|
Name |
Accession |
Description |
Interval |
E-value |
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
25-294 |
9.73e-142 |
|
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: 400.51 E-value: 9.73e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGInVLSDDQD 184
Cdd:cd06321 81 AGIIVVAVDVAAEGADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPPVSAVIDRVNGCKEALAEYPGI-KLVDDQN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 185 AKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNIIITSVDGAPDIEEALK-GNTMVEASASQDPYA 263
Cdd:cd06321 160 GKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPEAVAALKrEGSPFIATAAQDPYD 239
|
250 260 270
....*....|....*....|....*....|.
gi 1113985319 264 MAQMGVDVGVKILNGEKPAESMILMPSTLVT 294
Cdd:cd06321 240 MARKAVELALKILNGQEPAPELVLIPSTLVT 270
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
4-298 |
3.14e-77 |
|
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: 237.90 E-value: 3.14e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 4 LLLAGLVLAMSTVSAQAKDLNKIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVD 83
Cdd:COG1879 14 LALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELG--VELIVVDAEGDAAKQISQIEDLIAQGVD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 84 MILINAVDANAIEVAIKRAQKEGIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVI 160
Cdd:COG1879 92 AIIVSPVDPDALAPALKKAKAAGIPVVTVDsdVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGsPGAPAAN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 161 DRVNGCRSVFAKAPGINVLsDDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDG 239
Cdd:COG1879 172 ERTDGFKEALKEYPGIKVV-AEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRkGDVKVVGFDG 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1113985319 240 APDIEEALKGNTMVeASASQDPYAMAQMGVDVGVKILNGEKPaESMILMPSTLVTRENV 298
Cdd:COG1879 251 SPEALQAIKDGTID-ATVAQDPYLQGYLAVDAALKLLKGKEV-PKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
25-292 |
1.01e-69 |
|
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: 217.43 E-value: 1.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELG--VELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKG---ADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGPQ-VSAVIDRVNGCRSVFAKAPGINVLs 180
Cdd:cd01536 79 AGIPVVAVDTDIDGggdVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPgSSTAIDRTKGFKEALKKYPDIEIV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTMVeASASQ 259
Cdd:cd01536 158 AEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRtGDIKIVGVDGTPEALKAIKDGELD-ATVAQ 236
|
250 260 270
....*....|....*....|....*....|...
gi 1113985319 260 DPYAMAQMGVDVGVKILNGEKPaESMILMPSTL 292
Cdd:cd01536 237 DPYLQGYLAVEAAVKLLNGEKV-PKEILTPVTL 268
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
25-294 |
9.81e-58 |
|
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: 186.73 E-value: 9.81e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELG--VELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADAT--VQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGINVLSd 181
Cdd:cd06323 79 AGIPVITVDRSVTGGKVVshIASDNVAGGEMAAEYIAKKLGGKGKVVELQGiPGTSAARERGKGFHNAIAKYPKINVVA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNIIITSVDGAPDIEEALKGNTMVeASASQDP 261
Cdd:cd06323 158 SQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGTPDAVKAVKDGKLA-ATVAQQP 236
|
250 260 270
....*....|....*....|....*....|...
gi 1113985319 262 YAMAQMGVDVGVKILNGEKPAESmILMPSTLVT 294
Cdd:cd06323 237 EEMGAKAVETADKYLKGEKVPKK-IPVPLKLVT 268
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
25-301 |
4.19e-57 |
|
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: 185.17 E-value: 4.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEynPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKE--LNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGP-QVSAVIDRVNGCRSVFAKAPGINVLsD 181
Cdd:cd06313 79 AGIPLVGVNalIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVILEGPiGQSAQIDRGKGIENVLKKYPDIKVL-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQ-KIDAVFTINDPQAIGTDLAAKQLKRDNIIITSVDGAPDIEEALKGNTMVeASASQD 260
Cdd:cd06313 158 EQTANWSRDEAMSLMENWLQAYGdEIDGIIAQNDDMALGALQAVKAAGRDDIPVVGIDGIEDALQAVKSGELI-ATVLQD 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1113985319 261 PYAMAQMGVDVGVKILNGEkPAESMILMPSTLVTRENVGEY 301
Cdd:cd06313 237 AEAQGKGAVEVAVDAVKGE-GVEKKYYIPFVLVTKDNVDDY 276
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
25-292 |
1.37e-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: 380626 [Multi-domain] Cd Length: 267 Bit Score: 183.55 E-value: 1.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEynPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEA--NGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKG---ADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVLsD 181
Cdd:cd19971 79 AGIPVINVDTPVKDtdlVDSTIASDNYNAGKLCGEDMVKKLPEGAKIAVLDHPTAESCVDRIDGFLDAIKKNPKFEVV-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTMVeASASQD 260
Cdd:cd19971 158 QQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKlGDILVYGVDGSPDAKAAIKDGKMT-ATAAQS 236
|
250 260 270
....*....|....*....|....*....|..
gi 1113985319 261 PYAMAQMGVDVGVKILNGEKpAESMILMPSTL 292
Cdd:cd19971 237 PIEIGKKAVETAYKILNGEK-VEKEIVVPTFL 267
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
25-293 |
8.37e-55 |
|
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: 178.89 E-value: 8.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYnPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKY-PNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVDKLGGKGDVI-IQNGPQVSAVIDRVNGCRSVFAKAPGINVLsD 181
Cdd:cd06308 80 AGIPVIVLDrkVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVeIQGLPGSSPAIDRHKGFLEAIAKYPGIKIV-A 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPD-IEEALKGNTMveaSASQ 259
Cdd:cd06308 159 SQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGReKEIKIIGVDGLPEaGEKAVKDGIL---AATF 235
|
250 260 270
....*....|....*....|....*....|....
gi 1113985319 260 DPYAMAQMGVDVGVKILNGEKPaESMILMPSTLV 293
Cdd:cd06308 236 LYPTGGKEAIEAALKILNGEKV-PKEIVLPTPLI 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
26-294 |
1.72e-54 |
|
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: 178.24 E-value: 1.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKE 105
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELG--VKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKGADAT--VQTNNVQAGEIACQYIV-DKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVLSdD 182
Cdd:cd06322 80 GIPVFTVDVKADGAKVVthVGTDNYAGGKLAGEYALkALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKKYPNIEIVA-E 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 183 QDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTMVEASASQDP 261
Cdd:cd06322 159 QPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKeDKIKVIGFDGNPEAIKAIAKGGKIKADIAQQP 238
|
250 260 270
....*....|....*....|....*....|...
gi 1113985319 262 YAMAQMGVDVGVKILNGEkPAESMILMPSTLVT 294
Cdd:cd06322 239 DKIGQETVEAIVKYLAGE-TVEKEILIPPKLYT 270
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
25-294 |
8.72e-51 |
|
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: 168.95 E-value: 8.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYnPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEY-PGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD---VSAKGADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGINVLs 180
Cdd:cd06301 81 AGIPLVYVNrepDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGvLGHEAQILRTEGNKDVLAKYPGMKIV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAK-QLKRDNIIITSVDGAPDIEEALKGNTMvEASASQ 259
Cdd:cd06301 160 AEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEaAGKKDDILVAGIDATPDALKAMKAGRL-DATVFQ 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1113985319 260 DPYAMAQMGVDVGVKILNGEKpAESMILMPSTLVT 294
Cdd:cd06301 239 DAAGQGETAVDVAVKAAKGEE-VESDIWIPFELVT 272
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
26-280 |
3.64e-45 |
|
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: 154.00 E-value: 3.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNpNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKE 105
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELG-GEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKGA--DATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAK-APGINVLSD 181
Cdd:pfam13407 80 GIPVVTFDSDAPSSprLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGsPGDPNANERIDGFKKVLKEkYPGIKVVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQ-KIDAVFTINDPQAIGTDLAAKQL-KRDNIIITSVDGAPDIEEALKGNTMvEASASQ 259
Cdd:pfam13407 160 VEGTNWDPEKAQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAgLAGKVVVTGFDATPEALEAIKDGTI-DATVLQ 238
|
250 260
....*....|....*....|.
gi 1113985319 260 DPYAMAQMGVDVGVKILNGEK 280
Cdd:pfam13407 239 DPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
25-293 |
1.54e-43 |
|
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: 150.21 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYnPNAEVIAVSADyDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKEL-ADLEYKLVTSS-NANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAV-IDRVNGCRSVFAKAPGINVLsD 181
Cdd:cd06311 79 AGIPVVNFDrgLNVLIYDLYVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVnEERVAGFKEVIKGNPGIKIL-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNIIItsVDGAPDIEEALK----GNTMVEASA 257
Cdd:cd06311 158 MQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKV--MTGGGGSQEYFKrimdGDPIWPASA 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 1113985319 258 SQDPyAMAQMGVDVGVKILNGEKPAESMILMPSTLV 293
Cdd:cd06311 236 TYSP-AMIADAIKLAVLILKGGKTVEKEVIIPSTLV 270
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
25-294 |
6.74e-42 |
|
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: 145.84 E-value: 6.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAqK 104
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVDKL----GGKGDVIIQNG-PQVSAVIDRVNGCRSVFA-KAPGI 176
Cdd:cd20008 80 AGIPVVLVDsgANTDDYDAFLATDNVAAGALAADELAELLkasgGGKGKVAIISFqAGSQTLVDREEGFRDYIKeKYPDI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 177 NVLsDDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTMVeA 255
Cdd:cd20008 160 EIV-DVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKaGKIVLVGFDSSPDEVALLKSGVIK-A 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 1113985319 256 SASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVT 294
Cdd:cd20008 238 LVVQDPYQMGYEGVKTAVKALKGEEIVEKNVDTGVTVVT 276
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
25-301 |
4.58e-40 |
|
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: 141.20 E-value: 4.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRG--YELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGAD-----ATVQTNNVQAGEIACQYIVDKL-GGKGDVI-IQNGPQVSAVIDRVNGCRSVFAKAPGIN 177
Cdd:cd06309 79 AGIPVILVDRTIDGEDgslyvTFIGSDFVEEGRRAAEWLVKNYkGGKGNVVeLQGTAGSSVAIDRSKGFREVIKKHPNIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 178 VLsDDQDAKGSRDGGLNVMQGHLTRFQ-KIDAVFTINDPQAIGT----DLAAKQLKRDnIIITSVDGAPDIEEALKGNTM 252
Cdd:cd06309 159 IV-ASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAiqalKEAGLKPGKD-VLVVGIDGQKDALEAIKAGEL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1113985319 253 ---VEASASQDPYAmaqmgVDVGVKILNGEKPAEsMILMPSTLVTRENVGEY 301
Cdd:cd06309 237 natVECNPLFGPTA-----FDTIAKLLAGEKVPK-LIIVEERLFDKDNAAEE 282
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
25-294 |
2.29e-39 |
|
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: 139.11 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEynPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKK--KGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGA--DATVQTNNVQAGEIACQYIVDKLGGKGDV-IIQNGPQVSAVIDRVNGCRSVFAKAPGINVLsD 181
Cdd:cd19972 79 AGIPVIAVDRNPEDApgDTFIATDSVAAAKELGEWVIKQTGGKGEIaILHGQLGTTPEVDRTKGFQEALAEAPGIKVV-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDN-IIITSVDGAPDIEEALKGNTMvEASASQD 260
Cdd:cd19972 158 EQTADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHkIWVVGFDGDVAGLKAVKDGVL-DATMTQQ 236
|
250 260 270
....*....|....*....|....*....|....
