like |
cd19986 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
70-363 |
6.25e-40 |
|
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: 145.08 E-value: 6.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYA-KGARLIVGPMTSGEV 146
Cdd:cd19986 1 KIGVVAPLTGPAALNGEYQKNGAQLALEEINAAggVLGRPLELVVEDDQGTNTGAVNAVNKLISdDKVVAVIGPHYSTQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 147 SAVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLLK-TLGVKRAVIIYRNDAWGVGLRNAITNESN 225
Cdd:cd19986 81 LAVSPLVKEAKIPVITGGTSPKLTEQGNPYMFRIRPSDSVSAKALAKYAVeELGAKKIAILYDNDDFGTGGADVVTAALK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYDPDPKAFpTAVPEAIRKlSGAlgqpgsDAAIIFVTFEDDGIAAIQAAASDpvlSKVRWIGTDGIAYSD 305
Cdd:cd19986 161 ALGLEPVAVESYNTGDKDF-TAQLLKLKN-SGA------DVIIAWGHDAEAALIARQIRQLG---LDVPVIGSSSFATPT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18161589 306 ALikqvgkEMAAAKMLGTIAA----PDPNDPKYQEFKQRYKAKYGKDPvayDPYG---YDAAMML 363
Cdd:cd19986 230 VL------LLAGEALEGIYSVtdfvPSDPDPKVQAFVKKYKAKYGEDP---DLYSawyYDAMYLL 285
|
|
| PBP1_ABC_ligand_binding-like |
cd06340 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
71-383 |
6.71e-40 |
|
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: 146.55 E-value: 6.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDAN-----KMCPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSG 144
Cdd:cd06340 2 IGVLYPLSGPLALIGQEAKRGAELAVDEINaaggiKSLGGAKIELVVADTQSDPEVAASEAERLITQeGVVAIIGAYSSS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 145 EVSAVKSFADQNKIIIFSPSSTSPLLGIPG-DWVYRIVPTDFAQAAAIADLLKTL------GVKRAVIIYRNDAWGVGLR 217
Cdd:cd06340 82 VTLAASQVAERYGVPFVTASAVADEITERGfKYVFRTAPTASQFAEDAVDFLKELakkkgkKIKKVAIIYEDSAFGTSVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 218 NAITNESNKLGINIVASQGYDPDpkaFPTAVPEaIRKLSGAlgqpGSDaAIIFVTFEDDGIAAIQAAASDPVLSKVrWIG 297
Cdd:cd06340 162 KGLKKAAKKAGLEVVLDEPYPAG---ATDLSSE-VLKLKAA----KPD-VVFATSYTNDAILLLRTMKELGFKPKA-IIG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 298 TDGIAYSDALIKQVGKemAAAKMLGTIAAPDP---NDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDD 374
Cdd:cd06340 232 VGGGYSDPEFLKALGK--DAEGVFSVVPWSPDlakKKPGAKEVNERYKKKYGEDMTGHAARAYTAAWVLADALERAGSTD 309
|
....*....
gi 18161589 375 SDKVKATLE 383
Cdd:cd06340 310 PEAIRAAAA 318
|
|
| PBP1_ABC_HAAT-like |
cd19983 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-363 |
7.43e-38 |
|
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: 139.64 E-value: 7.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMcPNI---KFELLVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSGEVS 147
Cdd:cd19983 2 IGFVGGLTGRYSDLGVQGRNGAQLAVEEINAA-GGIngrPVELIIRDDQQDPEAAKAADRELIAGGVVAIIGHMTSAMTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIY--RNDAWGVGLRNAITNES 224
Cdd:cd19983 81 AVLPVINEAKVLMISPTVSTPELSGKDDYFFRVTPTTRESAQALARyAYNRGGLRRVAVIYdlSNRAYSESWLDNFRSEF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 225 NKLGINIVASQGYDP-DPKAFPTAV-------PEAIRKLSGALgqpgsDAAIIfvtfeddgiaAIQAAASDPVLskvrWI 296
Cdd:cd19983 161 EALGGRIVAEIPFSSgADVDFSDLArrllaskPDGLLLVASAV-----DTAML----------AQQIRKLGSKI----PL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18161589 297 GTDGIAYSDALIKQVGKemAAAKMLGTIA-APDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMML 363
Cdd:cd19983 222 FSSAWAATEELLELGGK--AVEGMLFSQAyDRNSSNPRYLAFKEAYEERFGREPSFAAAYAYEAAMVL 287
|
|
| PBP1_ABC_ligand_binding-like |
cd19980 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-413 |
5.76e-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: 138.12 E-value: 5.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNI--KFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVS 147
Cdd:cd19980 2 IGVIAPLSGPVAALGQQVLNGAKLAVEEINAKGGVLgrKLELVVEDDKCPPAEGVAAAKKLITDdKVPAIIGAWCSSVTL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPG-DWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNAITNESN 225
Cdd:cd19980 82 AVMPVAERAKVPLVVEISSAPKITEGGnPYVFRLNPTNSMLAKAFAKyLADKGKPKKVAFLAENDDYGRGAAEAFKKALK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYDPDPKAFPTAvpeaIRKLSGAlgqpGSDAaIIFVTFEDDGIAAI-QAAASDPvlsKVRWIGTDGIAYS 304
Cdd:cd19980 162 AKGVKVVATEYFDQGQTDFTTQ----LTKLKAA----NPDA-IFVVAETEDGALILkQARELGL---KQQLVGTGGTTSP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 305 DaLIKQVGKemAAAKMLGT-IAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKVKATLE 383
Cdd:cd19980 230 D-LIKLAGD--AAEGVYGAsIYAPTADNPANKAFVAAYKKKYGEPPDKFAALGYDAVMVIAEAIKKAGSTDPEKIRAAAL 306
|
330 340 350
....*....|....*....|....*....|
gi 18161589 384 qwgRQGTYQGVTGKVYLDEAGDrAYPNYVI 413
Cdd:cd19980 307 ---KKVDYKGPGGTIKFDEKGQ-AHKNVVL 332
|
|
| PBP1_ABC_ligand_binding-like |
cd06345 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-415 |
1.02e-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, 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: 132.39 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTggsQSYGIGVKNAVELAVEDANKMCPN--IKFELLVEDTGTNPQQALQKVQTLYA-KGARLIVGPMTSGEVS 147
Cdd:cd06345 2 IGVLGPLS---APAGEAMERGAELAVEEINAAGGIlgRKVELVVADTQGKPEDGVAAAERLITeDKVDAIVGGFRSEVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLL--GIPGD-----WVYRIVPTDFAQAAAIADLLKT-----LGVKRAVIIYRNDAWGVG 215
Cdd:cd06345 79 AAMEVAAEYKVPFIVTGAASPAItkKVKKDyekykYVFRVGPNNSYLGATVAEFLKDllvekLGFKKVAILAEDAAWGRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 216 LRNAITNESNKLGINIVASQGYDPDPKAFpTAVPEAIRKLsgalgqpGSDAAIIFVTFEDDGIAAIQAAASDPvlsKVRW 295
Cdd:cd06345 159 IAEALKKLLPEAGLEVVGVERFPTGTTDF-TPILSKIKAS-------GADVIVTIFSGPGGILLVKQWAELGV---PAPL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 296 IGTDGIAYSDALIKQVGKEMAAAKMLGTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDS 375
Cdd:cd06345 228 VGINVPAQDPEFWENTGGAGEYEITLAFAAPKAKVTPKTKPFVDAYKKKYGEAPNYTAYTAYDAIYILAEAIERAGSTDP 307
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 18161589 376 DKVKATLEqwgrQGTYQGVTGKVYLDEAGDraYPNYVIWG 415
Cdd:cd06345 308 DALVKALE----KTDYEGVRGRIKFDKKDE--YPHDVKYG 341
|
|
| PBP1_ABC_HAAT-like |
cd19988 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
70-365 |
2.24e-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: 380643 [Multi-domain] Cd Length: 302 Bit Score: 130.09 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAKGARL-IVGPMTSGEV 146
Cdd:cd19988 1 KIGVFGPLSGDAAPYGQAMLQGAELAVEEINAAggILGIPIELVVEDDEGLPAASVSAAKKLIYQDKVWaIIGSINSSCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 147 SAVKSFADQNKIIIFSPSSTSPLL---GIPgdWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNAITN 222
Cdd:cd19988 81 LAAIRVALKAGVPQINPGSSAPTItesGNP--WVFRCTPDDRQQAYALVDyAFEKLKVTKIAVLYVNDDYGRGGIDAFKD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 223 ESNKLGINIVASQGYDPDPKAFpTAVPEAIRKlSGAlgqpgsDAAIIFVTFEDDGIAAIQAAASDpvlSKVRWIGTDGIA 302
Cdd:cd19988 159 AAKKYGIEVVVEESYNRGDKDF-SPQLEKIKD-SGA------QAIVMWGQYTEGALIAKQARELG---LKQPLFGSDGLV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18161589 303 ySDALIKQVGKemAAAKMLGTIA-APDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQ 365
Cdd:cd19988 228 -TPKFIELAGD--AAEGAIATTPfLPDSDDPKVSAFVEKYKKRYGEEPDVFAAQAYDAMNILAG 288
|
|
| PBP1_ABC_ligand_binding-like |
cd06336 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
71-384 |
2.02e-33 |
|
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: 128.51 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMC------PNIKFELLVEDTGTNPQQALQKVQTL-YAKGARLIVGPMTS 143
Cdd:cd06336 2 IGFLGPLSGPAAAWGLPMLRGLELAADEINAAGgikvggKKYKVEVVSYDDKYTPAEAVAAARRLvSQDGVKFIFGPGGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 144 GEVSAVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLL-KTLGVKRAVIIYRNDAWGVGLRNAITN 222
Cdd:cd06336 82 AIAAAVQPVTERNKVLLLTAAFSDPILGPDNPLLFRIPPTPYEYAPPFIKWLkKNGPIKTVALIAPNDATGKDWAAAFVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 223 ESNKLGINIVASQGYDPDPKAFPTAV-------PEAIrKLSGAlgqPGSDAAIIFVTFEDDGIAAIqaaasdpvlskvrw 295
Cdd:cd06336 162 AWKAAGGEVVAEEFYDRGTTDFYPVLtkilalkPDAL-DLGGS---SPGPAGLIIKQARELGFKGP-------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 296 IGTDGIAYSDALIKQVGKEmAAAKMLGTIAAPDP--NDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMML---MQIAcql 370
Cdd:cd06336 224 FVSEGGAKADEILKEVGGE-AAEGFIGVLPADDDpiASPGAKAFVERYKKKYGEPPNSESALFYDAAYILvkaMEKA--- 299
|
330
....*....|....*
gi 18161589 371 GT-DDSDKVKATLEQ 384
Cdd:cd06336 300 GTvDDTKKIRAALAM 314
|
|
| PBP1_ABC_ligand_binding-like |
cd06335 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
71-399 |
4.36e-33 |
|
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: 127.73 E-value: 4.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVS 147
Cdd:cd06335 2 IGVIGPLTGPSAELGESARRGVELAVEEINAAggILGRKIELVERDDEANPTKAVQNAQELIDKeKVVAIIGPTNSGVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPGD----WVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNE 223
Cdd:cd06335 82 ATIPILQEAKIPLIIPVATGTAITKPPAkprnYIFRVAASDTLQADFLVDYAVKKGFKKIAILHDTTGYGQGGLKDVEAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 224 SNKLGINIVASQGYDPDPKAFptaVPEAIR-KLSGAlgqpgsDAAIIFvtfeddGIAAIQAAASDPvLSKVRW----IGT 298
Cdd:cd06335 162 LKKRGITPVATESFKIGDTDM---TPQLLKaKDAGA------DVILVY------GLGPDLAQILKA-MEKLGWkvplVGS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 299 DGIaySDALIKQVGKEMAAAKMLGTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPY---GYDAAMMLMQIACQLGTDDS 375
Cdd:cd06335 226 WGL--SMPNFIELAGPLAEGTIMTQTFIEDYLTPRAKKFIDAYKKKYGTDRIPSPVSaaqGYDAVYLLAAAIKQAGSTDG 303
|
330 340
....*....|....*....|....
