|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
4-337 |
2.31e-107 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 317.14 E-value: 2.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 4 NRRPTLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIRVGGPDtTVGLVIPDLGNPFFGAV 83
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTR-TIGVVVPDLSNPFFAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 84 ASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSvGAEHSHLKSHRAAGLPVVFLDRPGSGLATDSV 163
Cdd:COG1609 80 LRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGS-RLDDARLERLAEAGIPVVLIDRPLPDPGVPSV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 164 VSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALV-TNAHDQHGASAATSQLLGLA 242
Cdd:COG1609 159 GVDNRAGARLATEHLIELGHRRIAFIGG-PADSSSARERLAGYREALAEAGLPPDPELVvEGDFSAESGYEAARRLLARG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 243 DPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDRSRAR 319
Cdd:COG1609 238 PRPTAIFCANDLMALGALRALREAGLRvpeDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPE 317
|
330
....*....|....*...
gi 818924068 320 TVTVPTRLIIRGSGERPA 337
Cdd:COG1609 318 RVLLPPELVVRESTAPAP 335
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
67-328 |
1.19e-85 |
|
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: 259.37 E-value: 1.19e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSvGAEHSHLKSHRAAGL 146
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPS-SLDDELLEELLAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALV-TNA 225
Cdd:cd06267 80 PVVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGG-PLDLSTSRERLEGYRDALAEAGLPVDPELVvEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06267 159 FSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpeDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRA 238
|
250 260
....*....|....*....|....*.
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLI 328
Cdd:cd06267 239 AAELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
67-328 |
2.07e-79 |
|
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: 243.21 E-value: 2.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEhSHLKSHRAAGL 146
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNE-DLIEKLVKSGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGdLPAKLYTRRERLAGYRSALQESEIPYDRALVTNAH 226
Cdd:cd19977 80 PVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFIT-YPLELSTRQERLEGYKAALADHGLPVDEELIKHVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 227 DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTA 303
Cdd:cd19977 159 RQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRipdDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRKA 238
|
250 260
....*....|....*....|....*.
gi 818924068 304 ATTALARLDGDRSRA-RTVTVPTRLI 328
Cdd:cd19977 239 AELLLDRIENKPKGPpRQIVLPTELI 264
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
67-330 |
2.59e-74 |
|
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: 230.22 E-value: 2.59e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSvGAEHSHLKSHRAAGL 146
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPS-AGPSRELKRLLKHGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALV-TNA 225
Cdd:cd06280 80 PIVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITG-PLEISTTRERLAGYREALAEAGIPVDESLIfEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06280 159 STIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGleiPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRI 238
|
250 260
....*....|....*....|....*...
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLIIR 330
Cdd:cd06280 239 AAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
67-332 |
1.92e-72 |
|
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: 225.62 E-value: 1.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSvGAEHSHLKSHRAAGL 146
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPT-GENSEGLQALIAQGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLAT-DSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALVTNA 225
Cdd:cd06299 80 PVVFVDREVEGLGGvPVVTSDNRPGAREAVEYLVSLGHRRIGYISG-PLSTSTGRERLAAFRAALTAAGIPIDEELVAFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 -HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVVAQDPEEIGR 301
Cdd:cd06299 159 dFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGlriGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGR 238
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 302 TAATTALARLdGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06299 239 RAVELLLALI-ENGGRATSIRVPTELIPRES 268
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
67-330 |
2.75e-71 |
|
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: 222.44 E-value: 2.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGL 146
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLyTRRERLAGYRSALQESEIPYDRAL-VTNA 225
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSS-TRRERLAGFRAALAEAGLPLDESLiVPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06289 160 ATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLepgRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRR 239
|
250 260
....*....|....*....|....*...
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLIIR 330
Cdd:cd06289 240 AARLLLRRIEGPDTPPERIIIEPRLVVR 267
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-332 |
4.66e-63 |
|
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: 201.69 E-value: 4.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPsVGAEHSHLKSHRAAGL 146
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITP-ARDDAPDLQELAARGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALVTNAH 226
Cdd:cd06285 80 PVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAG-PLNASTGRDRLRGYRRALAEAGLPVPDERIVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 227 -DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06285 159 fTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLrvpEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRR 238
|
250 260 270
....*....|....*....|....*....|
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06285 239 AAELLLQLIEGGGRPPRSITLPPELVVRES 268
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
67-332 |
7.02e-63 |
|
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: 200.84 E-value: 7.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRIS--ILMVvpsvGAEHSHLKSHRAA 144
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDgvILLS----GRLDAELLSELSK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALVTN 224
Cdd:cd06284 77 RYPIVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHING-PLDNVYARERLEGYRRALAEAGLPVDEDLIIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 225 A-HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIG 300
Cdd:cd06284 156 GdFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRvpeDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIG 235
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 301 RTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06284 236 ETAAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
67-332 |
2.82e-62 |
|
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: 199.40 E-value: 2.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGL 146
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRrERLAGYRSALQESEIPYDRALVTNAH 226
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSR-ERLAGFRRALAEAGIEVPPSWIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 227 -DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06275 160 fEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlrvPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
|
250 260 270
....*....|....*....|....*....|
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06275 240 AVELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-332 |
3.51e-57 |
|
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: 186.28 E-value: 3.51e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGaEHSHLKSHrAAGL 146
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFG-DEELLKLL-AEGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFI-GdlPAKLYTRRERLAGYRSALQESEIPYDRALVTNA 225
Cdd:cd06290 79 PVVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHIsG--PEDHPDAQERYAGYRRALEDAGLEVDPRLIVEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 H-DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGR 301
Cdd:cd06290 157 DfTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRvpdDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGK 236
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 302 TAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06290 237 TAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-332 |
4.57e-57 |
|
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: 186.32 E-value: 4.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSvGAEHSHLKSHRAAGL 146
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPS-DDDLSHLARLRARGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALVTNAH 226
Cdd:cd06293 80 AVVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSG-PLRTRQVAERLAGARAAVAEAGLDPDEVVRELSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 227 DQHGAS---AATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIG 300
Cdd:cd06293 159 PDANAElgrAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRvpdDVSVVGYDDLPFAAAANPPLTTVRQPSYELG 238
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 301 RTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06293 239 RAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
67-332 |
4.77e-57 |
|
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: 185.92 E-value: 4.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGL 146
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAkLYTRRERLAGYRSALQESEIPYDRALV-TNA 225
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPS-TYNEHERIEGYKNALQDHNLPIDESWIySGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLGLaDPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd19976 160 SSLEGGYKAAEELLKS-KNPTAIFAGNDLIAMGVYRAALELGLKipeDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
|
250 260 270
....*....|....*....|....*....|
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd19976 239 AAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
67-332 |
2.00e-56 |
|
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to 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 I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380515 [Multi-domain] Cd Length: 273 Bit Score: 184.78 E-value: 2.00e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDL----GNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILmVVPSVGAEHSHLKSHR 142
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGF-VLASTRHDDPRVRYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 143 AAGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALV 222
Cdd:cd06292 80 EAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGG-PEGSVPSDDRLAGYRAALEEAGLPFDPGLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNAH-DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEPALSVVAQDPEE 298
Cdd:cd06292 159 VEGEnTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLrvgRDVSVVGFDDSPLAAFTHPPLTTVRQPIDE 238
|
250 260 270
....*....|....*....|....*....|....
gi 818924068 299 IGRTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06292 239 IGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
67-330 |
1.12e-54 |
|
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: 179.67 E-value: 1.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPsVGAEHSHLKSHRAAGL 146
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQP-TGNNNDAYLELAQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRRERLAGYRSALQESEIPyDRALVTNAH 226
Cdd:cd06283 80 PVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRRERLQGFLDALARYNIE-GDVYVIEIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 227 DQHGASAATSQLLGLAD-PPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06283 159 DTEDLQQALAAFLSQHDgGKTAIFAANGVVLLRVLRALKALGiriPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKA 238
|
250 260
....*....|....*....|....*...
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLIIR 330
Cdd:cd06283 239 AAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
67-330 |
2.31e-54 |
|
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: 178.87 E-value: 2.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHShLKSHRAAGL 146
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEE-LILIAEKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGdLPAKLYTRRERLAGYRSALQESEIPYDRALVTNAH 226
Cdd:cd06270 80 PLVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACIT-GPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 227 -DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06270 159 fTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKvpeDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQA 238
|
250 260
....*....|....*....|....*...
gi 818924068 303 AATTALARLDGDRSrARTVTVPTRLIIR 330
Cdd:cd06270 239 AAELALNLAYGEPL-PISHEFTPTLIER 265
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
67-332 |
8.79e-54 |
|
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: 177.74 E-value: 8.79e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLG-NPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLksHRAAG 145
Cdd:cd06288 1 TIGLITDDIAtTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLP--PELTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGdLPAKLYTRRERLAGYRSALQESEIPYDRALV-TN 224
Cdd:cd06288 79 IPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIG-GPEDSLATRLRLAGYRAALAEAGIPYDPSLVvHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 225 AHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGR 301
Cdd:cd06288 158 DWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRvpeDLSVVGFDNQELAAYLRPPLTTVALPYYEMGR 237
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 302 TAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06288 238 RAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-332 |
1.49e-51 |
|
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: 380504 [Multi-domain] Cd Length: 270 Bit Score: 172.04 E-value: 1.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGL 146
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELAAALARLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLaTDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALVTNAh 226
Cdd:cd06281 81 PVVLIDRDLPGD-IDSVLVDHRSGVRQATEYLLSLGHRRIALLTG-GPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLG- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 227 DQHGASA--ATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEPALSVVAQDPEEIGR 301
Cdd:cd06281 158 SFSADSGfrEAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLripGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGR 237
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 302 TAATTALARLDGDRSRA-RTVTVPTRLIIRGS 332
Cdd:cd06281 238 AAAELLLDRIEGPPAGPpRRIVVPTELILRDS 269
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
1-331 |
1.97e-51 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 173.74 E-value: 1.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 1 MAANRRPTLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIRvGGPDTTVGLVIPDLGNPFF 80
Cdd:PRK10014 1 MATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALR-GGQSGVIGLIVRDLSAPFY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 81 GAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGLPVVFLDRPGSGLAT 160
Cdd:PRK10014 80 AELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEEKGIPVVFASRASYLDDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 161 DSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLyTRRERLAGYRSALQESEIPYDRALVTN-AHDQHGASAATSQLL 239
Cdd:PRK10014 160 DTVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSL-TRAERVGGYCATLLKFGLPFHSEWVLEcTSSQKQAAEAITALL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 240 GLADPPTALFAGNNIVALGIVTELARTGR------------KDVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTA 307
Cdd:PRK10014 239 RHNPTISAVVCYNETIAMGAWFGLLRAGRqsgesgvdryfeQQVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRM 318
|
330 340
....*....|....*....|....