gi 1113985319 261 PYAMAQMGVDVGVKILNGeKPAESMILMPSTLVT 294
Cdd:cd19972 237 TQKMGRLAVDSAIDLLNG-KAVPKEQLQDAVLTT 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
25-298 |
3.27e-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: 380542 [Multi-domain] Cd Length: 278 Bit Score: 139.03 E-value: 3.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELG--YEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGAD--ATVQTNNVQAGEIACQYIVDKLGGKGD-----VIIQNGPQVSAVIDRVNGCRSVFAKApGIN 177
Cdd:cd06319 79 AKIPVVIADIGTGGGDyvSYIISDNYDGGYQAGEYLAEALKENGWgggsvGIIAIPQSRVNGQARTAGFEDALEEA-GVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 178 VLSDDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDN-IIITSVDGAPDIEEALKGNTMVeAS 256
Cdd:cd06319 158 EVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGdILVVGFDGDPEALDLIKDGKLD-GT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1113985319 257 ASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRENV 298
Cdd:cd06319 237 VAQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
25-302 |
7.81e-39 |
|
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: 138.53 E-value: 7.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPN-AEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQ 103
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLiKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVDVSAKGADAT--VQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGINVLs 180
Cdd:cd19996 81 AAGIPVVLFDSGVGSDKYTafVGVDDAAFGRVGAEWLVKQLGGKGNIIALRGiAGVSVSEDRWAGAKEVFKEYPGIKIV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNIIITSVDgAPDIEEALKGNTMVEASASQD 260
Cdd:cd19996 160 GEVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPMTGED-NNGFLKAWKELPGFKSIAPSY 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1113985319 261 PYAMAQMGVDVGVKILNGEKPAESMILmPSTLVTRENVGEYK 302
Cdd:cd19996 239 PPWLGATALDAALAALEGEPVPKYVYI-PLPVITDENLDQYV 279
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
25-289 |
3.69e-38 |
|
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: 135.98 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKeyNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAA--KLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGAD--ATVQTNNVQAGEIACQYIVDKLGGKGDVI-IQNGPQVSAVIDRVNGCRSVFAKAPGINVLSd 181
Cdd:cd19968 79 AGIPVVTVDRRAEGAApvPHVGADNVAGGREVAKFVVDKLPNGAKVIeLTGTPGSSPAIDRTKGFHEELAAGPKIKVVF- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRF-QKIDAVFTINDPQAIGTDLAAKQ--LKRDNIIITSVDGAPDIEEALKGNTMvEASAS 258
Cdd:cd19968 158 EQTGNFERDEGLTVMENILTSLpGPPDAIICANDDMALGAIEAMRAagLDLKKVKVIGFDAVPDALQAIKDGEL-YATVE 236
|
250 260 270
....*....|....*....|....*....|.
gi 1113985319 259 QDPYAMAQMGVDVGVKILNGEKPAESMILMP 289
Cdd:cd19968 237 QPPGGQARTALRILVDYLKDKKAPKKVNLKP 267
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
25-294 |
7.09e-38 |
|
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: 135.44 E-value: 7.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSA-DYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQ 103
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELG--VELDVQGPpTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVDVS---AKGADATVQTNNVQAGEIACQYIVDKLGGKGDV-IIQNGPQVSAVIDRVNGCRSVFAKAPGINVL 179
Cdd:cd20007 79 DAGIKVVTVDTTlgdPSFVLSQIASDNVAGGALAAEALAELIGGKGKVlVINSTPGVSTTDARVKGFAEEMKKYPGIKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 180 ----SDDQDAKGSrdgglNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQL-KRDNIIITSVDGAPDIEEALKGNTmVE 254
Cdd:cd20007 159 gvqySENDPAKAA-----SIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAgKTGKVKVVGFDASPAQVEQLKAGT-ID 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1113985319 255 ASASQDPYAMAQMGVDVGVKILNGeKPAESMILMPSTLVT 294
Cdd:cd20007 233 ALIAQKPAEIGYLAVEQAVAALTG-KPVPKDILTPFVVIT 271
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
25-298 |
1.41e-37 |
|
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: 134.70 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06320 1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD-------VSAKGADAT--VQTNNVQAGEIACQYIVDKLGGKGDV-IIQNGPQVSAVIDRVNGCRSVFAKAP 174
Cdd:cd06320 81 KGIPVINLDdavdadaLKKAGGKVTsfIGTDNVAAGALAAEYIAEKLPGGGKVaIIEGLPGNAAAEARTKGFKETFKKAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 175 GINVLSD---DQDAKGSRDGGLNVMQGHltrfQKIDAVFTINDPQAIGTDLAAKQL-KRDNIIITSVDGAPDIEEALKGN 250
Cdd:cd06320 161 GLKLVASqpaDWDRTKALDAATAILQAH----PDLKGIYAANDTMALGAVEAVKAAgKTGKVLVVGTDGIPEAKKSIKAG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1113985319 251 TMvEASASQDPYAMAQMGVDVGVKILNGEKPAESMILmPSTLVTRENV 298
Cdd:cd06320 237 EL-TATVAQYPYLEGAMAVEAALRLLQGQKVPAVVAT-PQALITKDNV 282
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
1-295 |
4.40e-37 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 134.06 E-value: 4.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 1 MKKL--LLAGLVLAMS-TVSAQAKDlnKIGISLGSLGNPFFVTMVNGATAKAKE--YNpnaeVIAVSADYDLNKQFTQVD 75
Cdd:PRK10653 3 MKKLatLVSAVALSATvSANAMAKD--TIALVVSTLNNPFFVSLKDGAQKEADKlgYN----LVVLDSQNNPAKELANVQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 76 NFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVDVSAKGAD--ATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNG 153
Cdd:PRK10653 77 DLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEvvSHIASDNVAGGKMAGDFIAKKLGEGAKVIQLEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 154 -PQVSAVIDRVNGCRSVfAKAPGINVLSDdQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNI 232
Cdd:PRK10653 157 iAGTSAARERGEGFKQA-VAAHKFNVLAS-QPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1113985319 233 IITSVDGAPDIEEALKGNTMVeASASQDPYAMAQMGVDVGVKILNGEKpAESMILMPSTLVTR 295
Cdd:PRK10653 235 MVVGFDGTPDGIKAVNRGKLA-ATIAQQPDQIGAIGVETADKVLKGEK-VEAKIPVDLKLVTK 295
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
25-294 |
4.46e-37 |
|
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: 133.22 E-value: 4.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEViaVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTV--FDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKG-ADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGP--QVSAVIdRVNGCRSVFAKAPGINVL 179
Cdd:cd19967 79 AGIPVFLIDreINAEGvAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKesDTNAQL-RSQGFHSVIDQYPELKMV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 180 SdDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDN-IIITSVDGAPDIEEALKGNTMVeASAS 258
Cdd:cd19967 158 A-QQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAGdVIIVGFDGSNDVRDAIKEGKIS-ATVL 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1113985319 259 QDPYAMAQMGVDVGVKIL-NGEKPAESMILMPSTLVT 294
Cdd:cd19967 236 QPAKLIARLAVEQADQYLkGGSTGKEEKQLFDCVLIT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
25-211 |
1.15e-35 |
|
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: 130.51 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPN---AEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKR 101
Cdd:cd19999 1 VIGVSNGYVGNEWRAQMIADFEEVAAEYKEEgviSDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 102 AQKEGIAVVAVDVSAKGADAT-VQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGINVL 179
Cdd:cd19999 81 AQAAGILVVSFDQPVSSPDAInVVIDQYKWAAIQAQWLAEQLGGKGNIVAINGvAGNPANEARVKAADDVFAKYPGIKVL 160
|
170 180 190
....*....|....*....|....*....|....
gi 1113985319 180 sddQDAKGSRDGGL--NVMQGHLTRFQKIDAVFT 211
Cdd:cd19999 161 ---ASVPGGWDQATaqQVMATLLATYPDIDGVLT 191
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
25-297 |
2.47e-34 |
|
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: 126.37 E-value: 2.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLG--VELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKGADAT-VQTNNVQAGEIACQYIVDKLGGKGD--VIIQNGPQVSAVIDRVNGCRSVFAKAP----- 174
Cdd:cd06318 79 AGIPVITVDsaLDPSANVATqVGRDNKQNGVLVGKEAAKALGGDPGkiIELSGDKGNEVSRDRRDGFLAGVNEYQlrkyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 175 --GINVLSDDQdAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNT 251
Cdd:cd06318 159 ksNIKVVAQPY-GNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMlDKVKVAGADGQKEALKLIKDGK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1113985319 252 MVeASASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTREN 297
Cdd:cd06318 238 YV-ATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPTALITKDN 282
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
25-280 |
2.87e-34 |
|
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: 125.92 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGA--DATVQTNNVQAGEIACQYIVDKLGGKGDV-IIQNGPQVSAVIDRVNGCRSVFAKAPGINVLSD 181
Cdd:cd06310 81 KGIPVIVIDSGIKGDayLSYIATDNYAAGRLAAQKLAEALGGKGKVaVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLK-RDNIIITSVDGAPDIEEALKgNTMVEASASQD 260
Cdd:cd06310 161 SQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKlSGQIKIVGFDSQEELLDALK-NGKIDALVVQN 239
|
250 260
....*....|....*....|
gi 1113985319 261 PYAMAQMGVDVGVKILNGEK 280
Cdd:cd06310 240 PYEIGYEGIKLALKLLKGEE 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
26-294 |
2.91e-34 |
|
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: 126.04 E-value: 2.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKE 105
Cdd:cd19973 2 IGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVS---AKGADATVQTNNVQAGEIACQYIVDKLGGKGDVI--IQNGPQVSAVIDRVNGCRSVFA---KAPGIN 177
Cdd:cd19973 82 GVLVIALDTPtdpIDAADATFATDNFKAGVLIGEWAKAALGAKDAKIatLDLTPGHTVGVLRHQGFLKGFGideKDPESN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 178 VLSDD------QDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQL-KRDNIIITSVDGA-PDIEEALKG 249
Cdd:cd19973 162 EDEDDsqvvgsADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAgKEKGVLIVSVDGGcPGVKDVKDG 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1113985319 250 ntMVEASASQDPYAMAQMGVDVGVKIL-NGEKPAESMILMPSTLVT 294
Cdd:cd19973 242 --IIGATSQQYPLRMAALGVEAIAAFAkTGGTKGSGFTDTGVTLVT 285
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
32-294 |
5.77e-34 |
|
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: 125.00 E-value: 5.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 32 SLGNPFFVTMVNGATAKAKEYNPNAEVIAvSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVA 111
Cdd:cd06314 8 GLNNPFWDLAEAGAEKAAKELGVNVEFVG-PQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 112 VDVSAKGAD--ATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGINVLS--DDQDak 186
Cdd:cd06314 87 FDSDAPDSKrlAYIGTDNYEAGREAGELMKKALPGGGKVAIITGgLGADNLNERIQGFKDALKGSPGIEIVDplSDND-- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 187 gSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKgNTMVEASASQDPYAMA 265
Cdd:cd06314 165 -DIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKvGKVKIVGFDTLPETLQGIK-DGVIAATVGQRPYEMG 242
|
250 260
....*....|....*....|....*....
gi 1113985319 266 QMGVDVGVKILNGEKPAESMILMPSTLVT 294
Cdd:cd06314 243 YLSVKLLYKLLKGGKPVPDVIDTGVDVVT 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
25-303 |
7.08e-33 |
|
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: 122.82 E-value: 7.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNA---EVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKR 101
Cdd:cd06300 1 TIGLSNTYAGNSWREQMIASLKADAAQSGQKGlvkELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 102 AQKEGIAVVAVD--VSAKGAdATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGINV 178
Cdd:cd06300 81 AADAGIPVVAFDgaVTSPDA-YNVSNDQVEWGRLGAKWLFEALGGKGNVLVVRGiAGAPASADRHAGVKEALAEYPGIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 179 LSDD----QDAKGSRdgglnVMQGHLTRFQKIDAVFTiNDPQAIGTDLAAKQLKRDNIIITSVDGAPD----IEEALKGN 250
Cdd:cd06300 160 VGEVfggwDEATAQT-----AMLDFLATHPQVDGVWT-QGGEDTGVLQAFQQAGRPPVPIVGGDENGFakqwWKHPKKGL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1113985319 251 TmveASASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRENVGEYKG 303
Cdd:cd06300 234 T---GAAVWPPPAIGAAGLEVALRLLEGQGPKPQSVLLPPPLITNDDAKAWYK 283
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
37-295 |
7.60e-33 |
|
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: 121.94 E-value: 7.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 37 FFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVD--V 114
Cdd:cd20006 15 FWQTVKSGAEAAAKEYGVDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDspV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 115 SAKGADATVQTNNVQAGEIACQYIVDKLGGKGDV-IIQNGPQVSAVIDRVNGCRSVFAKAPGINVLS---DDQDAKGSRD 190
Cdd:cd20006 95 NSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVaIVSFVKGSSTAIEREEGFKQALAEYPNIKIVEteyCDSDEEKAYE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 191 GGLNVmqghLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTmVEASASQDPYAMAQMGV 269
Cdd:cd20006 175 ITKEL----LSKYPDINGIVALNEQSTLGAARALKELGLgGKVKVVGFDSSVEEIQLLEEGI-IDALVVQNPFNMGYLSV 249
|
250 260
....*....|....*....|....*.