gi 18161589 376 DKVKATLEqwGRQGTYQGVTGKVY 399
Cdd:cd06335 304 KKIRAALE--NLKGYVGGVKTYNK 325
|
|
| PBP1_ABC_ligand_binding-like |
cd06343 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
66-384 |
3.29e-32 |
|
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: 125.37 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 66 KKTVYIGAALPLTGGSQSYGIGVKNAVELAVEDANKMcPNI---KFELLVEDTGTNPQQALQKVQTL-YAKGARLIVGPM 141
Cdd:cd06343 4 DDEIKIGTSLPLSGPAAAYGKPVRAGAAAYFDEVNAA-GGIngrKIELIVEDDGYDPARAVAAVRKLvEQDKVFAIVGGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 142 TSGEVSAVKSFADQNKIIIFSPSSTSPLLGIPG-DWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNA 219
Cdd:cd06343 83 GTPTNLAVRPYLNEAGVPQLFPATGASALSPPPkPYTFGVQPSYEDEGRILADyIVETLPAAKVAVLYQNDDFGKDGLEG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 220 ITNESNKLGINIVASQGYDPDPKAFpTAvpeAIRKLSGAlgqpGSDAAIIFVTFeDDGIAAIQAAASDPVlsKVRWIGTd 299
Cdd:cd06343 163 LKEALKAYGLEVVAEETYEPGDTDF-SS---QVLKLKAA----GADVVVLGTLP-KEAAAALKEAAKLGW--KPTFLGS- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 300 GIAYSDALIKQVGKEmAAAKMLGTIAAPDP---NDPKYQEFKQRYKAKYGKDPV-AYDPYGYDAAMMLMQIACQLGTD-D 374
Cdd:cd06343 231 SVSADPTTLAKAGGD-AAEGVYSASYLKDPtdaDDPAVKEFREAYKKYFPDDPPnAYALYGYAAAQVFVEALKRAGKDlT 309
|
330
....*....|
gi 18161589 375 SDKVKATLEQ 384
Cdd:cd06343 310 REGLIKALES 319
|
|
| PBP1_ABC_HAAT-like |
cd06344 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-405 |
3.41e-32 |
|
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: 125.03 E-value: 3.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYgigvKNAVELAVE--DANKMCPNIKFELLVEDTGTNPQQALQKVQTLYA-KGARLIVGPMTSGEVS 147
Cdd:cd06344 4 IGVAWPFAPDGDLF----LEGVELAVEeiNAAGGVLGRKIRLVEYDDEASVDKGLAIAQRFADnPDVVAVIGHRSSYVAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPG-DWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNK 226
Cdd:cd06344 80 PASIIYERAGLLMLSPGATAPKLTQHGfKYIFRNIPSDEDIARQLARYAARQGYKRIVIYYDDDSYGKGLANAFEEEARE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 227 LGINIVASQGYDPDPKAFptavPEAIRKLSGAlgqPGSDAaiIFVTFEDDGIAAIQAAASDpVLSKVRWIGTDGIaYSDA 306
Cdd:cd06344 160 LGITIVDRRSYSSDEEDF----RRLLSKWKAL---DFFDA--IFLAGSMPEGAEFIKQARE-LGIKVPIIGGDGL-DSPE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 307 LIKQVGKemAAAkmlGTIAA----PDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMML---MQIAcqlGTDDSDKVK 379
Cdd:cd06344 229 LIEIAGK--AAE---GVVVAtvfdPDDPRPEVRAFVEAFRKKYGREPDVWAAQGYDAVKLLaeaIEKA---GSTVPAKIA 300
|
330 340
....*....|....*....|....*.
gi 18161589 380 ATLEQwgrQGTYQGVTGKVYLDEAGD 405
Cdd:cd06344 301 SALRF---LENWEGVTGTYSFDANGD 323
|
|
| PBP1_ABC_ligand_binding-like |
cd06338 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
71-413 |
4.07e-32 |
|
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: 125.00 E-value: 4.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCP------NIKFELLVEDTGTNPQQAlqkvQTLYAK-----GARLIVG 139
Cdd:cd06338 2 IGASLSLTGPFAGEGKAQKRGYELWVEDVNAAGGvkgggkKRPVELVYYDDQSDPATA----VRLYEKlitedKVDLLLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 140 PMTSGEVSAVKSFADQNKIIIFSPSSTSPLLGIPG-DWVYRIVPTDFAQAAAIADLLKTLG--VKRAVIIYRNDAWGVGL 216
Cdd:cd06338 78 PYSSGLTLAAAPVAEKYGIPMIAGGAASDSIFERGyKYVFGVLPPASDYAKGLLDLLAELGpkPKTVAIVYEDDPFGKEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 217 RNAITNESNKLGINIVASQGYDPDPKAFpTAVPEAIRKlsgalgqpgSDAAIIFV-TFEDDGIAAIQAAASDPVLSKVRW 295
Cdd:cd06338 158 AEGAREAAKKAGLEVVYDESYPPGTTDF-SPLLTKVKA---------ANPDILLVgGYPPDAITLVRQMKELGYNPKAFF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 296 IGtdgIAYSDALIKQVGKEMAAAKMLGTIAAPDPNDPKY---QEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGT 372
Cdd:cd06338 228 LT---VGPAFPAFREALGKDAEGVLGPSQWEPSLPYKVFpgaKEFVKAYKEKFGEEPSYHAAAAYAAGQVLQQAIEKAGS 304
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 18161589 373 DDSDKVKATLeqwgRQGTYQGVTGKVYLDEAGDRAYPNYVI 413
Cdd:cd06338 305 LDPEKVRDAL----ASLDFDTVYGPIKFDETGLQIGKPMVV 341
|
|
| PBP1_ABC_ligand_binding-like |
cd19982 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
71-364 |
6.66e-32 |
|
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: 123.55 E-value: 6.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYA-KGARLIVGPMTSGEVS 147
Cdd:cd19982 2 IGAILSLTGPFAPFGEMFKNGYEMALEEINAAggIKGKKLELVIEDDQSKPQTALAAAEKLVSqDKVPLIVGGYSSGITL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPG-DWVYRIVPTDFAQAAAIADLLKTLG-VKRAVIIYRNDAWGVGLRNAITNESN 225
Cdd:cd19982 82 PVAAVAERQKIPLLVPTAADDDITKPGyKYVFRLNPPASIYAKALFDFFKELVkPKTIAILYENTAFGTSVAKAARRFAK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYD---PDPKAFPTAVPEAirklsgalgQPGsdaAIIFVTFEDDGIAAIQAAASDPVLSKVRWIGTDGIA 302
Cdd:cd19982 162 KRGIEVVADESYDkgaTDFKPLLNKVKAA---------NPD---VVYMVSYLNDAILLMRQAKELGLNPKLFAGGGAGFT 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18161589 303 YSDaLIKQVGKemaAAKMLGTIAA--PDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYdAAMMLM 364
Cdd:cd19982 230 IPE-FLKQAGP---LAEYVVTATLwsPDVKYPGAKEFYEKYKAKYGVEPSYHEAEAY-AALYVA 288
|
|
| PBP1_SBP-like |
cd19989 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
71-363 |
1.01e-30 |
|
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: 120.07 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMcPNI---KFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEV 146
Cdd:cd19989 2 IGVLTPLSGPYAALGEEARRGAQLAVEEINAA-GGIlgrPVELVVEDTEGKPATAVQKARKLVEQdGVDFLTGAVSSAVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 147 SAVKSFADQNKIIIFSPSSTSPLLGIP--GDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNES 224
Cdd:cd19989 81 LAVAPKAAELKVPYLVTVAADDELTGEncNRYTFRVNTSDRMIARALAPWLAENGGKKWYIVYADYAWGQSSAEAFKEAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 225 NKLGINIVASQGYDPDPKAFPTAVPEAIRklsgalgqpgSDA-AIIFVTFEDDGIAAIQAAASDPVLSKVRWIGTDGIAy 303
Cdd:cd19989 161 EELGGEVVGTLFAPLGTTDFSSYITQISD----------SGAdGLLLALAGSDAVNFLKQAGQFGLGKKYKIVGGILSI- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18161589 304 SDALIKQVGKEMAAAkmLGTIA-APDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMML 363
Cdd:cd19989 230 EPLALPALGDAAEGV--YGGVRyPPTLDTPANRAFVEAYEKEYGEAPDNFAGEAYEAMQAL 288
|
|
| PBP1_aromatic_compounds-like |
cd06332 |
type 1 periplasmic binding proteins of active transport systems predicted to be involved in ... |
71-412 |
1.10e-28 |
|
type 1 periplasmic binding proteins of active transport systems predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes; This group includes the type 1 periplasmic binding proteins of active transport systems that are predicted to be involved in transport of aromatic compounds such as 2-nitrobenzoic acid and alkylbenzenes; their substrate specificities are not well characterized, however. Members also exhibit close similarity to active transport systems for short chain amides and/or urea found in bacteria and archaea.