gi 818924068 308 LARLDGDRSRARTVTVPTRLIIRG 331
Cdd:PRK10014 319 MQRITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
67-332 |
4.07e-51 |
|
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: 170.75 E-value: 4.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVpsvGAEHS-----HLksh 141
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILT---GTEHTpatrkLL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 142 RAAGLPVV-FLDRPGSGLatDSVVST-NRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRRERLAGYRSALQESEIPYDR 219
Cdd:cd01575 75 RAAGIPVVeTWDLPDDPI--DMAVGFsNFAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFRDALAEAGLPLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 220 ALVTNAHDQHGASA-ATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQD 295
Cdd:cd01575 153 VLLVELPSSFALGReALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRvpgDIAIAGFGDLDIAAALPPALTTVRVP 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 818924068 296 PEEIGRTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd01575 233 RYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
67-332 |
5.99e-51 |
|
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: 170.01 E-value: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKShraaGL 146
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYKKL----NI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPgSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALVT-NA 225
Cdd:cd06291 77 PIVSIDRY-LSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGG-PSNNSPANERYRGFEDALKEAGIEYEIIEIDeND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd06291 155 FSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpeDVQIIGFDGIEISELLYPELTTIRQPIEEMAKE 234
|
250 260 270
....*....|....*....|....*....|
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06291 235 AVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-332 |
3.24e-49 |
|
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: 165.76 E-value: 3.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVvpsVGAEHSH-----LKSH 141
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLIL---VGSDHDPelfelLEQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 142 raaGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRRERLAGYRSALQESEIPYDRAL 221
Cdd:cd06273 78 ---QVPYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIRDALAERGLELPEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 222 VTNA-HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPE 297
Cdd:cd06273 155 VVEApYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISvpeDLSITGFDDLELAAHLSPPLTTVRVPAR 234
|
250 260 270
....*....|....*....|....*....|....*
gi 818924068 298 EIGRTAATTALARLDGDRSRARTVtVPTRLIIRGS 332
Cdd:cd06273 235 EIGELAARYLLALLEGGPPPKSVE-LETELIVRES 268
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
67-332 |
1.36e-47 |
|
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: 161.68 E-value: 1.36e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRiSILMVVPSVGAEHSHLKSHRAAGL 146
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARG-SAGVVLVTSDPTSRQLRLLRSAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATD-SVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRrERLAGYRSALQESEIPYDRALVTnA 225
Cdd:cd06296 80 PFVLIDPVGEPDPDLpSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGR-ARLAGYRAALAEAGIAVDPDLVR-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASA--ATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIG 300
Cdd:cd06296 158 GDFTYEAGyrAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRvpdDLSVIGFDDTPPARWTSPPLTTVHQPLREMG 237
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 301 RTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06296 238 AVAVRLLLRLLEGGPPDARRIELATELVVRGS 269
|
|
| fruct_sucro_rep |
TIGR02417 |
D-fructose-responsive transcription factor; Members of this family belong the lacI ... |
8-331 |
2.11e-47 |
|
D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]
Pssm-ID: 131470 [Multi-domain] Cd Length: 327 Bit Score: 163.00 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 8 TLADVAREVGVSAKTVSRVLNEDGP---ASAQTREQVLAAVAKLGFQPNLMARNIRVGGpDTTVGLVIPDLGNPFFGAVA 84
Cdd:TIGR02417 1 TLSDIAKLAGVSKTTASYVINGKAKeyrISQETVERVMAVVREQGYQPNIHAASLRAGR-SRTIGLVIPDLENYSYARIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 85 SSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGLPVVFLDRPGSGLATDSVV 164
Cdd:TIGR02417 80 KELEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDALIVASCMPPEDAYYQKLQNEGLPVVALDRSLDDEHFCSVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 165 STNRTGAHDGVAHLVAHGHRRIGFIGDLPaKLYTRRERLAGYRSALQESEIPYDRALVTNAHDQHGASAATSQLLGLADP 244
Cdd:TIGR02417 160 SDDVDAAAELIERLLSQHADEFWYLGAQP-ELSVSRDRLAGFRQALKQATLEVEWVYGGNYSRESGYQMFAKLCARLGRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 245 PTALFAGNNIVALGIVTELARTGR--KDVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDRSRARTVT 322
Cdd:TIGR02417 239 PQALFTTSYTLLEGVLDYMLERPLldSQLHLATFGDNYLLDFLPLPINSVAQQHRQLAWHALELALAAIDGKKPEPGQRY 318
|
....*....
gi 818924068 323 VPTRLIIRG 331
Cdd:TIGR02417 319 IPRTLQIRH 327
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
8-332 |
5.04e-47 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 162.20 E-value: 5.04e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 8 TLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIRVggpDTT--VGLVIPDLGNPFFGAVAS 85
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKV---NHTksIGLLATSSEAPYFAEIIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 86 SIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHS--HLKSHRAagLPVVFLD-RPGSGLATDS 162
Cdd:PRK10703 80 AVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLlaMLEEYRH--IPMVVMDwGEAKADFTDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 163 VVSTNRTGAHDGVAHLVAHGHRRIGFIgdlPAKLY--TRRERLAGYRSALQESEIPY-DRALVTNAHDQHGASAATSQLL 239
Cdd:PRK10703 158 IIDNAFEGGYLAGRYLIERGHRDIGVI---PGPLErnTGAGRLAGFMKAMEEANIKVpEEWIVQGDFEPESGYEAMQQIL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 240 GLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDRS 316
Cdd:PRK10703 235 SQKHRPTAVFCGGDIMAMGAICAADEMGLRvpqDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKRE 314
|
330
....*....|....*.
gi 818924068 317 RARTVTVPTRLIIRGS 332
Cdd:PRK10703 315 EPQTIEVHPRLVERRS 330
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
4-338 |
2.38e-46 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 160.54 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 4 NRRP-TLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIrVGGPDTTVGLVIPDLGNPFFGA 82
Cdd:PRK09526 2 KSKPvTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQL-AGKQSLTIGLATTSLALHAPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 83 VASSIEDTVRDRGLTLLMgSSADDPDRE--RALTDKFLARRIS-ILMVVPSVGAEHSHLkSHRAAGLPVVFLDRPGSGlA 159
Cdd:PRK09526 81 IAAAIKSRADQLGYSVVI-SMVERSGVEacQAAVNELLAQRVSgVIINVPLEDADAEKI-VADCADVPCLFLDVSPQS-P 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 160 TDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQEseipYDRALVTNAHDQHGASAA---TS 236
Cdd:PRK09526 158 VNSVSFDPEDGTRLGVEHLVELGHQRIALLAG-PESSVSARLRLAGWLEYLTD----YQLQPIAVREGDWSAMSGyqqTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 237 QLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDG 313
Cdd:PRK09526 233 QMLREGPVPSAILVANDQMALGVLRALHESGLRvpgQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQG 312
|
330 340
....*....|....*....|....*
gi 818924068 314 DRSRARTVtVPTRLIIRGSGERPAP 338
Cdd:PRK09526 313 QAVKGSQL-LPTSLVVRKSTAPPNT 336
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
67-332 |
6.32e-46 |
|
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: 157.33 E-value: 6.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRIS--ILMvvpSVGAEHSHLKSHRAA 144
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDgiIFA---SGTLTEENKQLLKNM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRRERLAGYRSALQESEIPYDRALV-T 223
Cdd:cd19975 78 NIPVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPRYEGYKKALKDAGLPIKENLIvE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 224 NAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIG 300
Cdd:cd19975 158 GDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRvpeDISVIGFDNTEIAEMSIPPLTTVSQPFYEMG 237
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 301 RTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd19975 238 KKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
67-328 |
3.98e-45 |
|
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 155.06 E-value: 3.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKShRAAGL 146
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLC-QAAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPaKLYTRRERLAGYRSALQESEIPYDRALV-TNA 225
Cdd:cd06274 80 PVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRP-ELPSTAERIRGFRAALAEAGITEGDDWIlAEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLG-LADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGR 301
Cdd:cd06274 159 YDRESGYQLMAELLArLGGLPQALFTSSLTLLEGVLRFLRERLGAipsDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIAE 238
|
250 260
....*....|....*....|....*..
