|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
50-323 |
1.46e-120 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 348.45 E-value: 1.46e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAk 129
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELG-VEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLI----GNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKD 205
Cdd:cd20008 79 DAGIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKYPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 206 VEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGT 285
Cdd:cd20008 159 IEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGVIKAL 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 1519460899 286 AVQMPTMMGSMGVQIVVDILGGKAPAEKDVDTGVTMVT 323
Cdd:cd20008 239 VVQDPYQMGYEGVKTAVKALKGEEIVEKNVDTGVTVVT 276
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
50-323 |
2.26e-90 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 271.42 E-value: 2.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd20005 1 YIAVISKGFQHQFWKAVKKGAEQAAKELG-VKITFEGPDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIV 209
Cdd:cd20005 80 EKGIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDIKVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQM 289
Cdd:cd20005 160 NVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAGSVTQN 239
|
250 260 270
....*....|....*....|....*....|....
gi 1519460899 290 PTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVT 323
Cdd:cd20005 240 PYGMGYKTVKAAVKALKGE-EVEKLIDTGAKWYD 272
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
3-326 |
3.12e-89 |
|
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: 269.87 E-value: 3.12e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 3 KSIGILLALVLVVSMFAGCGSKPAPSSAapadsssaapseaTAKETIKIALVTKMVDSPYWQTVKRAAEEKAKELGnVEV 82
Cdd:COG1879 1 KRLALLAAVLALALALAACGSAAAEAAA-------------AAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELG-VEL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 83 THLgpPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAEC 162
Cdd:COG1879 67 IVV--DAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 163 AKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKnNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGAN 242
Cdd:COG1879 145 AEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALK-EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAAN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 243 DQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQMPTMMGSMGVQIVVDILGGKAPaEKDVDTGVTMV 322
Cdd:COG1879 224 DGMALGAAQALKAAGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEV-PKEILTPPVLV 302
|
....
gi 1519460899 323 TFEN 326
Cdd:COG1879 303 TKEN 306
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
50-323 |
5.39e-86 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 260.22 E-value: 5.39e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSP--YWQTVKRAAEEKAKELgNVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQK 127
Cdd:cd20006 1 KIALILKSSDPNsdFWQTVKSGAEAAAKEY-GVDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKnNHKDVE 207
Cdd:cd20006 80 AKKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALA-EYPNIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 208 IVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNS-DDIKAgLKSGTIKGTA 286
Cdd:cd20006 159 IVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGKVKVVGFDSSvEEIQL-LEEGIIDALV 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1519460899 287 VQMPTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVT 323
Cdd:cd20006 238 VQNPFNMGYLSVQAAVDLLNGK-KIPKRIDTGSVVIT 273
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
50-321 |
5.71e-83 |
|
periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380478 [Multi-domain] Cd Length: 268 Bit Score: 252.49 E-value: 5.71e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTeaDIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELG-VELVVLDAQG--DVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKAN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPV-YDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNnHKDVEI 208
Cdd:cd01536 78 AAGIPVVAVDTDIDGGGdVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKK-YPDIEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 209 VGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:cd01536 157 VAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDATVAQ 236
|
250 260 270
....*....|....*....|....*....|...
gi 1519460899 289 MPTMMGSMGVQIVVDILGGKaPAEKDVDTGVTM 321
Cdd:cd01536 237 DPYLQGYLAVEAAVKLLNGE-KVPKEILTPVTL 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
50-323 |
1.30e-77 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 238.78 E-value: 1.30e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLG-VKIIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIV 209
Cdd:cd06310 80 DKGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQM 289
Cdd:cd06310 160 ASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQN 239
|
250 260 270
....*....|....*....|....*....|....
gi 1519460899 290 PTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVT 323
Cdd:cd06310 240 PYEIGYEGIKLALKLLKGE-EVPKNIDTGAELIT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
50-323 |
2.89e-74 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 230.20 E-value: 2.89e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELG-VEIYWRGPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIV 209
Cdd:cd20004 80 AQGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSASTTDRERGFLEALKKLAPGLKVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQM 289
Cdd:cd20004 160 DDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAGKVKFIGFDASDLLLDALRAGEISALVVQD 239
|
250 260 270
....*....|....*....|....*....|....
gi 1519460899 290 PTMMGSMGVQIVVDILGGKAPaEKDVDTGVTMVT 323
Cdd:cd20004 240 PYRMGYLGVKTAVAALRGKPV-PKRIDTGVVLVT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
50-323 |
1.52e-71 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 223.27 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTeADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELG-VELDVQGPPT-FDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEP-VYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKdVEI 208
Cdd:cd20007 79 DAGIKVVTVDTTLGDPsFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKKYPG-IKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 209 VGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:cd20007 158 LGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGFDASPAQVEQLKAGTIDALIAQ 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1519460899 289 MPTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVT 323
Cdd:cd20007 238 KPAEIGYLAVEQAVAALTGK-PVPKDILTPFVVIT 271
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
50-323 |
1.49e-67 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 212.83 E-value: 1.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPtEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELG-VNVEFVGPQ-KSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNnHKDVEIV 209
Cdd:cd06314 79 DKGIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKG-SPGIEIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQM 289
Cdd:cd06314 158 DPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQR 237
|
250 260 270
....*....|....*....|....*....|....
gi 1519460899 290 PTMMGSMGVQIVVDILGGKAPAEKDVDTGVTMVT 323
Cdd:cd06314 238 PYEMGYLSVKLLYKLLKGGKPVPDVIDTGVDVVT 271
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
50-326 |
2.76e-65 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 207.50 E-value: 2.76e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLG-VKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGI-------SEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNN 202
Cdd:cd06320 80 KKGIPVINLDDAVdadalkkAGGKVTSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 203 HKdVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTI 282
Cdd:cd06320 160 PG-LKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTDGIPEAKKSIKAGEL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1519460899 283 KGTAVQMPTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVTFEN 326
Cdd:cd06320 239 TATVAQYPYLEGAMAVEAALRLLQGQ-KVPAVVATPQALITKDN 281
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
51-309 |
3.39e-61 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 196.38 E-value: 3.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGNVEVthLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKD 130
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVI--VVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 131 AGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIVG 210
Cdd:pfam13407 79 AGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 211 V-QYCDSDPTKAANQATDFITANPD-IKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:pfam13407 159 EvEGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQ 238
|
250 260
....*....|....*....|.
gi 1519460899 289 MPTMMGSMGVQIVVDILGGKA 309
Cdd:pfam13407 239 DPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
50-315 |
5.14e-58 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 188.18 E-value: 5.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPptEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANG-DELITRDP--QLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVY-DAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAgTQTAIDRETGFTEEIKNNhKDVEI 208
Cdd:cd19971 78 EAGIPVINVDTPVKDTDLvDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPT-AESCVDRIDGFLDAIKKN-PKFEV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 209 VGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:cd19971 156 VAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLGDILVYGVDGSPDAKAAIKDGKMTATAAQ 235
|
250 260
....*....|....*....|....*..
gi 1519460899 289 MPTMMGSMGVQIVVDILGGKaPAEKDV 315
Cdd:cd19971 236 SPIEIGKKAVETAYKILNGE-KVEKEI 261
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
53-321 |
4.99e-56 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 183.69 E-value: 4.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 53 LVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTeADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAG 132
Cdd:cd19969 4 MVTFKSGHPYWDDVKEGFEDAGAELG-VKTEYTGPAT-ADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 133 IPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNfAAGTQTAIDRETGFTEEIKNNhKDVEIVGVQ 212
Cdd:cd19969 82 IPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLT-GPGQPNHEERVEGFKEAFAEY-PGIEVVAVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 213 YCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQMPTM 292
Cdd:cd19969 160 DDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVIDASIAQRPWM 239
|
250 260 270
....*....|....*....|....*....|....*....
gi 1519460899 293 MGSMGVQIVVDI----------LGGKAPAEKDVDTGVTM 321
Cdd:cd19969 240 MGYWSLQFLYDLanglvkdawqTAGVNPLPPYVDTGITI 278
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
50-323 |
1.88e-54 |
|
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380546 [Multi-domain] Cd Length: 268 Bit Score: 179.03 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELG-VELVVLD--AQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEAN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKdVEIV 209
Cdd:cd06323 78 EAGIPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYPK-INVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDsIMVVGFDNSDDIKAGLKSGTIKGTAVQM 289
Cdd:cd06323 157 ASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKD-VIVVGFDGTPDAVKAVKDGKLAATVAQQ 235
|
250 260 270
....*....|....*....|....*....|....
gi 1519460899 290 PTMMGSMGVQIVVDILGGKAPAEKdVDTGVTMVT 323
Cdd:cd06323 236 PEEMGAKAVETADKYLKGEKVPKK-IPVPLKLVT 268
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
50-323 |
6.59e-51 |
|
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380525 [Multi-domain] Cd Length: 296 Bit Score: 170.89 E-value: 6.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPpTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06302 1 KIAFVPKVVGIPYFDAAEEGAKKAAKELG-VEVVYTGP-TQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLA-TNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEI 208
Cdd:cd06302 79 DAGIKVITWDSDAPPSARDYFVNqADDEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKYPDIEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 209 VGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:cd06302 159 VDTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGKVAVTGIGLPNTARPYLKDGSVKEGVLW 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1519460899 289 MPTMMGSMGVQIVVDILGGKA-PAEKDVDTGVTMVT 323
Cdd:cd06302 239 DPAKLGYLTVYAAYQLLKGKGfTEDSDDVGTGGKVK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
50-326 |
1.78e-50 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 169.08 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGNVEVTHlgpPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTY---DQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLAN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKG----KVAIVNFAAGTQTAIDRETGFTEEIKnnHKD 205
Cdd:cd06319 78 EAKIPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKENGwgggSVGIIAIPQSRVNGQARTAGFEDALE--EAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 206 VEIVGV-QYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKG 284
Cdd:cd06319 156 VEEVALrQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDG 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1519460899 285 TAVQMPTMMGSMGVQIVVDILGGKAPAEKDVDTGVTMVTFEN 326
Cdd:cd06319 236 TVAQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSEN 277
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
50-308 |
2.81e-50 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 168.58 E-value: 2.81e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGNVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEANGYELLVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDS----------GISEPvydaFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEI 199
Cdd:cd19970 81 DAGIAVINIDNrldadalkegGINVP----FVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 200 KNNhkDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKS 279
Cdd:cd19970 157 EEA--GMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLLKD 234
|
250 260
....*....|....*....|....*....
gi 1519460899 280 GTIKGTAVQMPTMMGSMGVQIVVDILGGK 308
Cdd:cd19970 235 GKMLATIDQHPAKQAVYGIEYALKMLNGE 263
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
61-322 |
1.42e-49 |
|
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.
Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 166.57 E-value: 1.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 61 PYWQTVKRAAEEKAKELGNVEVTHlgppTEA--DIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMI 138
Cdd:cd06308 12 PWRAAMNEEIKAEAAKYPNVELIV----TDAqgDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 139 DSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKnNHKDVEIVGVQYCDSDP 218
Cdd:cd06308 88 DRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIA-KYPGIKIVASQDGDWLR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 219 TKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDN-SDDIKAGLKSGTIKGTAVqMPTmMGSMG 297
Cdd:cd06308 167 DKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGlPEAGEKAVKDGILAATFL-YPT-GGKEA 244
|
250 260
....*....|....*....|....*
gi 1519460899 298 VQIVVDILGGKaPAEKDVDTGVTMV 322
Cdd:cd06308 245 IEAALKILNGE-KVPKEIVLPTPLI 268
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
50-323 |
9.42e-48 |
|
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380622 [Multi-domain] Cd Length: 272 Bit Score: 162.11 E-value: 9.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELG-YEVTVFD--HQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGI-SEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNnHKDVEI 208
Cdd:cd19967 78 DAGIPVFLIDREInAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQ-YPELKM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 209 VGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:cd19967 157 VAQQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAGDVIIVGFDGSNDVRDAIKEGKISATVLQ 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1519460899 289 MPTMMGSMGVQIVVDIL-GGKAPAEKDVDTGVTMVT 323
Cdd:cd19967 237 PAKLIARLAVEQADQYLkGGSTGKEEKQLFDCVLIT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
50-323 |
1.84e-47 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 161.30 E-value: 1.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKA 128
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINpGAKVTVVD--ARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 129 KDAGIPVVMIDSGiSEPVyDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNfaaGTQ--TAIDRETGFTEEIKNNhKDV 206
Cdd:cd06321 79 KDAGIIVVAVDVA-AEGA-DATVTTDNVQAGYLACEYLVEQLGGKGKVAIID---GPPvsAVIDRVNGCKEALAEY-PGI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 207 EIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDsIMVVGFDNSDDIKAGLK--SGTIKG 284
Cdd:cd06321 153 KLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDD-IVITSVDGSPEAVAALKreGSPFIA 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1519460899 285 TAVQMPTMMGSMGVQIVVDILGGKAPAEKDVDTGVTMVT 323
Cdd:cd06321 232 TAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLVT 270
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
51-317 |
1.96e-47 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 162.35 E-value: 1.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKD 130
Cdd:PRK09701 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLG-VSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 131 AGIPVVMIDSGI-------SEPVYDAFLATNNVQAGAECAKLMSDLIGNK-GKVAIVNFAAGTQTAIDRETGFTEEIKNN 202
Cdd:PRK09701 106 KGIYLVNLDEKIdmdnlkkAGGNVEAFVTTDNVAVGAKGASFIIDKLGAEgGEVAIIEGKAGNASGEARRNGATEAFKKA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 203 hKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTI 282
Cdd:PRK09701 186 -SQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQM 264
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1519460899 283 KGTAVQMPTMMGSMGVQIVVD-------ILGGKAPAEKDVDT 317
Cdd:PRK09701 265 TATVAQNPADIGATGLKLMVDaeksgkvIPLDKAPEFKLVDS 306
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
48-323 |
1.41e-46 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 158.98 E-value: 1.41e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 48 TIKIALVTkmVDSPYWQTVKRAAEEKAKELGnVEVTHLGPptEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQK 127
Cdd:cd06322 1 TIGVSLLT--LQHPFFVDIKDAMKKEAAELG-VKVVVADA--NGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLM-SDLIGNKGKVAIVNFAAgTQTAIDRETGFTEEIKNnHKDV 206
Cdd:cd06322 76 ANEAGIPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYAlKALLGGGGKIAIIDYPE-VESVVLRVNGFKEAIKK-YPNI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 207 EIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDD-IKAGLKSGTIKGT 285
Cdd:cd06322 154 EIVAEQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVIGFDGNPEaIKAIAKGGKIKAD 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1519460899 286 AVQMPTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVT 323
Cdd:cd06322 234 IAQQPDKIGQETVEAIVKYLAGE-TVEKEILIPPKLYT 270
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
50-314 |
5.26e-45 |
|
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380658 Cd Length: 298 Bit Score: 155.51 E-value: 5.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELgNVEVTHLGPpTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd20003 1 TIAMIPKLVGVPYFTAAGQGAQEAAKEL-GVDVTYDGP-TEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLatNNV---QAGAECAKLMSDLIGNKGKVAIV--NFAAGTQTAIDREtgFTEEIKNNHK 204
Cdd:cd20003 79 KKGIKVVTWDSDVNPDARDFFV--NQAtpeGIGKTLVDMVAEQTGEKGKVAIVtsSPTATNQNAWIKA--MKAYIAEKYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 205 DVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKG 284
Cdd:cd20003 155 DMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAVTGLSTPNVMRPYVKDGTVKS 234
|
250 260 270
....*....|....*....|....*....|
gi 1519460899 285 TAVQMPTMMGSMGVQIVVDILGGKAPAEKD 314
Cdd:cd20003 235 VVLWDVVDLGYLAVYVARALADGTLLKVGD 264
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
64-320 |
1.70e-42 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 148.36 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 64 QTVKRAAEEKAKELGNVEvthlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGIS 143
Cdd:cd19972 19 QSVEAEAKKKGYKVITVD-------AKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 144 EPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNhKDVEIVGVQYCDSDPTKAAN 223
Cdd:cd19972 92 DAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEA-PGIKVVAEQTADWDQDEGFK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 224 QATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQMPTMMGSMGVQIVVD 303
Cdd:cd19972 171 VAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGRLAVDSAID 250
|
250
....*....|....*...
gi 1519460899 304 ILGGKA-PAEKDVDTGVT 320
Cdd:cd19972 251 LLNGKAvPKEQLQDAVLT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
70-322 |
6.00e-41 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 144.04 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 70 AEEKAKELGNVEVThlgPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGISEPVYDA 149
Cdd:cd06311 21 AEKQAKELADLEYK---LVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 150 FLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHkDVEIVGVQYCDSDPTKAANQATDFI 229
Cdd:cd06311 98 YVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNP-GIKILAMQAGDWTREDGLKVAQDIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 230 TANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSG--TIKGTAVQMPTMMGSmGVQIVVDILGG 307
Cdd:cd06311 177 TKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKVMTGGGGSQEYFKRIMDGdpIWPASATYSPAMIAD-AIKLAVLILKG 255
|
250
....*....|....*
gi 1519460899 308 KAPAEKDVDTGVTMV 322
Cdd:cd06311 256 GKTVEKEVIIPSTLV 270
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
50-322 |
2.45e-40 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380620 [Multi-domain] Cd Length: 272 Bit Score: 142.80 E-value: 2.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEkAKELGNVEVTHLGPPTeADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd19965 1 KFVFVTHVTTNPFFQPVKKGMDD-ACELLGAECQFTGPQT-FDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVM--IDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNK-GKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDV 206
Cdd:cd19965 79 DAGIPVVAfnVDAPGGENARLAFVGQDLYPAGYVLGKRIAEKFKPGgGHVLLGISTPGQSALEQRLDGIKQALKEYGRGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 207 EIVGVQYcDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTA 286
Cdd:cd19965 159 TYDVIDT-GTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDLVPEVLQGIKAGYIDFTI 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 1519460899 287 VQMPTMMGSMGV-QIVVDILGGKAPAekDVDTGVTMV 322
Cdd:cd19965 238 DQQPYLQGFYPVmQLFLYKKFGLSPF--DIDTGAAVV 272
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
50-326 |
1.69e-39 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 140.48 E-value: 1.69e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKElGNVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKE-LNVDLVVLD--GNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFtEEIKNNHKDVEIV 209
Cdd:cd06313 78 EAGIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGI-ENVLKKYPDIKVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPD-IKGIWGANDQSAVGVAQAVTEKGKGDsIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:cd06313 157 AEQTANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDD-IPVVGIDGIEDALQAVKSGELIATVLQ 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 1519460899 289 MPTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVTFEN 326
Cdd:cd06313 236 DAEAQGKGAVEVAVDAVKGE-GVEKKYYIPFVLVTKDN 272
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
51-326 |
1.83e-39 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 140.59 E-value: 1.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPptEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKD 130
Cdd:cd06317 2 IALVQINQQAQFFNQINQGAQAAAKDLG-VDLVVFNA--NDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 131 AGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLI----GNKGKVAIVNFAAgTQTAIDRETGFTEEIKNNHKdV 206
Cdd:cd06317 79 AGIPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGKYAADYIkaelGGQAKIGVVGALS-SLIQNQRQKGFEEALKANPG-V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 207 EIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDD-IKAGLKSGTIKGT 285
Cdd:cd06317 157 EIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQaIFLGIDEGVLQAV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1519460899 286 AVQMPTMMGSMGVQIVVDILGGKAPaEKDVDTGVTMVTFEN 326
Cdd:cd06317 237 VQQDPEKMGYEAVKAAVKAIKGEDV-EKTIDVPPTIVTKEN 276
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
62-333 |
1.32e-37 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 136.22 E-value: 1.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 62 YWQTVKRAAEEKAKELGNVEVThlgpptEADIDKQVQI--IETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMID 139
Cdd:cd19996 17 MIAEFEAEAAKLKKLIKELIYT------DAQGDTQKQIadIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 140 SGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKnNHKDVEIVGVQYCDSDPT 219
Cdd:cd19996 91 SGVGSDKYTAFVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGIAGVSVSEDRWAGAKEVFK-EYPGIKIVGEVYADWDYA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 220 KAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKgDSIMVVGFDNSDDIKAGLKSGTIKGTAVQMPTMMGSMGVQ 299
Cdd:cd19996 170 KAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGR-PLVPMTGEDNNGFLKAWKELPGFKSIAPSYPPWLGATALD 248
|
250 260 270
....*....|....*....|....*....|....*..
gi 1519460899 300 IVVDILGGKaPAEKDVDTGVTMVTFEN---YTRPAMD 333
Cdd:cd19996 249 AALAALEGE-PVPKYVYIPLPVITDENldqYVKPDLD 284
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
50-326 |
1.33e-37 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 135.62 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLG-VELVVTD--AQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGIS-EPVYDAFLATNNVQAGAECAKLMSDLIGNK-GKVAIVNFAAGTQTAIDRETGFTEEI------KN 201
Cdd:cd06318 78 AAGIPVITVDSALDpSANVATQVGRDNKQNGVLVGKEAAKALGGDpGKIIELSGDKGNEVSRDRRDGFLAGVneyqlrKY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 202 NHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGT 281
Cdd:cd06318 158 GKSNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQKEALKLIKDGK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1519460899 282 IKGTAVQMPTMMGSMGVQIVVDILGGKAPAEKDVDTGVTMVTFEN 326
Cdd:cd06318 238 YVATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPTALITKDN 282
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
50-318 |
5.91e-37 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380535 [Multi-domain] Cd Length: 272 Bit Score: 133.90 E-value: 5.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDS-PYWQTVKRAAEEKAKELGnVEVTHLGPPTeADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKA 128
Cdd:cd06312 1 TIYVISHGSPSdPFWSVVKKGAKDAAKDLG-VTVQYLGPQN-NDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 129 KDAGIPVVMIDSGISEPV----YDAFLATNNVQAGAECAKLMsdLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHK 204
Cdd:cd06312 79 VAAGIPVIAINSGDDRSKerlgALTYVGQDEYLAGQAAGERA--LEAGPKNALCVNHEPGNPGLEARCKGFADAFKGAGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 205 DVEIVGVqycDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKG 284
Cdd:cd06312 157 LVELLDV---GGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILF 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1519460899 285 TAVQMPTMMGSMGVQIVVDILG-GKAPAEKDVDTG 318
Cdd:cd06312 234 AIDQQPYLQGYLAVVFLYLYKRyGTLPPPEPILTG 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
51-323 |
1.18e-36 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380628 [Multi-domain] Cd Length: 285 Bit Score: 133.36 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKD 130
Cdd:cd19973 2 IGLITKTDTNPFFVKMKEGAQKAAKALG-IKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 131 AGIPVVMIDSGIsEPV--YDAFLATNNVQAG---AECAKlmSDLIGNKGKVAIVNFAAGTQTAIDRETGF---------T 196
Cdd:cd19973 81 AGVLVIALDTPT-DPIdaADATFATDNFKAGvliGEWAK--AALGAKDAKIATLDLTPGHTVGVLRHQGFlkgfgidekD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 197 EEIKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAG 276
Cdd:cd19973 158 PESNEDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLIVSVDGGCPGVKD 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1519460899 277 LKSGTIKGTAVQMPTMMGSMGVQIVVDIL-GGKAPAEKDVDTGVTMVT 323
Cdd:cd19973 238 VKDGIIGATSQQYPLRMAALGVEAIAAFAkTGGTKGSGFTDTGVTLVT 285
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
59-323 |
3.51e-36 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 131.91 E-value: 3.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 59 DSPYWQTVKRAAEEKAKELGN----VEVTHLgppTEADIDKQVQIIETCInDDYDGIILAACDKDALIAPVQKAKDAGIP 134
Cdd:cd06307 10 ENPFYELLRRAIEAAAAALRDrrvrLRIHFV---DSLDPEALAAALRRLA-AGCDGVALVAPDHPLVRAAIDELAARGIP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 135 VVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNK-GKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIVGVQY 213
Cdd:cd06307 86 VVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRpGKVLVILGSHRFRGHEEREAGFRSVLRERFPDLTVLEVLE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 214 CDSDPTKAANQATDFITANPDIKGIW---GANDqsavGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIkgTAV--Q 288
Cdd:cd06307 166 GLDDDELAYELLRELLARHPDLVGIYnagGGNE----GIARALREAGRARRVVFIGHELTPETRRLLRDGTI--DAVidQ 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1519460899 289 MPTMMGSMGVQIVVDILGGKAPAEKDVDTGVTMVT 323
Cdd:cd06307 240 DPELQARRAIEVLLAHLGGKGPAPPQPPIPIEIIT 274
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
60-322 |
1.19e-35 |
|
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.
Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 130.01 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 60 SPYWQTVKRAAEEKAKELGnVEVTHLgpptEA----DIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPV 135
Cdd:cd06306 11 DSYWVGVNYGIVDEAKRLG-VKLTVY----EAggytNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 136 VMIDSGISEPVYDAFLATNNVQAGAECAK-LMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNhkDVEIVGVQYC 214
Cdd:cd06306 86 IDLVNGIDSPKVAARVLVDFYDMGYLAGEyLVEHHPGKPVKVAWFPGPAGAGWAEDREKGFKEALAGS--NVEIVATKYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 215 DSDPTKAANQATDFITANPDIKGIWGaNDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAVQMPTMMG 294
Cdd:cd06306 164 DTGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQG 242
|
250 260
....*....|....*....|....*...
gi 1519460899 295 SMGVQIVVDILGGKaPAEKDVDTGVTMV 322
Cdd:cd06306 243 RIAVDQAVRALEGK-PVPKHVGPPILVV 269
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
60-312 |
4.28e-35 |
|
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.
Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 129.26 E-value: 4.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 60 SPYWQTVKRAAEEKAKELGnVEVTHLgpPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMID 139
Cdd:cd06309 11 SPWRVANTKSIKEAAKKRG-YELVYT--DANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 140 SGI---SEPVYDAFLATNNVQAGAECAKLMSDLIGNK-GKVAIVNFAAGTQTAIDRETGFTEEIKnNHKDVEIVGVQYCD 215
Cdd:cd06309 88 RTIdgeDGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGkGNVVELQGTAGSSVAIDRSKGFREVIK-KHPNIKIVASQSGN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 216 SDPTKAANQATDFITANP-DIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSDDIKAGLKSGTIKGTaVQMPTM 292
Cdd:cd06309 167 FTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLkpGKDVLVVGIDGQKDALEAIKAGELNAT-VECNPL 245
|
250 260
....*....|....*....|
gi 1519460899 293 MGSMGVQIVVDILGGKAPAE 312
Cdd:cd06309 246 FGPTAFDTIAKLLAGEKVPK 265
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
50-308 |
5.23e-34 |
|
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380655 Cd Length: 298 Bit Score: 126.60 E-value: 5.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPpTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELG-GELIFVGP-TTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLA-TNNVQAGAECAKLMSDLIGNKGKVAIVnfaAGTQTAIDRET---GFTEEI-KNNHK 204
Cdd:cd20000 79 AAGIKVVTFDSDVAPEARDLFVNqADADGIGRAQVDMMAELIGGEGEFAIL---SATPTATNQNAwidAMKKELaSPEYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 205 DVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGAndqSAVGV---AQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGT 281
Cdd:cd20000 156 GMKLVKVAYGDDDAQKSYQEAEALLQAYPDLKGIIAP---TTVGIaaaARALEDSGLKGKVKVTGLGLPSEMAKYVKDGT 232
|
250 260
....*....|....*....|....*..
gi 1519460899 282 IKGTAVQMPTMMGSMGVQIVVDILGGK 308
Cdd:cd20000 233 VPAFALWNPIDLGYLAAYAAAALAQGE 259
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
49-316 |
1.91e-33 |
|
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.
Pssm-ID: 380524 [Multi-domain] Cd Length: 272 Bit Score: 124.27 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 49 IKIALVTKMVDSPYWQTVKRAAEEKAKELGNVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKA 128
Cdd:cd06301 1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVD--AQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 129 KDAGIPVVMIDSG-ISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNnHKDVE 207
Cdd:cd06301 79 ADAGIPLVYVNREpDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAK-YPGMK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 208 IVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAV 287
Cdd:cd06301 158 IVAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDILVAGIDATPDALKAMKAGRLDATVF 237
|
250 260
....*....|....*....|....*....
gi 1519460899 288 QMPTMMGSMGVQIVVDILGGkAPAEKDVD 316
Cdd:cd06301 238 QDAAGQGETAVDVAVKAAKG-EEVESDIW 265
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
45-316 |
7.01e-32 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 120.96 E-value: 7.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 45 AKETIkiALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIA 123
Cdd:PRK10653 25 AKDTI--ALVVSTLNNPFFVSLKDGAQKEADKLGyNLVVLD----SQNNPAKELANVQDLTVRGTKILLINPTDSDAVGN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 124 PVQKAKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNh 203
Cdd:PRK10653 99 AVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAH- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 204 kDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDsIMVVGFDNSDDIKAGLKSGTIK 283
Cdd:PRK10653 178 -KFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-VMVVGFDGTPDGIKAVNRGKLA 255
|
250 260 270
....*....|....*....|....*....|....
gi 1519460899 284 GTAVQMPTMMGSMGVQIVVDILGG-KAPAEKDVD 316
Cdd:PRK10653 256 ATIAQQPDQIGAIGVETADKVLKGeKVEAKIPVD 289
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
50-323 |
1.58e-31 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 119.41 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLG-VKLVVLD--AQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKdVEIV 209
Cdd:cd19968 78 KAGIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGPK-IKVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANP-DIKGIWGANDQSAVGVAQAVTEKG-KGDSIMVVGFDNSDDIKAGLKSGTIKGTAV 287
Cdd:cd19968 157 FEQTGNFERDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAGlDLKKVKVIGFDAVPDALQAIKDGELYATVE 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1519460899 288 QMPTMMGSMGVQIVVDILGGKaPAEKDVDTGVTMVT 323
Cdd:cd19968 237 QPPGGQARTALRILVDYLKDK-KAPKKVNLKPKLIT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
50-329 |
1.93e-29 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 114.26 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLgppTEADID--KQVQIIETCINDDYDGIILAACDKDALIAPVQK 127
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEELG-IEVVAV---TDANFDpaKQITDLETLIALKPDIIISIPVDPVATAAAYKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMID---SGISEPV-YDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNH 203
Cdd:cd06316 77 VADAGIKLVFMDnvpDGLEAGKdYVSVVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKEKY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 204 KDVEIVGVQYcDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMV---VGFDNSDDIkagLKSG 280
Cdd:cd06316 157 PDIKIVAEQG-FADPNDAEEVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITtvdLGTEIALDM---AKGG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1519460899 281 TIKGTAVQMPTMMGS-MGVQIVVDILGGKAPAEKDVDTgvTMVTFENYTR 329
Cdd:cd06316 233 NVKGIGAQRPYDQGVaEALAAALALLGKEVPPFIGVPP--LAVTKDNLLE 280
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
64-326 |
6.34e-29 |
|
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380523 [Multi-domain] Cd Length: 302 Bit Score: 113.19 E-value: 6.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 64 QTVKRAAEEKAKE--LGNVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSG 141
Cdd:cd06300 19 ASLKADAAQSGQKglVKELIVAN----SNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 142 ISEPvyDAFLATNN-VQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNhKDVEIVGVQYCDSDPTK 220
Cdd:cd06300 95 VTSP--DAYNVSNDqVEWGRLGAKWLFEALGGKGNVLVVRGIAGAPASADRHAGVKEALAEY-PGIKVVGEVFGGWDEAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 221 AANQATDFITANPDIKGIWGANDqSAVGVAQAVTEKGKgDSIMVVGFDNSDDIKAGLKSGTI--KGTAVQMPTMMGSMGV 298
Cdd:cd06300 172 AQTAMLDFLATHPQVDGVWTQGG-EDTGVLQAFQQAGR-PPVPIVGGDENGFAKQWWKHPKKglTGAAVWPPPAIGAAGL 249
|
250 260
....*....|....*....|....*...
gi 1519460899 299 QIVVDILGGKAPAEKDVDTGVTMVTFEN 326
Cdd:cd06300 250 EVALRLLEGQGPKPQSVLLPPPLITNDD 277
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
50-307 |
1.38e-28 |
|
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380528 [Multi-domain] Cd Length: 273 Bit Score: 111.62 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLG-GTVIVFD--ANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYdAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIdRETGFTEEIKNNhKDVEIV 209
Cdd:cd06305 78 DAGIPVVTFDTDSQVPGV-NNITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDK-RYDIYKAVLKAN-PGIKKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPT---KAANQATDFITANPD--IKGIWGANDQSAVGVAQAVTEKGKGDsIMVVGFDNS-DDIKAGLKSGTI- 282
Cdd:cd06305 155 VAELGDVTPNtaaDAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTD-IKVYGVDISnQDLELMADEGSPw 233
|
250 260
....*....|....*....|....*
gi 1519460899 283 KGTAVQMPTMMGSMGVQIVVDILGG 307
Cdd:cd06305 234 VATAAQDPALIGTVAVRNVARKLAG 258
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
50-308 |
2.83e-28 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380656 Cd Length: 296 Bit Score: 111.21 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTeADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd20001 1 TIAVVVKVTGIAWFDRMETGVEQFAKDTG-VNVYQIGPAT-ADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMID-SGISEPVYD--AFlatNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDV 206
Cdd:cd20001 79 DAGIVVITHEaSNLKNVDYDveAF---DNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKANYPDM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 207 EIV-GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGT 285
Cdd:cd20001 156 LLVtDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGKIAVVGTGLPSVAGEYLEDGTIDYI 235
|
250 260
....*....|....*....|...
gi 1519460899 286 AVQMPTMMGSMGVQIVVDILGGK 308
Cdd:cd20001 236 QFWDPADAGYAMNALAVMVLEGE 258
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
59-282 |
3.99e-28 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380547 [Multi-domain] Cd Length: 317 Bit Score: 111.16 E-value: 3.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 59 DSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETcinddydgiILAACDK-DALIAPVQK--------- 127
Cdd:cd06324 11 DEPFWQNVTRFMQAAAKDLGiELEVLY----ANRNRFKMLELAEE---------LLARPPKpDYLILVNEKgvapellel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISE-------------PVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAA-----GTQTAI 189
Cdd:cd06324 78 AEQAKIPVFLINNDLTDeerallgkprekfKYWLGSIVPDNEQAGYLLAKALIKAARKKSDDGKIRVLAisgdkSTPASI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 190 DRETGFTEEIKNnHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGF 267
Cdd:cd06324 158 LREQGLRDALAE-HPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLkpGKDVLVGGI 236
|
250
....*....|....*
gi 1519460899 268 DNSDDIKAGLKSGTI 282
Cdd:cd06324 237 DWSPEALQAVKDGEL 251
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
51-322 |
2.85e-27 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 109.13 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVThlgpPTEADIDKQVQIIETCINDDYDGIILAACDKDAliAPVQKAK 129
Cdd:COG1609 64 IGVVVPDLSNPFFAELLRGIEEAARERGyQLLLA----NSDEDPEREREALRLLLSRRVDGLILAGSRLDD--ARLERLA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDaFLATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIV 209
Cdd:COG1609 138 EAGIPVVLIDRPLPDPGVP-SVGVDNRAGARLATEHLIEL-GHR-RIAFIGGPADSSSARERLAGYREALAEAGLPPDPE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSDDikAGLKSGTIkgTAV 287
Cdd:COG1609 215 LVVEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLrvPEDVSVVGFDDIPL--ARYLTPPL--TTV 290
|
250 260 270
....*....|....*....|....*....|....*.
gi 1519460899 288 QMPT-MMGSMGVQIVVDILGGKAPAEKDVDTGVTMV 322
Cdd:COG1609 291 RQPIeEMGRRAAELLLDRIEGPDAPPERVLLPPELV 326
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
51-315 |
5.20e-26 |
|
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.
Pssm-ID: 380491 [Multi-domain] Cd Length: 264 Bit Score: 104.14 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDAliAPVQKAK 129
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERGySLLLCN----TDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDaFLATNNVQAGAECAKLmsdLIGnKG--KVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVE 207
Cdd:cd06267 76 AAGIPVVLIDRRLDGLGVD-SVVVDNYAGAYLATEH---LIE-LGhrRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 208 IVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDN---SDDIKAGLksgti 282
Cdd:cd06267 151 PELVVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLrvPEDISVVGFDDiplAALLTPPL----- 225
|
250 260 270
....*....|....*....|....*....|....
gi 1519460899 283 kgTAVQMPT-MMGSMGVQIVVDILGGKAPAEKDV 315
Cdd:cd06267 226 --TTVRQPAyEMGRAAAELLLERIEGEEEPPRRI 257
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
50-314 |
9.61e-25 |
|
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.