Pssm-ID: 380555 [Multi-domain] Cd Length: 336 Bit Score: 115.39 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVSAV 149
Cdd:cd06332 2 IGLLAPLTGPFAALGEDMVRGFELALEEVGGEVAGRKVELVVEDDAGDPDTAVTKARKLVEQdKVDVLIGPLSGDEGLAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 150 KSFADQNKIIIFSPSSTSPLLG--IPGDWVYRIVPTDFAQAAAIADLL-KTLGVKRAVIIYRNDAWGVGLRNAITNESNK 226
Cdd:cd06332 82 APYAKEPGVPFINPVAGADDLTqrAKAPNFFRTSFTGSQWSAPLGDYAyKELGYKKVATIGSDYAFGYEQAAGFKRGFEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 227 LGINIVAsqgydpdpKAFPtavPEAIRKLSGALGQPGSDAAIIFVTFE-DDGIAAIQAAASDPVLSKVRWIGTdGIAYSD 305
Cdd:cd06332 162 AGGEVVQ--------EIWV---PLGTTDFSPYIAQIPSADDAVFAFLGgADAVRFLKQYREFGLKDKIPLIGG-GTTVDE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 306 ALIKQVGKEmaaakMLGTIA----APDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKVKat 381
Cdd:cd06332 230 SVLPAMGDA-----ALGIISashyAEGLDNPENKKFVAAYKKKFGKLPSLYAAGGYDGAQAILEALEAVGGDVSDKQA-- 302
|
330 340 350
....*....|....*....|....*....|.
gi 18161589 382 LEQWGRQGTYQGVTGKVYLDEAGDRAYPNYV 412
Cdd:cd06332 303 LAAALRKVKFDSPRGPFSFDENRNPVQNVYI 333
|
|
| PBP1_ABC_HAAT-like |
cd19985 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
70-365 |
2.63e-28 |
|
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: 113.91 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSG-EV 146
Cdd:cd19985 1 HIAVVGPMSGKSASKGKSMLRGAELYIDQINAAggINGKKVKLDVFDDQNDPDAARKAAQIIVSDKALAVIGHYYSSaSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 147 SAVKSFADqNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLLK-TLGVKRAVIIYRNDAWGVGLRNAITNESN 225
Cdd:cd19985 81 AAGKIYKK-AGIPAITPSATADAVTRDNPWYFRVIFNDSLQGRFLANYAKkVLKKDKVSIIYEEDSYGKSLASVFEATAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYDPDPKAFPTAVPEAIRKLSGALGQPGsdaaIIFVTFEDDGIAAIQAAASDPVLsKVRWIGTDGIAySD 305
Cdd:cd19985 160 ALGLKVLKKWSFDTDSSQLDQNLDQIVDELKKAPDEPG----VIFLATHADEGAKLIKKLRDAGL-KAPIIGPDSLA-SE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18161589 306 ALIKQVGKE--------------MAAAKMLGTIAapdpnDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQ 365
Cdd:cd19985 234 SFAQGFAEYpeekeepgyytdgiYATSPFIFDIA-----NEKAQKFRDTYQKRYGEEPSWIAAFAYDAAMLAIG 302
|
|
| PBP1_As_SBP-like |
cd06330 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
71-412 |
3.04e-26 |
|
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: 108.42 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKmcpN-----IKFELLVEDTGTNPQQALQKVQTL-YAKGARLIVGPMTSG 144
Cdd:cd06330 2 IGVITPLSGAAAVYGEPARNGAELAVEEINA---AggilgRKIELVVRDDKGKPDEAVRAARELvLQEGVDFLIGTISSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 145 EVSAVKSFADQNKII-IFSPSSTSPLLGIPG-DWVYRIVPTDFAQAAAIADLLKTL--GVKRAVIIYRNDAWGVGLRNAI 220
Cdd:cd06330 79 VALAVAPVAEELKVLfIATDAATDRLTEENFnPYVFRTSPNTYMDAVAAALYAAKKppDVKRWAGIGPDYEYGRDSWAAF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 221 TNESNKLGINI-VASQGYdpdPKAFPTAVPEAIRKLSGAlgqpGSDaAIIFVTFEDDGIAAIQAAASDPVLSKVRWIGTD 299
Cdd:cd06330 159 KAALKKLKPDVeVVGELW---PKLGATDYTAYITALLAA----KPD-GVFSSLWGGDLVTFVKQAKPYGLFDKTKVVSGL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 300 GIAYSDAliKQVGKEMAAAKMLGTIAAPD-PNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKV 378
Cdd:cd06330 231 GGGSEVL--QALGKEMPEGLIGGGRYPFGwPDTPLNKAFVEAYRAKYGEYPTYWAYEAYAAVMALKAAIEKAGSTDTDKV 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 18161589 379 KATLEqwgrqG-TYQGVTGKVYLDEAGDRA-YPNYV 412
Cdd:cd06330 309 IAALE-----GlTFDTPGGKITIRAEDHQAvQPVVV 339
|
|
| PBP1_RPA0668_benzoate-like |
cd20014 |
type 1 periplasmic binding-protein component of an ABC system (RPA0668), involved in in the ... |
71-383 |
1.86e-25 |
|
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: 106.55 E-value: 1.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVSAV 149
Cdd:cd20014 2 IGLLLPYSGVYAALGEDIRNGFQLYLDEHGGKLGGRPIELVKEDDEADPDVALQKARKLIEQdKVDVLVGPVSSGVALAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 150 KSFADQNKIIIFSPSSTSPLLG--IPGDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKL 227
Cdd:cd20014 82 RDVVEQAKVPLIVANAGANALTraACSPYIFRTSFSNWQLGYALGKYAAENVGKTVVTIASDYAAGREVVAGFKEGFEAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 228 GINIVasqgyDPDPKAFPTAVPeairkLSGALGQ-PGSDAAIIFVTFE-DDGIAAIQAAASDPVLSKVRWIGtDGIAYSD 305
Cdd:cd20014 162 GGKVV-----GEIWTPLGTTTD-----FSPYLTQiAASGPDAVYAFFAgADAVRFVKQYAEFGLKGKIPLYG-PGFLTDE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 306 ALIKQVGkemAAAKMLGTIA--APDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQI--ACQLGTDDSDKVKAT 381
Cdd:cd20014 231 DVLPALG---EAAEGIITVLhyAPTLDNPANRAFVAAYQAKYGRLPDVYAVQGYDAAQVIDAAleAVGGDTSDKDILAAA 307
|
..
gi 18161589 382 LE 383
Cdd:cd20014 308 LE 309
|
|
| PBP1_ABC_HAAT-like |
cd19981 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (Atpase Binding Cassette)-type ... |
71-363 |
1.28e-24 |
|
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: 103.14 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVS 147
Cdd:cd19981 2 IGFFAPLTGPAAADGKSALHGAELAVEQINAAggINGKKVELVVYDDQASPKQAVNIAQKLIEQdKVVAVVSGSYSGPTR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLL-KTLGVKRAVIIYRNDAWGVGLRNAITNESNK 226
Cdd:cd19981 82 AAAPIFQEAKVPMVSAYAVHPDITKAGDYVFRVAFLGPVQGRAGAEYAvKDLGAKKVAILTIDNDFGKSLAAGFKEEAKK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 227 LGINIVASQGYDPDPKAFpTAVPEAIRKLsgalgqpGSDaAIIFVTFEDDGIAAIQAAASDPVlsKVRWIGTDGIAySDA 306
Cdd:cd19981 162 LGAEIVSEYAYALGDRDF-RPILTKIKSA-------NPD-AIYASGYYAEAAPIVKQARELGI--KVPIIGQEGYD-SPK 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18161589 307 LIKqVGKEMAAAKMLGTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMML 363
Cdd:cd19981 230 FIE-IAGSAAEGVIITTSLNRDSDRPITQKFIKEYRKRYGIDPDMVAASTYDAVMVL 285
|
|
| PBP1_glutamate_receptors-like |
cd06269 |
ligand-binding domain of family C G-protein couples receptors (GPCRs), membrane bound guanylyl ... |
70-362 |
6.47e-20 |
|
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: 90.17 E-value: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQSyGIGVKNAVELAVEDANK---MCPNIKFELLVEDTGTNPQQALQKVQTL-YAKGARLIVGPMTSGE 145
Cdd:cd06269 1 TIGALLPVHDYLES-GAKVLPAFELALSDVNSrpdLLPKTTLGLAIRDSECNPTQALLSACDLlAAAKVVAILGPGCSAS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 146 VSAVKSFADQNKIIIFSPSSTSPLLGIPGDWVY--RIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNE 223
Cdd:cd06269 80 AAPVANLARHWDIPVLSYGATAPGLSDKSRYAYflRTVPPDSKQADAMLALVRRLGWNKVVLIYSDDEYGEFGLEGLEEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 224 SNKLGINIVASQGYDP-DPKAFPTAVPEAIRKlsgalgqpgsDAAIIFVTFEDDGIAAIQAAA--SDPVLSKVRWIGTDG 300
Cdd:cd06269 160 FQEKGGLITSRQSFDEnKDDDLTKLLRNLRDT----------EARVIILLASPDTARSLMLEAkrLDMTSKDYVWFVIDG 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18161589 301 IAYS-DALIKQVGKEMAAAKMLGTIAAPDPNDPKY---------QEFKQRYKAKYGKDPVaydPYGYDAAMM 362
Cdd:cd06269 230 EASSsDEHGDEARQAAEGAITVTLIFPVVKEFLKFsmelklkssKRKQGLNEEYELNNFA---AFFYDAVLA 298
|
|
| PBP1_ABC_ligand_binding-like |
cd19978 |
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ... |
69-384 |
1.04e-19 |
|
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: 89.94 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 69 VYIGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGE 145
Cdd:cd19978 1 IRLGMSAALSGPAAELGNEMKRGIEAAFNEVNAQggVNGRKIKLIALDDGYEPDRTVKNTKKLIEEdKVFALIGYVGTPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 146 VSAVKSFADQNKIIIFSPSSTSPLLGIPGD-WVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNAITNE 223
Cdd:cd19978 81 ALAALPLANEKKIPLFGPFTGAEFLRTPFLpYVFNLRASYADETEALVDyLVKTLGPKRIAIFYQNDAFGLAGLEGAKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 224 SNKLGINIVASQGYDPDpkafPTAVPEAIRKLSGAlgqpGSDAAIIFVT------FeddgIAAIQAAASDPVLSKVRWIG 297
Cdd:cd19978 161 LKKRGLTPVAEGSYTRN----TLDVEEALAKILKA----KPEAIILVGTyapaaeF----IRLARAAGLNPLFANVSFVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 298 tdgiaySDALIKQVGKemAAAKMLGTIAAPDPNDPKY---QEFKQRYKaKYGKDpVAYDPY---GYDAAMMLMQIACQLG 371
Cdd:cd19978 229 ------SEALALELGD--YGEGVIVSQVVPDPNDSSLpivKEYREAMK-KYGPN-APPDFVsleGYLAARLLVEALKKAG 298
|
330
....*....|....