gi 818924068 302 TAATTALARLDGdRSRARTVTVPTRLI 328
Cdd:cd06274 239 HAFELLDALIEG-QPEPGVIIIPPELI 264
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
8-330 |
2.82e-44 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 154.65 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 8 TLADVAREVGVSAKTVSRVLNedGPA-----SAQTREQVLAAVAKLGFQPNLMARNIRVGGpDTTVGLVIPDLGNPFFGA 82
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVIN--GKAkqyrvSDKTVEKVMAVVREHNYHPNAVAAGLRAGR-TRSIGLIIPDLENTSYAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 83 VASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGLPVVFLDRPGSGLATDS 162
Cdd:PRK11303 79 IAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEHPFYQRLQNDGLPIIALDRALDREHFTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 163 VVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAkLYTRRERLAGYRSALQESEIPYDRaLVTNAHDQHGASAATSQLLGLA 242
Cdd:PRK11303 159 VVSDDQDDAEMLAESLLKFPAESILLLGALPE-LSVSFEREQGFRQALKDDPREVHY-LYANSFEREAGAQLFEKWLETH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 243 DPPTALFAGNNIVALGIV-TELARTGR--KDVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDRSRAR 319
Cdd:PRK11303 237 PMPDALFTTSYTLLQGVLdVLLERPGElpSDLAIATFGDNELLDFLPCPVNAVAQQHRLIAERALELALAALDEPRKPKP 316
|
330
....*....|.
gi 818924068 320 TVTVPTRLIIR 330
Cdd:PRK11303 317 GLTRIRRNLKR 327
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
11-332 |
1.16e-43 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 152.93 E-value: 1.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 11 DVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIRVgGPDTTVGLVIPDLGNPFFGAVASSIEDT 90
Cdd:PRK10423 3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKL-NQTRTIGMLITASTNPFYSELVRGVERS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 91 VRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSvgaeHSHLKS----HRAAGLPVVFLD-RPGSGlATDSVVS 165
Cdd:PRK10423 82 CFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCT----ETHQPSreimQRYPSVPTVMMDwAPFDG-DSDLIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 166 TNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQES--EIPYDRALVTNAHDQHGASaATSQLLGLAD 243
Cdd:PRK10423 157 NSLLGGDLATQYLIDKGYTRIACITG-PLDKTPARLRLEGYRAAMKRAglNIPDGYEVTGDFEFNGGFD-AMQQLLALPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 244 PPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDRSRART 320
Cdd:PRK10423 235 RPQAVFTGNDAMAVGVYQALYQAGLsvpQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQR 314
|
330
....*....|..
gi 818924068 321 VTVPTRLIIRGS 332
Cdd:PRK10423 315 LQLTPELMERGS 326
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
67-332 |
7.61e-43 |
|
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 149.24 E-value: 7.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLM-GSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAG 145
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVePCDSDDEDLADRLRRFLSRSRPDGVILTPPLSDDPALLDALDELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRrERLAGYRSALQESEIPYDRALVT-- 223
Cdd:cd01545 81 IPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASA-ERLEGFRDALAEAGLPLDPDLVVqg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 224 NAHDQHGASAATsQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIG 300
Cdd:cd01545 160 DFTFESGLEAAE-ALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRvpdDLSVAGFDDSPIARLVWPPLTTVRQPIAEMA 238
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 301 RTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd01545 239 RRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-332 |
1.17e-42 |
|
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: 148.45 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALtDKFLARRISilMVVPSVGAEHSHLKSH-RAAG 145
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDAL-RQLLQYRVD--GVIVTSATLSSELAEEcARRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPyDRALVTNA 225
Cdd:cd06278 78 IPVVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGG-PEGTSTSRERERGFRAALAELGLP-PPAVEAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR----KDVAVVAFDDVALAEALEPALSVVAQDPEEIGR 301
Cdd:cd06278 156 YSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGlvvpEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAE 235
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 302 TAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06278 236 AAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
34-336 |
2.66e-42 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 148.99 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 34 SAQTREQVLAAVAKLGFQPNLMARNIRVGGPDTTVGLViPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERAL 113
Cdd:PRK11041 5 SQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIV-PDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 114 TDKFLARRISILMVVPS-----VGA-EHSHLKSHRAA-------GLPVVFLDrpgsglatdsvvstNRTGAHDGVAHLVA 180
Cdd:PRK11041 84 VNLIITKQIDGMLLLGSrlpfdASKeEQRNLPPMVMAnefapelELPTVHID--------------NLTAAFEAVNYLHE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 181 HGHRRIGFIG---DLPAKLYtrreRLAGYRSALQESEIPYDRALVTNAHDQHGASA-ATSQLLGLADPPTALFAGNNIVA 256
Cdd:PRK11041 150 LGHKRIACIAgpeEMPLCHY----RLQGYVQALRRCGITVDPQYIARGDFTFEAGAkALKQLLDLPQPPTAVFCHSDVMA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 257 LGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDRSRARTVTVPTRLIIRGSG 333
Cdd:PRK11041 226 LGALSQAKRMGLRvpqDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
...
gi 818924068 334 ERP 336
Cdd:PRK11041 306 AAP 308
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
67-332 |
6.87e-42 |
|
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380483 [Multi-domain] Cd Length: 274 Bit Score: 146.93 E-value: 6.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPS-VGAEHSHLKSHR--- 142
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTkSALPNPNLDLYEelq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 143 AAGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFI---GDLPAklytrRERLAGYRSALQESEIPYDR 219
Cdd:cd01541 81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIfksDDLQG-----VERYQGFIKALREAGLPIDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 220 ----ALVTNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVV 292
Cdd:cd01541 156 drilWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRvpeDLSVVGFDDSYLASLSEPPLTSV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 818924068 293 AQDPEEIGRTAATTALARLDGDRSRaRTVTVPTRLIIRGS 332
Cdd:cd01541 236 VHPKEELGRKAAELLLRMIEEGRKP-ESVIFPPELIERES 274
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-332 |
1.26e-40 |
|
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: 380629 [Multi-domain] Cd Length: 270 Bit Score: 143.46 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPD---LGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHshLKSHRA 143
Cdd:cd19974 1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGEISKEY--LEKLKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 144 AGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLpakLYTR--RERLAGYRSALQESEIPYDRA- 220
Cdd:cd19974 79 LGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDI---NYTSsfMDRYLGYRKALLEAGLPPEKEe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 221 LVTNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPE 297
Cdd:cd19974 156 WLLEDRDDGYGLTEEIELPLKLMLPTAFVCANDSIAIQLIKALKEKGYRvpeDISVVGFDNIELAELSTPPLTTVEVDKE 235
|
250 260 270
....*....|....*....|....*....|....*
gi 818924068 298 EIGRTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd19974 236 AMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
67-328 |
1.79e-40 |
|
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380665 [Multi-domain] Cd Length: 269 Bit Score: 143.08 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIP----DLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALtDKFLARRISILMVVPSVGAEHSHLKSHR 142
Cdd:cd20010 1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATY-RRLVERGRVDGFILARTRVNDPRIAYLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 143 AAGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALV 222
Cdd:cd20010 80 ERGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNG-PEELNFAHQRRDGYRAALAEAGLPVDPALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNA-HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDV-ALAEALEPALSVVAQDPE 297
Cdd:cd20010 159 REGpLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLspgKDVSVIGHDDLlPALEYFSPPLTTTRSSLR 238
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 298 EIGRTAATTALARLDGDRSRARTVTVPTRLI 328
Cdd:cd20010 239 DAGRRLAEMLLALIDGEPAAELQELWPPELI 269
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
67-333 |
2.78e-39 |
|
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: 139.73 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSvGAEHSHLKSHRA-AG 145
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVG-DAQGSEALELLEeEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFL--DRPGSGLATDSVvsTNRTGAHDGVAHLVAHGHRRIGFI-GDLPAKlyTR-RERLAGYRSALQES-------- 213
Cdd:cd06282 80 VPYVLLfnQTENSSHPFVSV--DNRLASYDVAEYLIALGHRRIAMVaGDFSAS--DRaRLRYQGYRDALKEAglkpipiv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 214 EIPydraLVTNAHdqhgaSAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALS 290
Cdd:cd06282 156 EVD----FPTNGL-----EEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRvpdDVSVIGFDGIAIGELLTPTLA 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 818924068 291 VVAQDPEEIGRTAATTALARLdGDRSRARTVTVPtrLIIRGSG 333
Cdd:cd06282 227 TVVQPSRDMGRAAADLLLAEI-EGESPPTSIRLP--HHLREGG 266
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
67-332 |
3.81e-39 |
|
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: 139.25 E-value: 3.81e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGS-SADDPDRERALTDKFLARRIS-ILMVVPSVGAEHshLKSHRAA 144
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATvDEDDPASVREALDRLLSQRVDgIIVIAPDEAVLE--ALRRLPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLD-RPGSGLATdsVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIPYDRALVT 223
Cdd:cd01574 79 GLPVVIVGsGPSPGVPT--VSIDQEEGARLATRHLLELGHRRIAHIAG-PLDWVDARARLRGWREALEEAGLPPPPVVEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 224 NAHDQHGASAAtsQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEPALSVVAQDPEEIG 300
Cdd:cd01574 156 DWSAASGYRAG--RRLLDDGPVTAVFAANDQMALGALRALHERGLrvpEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELG 233
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 301 RTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd01574 234 RRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
7-313 |
4.11e-38 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 138.74 E-value: 4.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 7 PTLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIRVGGPDtTVGLVIPDLGNPFFGAVASS 86
Cdd:PRK10727 2 ATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTE-TVGLVVGDVSDPFFGAMVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 87 IEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMV----VPSvgAEHSHLKSHraagLP-VVFLDRPGSGLATD 161