gi 1113985319 270 DVGVKILNGEKPaESMILMPSTLVTR 295
Cdd:cd20006 250 QAAVDLLNGKKI-PKRIDTGSVVITK 274
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
37-302 |
9.27e-32 |
|
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: 119.40 E-value: 9.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 37 FFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVD--V 114
Cdd:cd06317 13 FFNQINQGAQAAAKDLG--VDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDavI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 115 SAKGADATVQTNNVQAGEI----ACQYIVDKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVLSdDQDAKGSRD 190
Cdd:cd06317 91 PSDFQAAQVGVDNLEGGKEigkyAADYIKAELGGQAKIGVVGALSSLIQNQRQKGFEEALKANPGVEIVA-TVDGQNVQE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 191 GGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAK-QLKRDNIIITSVDGAPDIEEALKGNTMVEASASQDPYAMAQMGV 269
Cdd:cd06317 170 KALSAAENLLTANPDLDAIYATGEPALLGAVAAVRsQGRQGKIKVFGWDLTKQAIFLGIDEGVLQAVVQQDPEKMGYEAV 249
|
250 260 270
....*....|....*....|....*....|...
gi 1113985319 270 DVGVKILNGEKPaESMILMPSTLVTRENVGEYK 302
Cdd:cd06317 250 KAAVKAIKGEDV-EKTIDVPPTIVTKENVDQFR 281
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
25-295 |
1.24e-31 |
|
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: 118.87 E-value: 1.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADAT--VQTNNVQAGEIACQYIVDKLGGKGDVI-IQNGPQVSAVIDRVNGCRSVFAKAPGINVLSD 181
Cdd:cd20004 81 QGIPVVIIDSDLGGDAVIsfVATDNYAAGRLAAKRMAKLLNGKGKVAlLRLAKGSASTTDRERGFLEALKKLAPGLKVVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTmVEASASQD 260
Cdd:cd20004 161 DQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLaGKVKFIGFDASDLLLDALRAGE-ISALVVQD 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1113985319 261 PYAMAQMGVDVGVKILNGEKPAESMILmPSTLVTR 295
Cdd:cd20004 240 PYRMGYLGVKTAVAALRGKPVPKRIDT-GVVLVTK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
25-303 |
2.99e-31 |
|
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: 118.55 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNG--ATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRA 102
Cdd:cd19998 1 KIALSNSYSGNDWRQEMINIakAAAKQPPYADKVELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 103 QKEGIAVVAVD--VSAKGAdATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAV-IDRVNGCRSVFAKAPGINVL 179
Cdd:cd19998 81 CDAGIVVVAFDnvVDEPCA-YNVNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVdRDRYEGAKEVFKKYPDIKVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 180 SDDQ----DAKGSRdgglnVMQGHLTRFQKIDAVFTindpQAiGTDLAAKQLKRDNIIITSVDGapdieEALKGNTMVEA 255
Cdd:cd19998 160 AEYYgnwdDGTAQK-----AVADALAAHPDVDGVWT----QG-GETGVIKALQAAGHPLVPVGG-----EAENGFRKAML 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1113985319 256 ----------SASQDPYaMAQMGVDVGVKILNGEKPaESMILMPSTLVTRENVGEYKG 303
Cdd:cd19998 225 eplanglpgiSAGSPPA-LSAVALKLAVAVLEGEKE-PKTIELPLPWVTTDDVKLCQG 280
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
25-279 |
3.25e-30 |
|
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: 115.04 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKE---YNPNAEVIAVSADYDlnKQFTQVDNFIAAGVDMILINAVDANAIEVAIKR 101
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEangYELLVKGIKQETDIE--QQIAIVENLIAQKVDAIVIAPADSKALVPVLKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 102 AQKEGIAVVAVDV-------SAKGADAT-VQTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAK 172
Cdd:cd19970 79 AVDAGIAVINIDNrldadalKEGGINVPfVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGiPGADNAQQRKAGFLKAFEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 173 ApGINVLsDDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGtdlAAKQL----KRDNIIITSVDGAPDIEEALK 248
Cdd:cd19970 159 A-GMKIV-ASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALG---AIKAVdaagKAGKVLVVGFDNIPAVRPLLK 233
|
250 260 270
....*....|....*....|....*....|.
gi 1113985319 249 GNTMVeASASQDPYAMAQMGVDVGVKILNGE 279
Cdd:cd19970 234 DGKML-ATIDQHPAKQAVYGIEYALKMLNGE 263
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
25-301 |
3.60e-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: 112.72 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAV-SADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQ 103
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEELG--IEVVAVtDANFDPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVDVSAKGADAT------VQTNNVQAGEIACQYIVDKLGGKGDV-IIQNGPQVSAVIDRVNGCRSVFA-KAPG 175
Cdd:cd06316 79 DAGIKLVFMDNVPDGLEAGkdyvsvVSSDNRGNGQIAAELLAEAIGGKGKVgIIYHDADFYATNQRDKAFKDTLKeKYPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 176 INVLsDDQDAKGSRDGGlNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNIIITSVDGAPDIEEALKGNTMVEA 255
Cdd:cd06316 159 IKIV-AEQGFADPNDAE-EVASAMLTANPDIDGIYVSWDTPALGVISALRAAGRSDIKITTVDLGTEIALDMAKGGNVKG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1113985319 256 SASQDPYAMAQMGVDVGVKILNGeKPAESMILMPSTLVTRENVGEY 301
Cdd:cd06316 237 IGAQRPYDQGVAEALAAALALLG-KEVPPFIGVPPLAVTKDNLLEA 281
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
25-284 |
1.64e-28 |
|
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: 110.75 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd19992 1 KIGVSFPTQQEERWQKDKEYMEEEAKELG--VELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVDKlGGKGDVIIQNGPQVSAVIDRV-NGCRSVFAKAP---GINV 178
Cdd:cd19992 79 AGVPVISYDrlILNADVDLYVGRDNYKVGQLQAEYALEA-VPKGNYVILSGDPGDNNAQLItAGAMDVLQPAIdsgDIKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 179 LSdDQDAKG-SRDGGLNVMQGHLTRFQ-KIDAVFTINDPQAIGT--DLAAKQLKrDNIIITSVDGAPDIEEALKGNTMVe 254
Cdd:cd19992 158 VL-DQYVKGwSPDEAMKLVENALTANNnNIDAVLAPNDGMAGGAiqALKAQGLA-GKVFVTGQDAELAALKRIVEGTQT- 234
|
250 260 270
....*....|....*....|....*....|
gi 1113985319 255 ASASQDPYAMAQMGVDVGVKILNGEKPAES 284
Cdd:cd19992 235 MTVWKDLKELARAAADAAVKLAKGEKPQTT 264
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
25-282 |
5.59e-28 |
|
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: 109.21 E-value: 5.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEAGGYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAV--DVSAKGADATVQTNNVQAGEIACQYIVDKL-GGKGDVIIQNGPQ-VSAVIDRVNGCRSVfAKAPGINVLs 180
Cdd:cd06306 81 AGIPVIDLvnGIDSPKVAARVLVDFYDMGYLAGEYLVEHHpGKPVKVAWFPGPAgAGWAEDREKGFKEA-LAGSNVEIV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRDGGLNVMQGHLTRFQKIDAVftindpqaIGTDLAA-------KQL-KRDNIIITSVDGAPDIEEALKGNTm 252
Cdd:cd06306 159 ATKYGDTGKAVQLNLVEDALQAHPDIDYI--------VGNAVAAeaavgalREAgLTGKVKVVSTYLTPGVYRGIKRGK- 229
|
250 260 270
....*....|....*....|....*....|
gi 1113985319 253 VEASASQDPYAMAQMGVDVGVKILNGEKPA 282
Cdd:cd06306 230 ILAAPSDQPVLQGRIAVDQAVRALEGKPVP 259
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
37-296 |
3.44e-26 |
|
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: 104.25 E-value: 3.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 37 FFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVD--V 114
Cdd:cd20005 13 FWKAVKKGAEQAAKELGVKITFEGPDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVTFDsgV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 115 SAKGADATVQTNNVQAGEIACQYIVDKLGGKGDV-IIQNGPQVSAVIDRVNGCRSVFAKAPG----INVLSDDQDAKGSR 189
Cdd:cd20005 93 PSDLPLATVATDNYAAGALAADHLAELIGGKGKVaIVAHDATSETGIDRRDGFKDEIKEKYPdikvVNVQYGVGDHAKAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 190 DGGLNVMQGHLtrfqKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTMVeASASQDPYAMAQMG 268
Cdd:cd20005 173 DIAKAILQANP----DLKGIYATNEGAAIGVANALKEMGKlGKIKVVGFDSGEAQIDAIKNGVIA-GSVTQNPYGMGYKT 247
|
250 260
....*....|....*....|....*...
gi 1113985319 269 VDVGVKILNGEKPaESMILMPSTLVTRE 296
Cdd:cd20005 248 VKAAVKALKGEEV-EKLIDTGAKWYDKD 274
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
25-293 |
1.67e-25 |
|
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: 102.37 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLG--GTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDV-SAKGADATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVL---S 180
Cdd:cd06305 79 AGIPVVTFDTdSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDKRYDIYKAVLKANPGIKKIvaeL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRDgGLNVMQGHLTRFQK--IDAVFTINDPQAIGTDLAAKQLKRDNIIITSVDGAP-DIEEALKGNTMVEASA 257
Cdd:cd06305 159 GDVTPNTAAD-AQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDISNqDLELMADEGSPWVATA 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 1113985319 258 SQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLV 293
Cdd:cd06305 238 AQDPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT 273
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
26-299 |
2.26e-25 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 103.36 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILInaVDANAIEVAIKRAQKE 105
Cdd:COG1609 64 IGVVVPDLSNPFFAELLRGIEEAARERG--YQLLLANSDEDPEREREALRLLLSRRVDGLIL--AGSRLDDARLERLAEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQ-VSAVIDRVNGCRSVFAKApGINVLSDDQ 183
Cdd:COG1609 140 GIPVVLIDRPLPDPGVpSVGVDNRAGARLATEHLIEL--GHRRIAFIGGPAdSSSARERLAGYREALAEA-GLPPDPELV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 184 DAKG-SRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDgapDIEEAlkgnTMVE---AS 256
Cdd:COG1609 217 VEGDfSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLrvpEDVSVVGFD---DIPLA----RYLTpplTT 289
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1113985319 257 ASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRENVG 299
Cdd:COG1609 290 VRQPIEEMGRRAAELLLDRIEGPDAPPERVLLPPELVVRESTA 332
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
26-293 |
2.34e-24 |
|
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: 99.13 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGA--TAKAKEYNpnaeVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEvaIKRAQ 103
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIedAARERGYS----LLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDEL--LEELL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDkLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKApGINVLSDD 182
Cdd:cd06267 76 AAGIPVVLIDRRLDGLGVdSVVVDNYAGAYLATEHLIE-LGHRRIAFIGGPLDLSTSRERLEGYRDALAEA-GLPVDPEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 183 -QDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDgapDIEEAlkgnTMVE---A 255
Cdd:cd06267 154 vVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLrvpEDISVVGFD---DIPLA----ALLTpplT 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 1113985319 256 SASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLV 293
Cdd:cd06267 227 TVRQPAYEMGRAAAELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
1-295 |
5.61e-24 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 99.18 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 1 MKKLLLAGLVLAMSTVSAQAKDlnkIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAA 80
Cdd:PRK09701 5 LKYFSGTLVGLMLSTSAFAAAE---YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 81 GVDMILINAVDANAIEVAIKRAQKEGIAVVAVD--------VSAKGA-DATVQTNNVQAGEIACQYIVDKLGGK-GDVII 150
Cdd:PRK09701 82 NYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDekidmdnlKKAGGNvEAFVTTDNVAVGAKGASFIIDKLGAEgGEVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 151 QNGPQVSAV-IDRVNGCRSVFAKAPGINvLSDDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQL-K 228
Cdd:PRK09701 162 IEGKAGNASgEARRNGATEAFKKASQIK-LVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAgK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1113985319 229 RDNIIITSVDGAPDIEEALKGNTMVeASASQDPYAMAQMGVDVGVKILNGEK-----PAESMILMPSTLVTR 295
Cdd:PRK09701 241 TGKVLVVGTDGIPEARKMVEAGQMT-ATVAQNPADIGATGLKLMVDAEKSGKvipldKAPEFKLVDSILVTQ 311
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
33-269 |
1.24e-23 |
|
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: 97.41 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 33 LGNPFFVTMVNGATAKAKEYNPNAEVIAvSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAV 112
Cdd:cd19969 9 SGHPYWDDVKEGFEDAGAELGVKTEYTG-PATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 113 DVSAKGAD--ATVQTNNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVLS---DDQDAKG 187
Cdd:cd19969 88 DSDAPESKriSYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHEERVEGFKEAFAEYPGIEVVAvgdDNDDPEK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 188 SRDGGLNVMQGHltrfQKIDAVFTINDPQAIGTDLAAKQL-KRDNIIITSVDGAPDIEEALKgNTMVEASASQDPYAMAQ 266
Cdd:cd19969 168 AAQNTSALLQAH----PDLVGIFGVDASGGVGAAQAVREAgKTGKVKIVAFDDDPETLDLIK-DGVIDASIAQRPWMMGY 242
|
...