gi 18161589 372 TD-DSDKVKATLEQ 384
Cdd:cd19978 299 PPlTREKLLALEES 312
|
|
| PBP1_AmiC-like |
cd06331 |
type 1 periplasmic components of amide-binding protein (AmiC) and the active transport system ... |
71-413 |
1.43e-19 |
|
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: 89.20 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTL-YAKGARLIVGPMTSGEVS 147
Cdd:cd06331 2 IGLLTPLSGPASVYGRAIANGAELAVEEINAAggVLGRPVELVVEDDASDPATAVAAARRLiQQDKVDAIVGPITSATRN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDfaQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKL 227
Cdd:cd06331 82 AVAPVAERAKVPLLYPTFYEGGECSPYLFCFGEVPNQ--QLDPLIPWLMEEYGKKFYLIGSDYVWPRTMNDAARRVIEAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 228 GINIVASQgYDP-DPKAFPTAVpEAIRKlsgalgqpgSDAAIIFVTFE-DDGIAAIQAAASDPVLSKVRwigTDGIAYSD 305
Cdd:cd06331 160 GGEVVGEE-YLPlGTTDFSSVI-EKIKA---------SGADVVLSTLVgADAVTFLKQFAAAGLRRKVR---IAALLFDE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 306 ALIKQVGKEMAAakmlGTIAAPD----PNDPKYQEFKQRYKAKYGKD---PVAYDPYGYDAAMMLMQIACQLGTDDSDKV 378
Cdd:cd06331 226 NTLAGLGAEAAE----GIYSVLSyfqsLDTPENKAFVAAYRKKFGEDappITSLSEAAYEAVHLYAAAVEKAGSTDPEAV 301
|
330 340 350
....*....|....*....|....*....|....*
gi 18161589 379 KATLEqwgrQGTYQGVTGKVYLDEAGDRAYPNYVI 413
Cdd:cd06331 302 IAALP----GVSFDGPQGPVTMDPDNHHVRLNLYI 332
|
|
| PBP1_GABAb_receptor |
cd06366 |
ligand-binding domain of GABAb receptors, which are metabotropic transmembrane receptors for ... |
70-440 |
8.17e-19 |
|
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: 88.07 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQSY-GIGVKNAVELAVEDANK---MCPNIKFELLVEDTGTNPQQALQKVQTLYAKGAR--LIVGPMTS 143
Cdd:cd06366 1 YIGGLFPLSGSKGWWgGAGILPAAEMALEHINNrsdILPGYNLELIWNDTQCDPGLGLKALYDLLYTPPPkvMLLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 144 GEVSAVKSFADQNKIIIFSPSSTSPLLGipgD-----WVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRN 218
Cdd:cd06366 81 SVTEPVAEASKYWNLVQLSYAATSPALS---DrkrypYFFRTVPSDTAFNPARIALLKHFGWKRVATIYQNDEVFSSTAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 219 AITNESNKLGINIVASQGY-DPDPKafptavpEAIRKLSgalgqpGSDAAIIFVTF-EDDGIAAI-QAAASDPVLSKVRW 295
Cdd:cd06366 158 DLEELLEEANITIVATESFsSEDPT-------DQLENLK------EKDARIIIGLFyEDAARKVFcEAYKLGMYGPKYVW 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 296 IGTDgiAYSDALIKQVG-------KEMAAAkMLGTIA---APDPNDPK-------YQEFKQRYKAKYGKDPVAYD---PY 355
Cdd:cd06366 225 ILPG--WYDDNWWDVPDndvnctpEQMLEA-LEGHFStelLPLNPDNTktisgltAQEFLKEYLERLSNSNYTGSpyaPF 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 356 GYDA----AMMLMQIACQLG---------TDDSDKVKATLEQWGRQGTYQGVTGKVYLDEAGDRaYPNYVIWGvaLEGGQ 422
Cdd:cd06366 302 AYDAvwaiALALNKTIEKLAeynktledfTYNDKEMADLFLEAMNSTSFEGVSGPVSFDSKGDR-LGTVDIEQ--LQGGS 378
|
410
....*....|....*...
gi 18161589 423 PKYVdaAYYYGTDRKITI 440
Cdd:cd06366 379 YVKV--GLYDPNADSLLL 394
|
|
| PBP1_alkylbenzenes-like |
cd06360 |
type 1 periplasmic binding component of active transport systems predicted be involved in ... |
71-422 |
6.54e-18 |
|
type 1 periplasmic binding component of active transport systems predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; This group includes the type 1 periplasmic binding component of active transport systems that are predicted be involved in anaerobic biodegradation of alkylbenzenes such as toluene and ethylbenzene; their substrate specificity is not well characterized, however.
Pssm-ID: 380583 [Multi-domain] Cd Length: 357 Bit Score: 84.65 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVSAV 149
Cdd:cd06360 2 IGVLLPLTGPLAVNGEDVRDGFELYFDEIGNQVAGRKIELIVEDDEGKPDVGLTKARKLVERdKVHVLAGIVSSAVAYAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 150 KSFADQNKI-IIFSPSSTSPL---LGIPgdWVYRIVPTDFAQAAAIAD-LLKTLGVKRAVIIYRNDAWGVGLRNAITNES 224
Cdd:cd06360 82 RDYVVEQKIpLVISNAGAAPLtqeLASP--YIFRTSFSNGQYDAPFGQyAYEKLGYRRIAVMASDYAAGHEQAGAFARTF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 225 NKLGINIVASQgYDP----DPKAFPTAVpeairklsgalgQPGSDAAIIFVTFEDDGIAAIQAAASDPVLSKVRWIGTdG 300
Cdd:cd06360 160 KQAGGKVVQEI-YPPlgtaDFAPYLARI------------QQDAADAVWAFFAGADAIRFVKQYDEYGLKGKLPLVGI-G 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 301 IAYSDALIKQVGKemAAakmLGTIA----APDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLG--TDD 374
Cdd:cd06360 226 GLVDDAILPEQGD--AA---LGIVSylhySAALDTPENKAFVQAYRKKYGRDPGLYAEGGYVAARAIAEALEAVKgnVED 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 18161589 375 SDKVKATLeqwgRQGTYQGVTGKVYLDEAGDRAYPNYVIwGVALEGGQ 422
Cdd:cd06360 301 KEAFLEAL----RKVRFEAPRGPFRFDPYQQAVVTTYIR-RVEKVDGK 343
|
|
| PBP1_ABC_ligand_binding-like |
cd06326 |
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ... |
71-349 |
2.02e-17 |
|
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: 82.98 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKmcpN-----IKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSG 144
Cdd:cd06326 3 IGQSAPLSGPLAELGREYLAGAKAYFDQVNA---AggingRKIRLVTLDDGYDPARTVENTRQLIEQdKVVALFGYVGTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 145 EVSAVKSFADQNKIIIFSPSSTSPLLGIPGD-WVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNE 223
Cdd:cd06326 80 NVEAVLPLLEEAGVPLVGPLTGADSLREPGNpYVFHVRASYADEVEKIVRHLATLGLKRIAVVYQDDPFGKEGLAAAEAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 224 SNKLGINIVASQGYDPDpkafPTAVPEAIRKLSGAlgQPGsdaAIIFVTFEDDGIAAIQA--AASDPV----LSkvrwig 297
Cdd:cd06326 160 LAARGLEPVATAAVARN----AADVAAAAAALAAA--KPQ---AVVLIAAGKAAAAFIKAlrAAGGAAqfygLS------ 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 18161589 298 tdgIAYSDALIKQVGKemAAAKMLGTIAAPDPNDPKY---QEFKQRYKAKYGKDP 349
Cdd:cd06326 225 ---VVGAAALAKALGD--AARGVVVSQVVPNPWSTTLplvREYQAAMKAAGPKEP 274
|
|
| PBP1_GABAb_receptor_plant |
cd19990 |
periplasmic ligand-binding domain of Arabidopsis thaliana glutamate receptors and its close ... |
88-367 |
9.72e-17 |
|
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: 81.51 E-value: 9.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 88 VKNAVELAVEDANK--MCPNIKFELLVEDTGTNPQQAL-QKVQTLYAKGARLIVGPMTSGEVSAVKSFADQNKIIIFSPS 164
Cdd:cd19990 16 AKVAIEMAVSDFNSdsSSYGTKLVLHVRDSKGDPLQAAsAALDLIKNKKVEAIIGPQTSEEASFVAELGNKAQVPIISFS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 165 STSPLLGiPGDWVY--RIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKLGI---NIVASQgydp 239
Cdd:cd19990 96 ATSPTLS-SLRWPFfiRMTHNDSSQMKAIAAIVQSYGWRRVVLIYEDDDYGSGIIPYLSDALQEVGSrieYRVALP---- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 240 dPKAFPTAVPEAIRKLSGALGQpgsdaaiIFV--TFEDDGIAaiqaaasdpVLSKVR----------WIGTDGIA----Y 303
Cdd:cd19990 171 -PSSPEDSIEEELIKLKSMQSR-------VFVvhMSSLLASR---------LFQEAKklgmmekgyvWIVTDGITnlldS 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18161589 304 SDALIKQvgkemaaaKMLGTIA-APD-PNDPKYQEFKQRYKAKYGKD--------PVAYDPYGYDAAMMLMQIA 367
Cdd:cd19990 234 LDSSTIS--------SMQGVIGiKTYiPESSEFQDFKARFRKKFRSEypeeenaePNIYALRAYDAIWALAHAV 299
|
|
| PBP1_GPCR_family_C-like |
cd06350 |
ligand-binding domain of membrane-bound glutamate receptors that mediate excitatory ... |
70-341 |
2.84e-16 |
|
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: 79.65 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQS----------YGIGVKNAVELAVEDANK---MCPNIKFELLVEDTGTNPQQALQKV---------- 126
Cdd:cd06350 1 IIGGLFPVHYRDDAdfcccgilnpRGVQLVEAMIYAIEEINNdssLLPNVTLGYDIRDTCSSSSVALESSleflldngik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 127 -------QTLYAKGARLIVGPMTSGEVSAVKSFADQNKIIIFSPSSTSPLLG--IPGDWVYRIVPTDFAQAAAIADLLKT 197
Cdd:cd06350 81 llansngQNIGPPNIVAVIGAASSSVSIAVANLLGLFKIPQISYASTSPELSdkIRYPYFLRTVPSDTLQAKAIADLLKH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 198 LGVKRAVIIYRNDAWGVGLRNAITNESNKLGINIVASQGYDPDPKAfpTAVPEAIRKLsgaLGQPGSDAAIIFVTFEDdg 277
Cdd:cd06350 161 FNWNYVSTVYSDDDYGRSGIEAFEREAKERGICIAQTIVIPENSTE--DEIKRIIDKL---KSSPNAKVVVLFLTESD-- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18161589 278 IAAIQAAASDPVLSKVRWIGTDGIAYSDALIKQVGKEMAAAkmlGTIAAPDPNDPKYQEFKQRY 341
Cdd:cd06350 234 ARELLKEAKRRNLTGFTWIGSDGWGDSLVILEGYEDVLGGA---IGVVPRSKEIPGFDDYLKSY 294
|
|
| PBP1_NPR_GC-like |
cd06352 |
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of ... |
71-441 |
3.03e-16 |
|
ligand-binding domain of membrane guanylyl-cyclase receptors; Ligand-binding domain of membrane guanylyl-cyclase receptors. Membrane guanylyl cyclases (GC) have a single membrane-spanning region and are activated by endogenous and exogenous peptides. This family can be divided into three major subfamilies: the natriuretic peptide receptors (NPRs), sensory organ-specific membrane GCs, and the enterotoxin/guanylin receptors. The binding of peptide ligands to the receptor results in the activation of the cytosolic catalytic domain. Three types of NPRs have been cloned from mammalian tissues: NPR-A/GC-A, NPR-B/ GC-B, and NPR-C. In addition, two of the GCs, GC-D and GC-G, appear to be pseudogenes in humans. Atrial natriuretic peptide (ANP) and brain natriuretic peptide (BNP) are produced in the heart, and both bind to the NPR-A. NPR-C, also termed the clearance receptor, binds each of the natriuretic peptides and can alter circulating levels of these peptides. The ligand binding domain of the NPRs exhibits strong structural similarity to the type 1 periplasmic binding fold protein family.