Cdd:PRK10727 81 VEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVhakmIPD--AELASLMKQ----IPgMVLINRILPGFENR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 162 SVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAkLYTRRERLAGYRSALQESEIPYDRALVTNAH-DQHGASAATSQLLG 240
Cdd:PRK10727 155 CIALDDRYGAWLATRHLIQQGHTRIGYLCSNHS-ISDAEDRLQGYYDALAESGIPANDRLVTFGEpDESGGEQAMTELLG 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818924068 241 LADPPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDG 313
Cdd:PRK10727 234 RGRNFTAVACYNDSMAAGAMGVLNDNGidvPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADN 309
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
67-332 |
7.11e-38 |
|
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380502 [Multi-domain] Cd Length: 284 Bit Score: 136.57 E-value: 7.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPD-----LGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRE----RALTDKFlarrisilmVVPSVGAEHSH 137
Cdd:cd06279 1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAaavrNAAVDGF---------IVYGLSDDDPA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 138 LKSHRAAGLPVVFLDRP-GSGLAtdSVVSTNRTGAHDGVAHLVAHGHRRIGFIG---------------DLPAKLY-TRR 200
Cdd:cd06279 72 VAALRRRGLPLVVVDGPaPPGIP--SVGIDDRAAARAAARHLLDLGHRRIAILSlrldrgrergpvsaeRLAAATNsVAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 201 ERLAGYRSALQESEIPYDRALVTNA--HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVA 275
Cdd:cd06279 150 ERLAGYRDALEEAGLDLDDVPVVEApgNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRvpeDLSVTG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 818924068 276 FDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDrsRARTVTVPTRLIIRGS 332
Cdd:cd06279 230 FDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGA--PPRPVILPTELVVRAS 284
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
8-292 |
1.31e-36 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 134.90 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 8 TLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIRVGGPDtTVGLVIPDLGNPFFGAVASSI 87
Cdd:PRK10401 3 TIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSD-TIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 88 EDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVvpsvgaeHSHLKSHRAAG-----LP-VVFLDRPGSGLATD 161
Cdd:PRK10401 82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIV-------HSKALSDDELAqfmdqIPgMVLINRVVPGYAHR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 162 SVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAkLYTRRERLAGYRSALQESEI-PYDRALVTNAHDQHGASAATSQLLG 240
Cdd:PRK10401 155 CVCLDNVSGARMATRMLLNNGHQRIGYLSSSHG-IEDDAMRRAGWMSALKEQGIiPPESWIGTGTPDMQGGEAAMVELLG 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 818924068 241 LADPPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVV 292
Cdd:PRK10401 234 RNLQLTAVFAYNDNMAAGALTALKDNGiaiPLHLSIIGFDDIPIARYTDPQLTTV 288
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
147-332 |
1.61e-36 |
|
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 132.65 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGdlpAKLYTRR-------ERLAGYRSALQESEIPYDR 219
Cdd:cd01544 77 NIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIG---GKEYTSDdgeeiedPRLRAFREYMKEKGLYNEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 220 ALVTNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVVAQDP 296
Cdd:cd01544 154 YIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGikvPEDISIISFNDIEVAKYVTPPLTTVHIPT 233
|
170 180 190
....*....|....*....|....*....|....*.
gi 818924068 297 EEIGRTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd01544 234 EEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
67-328 |
1.03e-35 |
|
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: 130.40 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPD-----LGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRIS--ILMVV----PSVgaeh 135
Cdd:cd06294 1 TIGLVLPSsaeelFQNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDgfILLYSkeddPLI---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 136 SHLKSHraaGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRrERLAGYRSALQESEI 215
Cdd:cd06294 77 EYLKEE---GFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSI-DRLQGYKQALKEAGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 216 PYDRALVTNA-HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSV 291
Cdd:cd06294 153 PLDDDYILLLdFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRvpeDVSIISFNNSPLAELASPPLTS 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 818924068 292 VAQDPEEIGRTAATTALARLDGDRSRARTVTVPTRLI 328
Cdd:cd06294 233 VDINPYELGREAAKLLINLLEGPESLPKNVIVPHELI 269
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
177-332 |
2.01e-35 |
|
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: 126.30 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 177 HLVAHGHRRIGFIGDLPAK-LYTRRERLAGYRSALQESEIPYDRALVTnAHDQHGASAATSQLLGLADPPTALFAGNNIV 255
Cdd:pfam13377 1 HLAELGHRRIALIGPEGDRdDPYSDLRERGFREAARELGLDVEPTLYA-GDDEAEAAAARERLRWLGALPTAVFVANDEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 256 ALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:pfam13377 80 ALGVLQALREAGLRvpeDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERES 159
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
67-330 |
7.68e-35 |
|
ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to 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. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.
Pssm-ID: 380509 [Multi-domain] Cd Length: 262 Bit Score: 128.05 E-value: 7.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRI-SILMVvpSVGAEHSHLKSHRAAG 145
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIdGLIIT--SRENDWEVIEPYAKYG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 lPVVFLDRPGSglATDSVVSTNR-TGAHDGVAHLVAHGHRRIGFIGDLPAKL-YTRRERLAGYRSALQESEIPYDRALV- 222
Cdd:cd06286 79 -PIVLCEETDS--PDIPSVYIDRyEAYLEALEYLKEKGHRKIGYCLGRPESSsASTQARLKAYQDVLGEHGLSLREEWIf 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEpaLSVVAQDPEEI 299
Cdd:cd06286 156 TNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIrvpEDLAVIGFDNQPISELLN--LTTIDQPLEEM 233
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 300 GRTAATTALARLDGDrsRARTVTVPTRLIIR 330
Cdd:cd06286 234 GKEAFELLLSQLESK--EPTKKELPSKLIER 262
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
67-332 |
1.58e-34 |
|
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: 127.37 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIP-------DLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDREraltDKFLARRISILMVVPSVGAEHSHLK 139
Cdd:cd06295 5 TIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQL----ARLLDSGRADGLIVLGQGLDHDALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 140 SHRAAGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYtrRERLAGYRSALQESEIPYDR 219
Cdd:cd06295 81 ELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEV--ADRLQGYRDALAEAGLEADP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 220 ALVTNAHDQHGAS-AATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQD 295
Cdd:cd06295 159 SLLLSCDFTEESGyAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISvpgDVAVVGYDDIPLAAYFRPPLTTVRQD 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 818924068 296 PEEIGRTAATTALARLDGDrsRARTVTVPTRLIIRGS 332
Cdd:cd06295 239 LALAGRLLVEKLLALIAGE--PVTSSMLPVELVVRES 273
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
67-332 |
9.04e-29 |
|
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA 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: 380520 [Multi-domain] Cd Length: 268 Bit Score: 112.17 E-value: 9.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVpsvGAEHSHLKSHR--AA 144
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMA---SLDLTELFEEVivPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRPGSGLatDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTR---RERLAGYRSALQESEIPYDRA- 220
Cdd:cd06297 78 EKPVVLIDANSMGY--DCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTEtvfREREQGFLEALNKAGRPISSSr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 221 LVTNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEalEPALSVVAQDPE 297
Cdd:cd06297 156 MFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLrvgEDVAVIGFDGQPWAA--SPGLTTVRQPVE 233
|
250 260 270
....*....|....*....|....*....|....*
gi 818924068 298 EIGRTAATTALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06297 234 EMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
68-327 |
3.40e-28 |
|
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: 110.41 E-value: 3.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 68 VGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGLP 147
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQNVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 148 VVFLDR-PGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLyTRRERLAGYRSALQESEIPYDR-ALVTNA 225
Cdd:cd01537 82 VVFFDKePSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHP-DAEARLAGVIKELNDKGIKTEQlQLDTGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 226 HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRT 302
Cdd:cd01537 161 WDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRvpsDISVFGYDALPEALKSGPLLTTILQDANNLGKT 240
|
250 260
....*....|....*....|....*
gi 818924068 303 AATTALARLDGDRSRARTVTVPTRL 327
Cdd:cd01537 241 TFDLLLNLADNWKIDNKVVRVPYVL 265
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
78-332 |
7.93e-27 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 106.94 E-value: 7.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 78 PFFGAVASSIEDTVRDRGLTLLMGSSADDPDRER---ALTDKflarRIS-ILMVVPSVGAEHSHLksHRAAGLPVVFLDR 153
Cdd:cd06277 19 PFFSELIDGIEREARKYGYNLLISSVDIGDDFDEilkELTDD----QSSgIILLGTELEEKQIKL--FQDVSIPVVVVDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 154 PGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGdlpAKLYTR--RERLAGYRSALQESEIPYD--RALVTNAHDQH 229
Cdd:cd06277 93 YFEDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLA---SSYRIKnfEERRRGFRKAMRELGLSEDpePEFVVSVGPEG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 230 GASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATT 306
Cdd:cd06277 170 AYKDMKALLDTGPKLPTAFFAENDIIALGCIKALQEAGIRvpeDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRR 249
|
250 260
....*....|....*....|....*.
gi 818924068 307 ALARLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06277 250 LIEKIKDPDGGTLKILVSTKLVERGS 275
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
67-332 |
4.39e-25 |
|
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380521 [Multi-domain] Cd Length: 268 Bit Score: 101.98 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRIS-ILMVVPSVGAEhsHLKSHRAAG 145
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDgIIFMGDELTEE--IREEFKRSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYT-RRERLAGYRSALQESEIPYDRALVTN 224
Cdd:cd06298 79 VPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSG-PLKEYInNDKKLQGYKRALEEAGLEFNEPLIFE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 225 AHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGR 301
Cdd:cd06298 158 GDYDYDSGYELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKvpeDLEIIGFDNTRYATMSRPQLTSINQPLYDIGA 237
|
250 260 270
....*....|....*....|....*....|...