gi 1113985319 267 MGV 269
Cdd:cd19969 243 WSL 245
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
26-296 |
7.76e-21 |
|
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: 89.50 E-value: 7.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGA--TAKAKEYNpnaeVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANaievaIKRAQ 103
Cdd:cd06291 2 IGLIVPDISNPFFAELAKYIekELFKKGYK----MILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLD-----IEEYK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVDVSAKGADATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQ-VSAVIDRVNGCRSVFAKApGINVLSDD 182
Cdd:cd06291 73 KLNIPIVSIDRYLSEGIPSVSSDNYQGGRLAAEHLIEK--GCKKILHIGGPSnNSPANERYRGFEDALKEA-GIEYEIIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 183 QDAKG-SRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDGAPDIEEALKGNTMVEasas 258
Cdd:cd06291 150 IDENDfSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIrvpEDVQIIGFDGIEISELLYPELTTIR---- 225
|
250 260 270
....*....|....*....|....*....|....*...
gi 1113985319 259 QDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd06291 226 QPIEEMAKEAVELLLKLIEGEEIEESRIVLPVELIERE 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19997 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
25-307 |
1.38e-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: 380652 [Multi-domain] Cd Length: 305 Bit Score: 89.66 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPN---AEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKR 101
Cdd:cd19997 1 VIALSNSYAGNTWRQQMVDAFEEAAKKAKADgliADYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 102 AQKEGIAVVAVDVSAKGADATVQTNN-VQAGEIACQYIVDKLGGKGDVIIQNGPQVSAV-IDRVNGCRSVFAKAPGINVL 179
Cdd:cd19997 81 ACDAGIKVVVFDSGVTEPCAYILNNDfEDYGAASVEYVADRLGGKGNVLEVRGVAGTSPdEEIYAGQVEALKKYPDLKVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 180 SddqDAKGSRDGglNVMQ----GHLTRFQKIDAVFTINDpQAIGTDLAAKQLKRDNIIITSVDGAPDI---EEALKGNTM 252
Cdd:cd19997 161 A---EVYGNWTQ--SVAQkavtGILPSLPEVDAVITQGG-DGYGAAQAFEAAGRPLPIIIGGNRGEFLkwwQEEYAKNGY 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1113985319 253 VEASASQDPyAMAQMGVDVGVKILNGEKPAESMIlMPSTLVTRENVGEYKGWTSE 307
Cdd:cd19997 235 ETVSVSTDP-GQGSAAFWVALDILNGKDVPKEMI-LPVVTITEDDLDAWLAVTPD 287
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
46-286 |
4.23e-20 |
|
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: 88.11 E-value: 4.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 46 TAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVD--VSAKGADATV 123
Cdd:cd19995 23 EKAMKKLCPDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDrlILGGPADYYV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 124 QTNNVQAGEIACQYIVDKLGGKGD----VIIQNG-PQVSAVIDRVNGCRSVFAK--APGINVLSDDQDAKG-SRDGGLNV 195
Cdd:cd19995 103 SFDNVAVGEAQAQSLVDHLKAIGKkgvnIVMINGsPTDNNAGLFKKGAHEVLDPlgDSGELKLVCEYDTPDwDPANAQTA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 196 MQGHLTRFQ-KIDAVFTINDPQAIGTDLAAKQLKRDNIIITS-----VDGAPDIEEALKGNTMVEASasqdpYAMAQMGV 269
Cdd:cd19995 183 MEQALTKLGnNIDGVLSANDGLAGGAIAALKAQGLAGKVPVTgqdatVAGLQRILAGDQYMTVYKPI-----KKEAAAAA 257
|
250
....*....|....*..
gi 1113985319 270 DVGVKILNGEKPAESMI 286
Cdd:cd19995 258 KVAVALLKGETPPSDLV 274
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
26-295 |
8.12e-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: 86.93 E-value: 8.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYnpNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAV-DANAievAIKRAQK 104
Cdd:cd06280 2 IGLIVPDITNPFFTTIARGIEDAAEKH--GYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSaGPSR---ELKRLLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDkLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKApGINVlsdDQ 183
Cdd:cd06280 77 HGIPIVLIDREVEGLELdLVAGDNREGAYKAVKHLIE-LGHRRIGLITGPLEISTTRERLAGYREALAEA-GIPV---DE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 184 D----AKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLK---RDNIIITSVDGAPDIEEALKGNTMVeas 256
Cdd:cd06280 152 SlifeGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGleiPQDISVVGFDDSDWFEIVDPPLTVV--- 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 1113985319 257 aSQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTR 295
Cdd:cd06280 229 -AQPAYEIGRIAAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
25-286 |
1.07e-19 |
|
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: 87.25 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGG-KIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVV----AVDVSA-KGADAT--VQTNNVQAGEIACQYIV---------DKLG-GKGDVIIQNGPQVS-AVIDRVNGC 166
Cdd:cd01539 81 ANIPVIffnrEPSREDlKSYDKAyyVGTDAEESGIMQGEIIAdywkanpeiDKNGdGKIQYVMLKGEPGHqDAIARTKYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 167 RSVFAKApGINV-LSDDQDAKGSRDGGLNVMQGHLTRF-QKIDAVFTINDPQAIG--TDLAAKQLKRDN----IIITSVD 238
Cdd:cd01539 161 VKTLNDA-GIKTeQLAEDTANWDRAQAKDKMDAWLSKYgDKIELVIANNDDMALGaiEALKAAGYNTGDgdkyIPVFGVD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1113985319 239 GAPDIEEALKGNTMVeASASQDPYAMAQMGVDVGVKILNGEKPAESMI 286
Cdd:cd01539 240 ATPEALEAIKEGKML-GTVLNDAKAQAKAIYELAKNLANGKEPLETGY 286
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
28-269 |
4.13e-19 |
|
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: 84.98 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 28 ISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAvSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGI 107
Cdd:cd06312 5 ISHGSPSDPFWSVVKKGAKDAAKDLGVTVQYLG-PQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 108 AVVAV----DVSAK--GADATVQTNNVQAGEIACQYIVdKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKA-PGINVLS 180
Cdd:cd06312 84 PVIAInsgdDRSKErlGALTYVGQDEYLAGQAAGERAL-EAGPKNALCVNHEPGNPGLEARCKGFADAFKGAgILVELLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRdgglNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKgNTMVEASASQ 259
Cdd:cd06312 163 VGGDPTEAQ----EAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLkGKVKIGTFDLSPETLEAIK-DGKILFAIDQ 237
|
250
....*....|
gi 1113985319 260 DPYAMAQMGV 269
Cdd:cd06312 238 QPYLQGYLAV 247
|
|
| XylF |
COG4213 |
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ... |
25-300 |
6.82e-19 |
|
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];
Pssm-ID: 443359 [Multi-domain] Cd Length: 310 Bit Score: 85.19 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:COG4213 4 KIGVSLPTKTSERWIRDGDNFKAALKELG--YEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADAT--VQTNNVQAGEIACQYIVDKLG--GKGDVIIQNGPQvsaviDRVN------GCRSV---FA 171
Cdd:COG4213 82 AGIPVIAYDRLILNSDVDyyVSFDNVKVGELQGQYLVDGLPlkGKGNIELFGGSP-----TDNNatlffeGAMSVlqpYI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 172 KAPGINVLSdDQDAKG-SRDGGLNVMQGHLTRFQ-KIDAVFTINDPQAIG--TDLAAKQLKrDNIIITSVDGapDIeEAL 247
Cdd:COG4213 157 DSGKLVVVS-GQWTLGwDPETAQKRMENLLTANGnKVDAVLAPNDGLAGGiiQALKAQGLA-GKVVVTGQDA--EL-AAV 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113985319 248 KgnTMVEASASQDPY----AMAQMGVDVGVKILNGEKPAES-----------MILMPSTLVTRENVGE 300
Cdd:COG4213 232 Q--RILAGTQYMTVYkdtrELAEAAAELAVALAKGEKPEVNgtydngkkdvpSYLLEPVAVTKDNVKE 297
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
25-281 |
1.11e-18 |
|
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: 84.01 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEynPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEE--KGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADATVQT--NNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAVIDRVNGCRSV---FAKAPGINVL 179
Cdd:cd01538 79 EGIKVIAYDRLILNADVDYYIsfDNEKVGELQAQALLDAKPEGNYVLIGGSPTDNNAKLFRDGQMKVlqpAIDSGKIKVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 180 SDDQDAKGSRDGGLNVMQGHLTRF-QKIDAVFTINDPQAIGTDLAAK-QLKRDNIIITSVDG-APDIEEALKGNTMVeaS 256
Cdd:cd01538 159 GDQWVDDWLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKaQGLSGGVPVSGQDAdLAAIKRILAGTQTM--T 236
|
250 260
....*....|....*....|....*
gi 1113985319 257 ASQDPYAMAQMGVDVGVKILNGEKP 281
Cdd:cd01538 237 VYKDIRLLADAAAEVAVALMRGEKP 261
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd06302 |
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ... |
25-298 |
6.29e-18 |
|
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: 82.29 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAeVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd06302 1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEV-VYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADATV---QTNNVQAGEIACQYIVDKLGGKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGINVLS 180
Cdd:cd06302 80 AGIKVITWDSDAPPSARDYfvnQADDEGLGEALVDSLAKEIGGKGKVAILSGsLTATNLNAWIKAMKEYLKSKYPDIELV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTMVEAsASQ 259
Cdd:cd06302 160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKtGKVAVTGIGLPNTARPYLKDGSVKEG-VLW 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1113985319 260 DPYAMAQMGVDVGVKILNGEKPAES------------------MILMPSTLVTRENV 298
Cdd:cd06302 239 DPAKLGYLTVYAAYQLLKGKGFTEDsddvgtggkvkvdvaggeILLGPPLVFTKDNV 295
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
28-269 |
4.63e-17 |
|
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: 79.29 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 28 ISLGSLGNPFFVTMVNGATAKAKEYNPNAEViaVSADYDLNKQFTQVDNFIAAGVDMILIN-AVDANAIEVAIKRAQKEG 106
Cdd:cd19966 5 IPGGAPGDPFWTVVYNGAKDAAADLGVDLDY--VFSSWDPEKMVEQFKEAIAAKPDGIAIMgHPGDGAYTPLIEAAKKAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 107 IAVVAVDVSAKGA------DATVQTNNVQAGEIACQYIVDKLG-GKGDVIIQNG--PQVSAVIDRVNGCRSVFAKApGIN 177
Cdd:cd19966 83 IIVTSFNTDLPKLeygdcgLGYVGADLYAAGYTLAKELVKRGGlKTGDRVFVPGllPGQPYRVLRTKGVIDALKEA-GIK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 178 V----LSDDQDAKGSrdgGLNVMQGHLTRFQKIDAVFTIND--PQAIGTDLAAKQLKRDNIIITSVDGAPDIEEALKGNt 251
Cdd:cd19966 162 VdyleISLEPNKPAE---GIPVMTGYLAANPDVKAIVGDGGglTANVAKYLKAAGKKPGEIPVAGFDLSPATVQAIKSG- 237
|
250
....*....|....*...