Pssm-ID: 380575 [Multi-domain] Cd Length: 391 Bit Score: 80.09 E-value: 3.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIG-VKNAVELAVEDANKM---CPNIKFELLVEDTGTNPQQAL-QKVQTLYAKGARLIVGPMTSGE 145
Cdd:cd06352 2 VGVLAPSNSQSLPVGYArSAPAIDIAIERINSEgllLPGFNFEFTYRDSCCDESEAVgAAADLIYKRNVDVFIGPACSAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 146 VSAVKSFADQNKIIIFSPSSTSPLLGIPGDWVY--RIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWG-----VGLRN 218
Cdd:cd06352 82 ADAVGRLATYWNIPIITWGAVSASFLDKSRYPTltRTSPNSLSLAEALLALLKQFNWKRAAIIYSDDDSKcfsiaNDLED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 219 AItNESNKLGINIVASQGYDPDPKAfptavPEAIRKLSgalgqpgSDAAIIFVTFEDDGIAAIQAAASD----------- 287
Cdd:cd06352 162 AL-NQEDNLTISYYEFVEVNSDSDY-----SSILQEAK-------KRARIIVLCFDSETVRQFMLAAHDlgmtngeyvfi 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 288 ---------PVLSKVRWIGTDGiaySDALIKQvgkemAAAKMLgTIAAPDPNDPKYQEFKQRYKAkygkdpVAYDPYGYD 358
Cdd:cd06352 229 fielfkdgfGGNSTDGWERNDG---RDEDAKQ-----AYESLL-VISLSRPSNPEYDNFSKEVKA------RAKEPPFYC 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 359 A----------------AMML----MQIACQLGTDDSDKVKATLEQWGRqgTYQGVTGKVYLDEAGDRaYPNYVIWGVAL 418
Cdd:cd06352 294 YdaseeevspyaaalydAVYLyalaLNETLAEGGNYRNGTAIAQRMWNR--TFQGITGPVTIDSNGDR-DPDYALLDLDP 370
|
410 420
....*....|....*....|...
gi 18161589 419 EGGqpKYVDAAYYYGTDRKITIF 441
Cdd:cd06352 371 STG--KFVVVLTYDGTSNGLVVV 391
|
|
| PBP1_SBP-like |
cd06328 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
71-399 |
5.71e-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: 78.50 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDA--NKMCPN-IKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEV 146
Cdd:cd06328 2 IGVITSLTGPLAAYGKQTERGFELGLEYAtdGTMEVDgRKIEVIVKDDQGDPDTAKAAATELIGDdGVDILVGTVSSAVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 147 SAVKSFADQNKIIIFS-PSSTSPLLGIP-GDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNES 224
Cdd:cd06328 82 LALAPVAEQNKKILIVgPAAADSITGENwNKYTFRTSRNSWQDAIAGAKALADPLGKSVAFLAQDYAFGQDGVAAFKKAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 225 NKLGINIVASQGYDPDPKAFpTAVPEAIRKlsgalgqpgSDAAIIFVTFEDDGIAA-IQAAASDPVLSKVRwIGTDGI-- 301
Cdd:cd06328 162 EAKGGKIVGEELVPVTTTDF-TPYLQRILD---------AKPDVLFVAWAGTGALTlWQQLADQGVLDDIK-VVTGGPdi 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 302 ----AYSDALIKQVGkemaaakmLGTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQ-IACQLGTDDSD 376
Cdd:cd06328 231 atlaALGDALPGIEG--------LTYYYYGLPKNPVNDWLVKAHKERYNAPPDLFTAGGFAAAQAVVRaLEKAGGDTDVE 302
|
330 340
....*....|....*....|...
gi 18161589 377 KVKATLEQWgrqgTYQGVTGKVY 399
Cdd:cd06328 303 KLIAALEGL----TFETPKGKMT 321
|
|
| PBP1_ABC_ligand_binding-like |
cd19979 |
amino acid amide ABC transporter substrate binding protein haat family; This subgroup includes ... |
69-399 |
1.40e-15 |
|
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: 77.65 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 69 VYIGAALplTGGSQSYGIGVKNAVELAVEDANKMCP--NIKFELLVEDTGTNPQQALQKVQTL-YAKGARLIVGPMTSGE 145
Cdd:cd19979 2 IGLDADL--SGGSAASGEAIKRGIQLAIDEINAAGGllGRKLELVAKDHRGNPARGVDNLREFaADPDVLAVFGGLHSPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 146 VSAVKSFADQNKIIIFSP-SSTSPLL--GIPGDWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITN 222
Cdd:cd19979 80 LLAELDFIHELKIPYLVPwAAATPITrnGYSPNYIFRLSVDDSLAGPFLVEYALKKGCKRPALLLENTGWGRSNLKAMTK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 223 ESNKLGINIVASQgydpdpkAFPTAVPEAIRKLSgALGQPGSDaAIIFVTFEDDGIAAIQAAASD----PVLSKVRWIGT 298
Cdd:cd19979 160 ALAKKGLQPVGVE-------WFNWGDTDAKPQLR-ALKAAGAD-AILLVANAPEGAAIVKALAALperlPIISHWGITGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 299 DGIAYSDALIKQVGkemaaAKMLGTIA-APDPNDPKYQEFKQRYKAKYGKDPVAYD---PYG----YDAAMMLMQIACQL 370
Cdd:cd19979 231 DFPELPREALSKID-----LRFIQTFSfFDANQSPRGKQVLARYKRRYPVEDPESDipaPVGfahaYDLTHLLALAIEQA 305
|
330 340
....*....|....*....|....*....
gi 18161589 371 GTDDSDKVKATLEqwgRQGTYQGVTgKVY 399
Cdd:cd19979 306 GSTDRAAVRAALE---LLPPHEGLI-KTY 330
|
|
| PRK15404 |
PRK15404 |
high-affinity branched-chain amino acid ABC transporter substrate-binding protein; |
67-405 |
3.06e-13 |
|
high-affinity branched-chain amino acid ABC transporter substrate-binding protein;
Pssm-ID: 237959 [Multi-domain] Cd Length: 369 Bit Score: 70.82 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 67 KTVYIGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSG 144
Cdd:PRK15404 24 DDIKIAIVGPMSGPVAQYGDMEFTGARQAIEDINAKggIKGDKLEGVEYDDACDPKQAVAVANKVVNDGIKYVIGHLCSS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 145 EVSAVKSFADQNKIIIFSPSSTSPLLGIPG-DWVYRIVPTDFAQ--AAA--IADLLKTlgvKRAVIIYRNDAWGVGLRNA 219
Cdd:PRK15404 104 STQPASDIYEDEGILMITPAATAPELTARGyQLIFRTIGLDSDQgpTAAkyILEKVKP---KRIAVLHDKQQYGEGLARS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 220 ITNESNKLGINIVASQGYDPDPKAFPTavpeAIRKLSGAlgqpGSDaaiiFVTF----EDDGIAAIQAAASDpvlSKVRW 295
Cdd:PRK15404 181 VKDGLKKAGANVVFFEGITAGDKDFSA----LIAKLKKE----NVD----FVYYggyhPEMGQILRQAREAG---LKTQF 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 296 IGTDGIAYSDalIKQVGKEmAAAKMLGTIAAPDPNDPKYQEFKQRYKAKyGKDPV-AYDPYGYDAAMMLMQIACQLGTDD 374
Cdd:PRK15404 246 MGPEGVGNKS--LSNIAGP-ASEGMLVTLPKRYDQDPANKAIVDAFKAK-KQDPSgPFVWTTYAAVQSLAAGINRAGSDD 321
|
330 340 350
....*....|....*....|....*....|.
gi 18161589 375 SDKVKATLeqwgRQGTYQGVTGKVYLDEAGD 405
Cdd:PRK15404 322 PAKVAKYL----KANTFDTVIGPLSWDEKGD 348
|
|
| PBP1_ABC_transporter_GPCR_C-like |
cd04509 |
Family C of G-protein coupled receptors and their close homologs, the type 1 ... |
84-326 |
6.29e-13 |
|
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: 69.26 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 84 YGIGVKNAVELAVEDAN---KMCPNIKFELLVEDTGTNPQQALQKVQTL-----------------------YAKGARLI 137
Cdd:cd04509 25 YGIQRFEAMEQALDDINadpNLLPNNTLGIVIYDDCCDPKQALEQSNKFvndliqkdtsdvrctngeppvfvKPEGIKGV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 138 VGPMTSGEVSAVKSFADQNKIIIFSPSSTSPLLGIPG--DWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVG 215
Cdd:cd04509 105 IGHLCSSVTIPVSNILELFGIPQITYAATAPELSDDRgyQLFLRVVPLDSDQAPAMADIVKEKVWQYVSIVHDEGQYGEG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 216 LRNAITNESNKLGINIVASQGY--DPDPKAFPTavpeAIRKLsgaLGQPGSDAAIIFVTFEDDGIAAIQAAASDpVLSKV 293
Cdd:cd04509 185 GARAFQDGLKKGGLCIAFSDGItaGEKTKDFDR----LVARL---KKENNIRFVVYFGYHPEMGQILRAARRAG-LVGKF 256
|
250 260 270
....*....|....*....|....*....|....*...
gi 18161589 294 RWIGTDGIAYSDALIKQVGKEMAAA-----KMLGTIAA 326
Cdd:cd04509 257 QFMGSDGWANVSLSLNIAEESAEGLitikpKVWFVIAA 294
|
|
| PBP1_Nba-like |
cd06359 |
type 1 periplasmic binding component of active transport systems predicted to be involved in ... |
71-399 |
9.57e-13 |
|
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: 68.82 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVSAV 149
Cdd:cd06359 2 IGFITTLSGPAAVLGQDMRDGFNLALEQLGGKLGGLPVEVVVEDDQLKPDVAKQAAERLIERdKVDFVTGIIFSNVMLAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 150 -KSFADQNKIIIFSPSSTSPLLGipgdwvYRIVPTDF-------AQAAAIADLLKTLGVKRAVIIYRNDAWG----VGLR 217
Cdd:cd06359 82 vKPVVDSKVFYISANAGPSDLAG------KGCNPNFFvtswqndQLHEAAGKYANDKGYKRVYLLAPNYQAGkdalAGFK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 218 NAITNEsnklginiVASQGYDPDPKAFPTAVPEAIRKLsgalgqpGSDAAIIFVtFEDDGIAAIQAAASDPVLSKVRWIG 297
Cdd:cd06359 156 RTYKGE--------VVGEIYTPLGQLDFSAELAQIRAA-------KPDAVFAFY-PGGMGVNFVKQYAQAGLKKKIPLYT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 298 TdGIAYSDALIKQVGKEMAAAKmLGTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLG--TDDS 375
Cdd:cd06359 220 V-GTLDDEDLLPAMGDAALGVL-SVSQWSPDLDNPENKRFVAAFRKKYGRPPSNYAAQGYDAALLIDAAVKAVGgdLSDK 297
|
330 340
....*....|....*....|....