gi 818924068 302 TA--ATTALarLDGDRSRARTVTVPTRLIIRGS 332
Cdd:cd06298 238 VAmrLLTKL--MNKEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
67-328 |
8.54e-24 |
|
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 98.34 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHsHLKSHRAAGL 146
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDE-HRKALKKLKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSGLAtdSVVSTNRTGAHDGVAHLVAHGHRRIGFIG----DLPaklyTRRERLAGYRSALQESEIPYDRALV 222
Cdd:cd01542 80 PVVVLGQEHEGFS--CVYHDDYGAGKLLGEYLLKKGHKNIAYIGvdeeDIA----VGVARKQGYLDALKEHGIDEVEIVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNaHDQHGASAATSQLLgLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEI 299
Cdd:cd01542 154 TD-FSMESGYEAAKELL-KENKPDAIICATDNIALGAIKALRELGIKipeDISVAGFGGYDLSEFVSPSLTTVKFDYEEA 231
|
250 260
....*....|....*....|....*....
gi 818924068 300 GRTAATTALARLDGDRSrARTVTVPTRLI 328
Cdd:cd01542 232 GEKAAELLLDMIEGEKV-PKKQKLPYELI 259
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
5-314 |
2.39e-22 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 95.86 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 5 RRPTLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNlMARNIRVGGPDTTVGLVIPDLGNPFFGAVA 84
Cdd:PRK14987 4 KRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPN-RAPDILSNATSRAIGVLLPSLTNQVFAEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 85 SSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHShLKSHRAAGLPVVFLDRPGSGLATDSVV 164
Cdd:PRK14987 83 RGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRT-LKMIEVAGIPVVELMDSQSPCLDIAVG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 165 STNRTGAHDGVAHLVAHGHRRIGFIGdlpAKLYTRR-ERLAGYRSALQESEIPYDRALVTNAHDQHGASAATSQLLGLAD 243
Cdd:PRK14987 162 FDNFEAARQMTTAIIARGHRHIAYLG---ARLDERTiIKQKGYEQAMLDAGLVPYSVMVEQSSSYSSGIELIRQARREYP 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818924068 244 PPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGD 314
Cdd:PRK14987 239 QLDGVFCTNDDLAVGAAFECQRLGLKvpdDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGE 312
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
7-77 |
6.48e-21 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 84.95 E-value: 6.48e-21
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818924068 7 PTLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIRVGGPDtTVGLVIPDLGN 77
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTK-TIGLIVPDITN 70
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
41-328 |
7.88e-20 |
|
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: 88.44 E-value: 7.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 41 VLAAVAKLGFQPNLMARNIRVGGPDTTVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLAR 120
Cdd:COG1879 9 VLALALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 121 RISILMVVPSVGAEHSH-LKSHRAAGLPVVFLDRPGSGLATDSVVST-NRTGAHDGVAHLVAH--GHRRIGFIGDLPAkL 196
Cdd:COG1879 89 GVDAIIVSPVDPDALAPaLKKAKAAGIPVVTVDSDVDGSDRVAYVGSdNYAAGRLAAEYLAKAlgGKGKVAILTGSPG-A 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 197 YTRRERLAGYRSALQE-SEIPYDRALVTNAhDQHGASAATSQLLgLADP-PTALFAGNNIVALGIVTELARTGRK-DVAV 273
Cdd:COG1879 168 PAANERTDGFKEALKEyPGIKVVAEQYADW-DREKALEVMEDLL-QAHPdIDGIFAANDGMALGAAQALKAAGRKgDVKV 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 274 VAFDdvALAEALE-----PALSVVAQDPEEIGRTAATTALARLDGdRSRARTVTVPTRLI 328
Cdd:COG1879 246 VGFD--GSPEALQaikdgTIDATVAQDPYLQGYLAVDAALKLLKG-KEVPKEILTPPVLV 302
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
67-328 |
1.95e-18 |
|
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: 83.50 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVP-SVGAEHSHLKSHRAAG 145
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPtDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDL---PAKLYTrRERLAGYRSALqeSEIPYDRALV 222
Cdd:cd06323 81 IPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELqgiPGTSAA-RERGKGFHNAI--AKYPKINVVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNAHD---QHGASAATSQLLGLADpPTALFAGNNIVALGIVTELARTGRKDVAVVAFDD----VALAEALEPALSvVAQD 295
Cdd:cd06323 158 SQTADfdrTKGLNVMENLLQAHPD-IDAVFAHNDEMALGAIQALKAAGRKDVIVVGFDGtpdaVKAVKDGKLAAT-VAQQ 235
|
250 260 270
....*....|....*....|....*....|...
gi 818924068 296 PEEIGRTAATTALARLDGDRSrARTVTVPTRLI 328
Cdd:cd06323 236 PEEMGAKAVETADKYLKGEKV-PKKIPVPLKLV 267
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
67-330 |
1.27e-17 |
|
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: 81.79 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGL 146
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGYGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 147 PVVFLDRPGSG-LATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRRERLAGYRSALQESEIP---YDRALV 222
Cdd:pfam00532 83 PVIAADDAFDNpDGVPCVMPDDTQAGYESTQYLIAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGREvkiYHVATG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNaHDQHGASAATSQllgLADPPT--ALFAGNNIVALGIVTELARTGRKDV---------AVVAFDDVALAEA--LEPAL 289
Cdd:pfam00532 163 DN-DIPDAALAANAM---LVSHPTidAIVAMNDEAAMGAVRALLKQGRVKIpdivgiginSVVGFDGLSKAQDtgLYLSP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 818924068 290 SVVAQDP-EEIGRTAATTALARLDGDRSRARTVTVPTRLIIR 330
Cdd:pfam00532 239 LTVIQLPrQLLGIKASDMVYQWIPKFREHPRVLLIPRDFFKE 280
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
142-332 |
1.70e-17 |
|
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR 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: 380485 [Multi-domain] Cd Length: 265 Bit Score: 81.09 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 142 RAAGLPVVFLD--RPGSGLAtdSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRrERLAGYRSALQES------ 213
Cdd:cd01543 68 RRLGIPVVNVSgsRPEPGFP--RVTTDNEAIGRMAAEHLLERGFRHFAFCGF-RNAAWSR-ERGEGFREALREAgyechv 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 214 -EIPYDRALVTNAHDQHgasAATSQLLGLAdPPTALFAGNNIVALgIVTELARTGR----KDVAVVAFD-DVALAEALEP 287
Cdd:cd01543 144 yESPPSGSSRSWEEERE---ELADWLKSLP-KPVGIFACNDDRAR-QVLEACREAGirvpEEVAVLGVDnDELICELSSP 218
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 818924068 288 ALSVVAQDPEEIGRTAATTaLARL-DGDRSRARTVTV-PTRLIIRGS 332
Cdd:cd01543 219 PLSSIALDAEQIGYEAAEL-LDRLmRGERVPPEPILIpPLGVVTRQS 264
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
67-328 |
2.97e-17 |
|
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: 80.48 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVP-SVGAEHSHLKSHRAAG 145
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPtNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDS-VVSTNRTGAHDGVAHLVAH------GHRRIGFIgDLPAKLYTRRERLAGYRSALQESEIPYD 218
Cdd:cd06319 81 IPVVIADIGTGGGDYVSyIISDNYDGGYQAGEYLAEAlkengwGGGSVGII-AIPQSRVNGQARTAGFEDALEEAGVEEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 219 RALVTNAHDQHGASAATSQLLgLADPPT-ALFAGNNIVALGIVTELARTGRK-DVAVVAFD--DVALAEALEPALS-VVA 293
Cdd:cd06319 160 ALRQTPNSTVEETYSAAQDLL-AANPDIkGIFAQNDQMAQGALQAIEEAGRTgDILVVGFDgdPEALDLIKDGKLDgTVA 238
|
250 260 270
....*....|....*....|....*....|....*
gi 818924068 294 QDPEEIGRTAATTALARLDGDRSRARTVTVPTRLI 328
Cdd:cd06319 239 QQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLV 273
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
67-328 |
3.23e-17 |
|
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: 80.41 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDR--GLTLLMGSSADDPDRERALTDKFLARRISILMVVP--SVGAEhSHLKSHR 142
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEInpGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAadSAGIE-PAIKRAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 143 AAGLPVVFLDRPGSGlaTDSVVSTNRTGAHDGVA-HLVahghRRIGFIGDLP----AKLYTRRERLAGYRSALQESEipy 217
Cdd:cd06321 80 DAGIIVVAVDVAAEG--ADATVTTDNVQAGYLACeYLV----EQLGGKGKVAiidgPPVSAVIDRVNGCKEALAEYP--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 218 DRALVTNA---HDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRKDVAVVAFDD-----VALAEALEPAL 289
Cdd:cd06321 151 GIKLVDDQngkGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGspeavAALKREGSPFI 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 818924068 290 SVVAQDPEEIGRTAATTALARLDGDRSRARTVTVPTRLI 328
Cdd:cd06321 231 ATAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
67-325 |
7.17e-17 |
|
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: 79.15 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVP--SVGAEHShLKSHRAA 144
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPvdSEALVPA-VKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRPGSGLA-TDSVVST-NRTGAHDgVAHLVA---HGHRRIGFIGDLPAkLYTRRERLAGYRSALQESEIPYDR 219
Cdd:cd01536 80 GIPVVAVDTDIDGGGdVVAFVGTdNYEAGKL-AGEYLAealGGKGKVAILEGPPG-SSTAIDRTKGFKEALKKYPDIEIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 220 ALVTNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR-KDVAVVAFDdvALAEALE-----PALSVVA 293
Cdd:cd01536 158 AEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRtGDIKIVGVD--GTPEALKaikdgELDATVA 235
|
250 260 270
....*....|....*....|....*....|..