gi 1113985319 252 MVEASASQDPYAMAQMGV 269
Cdd:cd19966 238 YVNATIDQQPYLQGYLPV 255
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
26-298 |
1.70e-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: 380508 [Multi-domain] Cd Length: 269 Bit Score: 74.96 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKE--YNPnaeVIAVSADYDLNKQFTqVDNFIAAGVDMILINAVDANAIEVAIKRAQ 103
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARErgYTV---LLADTGDDPERELAA-LDSLLSRRVDGLIITPARDDAPDLQELAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 keGIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDkLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKApGINVLSDD 182
Cdd:cd06285 78 --GVPVVLVDRRIGDTALpSVTVDNELGGRLATRHLLE-LGHRRIAVVAGPLNASTGRDRLRGYRRALAEA-GLPVPDER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 183 QDAKGS-RDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDGAPDIEEALKGNTMVEasas 258
Cdd:cd06285 154 IVPGGFtIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLrvpEDLSVVGFDDIPLAAFLPPPLTTVR---- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1113985319 259 QDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRENV 298
Cdd:cd06285 230 QPKYEMGRRAAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
25-219 |
2.37e-15 |
|
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: 74.58 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd19991 1 KIGFSMDSLRVERWQRDRDYFVKKAKELG--AEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVdKLGGKGDVIIQNGPQV--SAVIDRvNGCRSVFA---KAPGIN 177
Cdd:cd19991 79 AGVPVLAYDrlILNADVDLYVSFDNEKVGELQAEALV-KAKPKGNYVLLGGSPTdnNAKLFR-EGQMKVLQpliDSGDIK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1113985319 178 VLSDDQDAKGSRDGGLNVMQGHLTRFQ-KIDAVFTINDPQAIG 219
Cdd:cd19991 157 VVGDQWVDDWDPEEALKIMENALTANNnKIDAVIASNDGTAGG 199
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
25-297 |
6.09e-15 |
|
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: 73.48 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd01540 1 KIGFIVKQPDQPWFQDEWKGAKKAAKELG--FEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADAT-----VQTNNVQAGEIACQYIVDKLGGKG-------DVIIQNGPQVSAVIDRVNGCRSVFAK 172
Cdd:cd01540 79 AGIPVIAVDDQLVDADPMkivpfVGIDAYKIGEAVGEWLAKEMKKRGwddvkevGVLAITMDTLSVCVDRTDGAKDALKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 173 A--PGINVLSDDQDAKGSrDGGLNVMQGHLTRFQKID--AVFTINDPQAIGTDLAAKQ--LKRDNIIITSVDG--APDIE 244
Cdd:cd01540 159 AgfPEDQIFQAPYKGTDT-EGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQagFDAEDIIGVGIGGylAADEE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1113985319 245 EAlKGNTMVEASASQDP----YAMAQMGVDVgvkILNGEKPAESmILMPSTLVTREN 297
Cdd:cd01540 238 FK-KQPTGFKASLYISPdkhgYIAAEELYNW---ITDGKPPPAE-TLTDGVIVTRDN 289
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
26-296 |
7.94e-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: 380516 [Multi-domain] Cd Length: 270 Bit Score: 73.07 E-value: 7.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYnpNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQke 105
Cdd:cd06293 2 IGLVVPDVSNPFFAEVARGVEDAARER--GYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRAR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDklGGKGDVIIQNGPQ-VSAVIDRVNGCRSVFAKAPG--INVLSD 181
Cdd:cd06293 78 GTAVVLLDRPAPGPAGcSVSVDDVQGGALAVDHLLE--LGHRRIAFVSGPLrTRQVAERLAGARAAVAEAGLdpDEVVRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGtdlAAKQLKRDNIII---TSVDGAPDIEEALKGN---TMVea 255
Cdd:cd06293 156 LSAPDANAELGRAAAAQLLAMPPRPTAVFAANDLLALG---LLAGLRRAGLRVpddVSVVGYDDLPFAAAANpplTTV-- 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1113985319 256 saSQDPYAMAQMGVDVGVKILNGEK-PAESMILMPStLVTRE 296
Cdd:cd06293 231 --RQPSYELGRAAADLLLDEIEGPGhPHEHVVFQPE-LVVRS 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19965 |
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ... |
32-263 |
1.39e-13 |
|
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: 69.61 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 32 SLGNPFFVTMVNGATAKAKEYNPNAEVIAvSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVA 111
Cdd:cd19965 8 VTTNPFFQPVKKGMDDACELLGAECQFTG-PQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 112 VDVSAKGADATVQT----NNVQAGEIACQYIVDKLG-GKGDVIIQNG-PQVSAVIDRVNGCRSVFAKAPGiNVLSDDQDA 185
Cdd:cd19965 87 FNVDAPGGENARLAfvgqDLYPAGYVLGKRIAEKFKpGGGHVLLGIStPGQSALEQRLDGIKQALKEYGR-GITYDVIDT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 186 KGSRDGGLNVMQGHLTRFQKIDAVFtinDPQAIGTDLAAKQLKRDNI----IITSVDGAPDIEEALKGNTmVEASASQDP 261
Cdd:cd19965 166 GTDLAEALSRIEAYYTAHPDIKAIF---ATGAFDTAGAGQAIKDLGLkgkvLVGGFDLVPEVLQGIKAGY-IDFTIDQQP 241
|
..
gi 1113985319 262 YA 263
Cdd:cd19965 242 YL 243
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
25-295 |
2.53e-13 |
|
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: 68.74 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPnaEVIAVsadydlnkQFTQVDNF-----------IAAGVDMILINAVDAN 93
Cdd:cd06307 1 RFGFLLPSPENPFYELLRRAIEAAAAALRD--RRVRL--------RIHFVDSLdpealaaalrrLAAGCDGVALVAPDHP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 94 AIEVAIKRAQKEGIAVVAV--DVSAKGADATVQTNNVQAGEIACQYIVDKLGGKGD--VIIQNGPQVSAVIDRVNGCRSV 169
Cdd:cd06307 71 LVRAAIDELAARGIPVVTLvsDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRPGkvLVILGSHRFRGHEEREAGFRSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 170 FA-KAPGINVL----SDDQDAKGSRdgglnVMQGHLTRFQKIDAVFTIN-DPQAIGTDLAAKQLKRDNIIITSvDGAPDI 243
Cdd:cd06307 151 LReRFPDLTVLevleGLDDDELAYE-----LLRELLARHPDLVGIYNAGgGNEGIARALREAGRARRVVFIGH-ELTPET 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1113985319 244 EEALKGNTMvEASASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTR 295
Cdd:cd06307 225 RRLLRDGTI-DAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR 275
|
|
| PBP1_LsrB_Quorum_Sensing |
cd20003 |
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ... |
25-283 |
6.29e-13 |
|
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: 67.69 E-value: 6.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEynPNAEVIAV-SADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQ 103
Cdd:cd20003 1 TIAMIPKLVGVPYFTAAGQGAQEAAKE--LGVDVTYDgPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVDVSAKGADATVQTNNVQAGEIACQYI---VDKLGGKGDVIIqngpqVSAVIDRVNGCRSV-FAKA------ 173
Cdd:cd20003 79 KKGIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVdmvAEQTGEKGKVAI-----VTSSPTATNQNAWIkAMKAyiaeky 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 174 PGINVLS---DDQDAKGSRDGGLNVMQGHLTrfqkIDAVFTINDPQAIGTDLAAKQLKRD-NIIITSVDGAPDIEEALKG 249
Cdd:cd20003 154 PDMKIVTtqyGQEDPAKSLQVAENILKAYPD----LKAIIAPDSVALPGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKD 229
|
250 260 270
....*....|....*....|....*....|....
gi 1113985319 250 NTmVEASASQDPYAMAQMGVDVGVKILNGEKPAE 283
Cdd:cd20003 230 GT-VKSVVLWDVVDLGYLAVYVARALADGTLLKV 262
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
26-297 |
2.67e-12 |
|
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: 65.73 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNPNaeVIAVSADYDLNKQFTQVDNFIAAGVDMILInAVDANAIEVAIKRAQKE 105
Cdd:cd19976 2 IGLIVPDISNPFFSELVRGIEDTLNELGYN--IILCNTYNDFEREKKYIQELKERNVDGIII-ASSNISDEAIIKLLKEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKGAD-ATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQVSA-VIDRVNGCRSVFAKApgiNVLSDDQ 183
Cdd:cd19976 79 KIPVVVLDRYIEDNDsDSVGVDDYRGGYEATKYLIEL--GHTRIGCIVGPPSTYnEHERIEGYKNALQDH---NLPIDES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 184 DAKGSRD---GGLnVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-----------DNIIITSVdgapdIEEALkg 249
Cdd:cd19976 154 WIYSGESsleGGY-KAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLkipedlsvigfDNIILSEY-----ITPAL-- 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1113985319 250 NTMveasaSQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTREN 297
Cdd:cd19976 226 TTI-----AQPIFEMGQEAAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_ABC_rhamnose |
cd20000 |
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ... |
25-150 |
4.41e-12 |
|
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: 65.36 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVS-ADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQ 103
Cdd:cd20000 1 RIAFLPKSLGNPYFDAARDGAKEAAKELG--GELIFVGpTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKAR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVD--VSAKGADATV-QTNNVQAGEIACQYIVDKLGGKGDVII 150
Cdd:cd20000 79 AAGIKVVTFDsdVAPEARDLFVnQADADGIGRAQVDMMAELIGGEGEFAI 128
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
31-302 |
1.49e-11 |
|
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: 64.16 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 31 GSLGNPFFVTMVNGATAKAKEYNPNAEVIavSADYDLNKQFTQVDNFIAA--GVDMILINAVDANAIEVaIKRAQKEGIA 108
Cdd:cd06324 8 GKEDEPFWQNVTRFMQAAAKDLGIELEVL--YANRNRFKMLELAEELLARppKPDYLILVNEKGVAPEL-LELAEQAKIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 109 VVAVDVSAKGAD---------------ATVQTNNVQAG-EIAcQYIVDKL-----GGKGDVIIQNG-PQVSAVIDRVNGC 166
Cdd:cd06324 85 VFLINNDLTDEErallgkprekfkywlGSIVPDNEQAGyLLA-KALIKAArkksdDGKIRVLAISGdKSTPASILREQGL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 167 RSVFAKAPGINVLsDDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRD---NIIITSVDGAPDI 243
Cdd:cd06324 164 RDALAEHPDVTLL-QIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpgkDVLVGGIDWSPEA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113985319 244 EEALKGNTMVeASA----SQDPYAMaqmgvdvgVKI---LNGEKPA--ESMILMPSTLVTRENVGEYK 302
Cdd:cd06324 243 LQAVKDGELT-ASVgghfLEGAWAL--------VLLydyHHGIDFAagTSVQLKPMLAITRDNVAQYL 301
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
26-296 |
2.34e-11 |
|
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member 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: 380522 [Multi-domain] Cd Length: 268 Bit Score: 63.07 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAieVAIKRAQKE 105
Cdd:cd06299 2 IGLLVPDIRNPFFAELASGIEDEARAHG--YSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENS--EGLQALIAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVD--VSAKGADATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQVSAVI-DRVNGCRSVFAKApGINVLSDD 182
Cdd:cd06299 78 GLPVVFVDreVEGLGGVPVVTSDNRPGAREAVEYLVSL--GHRRIGYISGPLSTSTGrERLAAFRAALTAA-GIPIDEEL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 183 QDAKGSR-DGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLK---RDNIIITSVDGAPDIEEALKGNTMVeasaS 258
Cdd:cd06299 155 VAFGDFRqDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFDDVPWFELLSPPLTVI----A 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1113985319 259 QDPYAMAQMGVDVGVKILNGEKPAESMILmPSTLVTRE 296
Cdd:cd06299 231 QPVERIGRRAVELLLALIENGGRATSIRV-PTELIPRE 267
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
32-296 |
2.65e-11 |
|
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: 62.56 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 32 SLGNPFFVTMVNG--ATAKAKEYNpnaeVIAVSADYDLNKQFTQVDNFIAAGVD-MILINAVdanaIEVAIKRAQKEGIA 108
Cdd:cd06284 8 NISNPFYSEILRGieDAAAEAGYD----VLLGDTDSDPEREDDLLDMLRSRRVDgVILLSGR----LDAELLSELSKRYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 109 VVAVDVSAKGAD-ATVQTNNVQAGEIACQYIVdKLGGKGDVIIqNGPQ--VSAvIDRVNGCRSVFAKApGINVLSDDQDA 185
Cdd:cd06284 80 IVQCCEYIPDSGvPSVSIDNEAAAYDATEYLI-SLGHRRIAHI-NGPLdnVYA-RERLEGYRRALAEA-GLPVDEDLIIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 186 KG-SRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGtdlAAKQLKRDNIII---TSVDGAPDIEEAlkgnTMVEAS---AS 258
Cdd:cd06284 156 GDfSFEAGYAAARALLALPERPTAIFCASDELAIG---AIKALRRAGLRVpedVSVIGFDDIEFA----EMFSPSlttIR 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 1113985319 259 QDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd06284 229 QPRYEIGETAAELLLEKIEGEGVPPEHIILPHELIVRE 266
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20002 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
34-150 |
2.71e-11 |
|
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: 63.11 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 34 GNPFFVTMVNGATAKAKEYNPNAEVIAvSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVD 113
Cdd:cd20002 10 GIPWFNRMEQGVKKAGKEFGVNAYQVG-PADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKGIVVITHE 88
|
90 100 110
....*....|....*....|....*....|....*....