gi 18161589 376 DKVKATLeqwgRQGTYQGVTGKVY 399
Cdd:cd06359 298 DALRAAL----RKADFKSVRGAFR 317
|
|
| PBP1_SBP-like |
cd20378 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
71-405 |
1.08e-12 |
|
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: 68.91 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNiKFELLVEDTGTNPQQALQKVQTLYA-KGARLIVGPMTSGEVSAV 149
Cdd:cd20378 2 LGGLVSMSGAFAAAGKLADRGMRLAVEEYGGALGR-PLKYITRDTEGKPGTGVRKVQEAIAqDGARFFIGGTLSSVALAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 150 KSFADQNKIIIFSPSSTSPLLGIP-GDWVYR-IVPTDFAQAAAIADLLKTLG-VKRAVIIYRNDAWGVGLRNAITNESNK 226
Cdd:cd20378 81 SEEAEKAGGVYITSGGADEITGSRcNRSTFRwSVPTYGAIRQTVRPVIKAMPkAKRWYTITPQYVFGESLLKNAKEVLKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 227 LGINIVASQGYDPDPKAFPTAVPEAIRklsgalGQPGsdaAIIFVTFEDDGIAAIQAAASDPVLSKVRWIGtdgiAYSDA 306
Cdd:cd20378 161 KGIEHVGNSYHSLGEREFSGYLTKAMA------ARPD---VLLILNFGSQAVDALRQAVSFGLKRKMKILV----AWSSG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 307 L--IKQVGKEMAAAKMLGTIAAPDPNDPKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKVKATLEq 384
Cdd:cd20378 228 LdqFQELGPDICEGVYFGAQYWHDVDTPANKALVKVYQAKFKETPSYALAAGYACTRMLLDAIDKAGSTDPAAVIKALE- 306
|
330 340
....*....|....*....|.
gi 18161589 385 wGRqgTYQGVTGKVYLDeAGD 405
Cdd:cd20378 307 -GL--KYDGITGDEEVR-AAD 323
|
|
| PBP1_SBP-like |
cd19987 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
70-383 |
1.23e-11 |
|
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: 65.81 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTGGSQSYGIGVKNAVELAVEDAN-------KMCPNI-------KFELLVEDTGTNPQQALQKVQTLYAK-GA 134
Cdd:cd19987 1 TIGLNVPLSGPYAPQGEDQRRGFELAVDHLNnggglvdKDSRLSgdgilgkKVELVTADTETKADTAVDNAKRLIEQdGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 135 RLIVGPMTSGEVSAVKSFADQNKIIIFSPSSTSPllGIPGD----WVYRIVPTDFAQAAAIADLLKTL--GVKRAVIIYR 208
Cdd:cd19987 81 VMITGGSSSAVAVAAQKLAQKEGVLYFAGLSHSN--DTTGKdchrYGFRECFNAHMSAKALAPYLVEKfgKDRKYFYLTA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 209 NDAWGVGLRNAITNESNKLGINIVASQGYDPDPKAFPTAVPEAirKLSGAlgqpgsdAAIIFVTFEDDGIAAIQAAASDP 288
Cdd:cd19987 159 DYTWGHSTEQSMREYTEAHGWKTVGNPATPLGETDFSAALLNA--ADSGA-------DVLVLVLFGRDMVNALKQAKQFG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 289 VLSKVRWIGTDgiaYSDALIKQVGKEmAAAKMLGTIA----APDPNDPKyQEFKQRYKAKYGKDPVAYDPYGYDAAMMLM 364
Cdd:cd19987 230 LLKKMDIVVPL---LTAFMAESVGPE-IMEGVLGTVNwhwsLPDDYSYA-FGKAEAFEKEYGAYPSQAAASAYVQVLQYA 304
|
330
....*....|....*....
gi 18161589 365 QIACQLGTDDSDKVKATLE 383
Cdd:cd19987 305 AAVERAGSFDPPAVIRALE 323
|
|
| PBP1_NPR-like |
cd06373 |
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of ... |
88-438 |
1.68e-10 |
|
Ligand binding domain of natriuretic peptide receptor (NPR) family; Ligand binding domain of natriuretic peptide receptor (NPR) family which consists of three different subtypes: type A natriuretic peptide receptor (NPR-A, or GC-A), type B natriuretic peptide receptors (NPR-B, or GC-B), and type C natriuretic peptide receptor (NPR-C). There are three types of natriuretic peptide (NP) ligands specific to the receptors: atrial NP (ANP), brain or B-type NP (BNP), and C-type NP (CNP). The NP family is thought to have arisen through gene duplication during evolution and plays an essential role in cardiovascular and body fluid homeostasis. ANP and BNP bind mainly to NPR-A, while CNP binds specifically to NPR-B. Both NPR-A and NPR-B have guanylyl cyclase catalytic activity and produces intracellular secondary messenger cGMP in response to peptide-ligand binding. Consequently, the NPR-A activation results in vasodilation and inhibition of vascular smooth muscle cell proliferation. NPR-C acts as the receptor for all the three members of NP family, and functions as a clearance receptor. Unlike NPR-A and -B, NPR-C lacks an intracellular guanylyl cyclase domain and is thought to exert biological actions by sequestration of released natriuretic peptides and/or inhibition of adenylyl cyclase.
Pssm-ID: 380596 [Multi-domain] Cd Length: 394 Bit Score: 62.29 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 88 VKNAVELAVED--ANKMCPNIKFELLVEDTGTNPQQALQKVQTLY-AKGARLIVGPMTSGEVSAVKSFADQNKIIIFSPS 164
Cdd:cd06373 19 VLPAIELALRRveRRGFLPGWRFQVHYRDTKCSDTLAPLAAVDLYcAKKVDVFLGPVCEYALAPVARYAGHWNVPVLTAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 165 STS---------PLLgipgdwvYRIVPTDFAQAAAIADLLKTLGVKRAVIIY-RNDAWGVGLRNA-ITNEsnklGINIVA 233
Cdd:cd06373 99 GLAagfddkteyPLL-------TRMGGSYVKLGEFVLTLLRHFGWRRVALLYhDNLRRKAGNSNCyFTLE----GIFNAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 234 SQGYDPDPKAFPTAVPEA--IRKLSGALGQPGSdaaIIFV-----TFEDDGIAA--------------IQAAASDPVLSK 292
Cdd:cd06373 168 TGERDSIHKSFDEFDETKddFEILLKRVSNSAR---IVILcaspdTVREIMLAAhelgmingeyvffnIDLFSSSSKGAR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 293 VRWIGTDGiaysdALIKQVGKEMAAAKMlgTIAAPDPNDPKYQEF----KQRYKAKYGKdpVAYDPYG--------YDAA 360
Cdd:cd06373 245 PWYRENDT-----DERNEKARKAYRALL--TVTLRRPDSPEYRNFseevKERAKEKYNY--FTYGDEEvnsfvgafHDAV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 361 MmLMQIAC----QLGTDDSDKVKATLEQWGRqgTYQGVTGKVYLDEAGDRaYPNYVIWgvALEGGQPKYVDAAYYYGTDR 436
Cdd:cd06373 316 L-LYALALnetlAEGGSPRNGTEITERMWNR--TFEGITGNVSIDANGDR-NADYSLL--DMNPVTGKFEVVANYFGNSK 389
|
..
gi 18161589 437 KI 438
Cdd:cd06373 390 QL 391
|
|
| PBP1_mGluR |
cd06362 |
ligand binding domain of metabotropic glutamate receptors (mGluR); Ligand binding domain of ... |
137-315 |
2.25e-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: 62.31 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 137 IVGPMTSGEVSAVKSFADQNKIIIFSPSSTSPLLGIPGDWVY--RIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGV 214
Cdd:cd06362 111 VIGAESSSVSIQVANLLRLFKIPQISYASTSDELSDKERYPYflRTVPSDSFQAKAIVDILLHFNWTYVSVVYSEGSYGE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 215 GLRNAITNESNKLGINIVASQG--YDPDPKAFptavPEAIRKLsgaLGQPGSDAAIIFVTFEDdgIAAIQAAA-SDPVLS 291
Cdd:cd06362 191 EGYKAFKKLARKAGICIAESERisQDSDEKDY----DDVIQKL---LQKKNARVVVLFADQED--IRGLLRAAkRLGASG 261
|
170 180
....*....|....*....|....