Pssm-ID: 380657 Cd Length: 295 Bit Score: 101.63 E-value: 9.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELgNVEVTHLGPPTeADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd20002 1 TIVTVVKLAGIPWFNRMEQGVKKAGKEF-GVNAYQVGPAD-ADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDS-GISEPVYDAFLAtNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEI 208
Cdd:cd20002 79 EKGIVVITHESpGQKGADWDVELI-DNEKFGEAQMELLAKEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNMKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 209 VGVQYCDSDPTKAANQAT-DFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIKGTAV 287
Cdd:cd20002 158 VTDRIPGGEDVDVSRQTTlELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSITEGYL 237
|
250 260
....*....|....*....|....*..
gi 1519460899 288 QMPTMMGSMGVQIVVDILGGKAPAEKD 314
Cdd:cd20002 238 WDPADAGYAMVYIAKMLLDGKRKEIGD 264
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
63-314 |
1.85e-24 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 100.74 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 63 WQTVKRAAEEKAKELGnVEVthLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGI 142
Cdd:cd19992 14 WQKDKEYMEEEAKELG-VEL--IFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 143 SEPVYDAFLATNNVQAGAECAKLMSDLIGnKGKVAIVNFAAGTQTAIDRETGFTEEIKNN--HKDVEIVGVQYCDS-DPT 219
Cdd:cd19992 91 LNADVDLYVGRDNYKVGQLQAEYALEAVP-KGNYVILSGDPGDNNAQLITAGAMDVLQPAidSGDIKIVLDQYVKGwSPD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 220 KAANQATDFITA-NPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFD-NSDDIKAgLKSGTIKGTAVQMPTMMGSMG 297
Cdd:cd19992 170 EAMKLVENALTAnNNNIDAVLAPNDGMAGGAIQALKAQGLAGKVFVTGQDaELAALKR-IVEGTQTMTVWKDLKELARAA 248
|
250
....*....|....*..
gi 1519460899 298 VQIVVDILGGKAPAEKD 314
Cdd:cd19992 249 ADAAVKLAKGEKPQTTD 265
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
49-320 |
6.96e-24 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 99.20 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 49 IKIALVTKMVDSPYWQTVKRAAEEKAKELGNVEVTHLGPptEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKA 128
Cdd:cd01539 1 IKIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDA--QNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 129 KDAGIPVVMIDSGISEPV---YD--AFLATNNVQAGAECAKLMSDLIGNK--------GKVAIVNF--AAGTQTAIDRET 193
Cdd:cd01539 79 KAANIPVIFFNREPSREDlksYDkaYYVGTDAEESGIMQGEIIADYWKANpeidkngdGKIQYVMLkgEPGHQDAIARTK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 194 GFTEEIKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPD-IKGIWGANDQSAVGVAQAVTEKG--KGDS---IMVVGF 267
Cdd:cd01539 159 YSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGynTGDGdkyIPVFGV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1519460899 268 DNSDDIKAGLKSGTIKGTAVQMPTMMGSMGVQIVVDILGGKAPAEKDVDTGVT 320
Cdd:cd01539 239 DATPEALEAIKEGKMLGTVLNDAKAQAKAIYELAKNLANGKEPLETGYKFLVE 291
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
50-327 |
7.60e-23 |
|
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380482 [Multi-domain] Cd Length: 294 Bit Score: 96.21 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:cd01540 1 KIGFIVKQPDQPWFQDEWKGAKKAAKELG-FEVIKID--AKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGI--SEPVYDA-FLATNNVQAGAECAKLMSDLIGNKG--KVAIVNFAAGT----QTAIDRETGFTEEIK 200
Cdd:cd01540 78 AAGIPVIAVDDQLvdADPMKIVpFVGIDAYKIGEAVGEWLAKEMKKRGwdDVKEVGVLAITmdtlSVCVDRTDGAKDALK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 201 -NNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKG--IWGANDQSAVGVAQAVTEKGKG-DSIMVVG---FDNSDDI 273
Cdd:cd01540 158 aAGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHwlVVGCNDEGVLGAVRALEQAGFDaEDIIGVGiggYLAADEE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1519460899 274 KAGLKSGtIKGTAVQMPTMMGSMGVQIVVD-ILGGKAPAEKDVdTGVTMVTFENY 327
Cdd:cd01540 238 FKKQPTG-FKASLYISPDKHGYIAAEELYNwITDGKPPPAETL-TDGVIVTRDNY 290
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
50-308 |
1.66e-22 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 96.02 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPpTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAK 129
Cdd:PRK15408 25 RIAFIPKLVGVGFFTSGGNGAKEAGKELG-VDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISePVYDAFLATNNV--QAGAECAKLMSDLIGN-KGKVAivnFAAGTQTAIDRETGFTE---EIKNNH 203
Cdd:PRK15408 103 QRGVKVLTWDSDTK-PECRSYYINQGTpeQLGSMLVEMAAKQVGKdKAKVA---FFYSSPTVTDQNQWVKEakaKIAKEH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 204 KDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWgANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSGTIK 283
Cdd:PRK15408 179 PGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAII-APDANALPAAAQAAENLKRDKVAIVGFSTPNVMRPYVKRGTVK 257
|
250 260
....*....|....*....|....*
gi 1519460899 284 GTAVQMPTMMGSMGVQIVVDILGGK 308
Cdd:PRK15408 258 EFGLWDVVQQGKISVYVANELLKKG 282
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
45-315 |
3.19e-20 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 90.01 E-value: 3.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 45 AKETIKI-ALVTKMVDSpYWQTVKRAAEEKAKELGnVEVTHLgpptEA----DIDKQVQIIETCINDDYDGIILAACDKD 119
Cdd:PRK10936 43 AKKAWKLcALYPHLKDS-YWLSVNYGMVEEAKRLG-VDLKVL----EAggyyNLAKQQQQLEQCVAWGADAILLGAVTPD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 120 ALIAPVQKAKdAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAK-LMSDLIGNKGKVAIVNF-----AAGTQTAidrET 193
Cdd:PRK10936 117 GLNPDLELQA-ANIPVIALVNGIDSPQVTTRVGVSWYQMGYQAGRyLAQWHPKGSKPLNVALLpgpegAGGSKAV---EQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 194 GFTEEIKNNhkDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGandqSAVGVAQAVTE---KGKGDSIMVVGFDNS 270
Cdd:PRK10936 193 GFRAAIAGS--DVRIVDIAYGDNDKELQRNLLQELLERHPDIDYIAG----SAVAAEAAIGElrgRNLTDKIKLVSFYLS 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1519460899 271 DDIKAGLKSGTIKGTAVQMPTMMGSMGVQIVVDILGGKaPAEKDV 315
Cdd:PRK10936 267 HQVYRGLKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGA-PVPGDV 310
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
51-310 |
3.33e-20 |
|
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380503 [Multi-domain] Cd Length: 266 Bit Score: 88.47 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACdKDALiAPVQKAK 129
Cdd:cd06280 2 IGLIVPDITNPFFTTIARGIEDAAEKHGyQVILAN----TDEDPEKEKRYLDSLLSKQVDGIILAPS-AGPS-RELKRLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAfLATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIV 209
Cdd:cd06280 76 KHGIPIVLIDREVEGLELDL-VAGDNREGAYKAVKHLIEL-GHR-RIGLITGPLEISTTRERLAGYREALAEAGIPVDES 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG--DSIMVVGFDNSDDikAGLKSGTIkgTAV 287
Cdd:cd06280 153 LIFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEipQDISVVGFDDSDW--FEIVDPPL--TVV 228
|
250 260
....*....|....*....|....
gi 1519460899 288 QMPTM-MGSMGVQIVVDILGGKAP 310
Cdd:cd06280 229 AQPAYeIGRIAAQLLLERIEGQGE 252
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
89-308 |
6.21e-20 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 88.52 E-value: 6.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGISEPvYDAFLATNNVQAGAECAKLMSD 168
Cdd:cd19999 42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSP-DAINVVIDQYKWAAIQAQWLAE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 169 LIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKnNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWgANDQSAVG 248
Cdd:cd19999 121 QLGGKGNIVAINGVAGNPANEARVKAADDVFA-KYPGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVL-TQDGMAEG 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519460899 249 VAQAVTEKGKGDSIMV----VGFDNS--DDIKAGLKSGtikgtAVQMPTMMGSMGVQIVVDILGGK 308
Cdd:cd19999 199 VLRAFQAAGKDPPVMTgdyrKGFLRKwkELDLPDFESI-----GVVNPPGIGATALRIAVRLLQGK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
61-318 |
1.23e-18 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380621 [Multi-domain] Cd Length: 278 Bit Score: 84.30 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 61 PYWQTVKRAAEEKAKELG-NVEVTHLGppteADIDKQVQIIETCINDDYDGIILAACDKDALIAP-VQKAKDAGIPVVMI 138
Cdd:cd19966 13 PFWTVVYNGAKDAAADLGvDLDYVFSS----WDPEKMVEQFKEAIAAKPDGIAIMGHPGDGAYTPlIEAAKKAGIIVTSF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 139 DSGISEPVY----DAFLATNNVQAGAECAKLMSD--LIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIVGvq 212
Cdd:cd19966 89 NTDLPKLEYgdcgLGYVGADLYAAGYTLAKELVKrgGLKTGDRVFVPGLLPGQPYRVLRTKGVIDALKEAGIKVDYLE-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 213 yCDSDPTKAANQA---TDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG-DSIMVVGFDNSDDIKAGLKSGTIKGTAVQ 288
Cdd:cd19966 167 -ISLEPNKPAEGIpvmTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKpGEIPVAGFDLSPATVQAIKSGYVNATIDQ 245
|
250 260 270
....*....|....*....|....*....|.
gi 1519460899 289 MPTMMGSMGV-QIVVDILGGKAPAekDVDTG 318
Cdd:cd19966 246 QPYLQGYLPVlQIYLTKKYGFSGL--DIDTG 274
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
45-319 |
1.43e-18 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 84.80 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 45 AKETIKIALVTKmvDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIA 123
Cdd:COG4213 1 GKIKIGVSLPTK--TSERWIRDGDNFKAALKELGyEVDVQN----ANGDVATQLSQIENMITKGADVLVIAPIDGTALAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 124 PVQKAKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIG--NKGKVAIVN----------FAAGT----QT 187
Cdd:COG4213 75 VLEKAKAAGIPVIAYDRLILNSDVDYYVSFDNVKVGELQGQYLVDGLPlkGKGNIELFGgsptdnnatlFFEGAmsvlQP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 188 AIDRetgfteeiknnhKDVEIVGVQYCDS-DPTKAANQATDFITANP-DIKGIWGANDQSAVGVAQAVTEKGKGDSIMVV 265
Cdd:COG4213 155 YIDS------------GKLVVVSGQWTLGwDPETAQKRMENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVT 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1519460899 266 GfdnSDDIKAGLKS---GTIKGTaVQMPT-MMGSMGVQIVVDIL-GGKAPAEKDVDTGV 319
Cdd:COG4213 223 G---QDAELAAVQRilaGTQYMT-VYKDTrELAEAAAELAVALAkGEKPEVNGTYDNGK 277
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
89-308 |
1.55e-18 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 84.65 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGISEP-VYDAFlaTNNVQAGAECAKLMS 167
Cdd:cd19998 41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVDEPcAYNVN--TDQAKAGEQTAQWLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 168 DLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNhKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGandQSA- 246
Cdd:cd19998 119 DKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKY-PDIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWT---QGGe 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519460899 247 VGVAQAVTEKGKGdsIMVVGFDNSDDIKAGLKSGTIKG----TAVQMPTmMGSMGVQIVVDILGGK 308
Cdd:cd19998 195 TGVIKALQAAGHP--LVPVGGEAENGFRKAMLEPLANGlpgiSAGSPPA-LSAVALKLAVAVLEGE 257
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
89-326 |
3.87e-18 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380652 [Multi-domain] Cd Length: 305 Bit Score: 83.49 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGISEP-VYdaFLATNNVQAGAECAKLMS 167
Cdd:cd19997 42 ADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTEPcAY--ILNNDFEDYGAASVEYVA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 168 DLIGNKGKVAIVNFAAGTQTAIDRETGFTEEIKnNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDqSAV 247
Cdd:cd19997 120 DRLGGKGNVLEVRGVAGTSPDEEIYAGQVEALK-KYPDLKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAVITQGG-DGY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 248 GVAQAVTEKGKgDSIMVVGFDNSDDIK----AGLKSGTIKGTAVQMPTmMGSMGVQIVVDILGGKAPAeKDVDTGVTMVT 323
Cdd:cd19997 198 GAAQAFEAAGR-PLPIIIGGNRGEFLKwwqeEYAKNGYETVSVSTDPG-QGSAAFWVALDILNGKDVP-KEMILPVVTIT 274
|
...