gi 818924068 294 QDPEEIGRTAATTALARLDGDRSRARTVTVPT 325
Cdd:cd01536 236 QDPYLQGYLAVEAAVKLLNGEKVPKEILTPVT 267
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
8-332 |
1.39e-16 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 79.42 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 8 TLADVAREVGVSAKTVSRVLNEDGPAS--AQTREQVLAAVAKLGFQPNLMARNIRVGGPDTTVGLVIP-----DLGNPFF 80
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNDDPTLNvkEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIYSyqqelEINDPYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 81 GAVASSIEDTVRDRGLTLL-MGSSADDPDreraltdkfLARRISILMVVPSVGAEHSHLKSHRAaglPVVFLDRPGSGLA 159
Cdd:PRK10339 83 LAIRHGIETQCEKLGIELTnCYEHSGLPD---------IKNVTGILIVGKPTPALRAAASALTD---NICFIDFHEPGSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 160 TDSVVSTNRTGAHDGVAHLVAHGHRRIGFIG--DLPAKLYTRRERLAGY---RSALQESEIpydraLVTNAHDQHGASAA 234
Cdd:PRK10339 151 YDAVDIDLARISKEIIDFYINQGVNRIGFIGgeDEPGKADIREVAFAEYgrlKQVVREEDI-----WRGGFSSSSGYELA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 235 tSQLLGLADPPTALFAGNNIVALGIVTELARTG---RKDVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARL 311
Cdd:PRK10339 226 -KQMLAREDYPKALFVASDSIAIGVLRAIHERGlniPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKA 304
|
330 340
....*....|....*....|.
gi 818924068 312 DGDRSRARTVTVPTRLIIRGS 332
Cdd:PRK10339 305 RDGRALPLLVFVPSKLKLRGT 325
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
171-314 |
1.52e-16 |
|
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380664 [Multi-domain] Cd Length: 266 Bit Score: 78.35 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 171 AHDGVAHLVAHGHRRIGFIgDLPAKLYTRRERLAGYRSALQESEIPY-DRALVTNAHDQHGASAATSQLLGLADPPTALF 249
Cdd:cd20009 106 AYEAVRRLAARGRRRIALV-APPRELTYAQHRLRGFRRALAEAGLEVePLLIVTLDSSAEAIRAAARRLLRQPPRPDGII 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818924068 250 AGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEPALSVVAQDPEEIGRTAATTALARLDGD 314
Cdd:cd20009 185 CASEIAALGALAGLEDAGLvvgRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGE 252
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
67-328 |
2.62e-15 |
|
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: 74.67 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPsVGAEHS--HLKSHRAA 144
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDP-ADADASiaAVKKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDR--PGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFI------GDLPAKLytrreRLAGYRSALQesEIP 216
Cdd:cd19967 80 GIPVFLIDReiNAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVellgkeSDTNAQL-----RSQGFHSVID--QYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 217 Y-DRALVTNAH-DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR-KDVAVVAFD---DVALAEALEPALS 290
Cdd:cd19967 153 ElKMVAQQSADwDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRaGDVIIVGFDgsnDVRDAIKEGKISA 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 818924068 291 VVAQDPEEIGRTAATTALARL-DGDRSRARTVTVPTRLI 328
Cdd:cd19967 233 TVLQPAKLIARLAVEQADQYLkGGSTGKEEKQLFDCVLI 271
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
145-330 |
6.50e-15 |
|
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to 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: 380496 [Multi-domain] Cd Length: 266 Bit Score: 73.56 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRPGSGLATDSVvsTNRTGAHDGVAHLVAHGHRRIGFIGDLpaKLYTR-RERLAGYRSALQESEIPY-DRALV 222
Cdd:cd06272 79 KIPIVLYNRESPKYSTVNV--DNEKAGRLAVLLLIQKGHKSIAYIGNP--NSNRNqTLRGKGFIETCEKHGIHLsDSIID 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALEPALSVVAQDPEEI 299
Cdd:cd06272 155 SRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISipeDISIVSYDNIPQEARSDPPLTVVGVPIEKI 234
|
170 180 190
....*....|....*....|....*....|.
gi 818924068 300 GRTAATTALARLDGDRSRARTVTVPTRLIIR 330
Cdd:cd06272 235 AEESLRLILKLIEGRENEIQQLILYPELIFR 265
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
68-313 |
6.69e-15 |
|
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: 73.50 E-value: 6.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 68 VGLVIPDLGNPFFGAVASSIEDTVRDRGLT-LLMGSSADDPDRERALTDKFLARRISILMVVP-SVGAEHSHLKSHRAAG 145
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPvDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVSTN-----RTGAHDGVAHLVAHGHRRI--GFIGDLPAklytrRERLAGYRSALQE--SEIP 216
Cdd:pfam13407 81 IPVVTFDSDAPSSPRLAYVGFDneaagEAAGELLAEALGGKGKVAIlsGSPGDPNA-----NERIDGFKKVLKEkyPGIK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 217 YDRALVTNAHDQHGASAATSQLLG-LADPPTALFAGNNIVALGIVTELARTGRKD-VAVVAFDdvALAEALEpAL----- 289
Cdd:pfam13407 156 VVAEVEGTNWDPEKAQQQMEALLTaYPNPLDGIISPNDGMAGGAAQALEAAGLAGkVVVTGFD--ATPEALE-AIkdgti 232
|
250 260
....*....|....*....|....*
gi 818924068 290 -SVVAQDPEEIGRTAATTALARLDG 313
Cdd:pfam13407 233 dATVLQDPYGQGYAAVELAAALLKG 257
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
10-60 |
9.18e-15 |
|
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.
Pssm-ID: 143331 [Multi-domain] Cd Length: 52 Bit Score: 67.82 E-value: 9.18e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 818924068 10 ADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPNLMARNIR 60
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLR 51
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
67-314 |
3.30e-14 |
|
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: 71.70 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPS-VGAEHSHLKSHRAAG 145
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAgATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDLPAKLYTRRE--RLAGYRSALQESEIPYDRALVT 223
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEvdRTKGFQEALAEAPGIKVVAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 224 NAHDQHGASAATSQLLGlADPP-TALFAGNNIVALGIVTELARTGR-KDVAVVAFD-DVALAEALEPAL--SVVAQDPEE 298
Cdd:cd19972 161 ADWDQDEGFKVAQDMLQ-ANPNiTVFFGQSDAMALGAAQAVKVAGLdHKIWVVGFDgDVAGLKAVKDGVldATMTQQTQK 239
|
250
....*....|....*.
gi 818924068 299 IGRTAATTALARLDGD 314
Cdd:cd19972 240 MGRLAVDSAIDLLNGK 255
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
144-313 |
7.80e-14 |
|
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380495 [Multi-domain] Cd Length: 264 Bit Score: 70.53 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 144 AGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFIGDlPAKLYTRRERLAGYRSALQESEIP-YDRALV 222
Cdd:cd06271 79 QNFPFVAHGRSD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVP-PARYSPHDRRLQGYVRA*RDAGLTgYPLDAD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 223 TNAhdqHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRK---DVAVVAFDDVALAEALE-PALSVVAQDPEE 298
Cdd:cd06271 158 TTL---EAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKigeDVSIIGKDSAPFLGAMItPPLTTVHAPIAE 234
|
170
....*....|....*
gi 818924068 299 IGRTAATTALARLDG 313
Cdd:cd06271 235 AGRELAKALLARIDG 249
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
43-330 |
2.20e-13 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 69.73 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 43 AAVAKLGFQPNLMARNirvggpdtTVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRI 122
Cdd:PRK10653 12 AVALSATVSANAMAKD--------TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 123 SILMVVPS-VGAEHSHLKSHRAAGLPVVFLDRPGS-GLATDSVVSTNRTG---AHDGVAHLVAHGHRRI---GFIGDLPA 194
Cdd:PRK10653 84 KILLINPTdSDAVGNAVKMANQANIPVITLDRGATkGEVVSHIASDNVAGgkmAGDFIAKKLGEGAKVIqleGIAGTSAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 195 klytrRERLAGYRSALQESEI--------PYDRALVTNAHDQHGASAATSQllgladpptALFAGNNIVALGIVTELART 266
Cdd:PRK10653 164 -----RERGEGFKQAVAAHKFnvlasqpaDFDRTKGLNVMQNLLTAHPDVQ---------AVFAQNDEMALGALRALQTA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818924068 267 GRKDVAVVAFD--DVALAEALEPALS-VVAQDPEEIGRTAATTALARLDGDRSRArTVTVPTRLIIR 330
Cdd:PRK10653 230 GKSDVMVVGFDgtPDGIKAVNRGKLAaTIAQQPDQIGAIGVETADKVLKGEKVEA-KIPVDLKLVTK 295
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
8-53 |
3.66e-13 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 63.04 E-value: 3.66e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 818924068 8 TLADVAREVGVSAKTVSRVLNEDGPASAQTREQVLAAVAKLGFQPN 53
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
67-328 |
8.06e-13 |
|
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: 67.69 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVP-SVGAEHSHLKSHRAAG 145