gi 18161589 292 KVRWIGTDGIAYSDALIKQVGKEM 315
Cdd:cd06362 262 RFIWLGSDGWGTNIDDLKGNEDVA 285
|
|
| PBP1_RPA0985_benzoate-like |
cd20013 |
type 1 periplasmic binding-protein component of an ABC system (RPA0985), involved in the ... |
71-401 |
7.57e-10 |
|
type 1 periplasmic binding-protein component of an ABC system (RPA0985), involved in the active transport of lignin-derived benzoate derivative compounds, and its close homologs; This group includes RPA0985 from Rhodopseudomonas palustris and its close homologs in other bacteria. Rpa0985 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: 380666 [Multi-domain] Cd Length: 356 Bit Score: 60.35 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNIKFELLVEDT-GTNPQQALQKVQTLYAK-GARLIVGPMTSGEVSA 148
Cdd:cd20013 2 VGVIGPFSGPFADYGKQFDRGIDLYLKLHGDKVGGRKVEVIYRDDgGPNPAVAKRLAQELIVRdKVQILIGFGFTPNALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 149 VKSFADQNKIIIFSPSSTSPllGIPGDWVYrIVPTDFAQ---AAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESN 225
Cdd:cd20013 82 VAPVATEAKTPTVIMNAATS--SITRKSPY-FVRTSFTMwqvAYPMGKWAAKNGIKKAYTAVADYAPGHDAETAFKKAFE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASqgyDPDPKAFPTAVPEAIRklsgaLGQPGSDAAIIFVTFEDDGIAAIQAAASDPVLSK-VRWIGTdGIAYS 304
Cdd:cd20013 159 AAGGKIVGS---IRVPLATPDFAPFMQR-----IKDAKPDAVFVFVPAGAPSIGFLKAYAERGLKEAgIKLLGT-GDATD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 305 DALIKQVGKEMAAAKMLGTIAAPDPNdPKYQEFKQRYKAKYGKDPVA--YDPYGYDAAMMLMQ-IACQLGTDDSDKVKAT 381
Cdd:cd20013 230 DDDLPAMGDAALGLITAGHYSAALDS-PENKAFVAAYQKAYGPDARPdfMAVAAYDGMALIYKmIKATGGKFDGDKAMAA 308
|
330 340
....*....|....*....|
gi 18161589 382 LEQWgrqgTYQGVTGKVYLD 401
Cdd:cd20013 309 VKGL----KWESPRGPISID 324
|
|
| PBP1_SBP-like |
cd06329 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
76-383 |
4.23e-09 |
|
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: 57.67 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 76 PLTGGSQSYGIGVKNAVELAVEDANKMCP--NIKFELLVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSGEVSAVKSFA 153
Cdd:cd06329 7 PLSGPFASVGEIYLKGLQFAIEEINAGGGllGRKIELVPFDNKGSPQEALIQLKKAIDQGIRFVLQGNSSAVAGALIDAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 154 DQ-------NKIIIFSPSSTSPllGIPGD----WVYRIVPTDFAQAAAIADLLKTLG-VKRAVIIYRNDAWGVGLRNAIT 221
Cdd:cd06329 87 EKhnqrnpdKRVLFLNYGAEAP--ELTGAkcsfWHFRFDANADMKMAALADYMKKDGsIKKVYLINQDYSFGRDVAAAAK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 222 NESNKL--GINIVasqGYDPDP----KAF-PTavpeaIRKL--SGA----LGQPGSDAAIIFVTFEDDGIaaiqaaasdp 288
Cdd:cd06329 165 KNLKKKrpDIEIV---GEDLHPlgkvKDFsPY-----IAKIkaSGAdtviTGNWGNDLTLLMKAARDSGL---------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 289 vlsKVRWIGTdgiaYSD-----ALIKQVGKEMAAAKMLGTIAAPDPNDPKYQEfkqRYKAKYGKDPVAYDPYGYDAAMML 363
Cdd:cd06329 227 ---KAPFYTY----YADgpgapAAIGEAGVGRLVAVAYWHPNPKTPELEKFAE---AFRAKYGRYPDFNIGRTYMGVEML 296
|
330 340
....*....|....*....|
gi 18161589 364 MQIACQLGTDDSDKVKATLE 383
Cdd:cd06329 297 AAAIKKAGSTDPEKVAKALE 316
|
|
| PBP1_ABC_ligand_binding-like |
cd06334 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
70-368 |
2.71e-08 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. 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: 55.33 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 70 YIGAALPLTG----GSQSYGIGVKNAVELAveDANKMCPNIKFELLVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSGE 145
Cdd:cd06334 1 KIGLLTDLTGptadVGKPYAQGVRDYLNYV--NEEGGINGVKIELEECDTGYKVPRAVACYKRLKAQDGVVAILGWGTGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 146 VSAVKSFADQNKIIIFSPSSTSPLL--GIPGDWVYRIVPTDFAQAAA----IADLLK-TLGVKRAVIIYRNDAWGVGLRN 218
Cdd:cd06334 79 TEALAPRVAKDKIPYISASYGRSLAddGKVFPYNFFVGATYSSQARAllkyIAQEWGgKLKGPKVAFVYHDSPFGREPIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 219 AITNESNKLGINIVAsqgyDPDPKAFPTAVPEAIRKLSGAlgqpGSDAAIIfvtfedDGIA-----AIQAAASDPVLSK- 292
Cdd:cd06334 159 ALKAYAKELGFEVVA----EQVPSPGALDATAQWLRIRRA----GPDYVII------QGTGgsvavIIKDAKRLGLKTKf 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 293 --VRWigtdgiAYSDALIKQVGkemAAAK--MLGTIAAPDPNDPKYQEFKQRYKAKYGKD-PVAYDPYGYDAAMMLMQIA 367
Cdd:cd06334 225 igNIW------GGDEDLIKLAG---DAAEgyVGVSPFAFGTDDPPGKEIVEEVAKKGKGDgPEEVGTVYYNRGWATAMLA 295
|
.
gi 18161589 368 C 368
Cdd:cd06334 296 V 296
|
|
| PBP1_SBP-like |
cd06327 |
periplasmic substrate-binding domain of active transport proteins (substrate binding proteins ... |
85-383 |
1.56e-07 |
|
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: 52.96 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 85 GIGVKNAVELAVEDANKMCPNIKFELLVEDTGTNPQQALQKVQTLY-AKGARLIVGPMTSGEVSAVKSFA-DQNKIIIFS 162
Cdd:cd06327 17 GPGSVEAAKMAVEDFGGKVLGRPIEVVSADHQNKPDVASAIAREWYdRDGVDAIVDVPNSAVALAVQKLAkEKKKIAIVT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 163 PSSTSPLLGI---PGDWVYriVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKLGINIVASqgydp 239
Cdd:cd06327 97 GAGSSDLTGKacsPYGVHW--AYDTYALARGTVKALVKQGGKSWFFITADYAFGHSLEADATAAVKAAGGKVVGS----- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 240 DPKAFPTAvpeairKLSGALGQ-PGSDA-AIIFVTFEDDGIAAIQAAASDPVLSKVRWIGTDGIAYSDalIKQVGKEMAA 317
Cdd:cd06327 170 VRHPLGTT------DFSSFLLQaQASGAdVIALANAGADLVNAVKQAREFGLTDGGQKLAALLLFITD--IHALGLDAAQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18161589 318 AKMLGTIAAPDPNDpKYQEFKQRYKAKYGKDPVAYDPYGYDAAMMLMQIACQLGTDDSDKVKATLE 383
Cdd:cd06327 242 GLYLTTAFYWDRDD-ATRAWAKRFFARTGKMPTMLQAGVYSAVLHYLKAVKAAGTDDADAVVAKMR 306
|
|
| LppC |
pfam04348 |
LppC putative lipoprotein; This family includes several bacterial outer membrane antigens, ... |
71-238 |
4.03e-07 |
|
LppC putative lipoprotein; This family includes several bacterial outer membrane antigens, whose molecular function is unknown.
Pssm-ID: 367906 [Multi-domain] Cd Length: 532 Bit Score: 52.12 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKMCPNIKfellVEDTGTNP-QQALQKVQtlyAKGARLIVGPMTSGEVSAV 149
Cdd:pfam04348 221 IALLLPLSGNLATIAATIRDGFLAAKYAEGNSNPQVQ----VFDTAATSlEDIYAQAK---AAGIDTVVGPLLKQNVDVL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 150 KSFADQNKII-IFSPSSTSPLLGIPGDWVYRIVPTDfaQAAAIADLLKTLGVKRAVIIYRNDAWGVGLRNAITNESNKLG 228
Cdd:pfam04348 294 LANPQLVQGIpVLALNSTDNSRAIAQLCYYGLSPED--EAESAANKMWNDGVRNPLVLVPQNDLGRRVVAAFNVRWQQLG 371
|
170
....*....|
gi 18161589 229 INIVASQGYD 238
Cdd:pfam04348 372 GTDAAIRFYN 381
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
71-325 |
1.84e-06 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 49.19 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALP-LTGGSQSYGIGVKNAVELAVEDANKMCPnikfellVEDTGTNPQQALQKVQTLYAKGARLIVGPMTSGEVSAV 149
Cdd:cd01391 2 IGVVTSsLHQIREQFGIQRVEAIFHTADKLGASVE-------IRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 150 KSFADQNKI--IIFSPSSTSPLLGIPGDWVYRIVPTDFAQAAAIADLLKTLGvKRAVIIYRNDAWGVG--LRNAITNESN 225
Cdd:cd01391 75 QNLAQLFDIpqLALDATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKN-WTYVAAIHGEGLNSGelRMAGFKELAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 226 KLGINIVASQGYDPDpkAFPTAVPEAIRKLsgalgQPGSDAAIIFVTFEDDGIAAIQAAASDPVLSKVRWIGTDGIAYSD 305
Cdd:cd01391 154 QEGICIVASDKADWN--AGEKGFDRALRKL-----REGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSDGWADRD 226
|
250 260
....*....|....*....|
gi 18161589 306 ALIKQVgkemaAAKMLGTIA 325
Cdd:cd01391 227 EVGYEV-----EANGLTTIK 241
|
|
| PBP1_amide_urea_BP-like |
cd06356 |
periplasmic component (FmdD) of an active transport system for short-chain amides and urea ... |
71-401 |
2.96e-05 |
|
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: 45.75 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 71 IGAALPLTGGSQSYGIGVKNAVELAVEDANKM--CPNIKFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVS 147
Cdd:cd06356 2 IGSIFDLSGGLNIYGKPMVHAMKLAVEEINAAggLLGRQIELVAYDTQSDMQKYTQYAQQLILRdKVDVVFGGITSASRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 148 AVKSFADQNKIIIFSPSSTSPllGIPGDWVyrivptdFAQAAAIADLLKTLgVKRAViiyrndawgvglrnaitnesNKL 227
Cdd:cd06356 82 AIRPILRRNKILYFYNTQYEG--GVCDKNT-------FCTGSTPEQQVSPL-IEWAI--------------------KKY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 228 G--INIVASQgYDpdpkaFPTAVPEAIRKLSGALGqpGSDAAIIFVTFE--DDG--IAAIQAAASDPVLSKVrwIGTDGI 301
Cdd:cd06356 132 GkkVYIIAAD-YN-----FGQISADWVKKYAKKNG--GEVVGEEFFPLDvtDFGptIQKIQAAKPDFVVSLL--VGGNHI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 302 AY-----SDALIKQVG------------KEMAAAKMLGTIAAP----DPNDPKYQEFKQRYKAKYGKDPVAYDP--YGYD 358
Cdd:cd06356 202 SFyrqwaAAGLKKKIPivstvfgagnehKVLSPPELEGMYVSYsyfeELDTPANKAFVAKWRAKYGDEPYINQEavGVYN 281
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18161589 359 AAMMLMQIACQLGTDDSDKVKATLEQwgrQGTYQGVTGKVYLD 401
Cdd:cd06356 282 AVYLWAEAVEKAGSTEREAVIAALES---GISFDGPSGTVTVD 321
|
|
| PBP1_NPR_B |
cd06384 |
ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B ... |
324-438 |
3.77e-05 |
|
ligand-binding domain of type B natriuretic peptide receptor; Ligand-binding domain of type B natriuretic peptide receptor (NPR-B). NPR-B is one of three known single membrane-spanning natriuretic peptide receptors that have been identified. Natriuretic peptides are family of structurally related but genetically distinct hormones/paracrine factors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. Like NPR-A (or GC-A), NPR-B (or GC-B) is a transmembrane guanylyl cyclase, an enzyme that catalyzes the synthesis of cGMP. NPR-B is the predominant natriuretic peptide receptor in the brain. The rank of order activation of NPR-B by natriuretic peptides is CNP>>ANP>BNP. Homozygous inactivating mutations in human NPR-B cause a form of short-limbed dwarfism known as acromesomelic dysplasia type Maroteaux.