gi 1519460899 324 FEN 326
Cdd:cd19997 275 EDD 277
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
89-322 |
2.24e-17 |
|
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380514 [Multi-domain] Cd Length: 264 Bit Score: 80.64 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAACDKDaliapVQKAKDAGIPVVMIDSGISEpvYDAFLATNNVQAGAECAKLmsd 168
Cdd:cd06291 37 SNEDEEKEKEYLEMLKRNKVDGIILGSHSLD-----IEEYKKLNIPIVSIDRYLSE--GIPSVSSDNYQGGRLAAEH--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 169 LIgNKG--KVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSA 246
Cdd:cd06291 107 LI-EKGckKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLA 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519460899 247 VGVAQAVTEKGK--GDSIMVVGFDNSDDIkaglKSGTIKGTAVQMPT-MMGSMGVQIVVDILGGKAPAEKDVDTGVTMV 322
Cdd:cd06291 186 IGVLKALQKLGIrvPEDVQIIGFDGIEIS----ELLYPELTTIRQPIeEMAKEAVELLLKLIEGEEIEESRIVLPVELI 260
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
51-311 |
4.30e-16 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 76.88 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIapVQKAK 129
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGyTVLLAD----TGDDPERELAALDSLLSRRVDGLIITPARDDAPD--LQELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 130 DAGIPVVMIDSGISEPVYDAFLaTNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIV 209
Cdd:cd06285 76 ARGVPVVLVDRRIGDTALPSVT-VDNELGGRLATRHLLEL-GHR-RIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSD---DIKAGLksgtikg 284
Cdd:cd06285 153 RIVPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLrvPEDLSVVGFDDIPlaaFLPPPL------- 225
|
250 260
....*....|....*....|....*...
gi 1519460899 285 TAVQMPTM-MGSMGVQIVVDILGGKAPA 311
Cdd:cd06285 226 TTVRQPKYeMGRRAAELLLQLIEGGGRP 253
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
63-268 |
6.60e-16 |
|
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380646 [Multi-domain] Cd Length: 284 Bit Score: 76.51 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 63 WQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSG 141
Cdd:cd19991 14 WQRDRDYFVKKAKELGaEVIVQS----ANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 142 ISEPVYDAFLATNNVQAGAECAKLMSDLIGnKGKVAIVNFAAGTQTAIDRETGFTEEIKN--NHKDVEIVGVQYCDS-DP 218
Cdd:cd19991 90 ILNADVDLYVSFDNEKVGELQAEALVKAKP-KGNYVLLGGSPTDNNAKLFREGQMKVLQPliDSGDIKVVGDQWVDDwDP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1519460899 219 TKAANQATDFITAN-PDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFD 268
Cdd:cd19991 169 EEALKIMENALTANnNKIDAVIASNDGTAGGAIQALAEQGLAGKVAVSGQD 219
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
51-271 |
8.40e-16 |
|
ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380631 [Multi-domain] Cd Length: 268 Bit Score: 76.13 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILA--ACDKDALIapvQK 127
Cdd:cd19976 2 IGLIVPDISNPFFSELVRGIEDTLNELGyNIILCN----TYNDFEREKKYIQELKERNVDGIIIAssNISDEAII---KL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISEPVYDAfLATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFteeiKNNHKDVE 207
Cdd:cd19976 75 LKEEKIPVVVLDRYIEDNDSDS-VGVDDYRGGYEATKYLIEL-GHT-RIGCIVGPPSTYNEHERIEGY----KNALQDHN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519460899 208 IVGVQ---YCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG--DSIMVVGFDNSD 271
Cdd:cd19976 148 LPIDEswiYSGESSLEGGYKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKipEDLSVIGFDNII 216
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
48-281 |
1.16e-15 |
|
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).
Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 76.01 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 48 TIKIALVTKMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIdkQVQIIETCINDDYDGIILA--ACDKDALIAPv 125
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHG-FDVFLLAVGDGEDT--LTNAIDLLLASGADGIIITtpAPSGDDITAK- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 126 qkAKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAECA-KLMSDliGNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHK 204
Cdd:pfam00532 77 --AEGYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTqYLIAE--GHKRPIAVMAGPASALTARERVQGFMAALAAAGR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519460899 205 DVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKG--KGDSImVVGFDNSDDIKAGLKSGT 281
Cdd:pfam00532 153 EVKIYHVATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrvKIPDI-VGIGINSVVGFDGLSKAQ 230
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
50-321 |
2.21e-15 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380650 [Multi-domain] Cd Length: 294 Bit Score: 75.40 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKA--KELGNVEVTHLGppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQK 127
Cdd:cd19995 1 KVAFLLPDTTSARWEQQDAPGFEKAmkKLCPDCKVIYQN--ANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGK----VAIVNFAAGTQTAIDRETGFTEEIK--N 201
Cdd:cd19995 79 AAQAGVPVIAYDRLILGGPADYYVSFDNVAVGEAQAQSLVDHLKAIGKkgvnIVMINGSPTDNNAGLFKKGAHEVLDplG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 202 NHKDVEIVGVQYC-DSDPTKAANQATDFITANP-DIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDdikAGLK- 278
Cdd:cd19995 159 DSGELKLVCEYDTpDWDPANAQTAMEQALTKLGnNIDGVLSANDGLAGGAIAALKAQGLAGKVPVTGQDATV---AGLQr 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1519460899 279 --SGTIKGTAVQMPTMMGSMGVQIVVDILGGKAPAEKDVDTGVTM 321
Cdd:cd19995 236 ilAGDQYMTVYKPIKKEAAAAAKVAVALLKGETPPSDLVTGTVTN 280
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
48-322 |
2.49e-15 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380480 [Multi-domain] Cd Length: 283 Bit Score: 75.15 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 48 TIKIALVTKmvDSPYWQTVKRAAEEKAKELGnveVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQK 127
Cdd:cd01538 1 KIGVSLPNL--REARWQTDRDIMVEQLEEKG---AKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISEPVYDAFLATNNVQAGAECAKLMSDLIGNKGKVAIVN---------FAAGTQTAIDRETgftee 198
Cdd:cd01538 76 AKAEGIKVIAYDRLILNADVDYYISFDNEKVGELQAQALLDAKPEGNYVLIGGsptdnnaklFRDGQMKVLQPAI----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 199 iknNHKDVEIVGVQYCDS-DPTKAANQATDFITAN-PDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSddiKAG 276
Cdd:cd01538 151 ---DSGKIKVVGDQWVDDwLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDAD---LAA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1519460899 277 LKS---GTIKGTAVQMPTMMGSMGVQIVVDILGGKAP-AEKDVDTGVTMV 322
Cdd:cd01538 225 IKRilaGTQTMTVYKDIRLLADAAAEVAVALMRGEKPpINGTTNNGLKDV 274
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
109-269 |
5.91e-15 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 73.72 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 109 DGIILAACDKDAliAPVQKAKDAGIPVVMIDSGISEPVYDAfLATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTA 188
Cdd:cd06278 56 DGVIVTSATLSS--ELAEECARRGIPVVLFNRVVEDPGVDS-VSCDNRAGGRLAADLLLAA-GHR-RIAFLGGPEGTSTS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 189 IDRETGFTEEIKNNHKDVEIVGVqyCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK---GDSIMVV 265
Cdd:cd06278 131 RERERGFRAALAELGLPPPAVEA--GDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGlvvPEDISVV 208
|
....
gi 1519460899 266 GFDN 269
Cdd:cd06278 209 GFDD 212
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
51-303 |
1.77e-14 |
|
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: 72.69 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTK---MVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIdkQVQIIETCINDDYDGIILAACDKDAlIAPVQK 127
Cdd:cd01391 2 IGVVTSslhQIREQFGIQRVEAIFHTADKLG-ASVEIRDSCWHGSV--ALEQSIEFIRDNIAGVIGPGSSSVA-IVIQNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISEPV------YDAFLATNNVQAGAECAKLMSDLigNKGKVAIVNFAAGTqTAIDRETGFTEEIKN 201
Cdd:cd01391 78 AQLFDIPQLALDATSQDLSdktlykYFLSVVFSDTLGARLGLDIVKRK--NWTYVAAIHGEGLN-SGELRMAGFKELAKQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 202 NhkDVEIVGVQYCDSDP-TKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSDDIKAGLKSG 280
Cdd:cd01391 155 E--GICIVASDKADWNAgEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSDGWADRDEVGYEV 232
|
250 260
....*....|....*....|....*
gi 1519460899 281 TIKGTA--VQMPTMMGSMGVQIVVD 303
Cdd:cd01391 233 EANGLTtiKQQKMGFGITAIKAMAD 257
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
62-315 |
2.67e-14 |
|
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380488 [Multi-domain] Cd Length: 265 Bit Score: 71.84 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 62 YWQTVkRAAEEKAKELG-NVEVTHLGPPTEADIDkqvQIIETCINDDYDGIILAACDKDALIAPVQKAkdAGIPVVMIDS 140
Cdd:cd01574 14 PASTL-AGIERAARERGySVSIATVDEDDPASVR---EALDRLLSQRVDGIIVIAPDEAVLEALRRLP--PGLPVVIVGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 141 GISEPVydAFLATNNVQAGAECAKLMSDLignkG--KVAIVnfaAGTQT---AIDRETGFTEEIKNNhkDVEIVGVQYCD 215
Cdd:cd01574 88 GPSPGV--PTVSIDQEEGARLATRHLLEL----GhrRIAHI---AGPLDwvdARARLRGWREALEEA--GLPPPPVVEGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 216 SDPtKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNsddikaglksgtIKGTAVQMPTM- 292
Cdd:cd01574 157 WSA-ASGYRAGRRLLDDGPVTAVFAANDQMALGALRALHERGLrvPEDVSVVGFDD------------IPEAAYFVPPLt 223
|
250 260 270
....*....|....*....|....*....|.
gi 1519460899 293 --------MGSMGVQIVVDILGGKAPAEKDV 315
Cdd:cd01574 224 tvrqdfaeLGRRAVELLLALIEGPAPPPESV 254
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
51-305 |
5.69e-14 |
|
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380483 [Multi-domain] Cd Length: 274 Bit Score: 71.05 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGNVEVTHLgppTEADIDKQVQIIETCINDDYDGIILAACdKDALIAP----VQ 126
Cdd:cd01541 2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLAL---TNNDVEKEREILESLLDQNVDGLIIEPT-KSALPNPnldlYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 127 KAKDAGIPVVMIDSGISEPVYDAFlATNNVQAGAECAKLmsdLIgNKG--KVAIVnFAAGTQTAIDRETGFTEEIKNNH- 203
Cdd:cd01541 78 ELQKKGIPVVFINSYYPELDAPSV-SLDDEKGGYLATKH---LI-DLGhrRIAGI-FKSDDLQGVERYQGFIKALREAGl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 204 --KDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK---GDsIMVVGFDNSDdikagL- 277
Cdd:cd01541 152 piDDDRILWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLrvpED-LSVVGFDDSY-----La 225
|
250 260
....*....|....*....|....*....
gi 1519460899 278 KSGTIKGTAVQMPTM-MGSMGVQIVVDIL 305
Cdd:cd01541 226 SLSEPPLTSVVHPKEeLGRKAAELLLRMI 254
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
60-313 |
6.55e-14 |
|
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380632 [Multi-domain] Cd Length: 264 Bit Score: 70.64 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 60 SPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDK-DALIapvQKAKDAGIPVVM 137
Cdd:cd19977 11 NPFFTSVVRGIEDEAYKNGyHVILCN----TDEDPEKEKKYIEMLRAKQVDGIIIAPTGGnEDLI---EKLVKSGIPVVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 138 IDSGISEPVYDAFLaTNNVQAGAECaklMSDLIGN-KGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVE---IVGVQY 213
Cdd:cd19977 84 VDRYIPGLDVDTVV-VDNFKGAYQA---TEHLIELgHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDeelIKHVDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 214 cdsdpTKAANQATD-FITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSDdiKAGLKSGTIkgTAVQMP 290
Cdd:cd19977 160 -----QDDVRKAISeLLKLEKPPDAIFAANNLITLEVLKAIKELGLriPDDIALIGFDDIP--WADLFNPPL--TVIAQP 230
|
250 260
....*....|....*....|....