gi 1113985319 114 V-SAKGADATVQT-NNVQAGEIACQYIVDKLGGKGDVII 150
Cdd:cd20002 89 SpGQKGADWDVELiDNEKFGEAQMELLAKEMGGKGEYAI 127
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
25-266 |
3.19e-11 |
|
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: 62.53 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQftQVDNFIAAGVDMILInAVDANAIEVAIKRAQK 104
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTN--AIDLLLASGADGIII-TTPAPSGDDITAKAEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADA--TVQTNNVQAGEIACQYIVdKLGGKGDVIIQNGPQ-VSAVIDRVNGCRSVFAKApGINVlSD 181
Cdd:pfam00532 80 YGIPVIAADDAFDNPDGvpCVMPDDTQAGYESTQYLI-AEGHKRPIAVMAGPAsALTARERVQGFMAALAAA-GREV-KI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKGSRD--GGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNII------ITSVDGAPDIEEAlkGNTMV 253
Cdd:pfam00532 157 YHVATGDNDipDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVKIPdivgigINSVVGFDGLSKA--QDTGL 234
|
250
....*....|...
gi 1113985319 254 EasasQDPYAMAQ 266
Cdd:pfam00532 235 Y----LSPLTVIQ 243
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
26-296 |
1.03e-10 |
|
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: 61.04 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNpNAEVIAVSADyDLNKQFTQVDNFIAAGVDMILINAVDANAIEvAIKRAQKE 105
Cdd:cd06289 2 VGLIVPDLSNPFFAELLAGIEEALEEAG-YLVFLANTGE-DPERQRRFLRRMLEQGVDGLILSPAAGTTAE-LLRRLKAW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAV--DVSAKGADaTVQTNNVQAGEIACQYIVDK-------LGGKGDViiqngpqvSAVIDRVNGCRSVFAKApGI 176
Cdd:cd06289 79 GIPVVLAlrDVPGSDLD-YVGIDNRLGAQLATEHLIALghrriafLGGLSDS--------STRRERLAGFRAALAEA-GL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 177 NVLSDDQ-DAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRD---NIIITSVDGAPDIEEALKGNTM 252
Cdd:cd06289 149 PLDESLIvPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEpgrDIAVVGFDDVPEAALWTPPLTT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1113985319 253 VEASAsqdpyamAQMGVDVGVKIL----NGEKPAESmILMPSTLVTRE 296
Cdd:cd06289 229 VSVHP-------REIGRRAARLLLrrieGPDTPPER-IIIEPRLVVRE 268
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
25-281 |
1.86e-10 |
|
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: 60.72 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTmvNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQK 104
Cdd:cd19994 1 KIGISLPTKSEERWIK--DGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 EGIAVVAVDVSAKGADAT---VQTNNVQAGEIACQYIVDKLGGKGD-----VIIQNGPQ---------------VSAVID 161
Cdd:cd19994 79 AGIPVIAYDRLIMNTDAVdyyVTFDNEKVGELQGQYLVDKLGLKDGkgpfnIELFAGSPddnnaqlffkgamevLQPYID 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 162 R-VNGCRSVFAKAPGINVLSDDQDAKGSRdgglnvMQGHLTRFQ----KIDAVFTINDPQAIG--TDLAAKQLKRDN-II 233
Cdd:cd19994 159 DgTLVVRSGQTTFEQVATPDWDTETAQAR------METLLSAYYtggkKLDAVLSPNDGIARGviEALKAAGYDTGPwPV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1113985319 234 ITSVDGAPDIEEALKGNTMvEASASQDPYAMAQMGVDVGVKILNGEKP 281
Cdd:cd19994 233 VTGQDAEDASVKSILDGEQ-SMTVFKDTRLLAKATVELVDALLEGEEV 279
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
36-296 |
2.38e-10 |
|
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: 59.87 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 36 PFFVTMVNGATAKAKEynpnAEVIAVSADYDLNKQFTQ--VDNFIAAGVDMILINAVDANAIEVAIKraqKEGIAVVAVD 113
Cdd:cd06288 13 PFAGDIIRGAQDAAEE----HGYLLLLANTGGDPELEAeaIRELLSRRVDGIIYASMHHREVTLPPE---LTDIPLVLLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 114 -VSAKGADATVQTNNVQAGEIACQYIVDkLGGKGDVIIqNGPQVS-AVIDRVNGCRSVFAKApGINVLSDDQDAKG-SRD 190
Cdd:cd06288 86 cFDDDPSLPSVVPDDEQGGYLATRHLIE-AGHRRIAFI-GGPEDSlATRLRLAGYRAALAEA-GIPYDPSLVVHGDwGRE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 191 GGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDGapdieealkgntmVEASASQDP------ 261
Cdd:cd06288 163 SGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLrvpEDLSVVGFDN-------------QELAAYLRPplttva 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 1113985319 262 ---YAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd06288 230 lpyYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERE 267
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
26-296 |
2.64e-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: 380501 [Multi-domain] Cd Length: 266 Bit Score: 59.85 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVdmILINAVDANAIevaIKRAQKE 105
Cdd:cd06278 2 VGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDALRQLLQYRVDGV--IVTSATLSSEL---AEECARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAV--DVSAKGADAtVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQ-VSAVIDRVNGCRSVFAKA--PGINVLS 180
Cdd:cd06278 77 GIPVVLFnrVVEDPGVDS-VSCDNRAGGRLAADLLLAA--GHRRIAFLGGPEgTSTSRERERGFRAALAELglPPPAVEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKGSRDGGLNVMQGHltrfQKIDAVFTINDPQAIGT-DLAAKQLKR---DNIIITSVDgapDIEEAlkgntmveAS 256
Cdd:cd06278 154 GDYSYEGGYEAARRLLAAP----DRPDAIFCANDLMALGAlDAARQEGGLvvpEDISVVGFD---DIPMA--------AW 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1113985319 257 AS-------QDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd06278 219 PSydlttvrQPIEEMAEAAVDLLLERIENPETPPERRVLPGELVERG 265
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
26-296 |
3.42e-10 |
|
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: 59.43 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKE--YNPnaeVIAVSaDYDLNKQFTQVDNFIAAGVD-MILINAVDAnaiEVAIKRA 102
Cdd:cd01575 2 VAVVVPSLSNSVFAETLQGLSDVLEPagYQL---LLGNT-GYSPEREEELIRALLSRRPAgLILTGTEHT---PATRKLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 103 QKEGIAVVAV-DVSAKGADATVQTNNVQAGEIACQYIVDK-------LGGKGDVIIQngpqvsaVIDRVNGCRSVFAKAP 174
Cdd:cd01575 75 RAAGIPVVETwDLPDDPIDMAVGFSNFAAGRAMARHLIERgyrriafVGARLDGDSR-------ARQRLEGFRDALAEAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 175 GINVLSDDQDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDG---APDIEEALk 248
Cdd:cd01575 148 LPLPLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIrvpGDIAIAGFGDldiAAALPPAL- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1113985319 249 gnTMVEAsasqDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd01575 227 --TTVRV----PRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRE 268
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
26-296 |
7.71e-10 |
|
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: 58.44 E-value: 7.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDLNKQFtqVDNFIAAGVDMILINAVDANAIEVAIKRAQke 105
Cdd:cd06296 2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDW--VRRAVARGSAGVVLVTSDPTSRQLRLLRSA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVD-VSAKGADA-TVQTNNVQAGEIACQYIVDkLGGKgDVIIQNGPQVS-AVIDRVNGCRSVFAKApgiNVLSDD 182
Cdd:cd06296 78 GIPFVLIDpVGEPDPDLpSVGATNWAGGRLATEHLLD-LGHR-RIAVITGPPRSvSGRARLAGYRAALAEA---GIAVDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 183 QDAKGSR---DGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDGAPDIEEALKGNTMVeas 256
Cdd:cd06296 153 DLVREGDftyEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLrvpDDLSVIGFDDTPPARWTSPPLTTV--- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1113985319 257 aSQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd06296 230 -HQPLREMGAVAVRLLLRLLEGGPPDARRIELATELVVRG 268
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
25-296 |
9.38e-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: 380513 [Multi-domain] Cd Length: 267 Bit Score: 58.01 E-value: 9.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 25 KIGISLGSLGNPFFVTMVNG--ATAKAKEYNPnaevIAVSADYDLNKQFTQVDNFIAAGVD-MILINAVDANAIEVAIKr 101
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGieEVLAESGYTL----IVSTSHWNADRELEILRLLLARKVDgIIVVGGFGDEELLKLLA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 102 aqkEGIAVVAVDVSAKGAD-ATVQTNNVQAGEIACQYIVDkLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKApGINVls 180
Cdd:cd06290 76 ---EGIPVVLVDRELEGLNlPVVNVDNEQGGYNATNHLID-LGHRRIVHISGPEDHPDAQERYAGYRRALEDA-GLEV-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 dDQDAKGSRD----GGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDGAPD---IEEALkgn 250
Cdd:cd06290 149 -DPRLIVEGDfteeSGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIrvpDDVSVIGFDDLPFskyTTPPL--- 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1113985319 251 TMVEasasQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd06290 225 TTVR----QPLYEMGKTAAEILLELIEGKGRPPRRIILPTELVIRE 266
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
26-293 |
2.50e-09 |
|
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: 56.77 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGA--TAKAKEYNpnaeVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANaiEVAIKRAQ 103
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIedEAYKNGYH----VILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGN--EDLIEKLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 104 KEGIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDKlGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKA----PGINV 178
Cdd:cd19977 76 KSGIPVVFVDRYIPGLDVdTVVVDNFKGAYQATEHLIEL-GHKRIAFITYPLELSTRQERLEGYKAALADHglpvDEELI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 179 LSDDQdakgsRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDgapDIEEALKGNTMVEA 255
Cdd:cd19977 155 KHVDR-----QDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLripDDIALIGFD---DIPWADLFNPPLTV 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 1113985319 256 SAsQDPYAMAQMGVDVGVKILNGEKPAES-MILMPSTLV 293
Cdd:cd19977 227 IA-QPTYEIGRKAAELLLDRIENKPKGPPrQIVLPTELI 264
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
26-292 |
3.52e-09 |
|
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: 56.49 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEynPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKrAQKE 105
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQ--PGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEK-ARGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKGADAT--VQTNNVQAGEIACQYIVdKLGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVLSDDQ 183
Cdd:cd01537 79 NVPVVFFDKEPSRYDKAyyVITDSKEGGIIQGDLLA-KHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 184 DAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRDNIIITSVDGAPDIEEALKgNTMVEASASQDPYA 263
Cdd:cd01537 158 TGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALK-SGPLLTTILQDANN 236
|
250 260
....*....|....*....|....*....