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPvDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDRPGSGLATDSVVST-NRTG---AHDGVAHLVAHGHRRIGFIGDLpaKLYTRRERLAGYRSALQE-------SE 214
Cdd:cd06322 81 IPVFTVDVKADGAKVVTHVGTdNYAGgklAGEYALKALLGGGGKIAIIDYP--EVESVVLRVNGFKEAIKKypnieivAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 215 IPYDRALVTnahdqhgASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR-KDVAVVAFDdvALAEALE------P 287
Cdd:cd06322 159 QPGDGRREE-------ALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKeDKIKVIGFD--GNPEAIKaiakggK 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 818924068 288 ALSVVAQDPEEIGRTAATTALARLDGDrSRARTVTVPTRLI 328
Cdd:cd06322 230 IKADIAQQPDKIGQETVEAIVKYLAGE-TVEKEILIPPKLY 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
67-327 |
7.98e-12 |
|
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: 64.53 E-value: 7.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVP--SVGAEHShLKSHRAA 144
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPvdSEGIRPA-LEAAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRPGSGL-ATDSVVSTNRTGAHDGVAHLVAHGHR---RIGFIgDLPAKLYTrRERLAGYRSALQEseipYDRA 220
Cdd:cd19971 80 GIPVINVDTPVKDTdLVDSTIASDNYNAGKLCGEDMVKKLPegaKIAVL-DHPTAESC-VDRIDGFLDAIKK----NPKF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 221 LVTNAHDQHGASA----ATSQLLGLADPPTALFAGNNIVALGIVTELARTGR-KDVAVVAFDDVALAEAL---EPALSVV 292
Cdd:cd19971 154 EVVAQQDGKGQLEvampIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKlGDILVYGVDGSPDAKAAikdGKMTATA 233
|
250 260 270
....*....|....*....|....*....|....*
gi 818924068 293 AQDPEEIGRTAATTALARLDGDRSRARTVtVPTRL 327
Cdd:cd19971 234 AQSPIEIGKKAVETAYKILNGEKVEKEIV-VPTFL 267
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
68-328 |
8.69e-10 |
|
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: 58.81 E-value: 8.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 68 VGLVIPDLGNPFFGAVASSIEDTVRDRG--LTLLMGSSADDPDRERALTDKFLARRISILMVVP-SVGAEHSHLKSHRAA 144
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGvkVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPiSDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRP-------GSGLATDSVVSTN-----RTGAHDGVAHLVAHGhrRIGFIGDLPAKlYTRRERLAGYRSALQE 212
Cdd:cd06320 82 GIPVINLDDAvdadalkKAGGKVTSFIGTDnvaagALAAEYIAEKLPGGG--KVAIIEGLPGN-AAAEARTKGFKETFKK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 213 SEiPYDRALVTNAH-DQHGASAATSQLLGlADPP-TALFAGNNIVALGIVTELARTGRK-DVAVVAFDDValAEALEpal 289
Cdd:cd06320 159 AP-GLKLVASQPADwDRTKALDAATAILQ-AHPDlKGIYAANDTMALGAVEAVKAAGKTgKVLVVGTDGI--PEAKK--- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 818924068 290 SV--------VAQDPEEIGRTAATTALARLDGdRSRARTVTVPTRLI 328
Cdd:cd06320 232 SIkageltatVAQYPYLEGAMAVEAALRLLQG-QKVPAVVATPQALI 277
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
67-330 |
5.28e-09 |
|
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: 56.47 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRE--RALTDKFLARRISILMVVPS-VGAEHSHLKSHRA 143
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPSREDDVEaqIQIIEYFIDQGVDGIVLAPLdRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 144 AGLPVVFLDRPGSGLATDSVVSTN-----RTGAhdgvAHLVA--HGHRRIGFIGDLPAKLYTrRERLAGYRSALQESEip 216
Cdd:cd20004 81 QGIPVVIIDSDLGGDAVISFVATDnyaagRLAA----KRMAKllNGKGKVALLRLAKGSAST-TDRERGFLEALKKLA-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 217 YDRALVTNAH---DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR-KDVAVVAFD-DVALAEALEPAL-- 289
Cdd:cd20004 154 PGLKVVDDQYaggTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLaGKVKFIGFDaSDLLLDALRAGEis 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 818924068 290 SVVAQDPEEIGRTAATTALARLDGDRSRARTVTvPTRLIIR 330
Cdd:cd20004 234 ALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDT-GVVLVTK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
67-335 |
5.50e-09 |
|
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: 56.23 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVP-SVGAEHSHLKSHRAAG 145
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAiDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 146 LPVVFLDR--PGSGLATDSVVSTNRTGAHDG--VAHLVA---HGHRRIGFIGDLPAklYTRRERLAGYRSAL-------- 210
Cdd:cd06317 81 IPVIAYDAviPSDFQAAQVGVDNLEGGKEIGkyAADYIKaelGGQAKIGVVGALSS--LIQNQRQKGFEEALkanpgvei 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 211 ---QESEIPYDRALvtnahdqhgaSAATSQLLGLADpPTALFAGNNIVALGIVTELARTGR-KDVAVVAFDDVA-LAEAL 285
Cdd:cd06317 159 vatVDGQNVQEKAL----------SAAENLLTANPD-LDAIYATGEPALLGAVAAVRSQGRqGKIKVFGWDLTKqAIFLG 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 818924068 286 EPA---LSVVAQDPEEIGRTAATTALARLDGDRSrARTVTVPTRLIIRGSGER 335
Cdd:cd06317 228 IDEgvlQAVVQQDPEKMGYEAVKAAVKAIKGEDV-EKTIDVPPTIVTKENVDQ 279
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
67-328 |
7.51e-09 |
|
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: 56.07 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSV--GAEhSHLKSHRAA 144
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDatGWD-PVLKEAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRPGSGLATDSVVSTNRT-------GAHDGVAHLVAHGHRRI----GFIGDLPAklytrRERLAGYRSALQES 213
Cdd:cd06309 80 GIPVILVDRTIDGEDGSLYVTFIGSdfveegrRAAEWLVKNYKGGKGNVvelqGTAGSSVA-----IDRSKGFREVIKKH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 214 EipyDRALVTNahdQHG------ASAATSQLLgLADPP--TALFAGNNIVALGIVTELARTGR---KDVAVVAFDdvALA 282
Cdd:cd06309 155 P---NIKIVAS---QSGnftrekGQKVMENLL-QAGPGdiDVIYAHNDDMALGAIQALKEAGLkpgKDVLVVGID--GQK 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 818924068 283 EALEP-----ALSVVAQDPeEIGRTAATTALARLDGDRSrARTVTVPTRLI 328
Cdd:cd06309 226 DALEAikageLNATVECNP-LFGPTAFDTIAKLLAGEKV-PKLIIVEERLF 274
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
133-332 |
8.77e-09 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 55.50 E-value: 8.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 133 AEHSHLKSHRAAGLPVVFLDR-PGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIG-FIGDLPAKLYTRRERLagYRSAL 210
Cdd:cd06287 67 VEDPILARLRQRGVPVVSIGRaPGTDEPVPYVDLQSAATARLLLEHLHGAGARQVAlLTGSSRRNSSLESEAA--YLRFA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 211 QESEIPYDRALVTNAHDQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR---KDVAVVAFDDVALAEALEP 287
Cdd:cd06287 145 QEYGTTPVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRsvpEDLMVVTRYDGIRARTADP 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 818924068 288 ALSVVAQDPEEIGRTAATTALARLDGdRSRARTVTVPTRLIIRGS 332
Cdd:cd06287 225 PLTAVDLHLDRVARTAIDLLFASLSG-EERSVEVGPAPELVVRAS 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
67-322 |
1.94e-08 |
|
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: 54.66 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTL--LMGSSADDPDRERALTDKFLARRISILMVVPsVGAEHS--HLKSHR 142
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIifVGPESEEDVAGQNSLLEELINKKPDAIVVAP-LDSEDLvdPLKDAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 143 AAGLPVVFLDrpgSGLATDSVVST----NRTG---AHDGVAHLVAhGHRRIGFIgDLPAKLYTRRERLAGYRSALQES-- 213
Cdd:cd06310 80 DKGIPVIVID---SGIKGDAYLSYiatdNYAAgrlAAQKLAEALG-GKGKVAVL-SLTAGNSTTDQREEGFKEYLKKHpg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 214 -----EIPYdralvtnAHDQHGASA-ATSQLLGLADPPTALFAGNNIVALGIVTELARTGRKD-VAVVAFD-DVALAEAL 285
Cdd:cd06310 155 gikvlASQY-------AGSDYAKAAnETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGqIKIVGFDsQEELLDAL 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 818924068 286 EPAL--SVVAQDPEEIGRTAATTALARLDGDRSRARTVT 322
Cdd:cd06310 228 KNGKidALVVQNPYEIGYEGIKLALKLLKGEEVPKNIDT 266
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
67-328 |
2.00e-08 |
|
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: 54.72 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILM--------VVPSVGAEHshl 138
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLIlnpvdpegLTPAVKAAK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 139 kshrAAGLPVVFLDRPGSGLAtdSVVSTNRTGAHDGVahlVAHGHRRIGFIGDLPAKLY---------TRRERLAGYRSA 209
Cdd:cd06318 78 ----AAGIPVITVDSALDPSA--NVATQVGRDNKQNG---VLVGKEAAKALGGDPGKIIelsgdkgneVSRDRRDGFLAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 210 LQESEIPYDRA----LVTNAH---DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGR-KDVAVVAFDdvAL 281
Cdd:cd06318 149 VNEYQLRKYGKsnikVVAQPYgnwIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMlDKVKVAGAD--GQ 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 818924068 282 AEALE-----PALSVVAQDPEEIGRTAATTALARLDGDRSRARTVTVPTRLI 328