gi 1519460899 291 TM-MGSMGVQIVVDILGGKAPAEK 313
Cdd:cd19977 231 TYeIGRKAAELLLDRIENKPKGPP 254
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
60-271 |
9.25e-14 |
|
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380507 [Multi-domain] Cd Length: 267 Bit Score: 70.26 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 60 SPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDkdaLIAPVQKAKDAGIPVVMI 138
Cdd:cd06284 11 NPFYSEILRGIEDAAAEAGyDVLLGD----TDSDPEREDDLLDMLRSRRVDGVILLSGR---LDAELLSELSKRYPIVQC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 139 dsgiSEPVYDA---FLATNNVQAGAEcakLMSDLI--GNKgKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIVGVQY 213
Cdd:cd06284 84 ----CEYIPDSgvpSVSIDNEAAAYD---ATEYLIslGHR-RIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 214 CDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSD 271
Cdd:cd06284 156 GDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLrvPEDVSVIGFDDIE 215
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
48-317 |
1.28e-13 |
|
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380649 [Multi-domain] Cd Length: 304 Bit Score: 70.35 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 48 TIKIALVTKmvDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQ 126
Cdd:cd19994 1 KIGISLPTK--SEERWIKDGENLKSELEEAGyTVDLQY----ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 127 KAKDAGIPVVMIDSGISE-PVYDAFLATNNVQAGAECAK-LMSDLIGNKGKVAI-VNFAAGTQTAIDRETGF-------- 195
Cdd:cd19994 75 EAKDAGIPVIAYDRLIMNtDAVDYYVTFDNEKVGELQGQyLVDKLGLKDGKGPFnIELFAGSPDDNNAQLFFkgamevlq 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 196 ------TEEIKNNHKDVEIVGVQycDSDPTKAANQATDFITANP----DIKGIWGANDQSAVGVAQAVTEKGKGDSIM-- 263
Cdd:cd19994 155 pyiddgTLVVRSGQTTFEQVATP--DWDTETAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYDTGPWpv 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1519460899 264 VVGFDNSDD----IKAGLKSGTI-KGTAVqmptmMGSMGVQIVVDILGGKAPAEKDVDT 317
Cdd:cd19994 233 VTGQDAEDAsvksILDGEQSMTVfKDTRL-----LAKATVELVDALLEGEEVEVNDTKT 286
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
63-312 |
1.86e-13 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 69.81 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 63 WQTVKRAAEEKAKELGnveVTHLGPPTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVQKAKDAGIPVVMIDSGI 142
Cdd:cd19993 14 WKTDEAAMKKALEKAG---AKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 143 SEPvyDAFLAT-NNVQAGAECAKLMSDLIgNKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHK--DVEIVGVQYCDS-DP 218
Cdd:cd19993 91 ENP--IAFYISfDNVEVGRMQARGVLKAK-PEGNYVFIKGSPTDPNADFLRAGQMEVLQPAIDsgKIKIVGEQYTDGwKP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 219 TKAANQATDFITANP-DIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSddiKAGLKS---GTIKGTAVQMPTMMG 294
Cdd:cd19993 168 ANAQKNMEQILTANNnKVDAVVASNDGTAGGAVAALAAQGLAGKVPVSGQDAD---KAALNRialGTQTVTVWKDARELG 244
|
250
....*....|....*...
gi 1519460899 295 SMGVQIVVDILGGKAPAE 312
Cdd:cd19993 245 KEAAEIAVELAKGTKIEA 262
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
51-310 |
7.45e-13 |
|
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380511 [Multi-domain] Cd Length: 268 Bit Score: 67.57 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVT-KMVDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAPVqka 128
Cdd:cd06288 2 IGLITdDIATTPFAGDIIRGAQDAAEEHGyLLLLAN----TGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 129 KDAGIPVVMI-----DSGISEPVYDaflatnNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFTEEIKNNH 203
Cdd:cd06288 75 ELTDIPLVLLncfddDPSLPSVVPD------DEQGGYLATRHLIEA-GHR-RIAFIGGPEDSLATRLRLAGYRAALAEAG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 204 KDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSDDIKA---GLk 278
Cdd:cd06288 147 IPYDPSLVVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLrvPEDLSVVGFDNQELAAYlrpPL- 225
|
250 260 270
....*....|....*....|....*....|...
gi 1519460899 279 sgtikgTAVQMP-TMMGSMGVQIVVDILGGKAP 310
Cdd:cd06288 226 ------TTVALPyYEMGRRAAELLLDGIEGEPP 252
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
51-323 |
1.14e-12 |
|
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380519 [Multi-domain] Cd Length: 270 Bit Score: 67.30 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGNVEVTHlgpPTEADIDKQVQIIETCINDDYDGIILAACDKDALIapVQKAKD 130
Cdd:cd06296 2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVT---ATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQ--LRLLRS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 131 AGIPVVMIDSgISEPVYDAF-LATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVEIV 209
Cdd:cd06296 77 AGIPFVLIDP-VGEPDPDLPsVGATNWAGGRLATEHLLDL-GHR-RIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 210 GVQYCDSDPTKAANQATDFIT-ANPDIkGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSDdiKAGLKSGTIkgTA 286
Cdd:cd06296 154 LVREGDFTYEAGYRAARELLElPDPPT-AVFAGNDEQALGVYRAARALGLrvPDDLSVIGFDDTP--PARWTSPPL--TT 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 1519460899 287 VQMPTM-MGSMGVQIVVDILGGKAPAEKDVDTGVTMVT 323
Cdd:cd06296 229 VHQPLReMGAVAVRLLLRLLEGGPPDARRIELATELVV 266
|
|
| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
44-310 |
2.97e-11 |
|
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.
Pssm-ID: 380526 [Multi-domain] Cd Length: 320 Bit Score: 63.54 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 44 TAKETIKIALV--TKMVdSPYWQTVKRAAEEKAKELG---NVEVTHLGPptEADIDKQVQIIETCINDDYDGIILAacdK 118
Cdd:cd06303 23 TQKRPVKIAVVypGLQV-SDYWRRSIVSFRKRLDELGikyQLDEFFTRP--GAEIRLQALQIREMLKSDPDYLIFT---L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 119 DALIAP--VQKAKDAGIPVVMIDSgISEPVYD-------AFLATNNVQAGAECAKLMSDLIGNKGKVAIVNFAAGTqtaI 189
Cdd:cd06303 97 DALRHRrfVEILLDSGKPKLILQN-ITTPLRDwdnhqplLYVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTEGY---V 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 190 DRETG--FTEEIkNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGF 267
Cdd:cd06303 173 SDQRGdtFIDEV-ARHSNLELVSAYYTDFDRESAREAARALLARHPDLDFIYACSTDIALGAIDALQELGRETDIMINGW 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1519460899 268 DNSDDIKAGLKSGTIKGTAVQMPTMMG-SMGVQIVVDILGGKAP 310
Cdd:cd06303 252 GGGSAELDALQKGGLDVTVMRMNDDNGiAMAEAIKLDLEGREVP 295
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
92-313 |
5.78e-11 |
|
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380506 [Multi-domain] Cd Length: 266 Bit Score: 62.18 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 92 DIDKQVQIIETCINDDYDGIILAACDKDAliAPVQKAKDAGIPVVMIDSGISEPVYDaFLATNNVQAGAECAKLMSDlig 171
Cdd:cd06283 40 DPEKERDYIESLLSQRVDGLILQPTGNNN--DAYLELAQKGLPVVLVDRQIEPLNWD-TVVTDNYDATYEATEHLKE--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 172 nKGKVAIVNFA---AGTQTAIDRETGFTEEIKNNHKDVEIVGVQYcdSDPTKAANQATDFITANPD-IKGIWGANDQSAV 247
Cdd:cd06283 114 -QGYERIVFVTepiKGISTRRERLQGFLDALARYNIEGDVYVIEI--EDTEDLQQALAAFLSQHDGgKTAIFAANGVVLL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519460899 248 GVAQAVTEKGK--GDSIMVVGFDNSDdiKAGLKSGTIKgTAVQMPTMMGSMGVQIVVDILGGKAPAEK 313
Cdd:cd06283 191 RVLRALKALGIriPDDVGLCGFDDWD--WADLIGPGIT-TIRQPTYEIGKAAAEILLERIEGDSGEPK 255
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
51-315 |
1.41e-10 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 61.13 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGNVEVThlgPPTEADIDKQVQIIETCINDDYDGIILAACDKDalIAPVQKAKD 130
Cdd:cd06293 2 IGLVVPDVSNPFFAEVARGVEDAARERGYAVVL---CNSGRDPERERRYLEMLESQRVRGLIVTPSDDD--LSHLARLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 131 AGIPVVMIDSGISEPVYDAfLATNNVQAGAECAklmSDLIG-NKGKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDV--E 207
Cdd:cd06293 77 RGTAVVLLDRPAPGPAGCS-VSVDDVQGGALAV---DHLLElGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPdeV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 208 IVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG--DSIMVVGFdnsDDIkAGLKSGTIKGT 285
Cdd:cd06293 153 VRELSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpDDVSVVGY---DDL-PFAAAANPPLT 228
|
250 260 270
....*....|....*....|....*....|.
gi 1519460899 286 AVQMPT-MMGSMGVQIVVDILGGKAPAEKDV 315
Cdd:cd06293 229 TVRQPSyELGRAAADLLLDEIEGPGHPHEHV 259
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
51-271 |
2.74e-10 |
|
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380494 [Multi-domain] Cd Length: 266 Bit Score: 60.23 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGNvevtHL----GpptEADIDKQVQIIETCINDDYDGIIL--AACDKDALIAP 124
Cdd:cd06270 2 IGLVVPDLSGPFFGSLLKGAERVARAHGK----QLlitsG---HHDAEEEREAIEFLLDRRCDAIILhsRALSDEELILI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 125 VQKakdaGIPVVMID---SGISEP-VYdaflaTNNVQAGaecaKLMSDLIGNKG--KVAIVNFAAGTQTAIDRETGFTEE 198
Cdd:cd06270 75 AEK----IPPLVVINryiPGLADRcVW-----LDNEQGG----RLAAEHLLDLGhrRIACITGPLDIPDARERLAGYRDA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519460899 199 IKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSD 271
Cdd:cd06270 142 LAEAGIPLDPSLIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIkvPEDVSVIGFDDVP 216
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
50-313 |
8.22e-10 |
|
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 58.69 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKM-----VDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEadidkqvqiIETCINDDYDGII-LAACDKDALia 123
Cdd:cd01544 1 TIGIIQWYseeeeLEDPYYLSIRLGIEKEAKKLG-YEIKTIFRDDE---------DLESLLEKVDGIIaIGKFSKEEI-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 124 pvQKAKDAGIPVVMIDSGISEPVYDAflATNNVQAGAEcaKLMSDLIgNKG--KVAIV----NFAAGTQTAID-RETGFT 196
Cdd:cd01544 69 --EKLKKLNPNIVFVDSNPDPDGFDS--VVPDFEQAVR--QALDYLI-ELGhrRIGFIggkeYTSDDGEEIEDpRLRAFR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 197 EEIKNNHKDVEIVgVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSDDIK 274
Cdd:cd01544 142 EYMKEKGLYNEEY-IYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIkvPEDISIISFNDIEVAK 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1519460899 275 A---GLksgtikgTAVQMPT-MMGSMGVQIVVD-ILGGKAPAEK 313
Cdd:cd01544 221 YvtpPL-------TTVHIPTeEMGRTAVRLLLErINGGRTIPKK 257
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
109-270 |
1.43e-09 |
|
ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380517 [Multi-domain] Cd Length: 269 Bit Score: 57.98 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 109 DGII-LAACDKDALIapvQKAKDAGIPVVMIdsGISEPVYDAFLATN-NVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQ 186
Cdd:cd06294 62 DGFIlLYSKEDDPLI---EYLKEEGFPFVVI--GKPLDDNDVLYVDNdNVQAGYEATEYLIDK-GHK-RIAFIGGDKNLV 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 187 TAIDRETGFTEEIKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG--DSIMV 264
Cdd:cd06294 135 VSIDRLQGYKQALKEAGLPLDDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRvpEDVSI 214
|
....*.
gi 1519460899 265 VGFDNS 270
Cdd:cd06294 215 ISFNNS 220
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
51-313 |
4.12e-09 |
|
ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380630 [Multi-domain] Cd Length: 269 Bit Score: 56.41 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELG-NVEVTHlgppTEADIDKQVQIIETCINDDYDGIILA-ACDKDALIapvQKA 128
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGySVILCN----TGSDEEREKKYLQLLKEKRVDGIIFAsGTLTEENK---QLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 129 KDAGIPVVMIdSGISEPVYDAFLATNNVQAGAECAKLmsdLIgNKG--KVAIVNFAAGTQTA-IDRETGFTEEIKNNHKD 205
Cdd:cd19975 75 KNMNIPVVLV-STESEDPDIPSVKIDDYQAAYDATNY---LI-KKGhrKIAMISGPLDDPNAgYPRYEGYKKALKDAGLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 206 VEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG--DSIMVVGFDNSDDIKAGLKSGTik 283
Cdd:cd19975 150 IKENLIVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRvpEDISVIGFDNTEIAEMSIPPLT-- 227
|
250 260 270
....*....|....*....|....*....|
gi 1519460899 284 gTAVQMPTMMGSMGVQIVVDILGGKAPAEK 313
Cdd:cd19975 228 -TVSQPFYEMGKKAVELLLDLIKNEKKEEK 256
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
50-315 |
1.01e-08 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 55.31 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVTKMVDSPYWQTVKRAAEEKAKELGnveVTHLGPPTEADIDKQVQIIETCINDDYDGIILAA--CDKDALiapvqK 127
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESG---YTLIVSTSHWNADRELEILRLLLARKVDGIIVVGgfGDEELL-----K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 128 AKDAGIPVVMIDSGISEPVYDAfLATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFTEEIKNNHKDVE 207
Cdd:cd06290 73 LLAEGIPVVLVDRELEGLNLPV-VNVDNEQGGYNATNHLIDL-GHR-RIVHISGPEDHPDAQERYAGYRRALEDAGLEVD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 208 IVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG--DSIMVVGFDNSddikAGLKSGTIKGT 285
Cdd:cd06290 150 PRLIVEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRvpDDVSVIGFDDL----PFSKYTTPPLT 225
|
250 260 270
....*....|....*....|....*....|.
gi 1519460899 286 AVQMPTM-MGSMGVQIVVDILGGKAPAEKDV 315
Cdd:cd06290 226 TVRQPLYeMGKTAAEILLELIEGKGRPPRRI 256
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
51-304 |
1.52e-08 |
|
Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.