gi 1113985319 264 MAQMGVDVGVKILNGEKPAESMILMPSTL 292
Cdd:cd01537 237 LGKTTFDLLLNLADNWKIDNKVVRVPYVL 265
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
26-296 |
3.82e-09 |
|
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: 56.37 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAvDANAIEVAIKRAQKe 105
Cdd:cd06270 2 IGLVVPDLSGPFFGSLLKGAERVARAHG--KQLLITSGHHDAEEEREAIEFLLDRRCDAIILHS-RALSDEELILIAEK- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKG-ADATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQVSA-VIDRVNGCRSVFAKApGINvLSDD- 182
Cdd:cd06270 78 IPPLVVINRYIPGlADRCVWLDNEQGGRLAAEHLLDL--GHRRIACITGPLDIPdARERLAGYRDALAEA-GIP-LDPSl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 183 -QDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGtdlAAKQLKRDNIII---TSVDGAPDIEEA------LkgnTM 252
Cdd:cd06270 154 iIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIG---ALAALHEAGIKVpedVSVIGFDDVPLArylspkL---TT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1113985319 253 VEASASQdpyaMAQMGVDVGVKILNGEKPAESMILMPsTLVTRE 296
Cdd:cd06270 228 VHYPIEE----MAQAAAELALNLAYGEPLPISHEFTP-TLIERD 266
|
|
| PBP1_LsrB_Quorum_Sensing-like |
cd20001 |
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ... |
34-280 |
3.95e-09 |
|
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: 56.52 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 34 GNPFFVTMVNGATAKAKEYNPNAEVIAvSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVD 113
Cdd:cd20001 10 GIAWFDRMETGVEQFAKDTGVNVYQIG-PATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDAGIVVITHE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 114 VS-AKGADATVQT-NNVQAGEIACQYIVDKLGGKGDVIIQNGPQVSAV-IDRVNGCRSVFAKA-PGINVLSDDQDAKGSR 189
Cdd:cd20001 89 ASnLKNVDYDVEAfDNAAYGAFIMDKLAEAMGGKGKYVTFVGSLTSTShMEWANAAVAYQKANyPDMLLVTDRVETNDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 190 DGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR-DNIIITSVDGAPDIEEALKGNTMVEASAsQDP----YAM 264
Cdd:cd20001 169 ETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLqGKIAVVGTGLPSVAGEYLEDGTIDYIQF-WDPadagYAM 247
|
250
....*....|....*.
gi 1113985319 265 AQMgvdvGVKILNGEK 280
Cdd:cd20001 248 NAL----AVMVLEGEK 259
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
56-283 |
5.58e-09 |
|
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: 55.95 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 56 AEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVDVSAKGADATVQT-NNVQAGEIA 134
Cdd:cd19993 30 AKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLIENPIAFYISfDNVEVGRMQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 135 CQYIVdKLGGKGDVIIQNGPQVSAVIDRV-NGCRSVFAKA---PGINVLSDDQDAKGSRDGGLNVMQGHLTRF-QKIDAV 209
Cdd:cd19993 110 ARGVL-KAKPEGNYVFIKGSPTDPNADFLrAGQMEVLQPAidsGKIKIVGEQYTDGWKPANAQKNMEQILTANnNKVDAV 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113985319 210 FTINDPQAIG--TDLAAKQLkRDNIIITSVDGApdiEEALKGNTMVEASAS--QDPYAMAQMGVDVGVKILNGEKPAE 283
Cdd:cd19993 189 VASNDGTAGGavAALAAQGL-AGKVPVSGQDAD---KAALNRIALGTQTVTvwKDARELGKEAAEIAVELAKGTKIEA 262
|
|
| xylF |
PRK10355 |
D-xylose ABC transporter substrate-binding protein; |
1-219 |
1.93e-08 |
|
D-xylose ABC transporter substrate-binding protein;
Pssm-ID: 182403 [Multi-domain] Cd Length: 330 Bit Score: 54.75 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 1 MKKLLLAGLVLAMSTVSAQAKDLnKIGISLGSLGNPFFVTMVNGATAKAKEYNpnAEVIAVSADYDLNKQFTQVDNFIAA 80
Cdd:PRK10355 4 KNILLTLCASLLLTSVAAHAKEV-KIGMAIDDLRLERWQKDRDIFVKKAESLG--AKVFVQSANGNEETQMSQIENMINR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 81 GVDMILINAVDANAIEVAIKRAQKEGIAVVAVDVSAKGADAT--VQTNNVQAGEIACQYIVDKLgGKGDVIIQNGPQV-- 156
Cdd:PRK10355 81 GVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDfyISFDNEKVGELQAKALVDKV-PQGNYFLMGGSPVdn 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1113985319 157 SAVIDRvNGCRSV---FAKAPGINVLSDDQDAKGSRDGGLNVMQGHLT-RFQKIDAVFTINDPQAIG 219
Cdd:PRK10355 160 NAKLFR-AGQMKVlkpYIDSGKIKVVGDQWVDGWLPENALKIMENALTaNNNKIDAVVASNDATAGG 225
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
26-296 |
2.29e-08 |
|
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: 54.10 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNPNaeVIAVSADYDLNKQFTQVDNFIAAGVD-MILINAVDANAIEVAIKRAQk 104
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYS--VILCNTGSDEEREKKYLQLLKEKRVDgIIFASGTLTEENKQLLKNMN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 egIAVVAVDVSAKGAD-ATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQV--SAVIDRVNGCRSVFAKApGINVlSD 181
Cdd:cd19975 79 --IPVVLVSTESEDPDiPSVKIDDYQAAYDATNYLIKK--GHRKIAMISGPLDdpNAGYPRYEGYKKALKDA-GLPI-KE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 DQDAKG--SRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGtdlAAKQLKRDNIII---TSVDGAPDIEEALKGNTMVeAS 256
Cdd:cd19975 153 NLIVEGdfSFKSGYQAMKRLLKNKKLPTAVFAASDEMALG---VISAAYDHGIRVpedISVIGFDNTEIAEMSIPPL-TT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1113985319 257 ASQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd19975 229 VSQPFYEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERE 268
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
26-296 |
4.66e-08 |
|
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: 53.03 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGA--TAKAKEYNpnaeVIAVSADYDLNKQFTQVDNFIAAGVD-MILINAVDANAIEVAIkrA 102
Cdd:cd06275 2 IGLLVTSSENPFFAEVVRGVedACFRAGYS----LILCNSDNDPEKQRAYLDMLAEKRVDgLLLMCSEMTDDDAELL--A 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 103 QKEGIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQVSAVI-DRVNGCRSVFAKApGINVLS 180
Cdd:cd06275 76 ALRSIPVVVLDREIAGDNAdAVLDDSFQGGYLATRHLIEL--GHRRIGCITGPLEHSVSrERLAGFRRALAEA-GIEVPP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DD-QDAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGtdlAAKQLKRDNIII---TSVDGAPDIE------EALkgn 250
Cdd:cd06275 153 SWiVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALG---ALRAAQEQGLRVpqdISIIGYDDIElaryfsPAL--- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1113985319 251 TMVeasaSQDPYAMAQMGVDVGV-KILNGEKPAESmILMPSTLVTRE 296
Cdd:cd06275 227 TTI----HQPKDELGELAVELLLdRIENKREEPQS-IVLEPELIERE 268
|
|
| PRK10936 |
PRK10936 |
TMAO reductase system periplasmic protein TorT; Provisional |
44-283 |
6.01e-08 |
|
TMAO reductase system periplasmic protein TorT; Provisional
Pssm-ID: 236801 [Multi-domain] Cd Length: 343 Bit Score: 53.41 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 44 GATAKAKEYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKeGIAVVAV--DVSAKGADA 121
Cdd:PRK10936 67 GMVEEAKRLGVDLKVLEAGGYYNLAKQQQQLEQCVAWGADAILLGAVTPDGLNPDLELQAA-NIPVIALvnGIDSPQVTT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 122 TVQTNNVQAGEIACQYIVDKL---GGKGDVIIQNGPQVSAVIDRVN-GCRSVFAKAPgINVlSDDQDAKGSRDGGLNVMQ 197
Cdd:PRK10936 146 RVGVSWYQMGYQAGRYLAQWHpkgSKPLNVALLPGPEGAGGSKAVEqGFRAAIAGSD-VRI-VDIAYGDNDKELQRNLLQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 198 GHLTRFQKID-----AVfTINdpQAIGTdLAAKQLkRDNIIITSVDGAPDIEEALKGNTmVEASASQDPYAMAQMGVDVG 272
Cdd:PRK10936 224 ELLERHPDIDyiagsAV-AAE--AAIGE-LRGRNL-TDKIKLVSFYLSHQVYRGLKRGK-VLAAPSDQMVLQGRLAIDQA 297
|
250
....*....|.
gi 1113985319 273 VKILNGEKPAE 283
Cdd:PRK10936 298 VRQLEGAPVPG 308
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
26-141 |
1.22e-07 |
|
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: 51.78 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYnpNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIevAIKRAQKE 105
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIEDVCREA--GYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNND--AYLELAQK 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1113985319 106 GIAVVAVDVSAKGADA-TVQTNNVQAGEIACQYIVDK 141
Cdd:cd06283 78 GLPVVLVDRQIEPLNWdTVVTDNYDATYEATEHLKEQ 114
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
74-296 |
2.95e-07 |
|
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: 50.66 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 74 VDNFIAAGVDMILINAVDANAIEVAikRAQKEGIAVVAVDVSAKGADATVQTNNVQAGEIACQYIVDkLGGKGDVIIqNG 153
Cdd:cd01574 49 LDRLLSQRVDGIIVIAPDEAVLEAL--RRLPPGLPVVIVGSGPSPGVPTVSIDQEEGARLATRHLLE-LGHRRIAHI-AG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 154 PQVS-AVIDRVNGCRSVFAKAPGIN--VLSDDQDAKGSRDGGLnvmqgHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR- 229
Cdd:cd01574 125 PLDWvDARARLRGWREALEEAGLPPppVVEGDWSAASGYRAGR-----RLLDDGPVTAVFAANDQMALGALRALHERGLr 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1113985319 230 --DNIiitSVDGAPDIEEA------LkgnTMVeasaSQDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLVTRE 296
Cdd:cd01574 200 vpEDV---SVVGFDDIPEAayfvppL---TTV----RQDFAELGRRAVELLLALIEGPAPPPESVLLPPELVVRE 264
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
26-296 |
1.03e-06 |
|
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: 380497 [Multi-domain] Cd Length: 268 Bit Score: 49.04 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNPNAeVIAVSaDYDLNKQFTQVDNFIAAGVD-MILINAVDANAIEVAIKRAQk 104
Cdd:cd06273 2 IGAIVPTLDNAIFARAIQALQQTLAEAGYTL-LLATS-EYDPARELEQVRALIERGVDgLILVGSDHDPELFELLEQRQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 105 egIAVVAVDVSAKGAD-ATVQTNNVQAGEIACQYIVDkLGGKgDVIIQNGPQVSA--VIDRVNGCRSVFAKA----PGIN 177
Cdd:cd06273 79 --VPYVLTWSYDEDSPhPSIGFDNRAAAARAAQHLLD-LGHR-RIAVISGPTAGNdrARARLAGIRDALAERglelPEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 178 VLSDDQDAKGSRDGglnvMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKRD---NIIITSVDGapdieealkgntmVE 254
Cdd:cd06273 155 VVEAPYSIEEGREA----LRRLLARPPRPTAIICGNDVLALGALAECRRLGISvpeDLSITGFDD-------------LE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1113985319 255 ASASQDP---------YAMAQMGVDVGVKILNGEKPAESMILmPSTLVTRE 296
Cdd:cd06273 218 LAAHLSPplttvrvpaREIGELAARYLLALLEGGPPPKSVEL-ETELIVRE 267
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
17-246 |
2.97e-06 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 48.16 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 17 SAQAKDL-----NKIGISLGSLGNPFFVTMVNGATAKAkeYNPNAEVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVD 91
Cdd:PRK10423 45 SALARSLklnqtRTIGMLITASTNPFYSELVRGVERSC--FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 92 ANAIEVAIKRaQKEGIAVVAVDVSA-KGADATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQ-VSAVIDRVNGCRSV 169
Cdd:PRK10423 123 THQPSREIMQ-RYPSVPTVMMDWAPfDGDSDLIQDNSLLGGDLATQYLIDK--GYTRIACITGPLdKTPARLRLEGYRAA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 170 FAKA-----PGINVLSDDQDAkgsrdGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQ----LKRDniiiTSVDGA 240
Cdd:PRK10423 200 MKRAglnipDGYEVTGDFEFN-----GGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQaglsVPQD----IAVIGY 270
|
....*.