Pssm-ID: 380607 [Multi-domain] Cd Length: 399 Bit Score: 45.62 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 324 IAAPDPNDPKYQEFK----QRYKAKYGkdpVAYDPY--------GYDAAMMLMQI---ACQLGTDDSDKVKATLEQWGRQ 388
Cdd:cd06384 274 ITYKEPDNPEYQEFQreliARAKQEFG---VQLNPSlmnliagcFYDGVLLYAQAlneTLREGGSQKDGLNIVEKMQDRR 350
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 18161589 389 gtYQGVTGKVYLDEAGDRAyPNYVIWGVA-LEGGQpkYVDAAYYYGTDRKI 438
Cdd:cd06384 351 --FWGVTGLVSMDKNNDRD-TDFNLWAMTdHESGQ--YEVVAHYNGAEKQI 396
|
|
| PBP1_FmdD-like |
cd06355 |
periplasmic component (FmdD) of an active transport system for short-chain amides and urea ... |
244-402 |
9.32e-05 |
|
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: 44.49 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 244 FPTAVPEAIRKLSGALGqpGSDAAIIFVTFE----DDGIAAIQAAASDPVLSKVrwIGTDGIAYSDALIKQ--------- 310
Cdd:cd06355 144 FPRTANKIIRDQLKALG--GEVVGEEYVPLGgtdfDAIVAKIKAFKPDVIVNTL--NGDSNIAFFKQLAAAgitasdlpv 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 311 ----VGK-EMAA---AKMLGTIAA----PDPNDPKYQEFKQRYKAKYGKDPVAYDPY--GYDAAMMLMQIACQLGTDDSD 376
Cdd:cd06355 220 lsfsVSEaELRAigpEELAGHYAAwnyfQSLDTPENQAFVEAFKAKYGADRVTSDPMeaAYLGVYLWAQAVEKAGSFDPD 299
|
170 180
....*....|....*....|....*.
gi 18161589 377 KVKATLeqwgRQGTYQGVTGKVYLDE 402
Cdd:cd06355 300 AVRAAL----KGQSFEAPGGTVTVDP 321
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
66-325 |
1.60e-04 |
|
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];
Pssm-ID: 441483 [Multi-domain] Cd Length: 307 Bit Score: 43.37 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 66 KKTVYIGAALPltGGSQSYGIGVKNAVELAVEDANkmcpnikFELLVEDTGTNPQQALQKVQTLYAKGAR-LIVGPMTSG 144
Cdd:COG1879 31 AKGKTIGFVVK--TLGNPFFVAVRKGAEAAAKELG-------VELIVVDAEGDAAKQISQIEDLIAQGVDaIIVSPVDPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 145 EVSAVKSFADQNKIIIFSPSSTSPllgiPGDWVYRIVPTDFAQAAAIADLL-KTLGVKRAVIIYR-------NDAWGVGL 216
Cdd:COG1879 102 ALAPALKKAKAAGIPVVTVDSDVD----GSDRVAYVGSDNYAAGRLAAEYLaKALGGKGKVAILTgspgapaANERTDGF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 217 RNAITNESnklGINIVASQGYDPDPkafptavPEAIRKLSGALgQPGSDAAIIFVTFEDDGIAAIQAAASDPVLSKVRWI 296
Cdd:COG1879 178 KEALKEYP---GIKVVAEQYADWDR-------EKALEVMEDLL-QAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVV 246
|
250 260
....*....|....*....|....*....
gi 18161589 297 GTDGIAysDALikqvgKEMAAAKMLGTIA 325
Cdd:COG1879 247 GFDGSP--EAL-----QAIKDGTIDATVA 268
|
|
| PBP1_ABC_ligand_binding-like |
cd06341 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
107-363 |
4.73e-04 |
|
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: 42.29 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 107 KFELLVEDTGTNPQQALQKVQTLYAK-GARLIVGPMTSGEVSAVKSFADQNKIIIFSPSSTSPLLGIPGDWVYRIVPTDF 185
Cdd:cd06341 40 KVEYVWCDDQSDPATNLQAARQLVEDeKVFALVGSSSAASGSANDYLAQAGIPVVGGAGVSVWCFRNMFSNFFSLGGGGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 186 AQAAaiADLLKTLGVKRAVIIYRN-DAWGVGLRNAITNESNKLGINIVASQGYdPDPKAFPTAVPEAIRKlSGAlgqpgs 264
Cdd:cd06341 120 TTTY--GQYAAALGGTKAAVVVTDiPAASQQLAQQLAASLRAAGVEVVGTAPY-AAAAPDYTAVAQAAKA-AGA------ 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 265 DaAIIFVTFEDDGIAAIQAAASdpVLSKVRWIGTDGiAYSDALIKQVGKEMAAAKMLGTIAAPDPNDPKYQEFK---QRY 341
Cdd:cd06341 190 D-AVVGVLDPDVAARVLKAARA--QGLDLKVALSPS-GYDPSVLAAYGAALAGVSVASTFLPFEADTPAVKAYRaamAKY 265
|
250 260
....*....|....*....|..
gi 18161589 342 KAKYGKDPVAYDPYGYDAAMML 363
Cdd:cd06341 266 APELQDPLQQFALSGYIAADLF 287
|
|
| PBP1_GPC6A-like |
cd06361 |
ligand-binding domain of the promiscuous L-alpha-amino acid receptor GPRC6A which is a ... |
95-213 |
7.26e-04 |
|
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: 41.59 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 95 AVEDANK--MCPNIKFELLVEDTGTNPQQALQKVQTLYAKGARL-----------------IVGPmTSGEVS-AVKSFAD 154
Cdd:cd06361 44 AIEMINNstLLPGIKLGYEIYDTCSDVTKALQATLRLLSKFNSSnellecdytdyvppvkaVIGA-SYSEISiAVARLLN 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18161589 155 QNKIIIFSPSSTSPLLG----IPGdwVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWG 213
Cdd:cd06361 123 LQLIPQISYESSAPILSdklrFPS--FLRTVPSDFHQTKAMAKLISHFGWNWVGIIYTDDDYG 183
|
|
| PBP1_iGluR_Kainate |
cd06382 |
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate ... |
89-210 |
1.33e-03 |
|
N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the kainate receptors, non-NMDA ionotropic receptors which respond to the neurotransmitter glutamate. While this N-terminal domain belongs to the periplasmic-binding fold type 1 superfamily, the glutamate-binding domain of the iGluR is structurally homologous to the periplasmic-binding fold type 2. The LIVBP-like domain of iGluRs is thought to play a role in the initial assembly of iGluR subunits, but it is not well understood how this domain is arranged and functions in intact iGluR. Kainate receptors have five subunits, GluR5, GluR6, GluR7, KA1 and KA2, which are structurally similar to AMPA and NMDA subunits of ionotropic glutamate receptors. KA1 and KA2 subunits can only form functional receptors with one of the GluR5-7 subunits. Moreover, GluR5-7 can also form functional homomeric receptor channels activated by kainate and glutamate when expressed in heterologous systems. Kainate receptors are involved in excitatory neurotransmission by activating postsynaptic receptors and in inhibitory neurotransmission by modulating release of the inhibitory neurotransmitter GABA through a presynaptic mechanism. Kainate receptors are closely related to AMAP receptors. In contrast of AMPA receptors, kainate receptors play only a minor role in signaling at synapses and their function is not well defined.
Pssm-ID: 380605 Cd Length: 335 Bit Score: 40.67 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 89 KNAVELAVEDANKM--CPNIKFELLVED-TGTNPQQALQKVQTLYAKGARLIVGPmTSGEVSA-VKSFADQNKI--IIFS 162
Cdd:cd06382 14 EIAFKYAVDRINRErtLPNTKLVPDIERvPRDDSFEASKKVCELLEEGVAAIFGP-SSPSSSDiVQSICDALEIphIETR 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18161589 163 PSSTSPllgiPGDW----VYrivPTDFAQAAAIADLLKTLGVKRAVIIYRND 210
Cdd:cd06382 93 WDPKES----NRDTftinLY---PDPDALSKAYADLVKSLNWKSFTILYEDD 137
|
|
| PBP1_NPR_A |
cd06385 |
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A ... |
317-438 |
1.73e-03 |
|
Ligand-binding domain of type A natriuretic peptide receptor; Ligand-binding domain of type A natriuretic peptide receptor (NPR-A). NPR-A is one of three known single membrane-spanning natriuretic peptide receptors that regulate blood volume, blood pressure, ventricular hypertrophy, pulmonary hypertension, fat metabolism, and long bone growth. In mammals there are three natriuretic peptides: ANP, BNP, and CNP. NPR-A is highly expressed in kidney, adrenal, terminal ileum, adipose, aortic, and lung tissues. The rank order of NPR-A activation by natriuretic peptides is ANP>BNP>>CNP. Single allele-inactivating mutations in the promoter of human NPR-A are associated with hypertension and heart failure.
Pssm-ID: 380608 [Multi-domain] Cd Length: 408 Bit Score: 40.57 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 317 AAKMLGTIAAPDPNDPKYQEFKQRYKAKygkdpvAYDPYGYDAAMMLMQIACQLGTDD----SDKVKATLEQ-------- 384
Cdd:cd06385 270 AFQAVKIITYKEPDNPEYKEFLKQLKTE------AMEMFNFTVEDGLMNLIAASFHDGvllyAHAVNETLAHggtvtngs 343
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 385 ------WGRqgTYQGVTGKVYLDEAGDRAYpNYVIWGVALEGGQPKYVdaAYYYGTDRKI 438
Cdd:cd06385 344 aitqrmWNR--SFYGVTGYVKIDENGDRET-DFSLWDMDPETGAFQIV--SNYNGTSKEL 398
|
|
| PBP1_mGluR_groupIII |
cd06376 |
ligand-binding domain of the group III metabotropic glutamate receptor; Ligand-binding domain ... |
157-299 |
3.65e-03 |
|
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: 39.40 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18161589 157 KIIIFSPSSTSPLLGIPG--DWVYRIVPTDFAQAAAIADLLKTLGVKRAVIIYRNDAWG-VGLRNAITNESNKLGINIVA 233
Cdd:cd06376 131 QIPQISYASTAPELSDDRryDFFSRVVPPDSFQAQAMVDIVKALGWNYVSTLASEGNYGeKGVESFVQISREAGGVCIAQ 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18161589 234 SQGYDPDPKafPTAVPEAIRKLsgaLGQPGSDAAIIFVTfEDDGIAAIQAAASDPVLSKVRWIGTD 299
Cdd:cd06376 211 SEKIPRERR--TGDFDKIIKRL---LETPNARAVVIFAD-EDDIRRVLAAAKRANKTGHFLWVGSD 270
|
|
| |