Pssm-ID: 380479 [Multi-domain] Cd Length: 265 Bit Score: 54.94 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKELGnveVTHLGPPTEADIDKQVQIIETCINDDYDGIILAaCDKDALIAPVQKAKD 130
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPG---VQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAIN-LVDPAAAGVAEKARG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 131 AGIPVVMIDSGISEPVYDAFLATNNVQAGaecaKLMSDLIGNKGKVAIVNFAA--GTQTAIDRETGFTEEIKNNHKDVEI 208
Cdd:cd01537 78 QNVPVVFFDKEPSRYDKAYYVITDSKEGG----IIQGDLLAKHGHIQIVLLKGplGHPDAEARLAGVIKELNDKGIKTEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 209 VGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSDDikaGLKSGTIKGTA 286
Cdd:cd01537 154 LQLDTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLrvPSDISVFGYDALPE---ALKSGPLLTTI 230
|
250
....*....|....*...
gi 1519460899 287 VQMPTMMGSMGVQIVVDI 304
Cdd:cd01537 231 LQDANNLGKTTFDLLLNL 248
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
89-269 |
1.69e-08 |
|
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380512 [Multi-domain] Cd Length: 268 Bit Score: 54.88 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAACD--KDALIAPVqkaKDAGIPVVMidsgISEPVYDA---FLATNNVQAGAECA 163
Cdd:cd06289 37 TGEDPERQRRFLRRMLEQGVDGLILSPAAgtTAELLRRL---KAWGIPVVL----ALRDVPGSdldYVGIDNRLGAQLAT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 164 KLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFTEEIKNnhKDVEIVGVQYCDSDPTK--AANQATDFITANPDIKGIWGA 241
Cdd:cd06289 110 EHLIAL-GHR-RIAFLGGLSDSSTRRERLAGFRAALAE--AGLPLDESLIVPGPATReaGAEAARELLDAAPPPTAVVCF 185
|
170 180 190
....*....|....*....|....*....|
gi 1519460899 242 NDQSAVGVAQAVTEKGK--GDSIMVVGFDN 269
Cdd:cd06289 186 NDLVALGAMLALRRRGLepGRDIAVVGFDD 215
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
59-269 |
3.79e-08 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 53.78 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 59 DSPYWQTVKRAAEEKAKELG-NVEVTHLGppTEADIDKQVQIIEtciNDDYDGIILAACDKDAliAPVQKAKDAGIPVVM 137
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGyNLLISSVD--IGDDFDEILKELT---DDQSSGIILLGTELEE--KQIKLFQDVSIPVVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 138 IDSGISEPVYDaFLATNNVQAGAECAKLMSDL----IGN-KGKVAIVNF---AAGTQTAIdRETGFTEEIKNNhkdveiv 209
Cdd:cd06277 90 VDNYFEDLNFD-CVVIDNEDGAYEAVKYLVELghtrIGYlASSYRIKNFeerRRGFRKAM-RELGLSEDPEPE------- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519460899 210 gvQYCDSDPTKAANQATDFITANPDIKGIWGA-NDQSAVGVAQAVTEKG---KGDsIMVVGFDN 269
Cdd:cd06277 161 --FVVSVGPEGAYKDMKALLDTGPKLPTAFFAeNDIIALGCIKALQEAGirvPED-VSVIGFDD 221
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
89-311 |
5.47e-08 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 53.06 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAACDKDALIApVQKAKDAGIPVVMIDSGISEPVYdAFLATNNVQAGAECAKLMSD 168
Cdd:cd06282 37 TDYDPARELDAVETLLEQRVDGLILTVGDAQGSEA-LELLEEEGVPYVLLFNQTENSSH-PFVSVDNRLASYDVAEYLIA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 169 LiGNK--GKVAiVNFAAgTQTAIDRETGFTEEIknNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSA 246
Cdd:cd06282 115 L-GHRriAMVA-GDFSA-SDRARLRYQGYRDAL--KEAGLKPIPIVEVDFPTNGLEEALTSLLSGPNPPTALFCSNDLLA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519460899 247 VGVAQAVTEKGKG--DSIMVVGFdnsDDIKAGLKSGTIKGTAVQMPTMMGSMGVQIVVDILGGKAPA 311
Cdd:cd06282 190 LSVISALRRLGIRvpDDVSVIGF---DGIAIGELLTPTLATVVQPSRDMGRAAADLLLAEIEGESPP 253
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
109-317 |
7.30e-08 |
|
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380502 [Multi-domain] Cd Length: 284 Bit Score: 52.98 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 109 DGIILAACDKDALIapVQKAKDAGIPVVMIDSGISEPVydAFLATNNVQAGAECAKLMSDLiGNKgKVAIVNF------- 181
Cdd:cd06279 58 DGFIVYGLSDDDPA--VAALRRRGLPLVVVDGPAPPGI--PSVGIDDRAAARAAARHLLDL-GHR-RIAILSLrldrgre 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 182 ----------AAGTQTAIDRETGFTEEIK-NNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVA 250
Cdd:cd06279 132 rgpvsaerlaAATNSVARERLAGYRDALEeAGLDLDDVPVVEAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGAL 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 251 QAVTEKGK---GDsIMVVGFDNSDDIKAGLKSGTikgTAVQMPTMMGSMGVQIVVDILGGKAPAEKDVDT 317
Cdd:cd06279 212 RAARERGLrvpED-LSVTGFDDIPEAAAADPGLT---TVRQPAVEKGRAAARLLLGLLPGAPPRPVILPT 277
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
182-323 |
5.53e-07 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 48.87 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 182 AAGTQTAIDRETGFTEEIKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDikGIWGANDQSAVGVAQAVTEKGK--G 259
Cdd:pfam13377 18 DRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGALPT--AVFVANDEVALGVLQALREAGLrvP 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519460899 260 DSIMVVGFDNSDdiKAGLKSGTIkgTAVQMPTM-MGSMGVQIVVDILGGKAPAEKDVDTGVTMVT 323
Cdd:pfam13377 96 EDLSVIGFDDSP--LAALVSPPL--TTVRVDAEeLGRAAAELLLDLLNGEPAPPERVLLPPELVE 156
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
51-269 |
9.52e-07 |
|
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380499 [Multi-domain] Cd Length: 269 Bit Score: 49.56 E-value: 9.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 51 IALVTKMVDSPYWQTVKRAAEEKAKE------LGNvevthlgppTEADIDKQVQIIETCINDDYDGIILAACDKDALIAP 124
Cdd:cd06275 2 IGLLVTSSENPFFAEVVRGVEDACFRagysliLCN---------SDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 125 VQkAKDAGIPVVMIDSGISEPVYDAFLaTNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQTAIDRETGFT---EEIKN 201
Cdd:cd06275 73 LL-AALRSIPVVVLDREIAGDNADAVL-DDSFQGGYLATRHLIEL-GHR-RIGCITGPLEHSVSRERLAGFRralAEAGI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 202 NHKDVEIVGVQYCDSDPTKAANQatdFITANPDIKGIWGANDQSAVGVAQAVTEKG--KGDSIMVVGFDN 269
Cdd:cd06275 149 EVPPSWIVEGDFEPEGGYEAMQR---LLSQPPRPTAVFACNDMMALGALRAAQEQGlrVPQDISIIGYDD 215
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
109-269 |
1.13e-06 |
|
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380665 [Multi-domain] Cd Length: 269 Bit Score: 49.09 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 109 DGIILAA-CDKDALIAPVQKAkdaGIPVVMIDSGISEPVYdAFLATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQT 187
Cdd:cd20010 61 DGFILARtRVNDPRIAYLLER---GIPFVVHGRSESGAPY-AWVDIDNEGAFRRATRRLLAL-GHR-RIALLNGPEELNF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 188 AIDRETGFTEEIKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGK--GDSIMVV 265
Cdd:cd20010 135 AHQRRDGYRAALAEAGLPVDPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLspGKDVSVI 214
|
....
gi 1519460899 266 GFDN 269
Cdd:cd20010 215 GHDD 218
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
89-271 |
1.65e-06 |
|
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 48.65 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAA---CDKDaliapVQKAKDAGIPVVMI---DSGISEPVYDAFLAtnnvqagaec 162
Cdd:cd01542 37 TNLDEEREIEYLETLARQKVDGIILFAteiTDEH-----RKALKKLKIPVVVLgqeHEGFSCVYHDDYGA---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 163 AKLMSDLIGNKGKVAIV-------NFAAGtqtaIDRETGFTEEIKNNHKDVEIVgvQYCDSDPTKAANQATDFITANPdI 235
Cdd:cd01542 102 GKLLGEYLLKKGHKNIAyigvdeeDIAVG----VARKQGYLDALKEHGIDEVEI--VETDFSMESGYEAAKELLKENK-P 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1519460899 236 KGIWGANDQSAVGVAQAVTEKGK--GDSIMVVGFDNSD 271
Cdd:cd01542 175 DAIICATDNIALGAIKALRELGIkiPEDISVAGFGGYD 212
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
109-315 |
3.24e-06 |
|
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380495 [Multi-domain] Cd Length: 264 Bit Score: 47.80 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 109 DGIILAACDKDAliAPVQKAKDAGIPVVMIdsGISEPVYD-AFLATNNvQAGAECAklMSDLIG-NKGKVAIVNFAAGTQ 186
Cdd:cd06271 59 DGVILSEIEPND--PRVQFLTKQNFPFVAH--GRSD*PIGhAWVDIDN-EAGAYEA--VERLAGlGHRRIAFIVPPARYS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 187 TAIDRETGFTEeiknNHKDVEIVG-VQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKG--KGDSIM 263
Cdd:cd06271 132 PHDRRLQGYVR----A*RDAGLTGyPLDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGlkIGEDVS 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1519460899 264 VVGFDNSDDIKAGLKSGTikgTAVQMP-TMMGSMGVQIVVDILGGKAPAEKDV 315
Cdd:cd06271 208 IIGKDSAPFLGAMITPPL---TTVHAPiAEAGRELAKALLARIDGEDPETLQV 257
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
109-270 |
4.26e-06 |
|
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 47.55 E-value: 4.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 109 DGIILAA--CDKDALIAPVQkakDAGIPVVMIdSGISEPVYDAFLATNNVQAGAECAKLMSDLiGNKgKVAIVNFAAGTQ 186
Cdd:cd01545 58 DGVILTPplSDDPALLDALD---ELGIPYVRI-APGTDDDRSPSVRIDDRAAAREMTRHLIAL-GHR-RIGFIAGPPDHG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 187 TAIDRETGFTEEIKNNHKDVEIVGVQYCDSDPTKAANQATDFITANPDIKGIWGANDQSAVGVAQAVTEKGKG--DSIMV 264
Cdd:cd01545 132 ASAERLEGFRDALAEAGLPLDPDLVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRvpDDLSV 211
|
....*.