gi 1113985319 241 PDIEEA 246
Cdd:PRK10423 271 DDIELA 276
|
|
| PRK15408 |
PRK15408 |
autoinducer 2 ABC transporter substrate-binding protein LsrB; |
1-235 |
6.70e-06 |
|
autoinducer 2 ABC transporter substrate-binding protein LsrB;
Pssm-ID: 237961 Cd Length: 336 Bit Score: 47.10 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 1 MKKLLLAGLV-LAMSTVSAQAKDlnKIGISLGSLGNPFFVTMVNGATAKAKEynpnaevIAVSADYD------LNKQFTQ 73
Cdd:PRK15408 2 KKKIALVSALgIALISMTVQAAE--RIAFIPKLVGVGFFTSGGNGAKEAGKE-------LGVDVTYDgptepsVSGQVQL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 74 VDNFIAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVDVSAKGADATVQTNN---VQAGEIACQYIVDKLGG-KGDV- 148
Cdd:PRK15408 73 INNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQgtpEQLGSMLVEMAAKQVGKdKAKVa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 149 IIQNGPQVSAVIDRVNGCRSVFAKA-PGINVLSDD---QDAKGSrdggLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAA 224
Cdd:PRK15408 153 FFYSSPTVTDQNQWVKEAKAKIAKEhPGWEIVTTQfgyNDATKS----LQTAEGILKAYPDLDAIIAPDANALPAAAQAA 228
|
250
....*....|.
gi 1113985319 225 KQLKRDNIIIT 235
Cdd:PRK15408 229 ENLKRDKVAIV 239
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
26-287 |
1.00e-05 |
|
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: 46.12 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 26 IGISLGSLGNPFFVTMVNGATAKAKEYNPNaeVIAVSADYDLNKQFTQVDNFIAAGVDMILINAVDANAIEVAIKRAQKE 105
Cdd:cd06282 2 IGVLIPSLNNPVFAEAAQGIQRAARAAGYS--LLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALELLEEEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 106 GIAVVAVDVSAKGADATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQVSA--VIDRVNGCRSVFAKApGINVLSD-- 181
Cdd:cd06282 80 VPYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIAL--GHRRIAMVAGDFSASdrARLRYQGYRDALKEA-GLKPIPIve 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 182 -DQDAKGSRDGGLNVMQGHltrfQKIDAVFTINDPQAIGTdlaAKQLKR------DNIIITSVDGapdIEEAlkgnTMVE 254
Cdd:cd06282 157 vDFPTNGLEEALTSLLSGP----NPPTALFCSNDLLALSV---ISALRRlgirvpDDVSVIGFDG---IAIG----ELLT 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 1113985319 255 ---ASASQDPYAMAQMGVDVGVKILNGEKPAESMIL 287
Cdd:cd06282 223 ptlATVVQPSRDMGRAAADLLLAEIEGESPPTSIRL 258
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
34-293 |
1.35e-05 |
|
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: 45.65 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 34 GNPFFVTMVNGATAKAKEYNPNaevIAVSADYDLNKQFTQVDNFIAAG-VD-MILINAVDANAIevaIKRAQKEGIAVVA 111
Cdd:cd06294 15 QNPFFSEVLRGISQVANENGYS---LLLATGNTEEELLEEVKRMVRGRrVDgFILLYSKEDDPL---IEYLKEEGFPFVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 112 VDVSAKGADAT-VQTNNVQAGEIACQYIVDK-------LGGKGDVIIqngpqvsaVIDRVNGCRSVFAKApGInVLSDDQ 183
Cdd:cd06294 89 IGKPLDDNDVLyVDNDNVQAGYEATEYLIDKghkriafIGGDKNLVV--------SIDRLQGYKQALKEA-GL-PLDDDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 184 --DAKGSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDGAPDIEEALKGNTMVEAsas 258
Cdd:cd06294 159 ilLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLrvpEDVSIISFNNSPLAELASPPLTSVDI--- 235
|
250 260 270
....*....|....*....|....*....|....*
gi 1113985319 259 qDPYAMAQMGVDVGVKILNGEKPAESMILMPSTLV 293
Cdd:cd06294 236 -NPYELGREAAKLLINLLEGPESLPKNVIVPHELI 269
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
122-296 |
2.60e-05 |
|
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. 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: 380518 [Multi-domain] Cd Length: 273 Bit Score: 44.93 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 122 TVQTNNVQAGEIACQYIVDklGGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVLSDDQDAKGSRDGGLNVMQGHLT 201
Cdd:cd06295 103 SVGSDNVKGGALATEHLIE--IGRRRIAFLGDPPHPEVADRLQGYRDALAEAGLEADPSLLLSCDFTEESGYAAMRALLD 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 202 RFQKIDAVFTINDPQAIGtdlAAKQLKRDNIII---TSVDGAPDIEEALKGN---TMVEasasQDpyaMAQMG---VDVG 272
Cdd:cd06295 181 SGTAFDAIFAASDLIAMG---AIRALRERGISVpgdVAVVGYDDIPLAAYFRpplTTVR----QD---LALAGrllVEKL 250
|
170 180
....*....|....*....|....
gi 1113985319 273 VKILNGEKPAESMilMPSTLVTRE 296
Cdd:cd06295 251 LALIAGEPVTSSM--LPVELVVRE 272
|
|
| PBP1_ABC_sugar_binding-like |
cd06315 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
78-150 |
2.76e-05 |
|
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: 45.03 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 78 IAAGVDMILINAVDANAIEVAIKRAQKEGIAVVAVDVSAK-------GADATVQTNNVQAGEIACQYIVDKLGGKGDVII 150
Cdd:cd06315 53 LALKPDGIILGGDDAVELQEPLKKAVKAGIPVVGWHAAASpgpipelGLFTNITTDPREVAETAAALVIAQSGGKAGVVI 132
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
29-270 |
6.59e-05 |
|
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: 43.80 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 29 SLGSLGNPFFVTMVNGATAKAKEYNPNAEVIAVSADYDlnKQFTQVDNFIAAGVDMILINAVDANAIEVAIkRAQKEGIA 108
Cdd:cd01391 8 SLHQIREQFGIQRVEAIFHTADKLGASVEIRDSCWHGS--VALEQSIEFIRDNIAGVIGPGSSSVAIVIQN-LAQLFDIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 109 VVAVDVSAKGAD--------ATVQTNNVQAGEIACQYIVDKlgGKGDVIIQNGPQVSAVIDRVNGCRSVFAKAPGINVLS 180
Cdd:cd01391 85 QLALDATSQDLSdktlykyfLSVVFSDTLGARLGLDIVKRK--NWTYVAAIHGEGLNSGELRMAGFKELAKQEGICIVAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 181 DDQDAKgSRDGGLNVMQGHLTRFQKIDAVFTINDPQAIGTDLAAKQL-KRDNIIITSVDGAPDIEEALKG-NTMVEASAS 258
Cdd:cd01391 163 DKADWN-AGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLgLVGDVSVIGSDGWADRDEVGYEvEANGLTTIK 241
|
250
....*....|..
gi 1113985319 259 QDPYAMAQMGVD 270
Cdd:cd01391 242 QQKMGFGITAIK 253
|
|
| PBP1_Med-like |
cd06353 |
periplasmic binding domain of the basic membrane lipoprotein Med in Bacillus and its close ... |
6-153 |
1.16e-03 |
|
periplasmic binding domain of the basic membrane lipoprotein Med in Bacillus and its close homologs from other bacteria and Archaea; Periplasmic binding domain of the basic membrane lipoprotein Med in Bacillus and its close homologs from other bacteria and Archaea. Med, a cell-surface localized protein, which regulates the competence transcription factor gene comK in Bacillus subtilis, lacks the DNA binding domain when compared with structures of transcription regulators from the LacI family. Nevertheless, Med has significant overall sequence homology to various periplasmic substrate-binding proteins. Moreover, the structure of Med shows a striking similarity to PnrA, a periplasmic nucleoside binding protein of an ATP-binding cassette transport system. Members of this group contain the type 1 periplasmic sugar-binding protein-like fold.
Pssm-ID: 380576 Cd Length: 260 Bit Score: 39.95 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 6 LAGLVLAMSTvsaqakDLNKIGISLGSLGNPFfvtmVNGATAKAKEYNPNAEVIA--VSADYDLNKQFTQVDNFIAAGVD 83
Cdd:cd06353 109 FAGMLAAHMT------KTNKVGVIAAFPWQPE----VEGFEEGVKYVSPEAKVLVrfVNDWDDGEKAMELAQELISQGVD 178
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1113985319 84 mILINAVDANAIEVaIKRAQKEGIAVVA--VDVSAKGADaTVQTNNVQA-----GEIACQYIVDKL-GGKGDVIIQNG 153
Cdd:cd06353 179 -VVYPAGDGFNVEV-IEQAKEDGLYAIGyiDDQSYIGPN-TVLTSTVQDvpqlyEAIANQFNEGELtPGNITYDFNDG 253
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
207-296 |
4.39e-03 |
|
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: 37.32 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 207 DAVFTINDPQAIGTDLAAKQLKR---DNIIITSVDGAPDIEEALKGNTMVeasaSQDPYAMAQMGVDVGVKILNGEKPAE 283
Cdd:pfam13377 70 TAVFVANDEVALGVLQALREAGLrvpEDLSVIGFDDSPLAALVSPPLTTV----RVDAEELGRAAAELLLDLLNGEPAPP 145
|
90
....*....|...
gi 1113985319 284 SMILMPSTLVTRE 296
Cdd:pfam13377 146 ERVLLPPELVERE 158
|
|
| PBP1_BmpA_Med_PnrA-like |
cd06304 |
periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and ... |
6-98 |
7.69e-03 |
|
periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria; Periplasmic binding component of a family of basic membrane lipoproteins from Borrelia 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: 380527 Cd Length: 262 Bit Score: 37.13 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1113985319 6 LAGLVLAMSTVSaqakdlNKIGIsLGSLGNPFFVTMVNGATAKAKEYNPNAEV-IAVSADYD---LNKQFTQvdNFIAAG 81
Cdd:cd06304 109 LAGALAALMTKT------GKVGF-VGGMEIPPIKRLLAGFEAGAKAVNPDAKVlVAYTGSWDdvaKAKEAAL--AMIAQG 179
|
90
....*....|....*....
gi 1113985319 82 VDMILI--NAVDANAIEVA 98
Cdd:cd06304 180 ADVIFGaaNAAGLGVIEAA 198
|
|
| |