Cdd:cd06318 227 KEALKlikdgKYVATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPTALI 278
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
67-327 |
2.40e-08 |
|
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: 54.56 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDR-GLTLLM--GSSADDPDRERALTDKFLARRISILMVVP--SVGAEHSHLKSH 141
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEAnGYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPadSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 142 RAaGLPVVFLDR-------PGSGLATDSVVSTNRTGAHDGVAHLVAH--GHRRIGFIGDLPAKlYTRRERLAGYRSALQE 212
Cdd:cd19970 81 DA-GIAVINIDNrldadalKEGGINVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGA-DNAQQRKAGFLKAFEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 213 SEIpyDRALVTNAH-DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRKD-VAVVAFDDVALAEALEPALS 290
Cdd:cd19970 159 AGM--KIVASQSANwEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 818924068 291 VVA---QDPEEIGRTAATTALARLDGDRSRArTVTVPTRL 327
Cdd:cd19970 237 MLAtidQHPAKQAVYGIEYALKMLNGEEVPG-WVKTPVEL 275
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
67-322 |
2.81e-08 |
|
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: 54.17 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLM-GSSADDPDRERALTDKFLARRISILMVVP-SVGAEHSHLKSHRAA 144
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVqGPPTFDPTLQTPIVNAVIAKKPDALLIAPtDPQALIAPLKRAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDRP--GSGLATDSVVSTNRTG---AHDGVAHLVaHGHRRIGFIGDLPAkLYTRRERLAGYRSALQ-ESEIPYd 218
Cdd:cd20007 81 GIKVVTVDTTlgDPSFVLSQIASDNVAGgalAAEALAELI-GGKGKVLVINSTPG-VSTTDARVKGFAEEMKkYPGIKV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 219 raLVT--NAHDQHGASAATSQLLgLADPP-TALFAGNNIVALGIVTELARTGRKD-VAVVAFD-DVALAEALEPAL--SV 291
Cdd:cd20007 158 --LGVqySENDPAKAASIVAAAL-QANPDlAGIFGTNTFSAEGAAAALRNAGKTGkVKVVGFDaSPAQVEQLKAGTidAL 234
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 292 VAQDPEEIGRTAATTALARLDGDRSRARTVT 322
Cdd:cd20007 235 IAQKPAEIGYLAVEQAVAALTGKPVPKDILT 265
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
67-312 |
5.66e-07 |
|
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: 50.31 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSAD-DPDRERALTDKFLARRISILMVVP----SVGAEHshlKSH 141
Cdd:cd06316 1 KVAIAMHTTGSDWSRLQVAGIKDTFEELGIEVVAVTDANfDPAKQITDLETLIALKPDIIISIPvdpvATAAAY---KKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 142 RAAGLPVVFLDRPGSGLA--TD--SVVSTNRTGAHDGVAHLVAH---GHRRIGFIgDLPAKLYTRRERLAGYRSALQEsE 214
Cdd:cd06316 78 ADAGIKLVFMDNVPDGLEagKDyvSVVSSDNRGNGQIAAELLAEaigGKGKVGII-YHDADFYATNQRDKAFKDTLKE-K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 215 IPyDRALVT--NAHDQHGASAATSQLLgLADPP-TALFAGNNIVALGIVTELARTGRKDVAVVAFD-DVALAEAL---EP 287
Cdd:cd06316 156 YP-DIKIVAeqGFADPNDAEEVASAML-TANPDiDGIYVSWDTPALGVISALRAAGRSDIKITTVDlGTEIALDMakgGN 233
|
250 260
....*....|....*....|....*.
gi 818924068 288 ALSVVAQDPEEIGRTAAT-TALARLD 312
Cdd:cd06316 234 VKGIGAQRPYDQGVAEALaAALALLG 259
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
142-328 |
2.38e-06 |
|
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: 48.36 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 142 RAAGLPVVFLDRPGSGLATDSVVSTNRTGAHDGVAHLVAHGHR---RIGFIGDLP-AKLYTRRERlaGYRSALQEseipY 217
Cdd:cd20006 81 KKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGekgKVAIVSFVKgSSTAIEREE--GFKQALAE----Y 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 218 DRALVTNAH----DQHGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTGRKD-VAVVAFD-DVALAEALEP---- 287
Cdd:cd20006 155 PNIKIVETEycdsDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGkVKVVGFDsSVEEIQLLEEgiid 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 818924068 288 ALsvVAQDPEEIGRTAATTALARLDGdRSRARTVTVPTRLI 328
Cdd:cd20006 235 AL--VVQNPFNMGYLSVQAAVDLLNG-KKIPKRIDTGSVVI 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
67-315 |
2.89e-06 |
|
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: 47.99 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRG--LTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAA 144
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGveVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 145 GLPVVFLDrpgSGLATDSVVST----N----RTGAHDGVAHLVAHG--HRRIGFIGDLPAKlYTRRERLAGYRSALQEse 214
Cdd:cd20008 81 GIPVVLVD---SGANTDDYDAFlatdNvaagALAADELAELLKASGggKGKVAIISFQAGS-QTLVDREEGFRDYIKE-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 215 ipYDRALVTNAH-----DQHGASAATSQLLgLADPP-TALFAGNNIVALGIVTELARTGR-KDVAVVAFDDVALAEALEP 287
Cdd:cd20008 155 --KYPDIEIVDVqysdgDIAKALNQTTDLL-TANPDlVGIFGANNPSAVGVAQALAEAGKaGKIVLVGFDSSPDEVALLK 231
|
250 260 270
....*....|....*....|....*....|.
gi 818924068 288 A---LSVVAQDPEEIGRTAATTALARLDGDR 315
Cdd:cd20008 232 SgviKALVVQDPYQMGYEGVKTAVKALKGEE 262
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
77-303 |
3.17e-06 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 48.03 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 77 NPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPSVGAEHSHLKSHRAAGLPVVFLD---- 152
Cdd:cd01391 14 EQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQLFDIPQLALDatsq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 153 ---RPGSGLATDSVVSTNRTGAHDGVAHLVAHGHRRIGFI-GDLPAklyTRRERLAGYRSALQESEIPYDRALVTNAHDQ 228
Cdd:cd01391 94 dlsDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIhGEGLN---SGELRMAGFKELAKQEGICIVASDKADWNAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 229 HGASAATSQLLGLADPPTALFAGNNIVALGIVTELARTG-RKDVAVVAFDDVALAEALE-----PALSVVAQDPEEIGRT 302
Cdd:cd01391 171 EKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGlVGDVSVIGSDGWADRDEVGyeveaNGLTTIKQQKMGFGIT 250
|
.
gi 818924068 303 A 303
Cdd:cd01391 251 A 251
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
67-329 |
5.15e-06 |
|
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: 47.38 E-value: 5.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 67 TVGLVIPDLGNPFFGAVASSIEDTVRDRGLTLLMGSSADDPDRERALTDKFLARRISILMVVPS-----VGAEHSHLKsh 141
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIdvkalVPAIEAAIK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 142 raAGLPVVFLDRPGSGLA-TDSVVSTNRTG---AHDGVAHLVAHGHRRIGFIGDLPAKlyTRRERLAGYRSALQESEipy 217
Cdd:cd19968 79 --AGIPVVTVDRRAEGAApVPHVGADNVAGgreVAKFVVDKLPNGAKVIELTGTPGSS--PAIDRTKGFHEELAAGP--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 218 DRALVTN-----AHDQhGASAATSQLLGLADPPTALFAGNNIVALGIVtELART---GRKDVAVVAFDdvALAEALEP-- 287
Cdd:cd19968 152 KIKVVFEqtgnfERDE-GLTVMENILTSLPGPPDAIICANDDMALGAI-EAMRAaglDLKKVKVIGFD--AVPDALQAik 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 818924068 288 ---ALSVVAQDPEEIGRTAATTALARLDgDRSRARTVTVPTRLII 329
Cdd:cd19968 228 dgeLYATVEQPPGGQARTALRILVDYLK-DKKAPKKVNLKPKLIT 271
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
246-329 |
1.01e-05 |
|
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: 46.52 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 246 TALFAGNNIVALGIVTELARTGRKDVAVVAFD----DVAL-AEALEPALSVVAQDPEEIGRTAATTALARLDGDRSrART 320
Cdd:cd06305 186 DAIWAAWDEPAKGAVQALEEAGRTDIKVYGVDisnqDLELmADEGSPWVATAAQDPALIGTVAVRNVARKLAGEDL-PDK 264
|
....*....
gi 818924068 321 VTVPTRLII 329
Cdd:cd06305 265 YSLVPVLIT 273
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
68-330 |
2.04e-05 |
|
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: 45.63 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 68 VGLVIPDLGNPFFGAVASSIE---DTVRDRGLTLLMGSSAD-DPDRERALTDKfLARRISILMVV----PSVGAEHSHLk 139
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEaaaAALRDRRVRLRIHFVDSlDPEALAAALRR-LAAGCDGVALVapdhPLVRAAIDEL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 140 shRAAGLPVVFL--DRPGSGLA----TDSVVStNRTGAHdGVAHLVAHGHRRIG-FIGDLpaKLYTRRERLAGYRSALQE 212
Cdd:cd06307 80 --AARGIPVVTLvsDLPGSRRLayvgIDNRAA-GRTAAW-LMGRFLGRRPGKVLvILGSH--RFRGHEEREAGFRSVLRE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818924068 213 S----EIpydRALVTNAHDQHGASAATSQLLGLADPPTALF---AGNNivalGIVTELARTGR-KDVAVVAFDdvaLAEA 284
Cdd:cd06307 154 RfpdlTV---LEVLEGLDDDELAYELLRELLARHPDLVGIYnagGGNE----GIARALREAGRaRRVVFIGHE---LTPE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 818924068 285 LEPALS------VVAQDPEEIGRTAATTALARLDGDRSRARTVTVPTRLIIR 330
Cdd:cd06307 224 TRRLLRdgtidaVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR 275
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