gi 1519460899 265 VGFDNS 270
Cdd:cd01545 212 AGFDDS 217
|
|
| Med |
COG1744 |
Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC superfamily, includes NupN [Signal ... |
44-268 |
3.90e-05 |
|
Lipoprotein Med, regulator of KinD/Spo0A, PBP1-ABC superfamily, includes NupN [Signal transduction mechanisms];
Pssm-ID: 441350 Cd Length: 300 Bit Score: 44.75 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 44 TAKETIKIALVTkmV----DSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIdkqVQIIETCINDDYDGIILAAcdkD 119
Cdd:COG1744 1 AAAEKLKVALVY--VggigDKSFNQAAYEGLEAAEKELG-VEVKYVESVPEADY---EPALRQLAEQGYDLIIGVG---F 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 120 ALIAPVQK-AKDA-GIPVVMIDSGISEP--VYDAFLATNNVQ--AGAECAkLMSDlignKGKVAIVnfaAGTQT-AIDR- 191
Cdd:COG1744 72 GFADALLKvAKEFpDVKFAIIDGYVDGApnVASYFFREEEGSylAGVLAA-LMTK----TGKVGFV---GGMPIpEVIRf 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519460899 192 ETGFTEEIKNNHKDVEIVgVQYCDS--DPTKAANQATDFITANPDIkgIWGANDQSAVGVAQAVTEKGKgdsIMVVGFD 268
Cdd:COG1744 144 INGFALGAKYVNPDIKVL-VVYTGSfsDPAKGKEAALALIDQGADV--IFQAAGGTGVGVIQAAKEAGK---VYAIGVD 216
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
71-229 |
4.13e-05 |
|
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 44.50 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 71 EEKAKELGNVEV---THLGPPTEAdidkqvQIIETCINDDYDGIILAACDKDalIAPVQKAKDAGIPVVMIDSGISEPVY 147
Cdd:cd06274 22 ERLARERGLQLLiacSDDDPEQER------RLVENLIARQVDGLIVAPSTPP--DDIYYLCQAAGLPVVFLDRPFSGSDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 148 DaFLATNNVQAGAECAKLMSDLIGNKgkvaIVNFAAGTQ--TAIDRETGFTEEIKNNHKDVEIVGVQYCDSDPTKAANQA 225
Cdd:cd06274 94 P-SVVSDNRAGARALTEKLLAAGPGE----IYFLGGRPElpSTAERIRGFRAALAEAGITEGDDWILAEGYDRESGYQLM 168
|
....
gi 1519460899 226 TDFI 229
Cdd:cd06274 169 AELL 172
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
109-178 |
1.63e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380538 Cd Length: 278 Bit Score: 42.72 E-value: 1.63e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519460899 109 DGIILAACDKDALIAPVQKAKDAGIPVVMIDSG-ISEPVYDAFLATNNVQAGAECAKLMSDLI----GNKGKVAI 178
Cdd:cd06315 58 DGIILGGDDAVELQEPLKKAVKAGIPVVGWHAAaSPGPIPELGLFTNITTDPREVAETAAALViaqsGGKAGVVI 132
|
|
| COG2984 |
COG2984 |
ABC-type uncharacterized transport system, periplasmic component [General function prediction ... |
47-317 |
2.58e-04 |
|
ABC-type uncharacterized transport system, periplasmic component [General function prediction only];
Pssm-ID: 442223 Cd Length: 284 Bit Score: 42.20 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 47 ETIKIaLVTKMVDSPYWQTVKRAAEEKAKELG---NVEVTHLGPptEADIDKQVQIIETCINDDYDGIIlaACDKDALIA 123
Cdd:COG2984 1 KPKKI-GILQISEHPALDAAREGFKDGLAEAGygkNLKLDYQNA--QGDQATAAQIAAKLVADKPDLIV--AIGTPAAQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 124 PVQKAKDagIPVVMidSGISEPVYDAFLATNNVQAG-----------AECAKLMSDLIGNKGKVAIVNFAAGTQTAIDRE 192
Cdd:COG2984 76 AANATKD--IPVVF--TAVTDPVGAGLVKSLEKPGGnvtgvsdllpiEKQLELIKKLLPDAKRIGVLYNPSEANSVAQVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 193 TgFTEEIKNNHKDVEIVGVqycdsDPTKAANQAtdFITANPDIKGIWGANDQSAVGVAQAVTEKGKGDSIMVVGFDNSdd 272
Cdd:COG2984 152 E-LKKAAKKLGLELVEATV-----TSSNEIQQA--LQSLAGKVDAIYVPTDNTVVSALEAIAKVAARAKIPVFGGDDS-- 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1519460899 273 ikaGLKSGTIkGTAVQMPTMMGSMGVQIVVDILGGKAPAEKDVDT 317
Cdd:COG2984 222 ---SVKAGAL-AGYGIDYYELGRQAAEMALRILKGEKPADIPVET 262
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
109-322 |
8.48e-04 |
|
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380489 [Multi-domain] Cd Length: 269 Bit Score: 40.56 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 109 DGIILAACDKDAliAPVQKAKDAGIPVV-MIDSGiSEPVyDAFLATNNVQAGAECAKLmsdLIGnKG--KVAIVNFAAGT 185
Cdd:cd01575 57 AGLILTGTEHTP--ATRKLLRAAGIPVVeTWDLP-DDPI-DMAVGFSNFAAGRAMARH---LIE-RGyrRIAFVGARLDG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 186 QT-AIDRETGFTEEIKNNHkdVEIVGVQYCDSDPT-KAANQAT-DFITANPDIKGIWGANDQSAVGVAQAVTEKGK---G 259
Cdd:cd01575 129 DSrARQRLEGFRDALAEAG--LPLPLVLLVELPSSfALGREALaELLARHPDLDAIFCSNDDLALGALFECQRRGIrvpG 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519460899 260 DsIMVVGFDNSDdIKAGLkSGTIkgTAVQMPTM-MGSMGVQIVVDILGGKAPAEKDVDTGVTMV 322
Cdd:cd01575 207 D-IAIAGFGDLD-IAAAL-PPAL--TTVRVPRYeIGRKAAELLLARLEGEEPEPRVVDLGFELV 265
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
107-275 |
8.84e-04 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 40.48 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 107 DYDG-IILAACDKDALIapvQKAKDAGIPVVMI--DSGISEPV--YDaflatnnVQAGAECAKLMSDLIGNKG-KVAIVN 180
Cdd:cd06287 56 DVDGaIVVEPTVEDPIL---ARLRQRGVPVVSIgrAPGTDEPVpyVD-------LQSAATARLLLEHLHGAGArQVALLT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 181 FAAGTQTAIDRETGFTEEIKNNHKDVEIVGVQycDSDPTKAANQAT-DFITANPDIKGIWGANDQSAVGVAQAVTEKGKG 259
Cdd:cd06287 126 GSSRRNSSLESEAAYLRFAQEYGTTPVVYKVP--ESEGERAGYEAAaALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRS 203
|
170
....*....|....*...
gi 1519460899 260 --DSIMVVgfDNSDDIKA 275
Cdd:cd06287 204 vpEDLMVV--TRYDGIRA 219
|
|
| PBP1_PrnA-like |
cd06354 |
periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its ... |
50-268 |
9.80e-04 |
|
periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea; Periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea. The PnrA lipoprotein, also known as Tp0319 or TmpC, represents a novel family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC) transport system (pnrABCDE). It shows a striking structural similarity to another basic membrane lipoprotein Med which regulates the competence transcription factor gene, comK, in Bacillus subtilis. The members of PnrA-like subgroup are likely to have similar nucleoside-binding functions and a similar type 1 periplasmic sugar-binding protein-like fold.
Pssm-ID: 380577 Cd Length: 268 Bit Score: 40.24 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVT---KMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPPTEADIdkqVQIIETCINDDYDGIIL------AACDKDA 120
Cdd:cd06354 1 KVALVTdsgGIGDKSFNQSAWEGLQRAAKELG-IKVKYLESKSDADY---EPNLRALADEGYDLIITvgfamaDAVEEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 121 LIAPVQKakdagipVVMIDSGISEP-------VYD----AFLAtnnvqaGAEcAKLMSdligNKGKVAIVnfaAGTQT-A 188
Cdd:cd06354 77 KANPDTK-------FIIIDATVDETppnvrsiVFReeeaAFLA------GYL-AALMT----KTGKVGFI---GGMDIpP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 189 IDR-ETGFTEEIKNNHKDVEI---VGVQYCDS--DPTKAANQATDFITANPDIkgIWGANDQSAVGVAQAVTEKGKgdsi 262
Cdd:cd06354 136 VRRfEDGFAAGAKYANPDIVVdvtVIGTYAGSfnDPAKGKAIAQEMIDQGADV--IFAAAGGTGLGVIEAAKEAGK---- 209
|
....*.
gi 1519460899 263 MVVGFD 268
Cdd:cd06354 210 YAIGVD 215
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
89-270 |
1.01e-03 |
|
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380521 [Multi-domain] Cd Length: 268 Bit Score: 40.35 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 89 TEADIDKQVQIIETCINDDYDGIILAACDKDALIapVQKAKDAGIPVVMIDSGISEPVYDAfLATNNVQAGAECAKLMSD 168
Cdd:cd06298 37 SDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEI--REEFKRSPVPVVLAGTVDSDHEIPS-VNIDYEQAAYDATKSLID 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 169 LiGNKgKVAIVNFAAGTQTAID-RETGFTEEIKNNHKDVE---IVGVQYCDSDPTKAANQatdfITANPDIKGIWGANDQ 244
Cdd:cd06298 114 K-GHK-KIAFVSGPLKEYINNDkKLQGYKRALEEAGLEFNeplIFEGDYDYDSGYELYEE----LLESGEPDAAIVVRDE 187
|
170 180
....*....|....*....|....*...
gi 1519460899 245 SAVGVAQAVTEKGKG--DSIMVVGFDNS 270
Cdd:cd06298 188 IAVGLLNAAQDRGLKvpEDLEIIGFDNT 215
|
|
| PBP1_As_SBP-like |
cd06330 |
periplasmic substrate-binding domain of active transport proteins; Periplasmic ... |
122-241 |
1.69e-03 |
|
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: 39.85 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 122 IAPVqkAKDAGIPVVMIDSGISEPVYDAF------LATNNVQAGAECAKLMSDLIGNKGKVAIVN--FAAGTQTAidreT 193
Cdd:cd06330 83 VAPV--AEELKVLFIATDAATDRLTEENFnpyvfrTSPNTYMDAVAAALYAAKKPPDVKRWAGIGpdYEYGRDSW----A 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1519460899 194 GFTEEIKNNHKDVEIVGVQYcdsdPTKAANQATDFIT----ANPDI--KGIWGA 241
Cdd:cd06330 157 AFKAALKKLKPDVEVVGELW----PKLGATDYTAYITallaAKPDGvfSSLWGG 206
|
|
| AnsA |
COG0252 |
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal ... |
99-149 |
4.32e-03 |
|
L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Translation, ribosomal structure and biogenesis, Amino acid transport and metabolism];
Pssm-ID: 440022 [Multi-domain] Cd Length: 325 Bit Score: 38.57 E-value: 4.32e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 99 IIETCINDDYDGIILAA------CDkdALIAPVQKAKDAGIPVVMI---DSGISEPVYDA 149
Cdd:COG0252 225 LLDALLAAGVKGIVLEGtgagnvPP--ALLPALKRAIERGVPVVVTsrcPEGRVNGVYGG 282
|
|
| PBP1_BMP-like |
cd19964 |
periplasmic binding component of a basic membrane lipoprotein (BMP) from Aeropyrum pernix K1 ... |
50-273 |
8.34e-03 |
|
periplasmic binding component of a basic membrane lipoprotein (BMP) from Aeropyrum pernix K1 and its close homologs in other bacteria; Periplasmic binding component of a family of basic membrane lipoproteins from Aeropyrum pernix K1 and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold.
Pssm-ID: 380619 Cd Length: 263 Bit Score: 37.19 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 50 KIALVT--KMVDSPYWQTVKRAAEEKAKELGnVEVTHLGPpteADIDKQVQIIETCINDDYDGIILAACD-KDALIAPVQ 126
Cdd:cd19964 1 KVALVTpgPLGDKSFNDSAAAGLKKLAEELG-VEIKVIEA---GDASKYEEQLRAAAEAGYDVIVATGDDlADALEKVAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519460899 127 KAKDagIPVVMIDSGISEP---VYDAFLATNNVQ--AGAeCAKLMSDlignKGKVAIVnfaAGTQTAIDRE--TGFTEEI 199
Cdd:cd19964 77 EYPD--QKFILLDTDIDEKlpnVASVSFDQNEGSylAGV-VAALMTK----TGVVGFV---GGMDIPVINDflAGYEAGA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519460899 200 KNNHKDVEIVgVQYCDS--DPTKAANQATDFITANPDIkgIWGANDQSAVGVAQAVTEKGkgdsIMVVGFD-NSDDI 273
Cdd:cd19964 147 KYVNPDIKVI-VSYVGSftDPAKGKELALALYNQGADV--IFQVAGGSGLGVIEAAAEAG----KYAIGVDsDQNDI 216
|
|
| |
