|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
5-348 |
7.51e-121 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 351.81 E-value: 7.51e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 5 KKKATIKDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQL 84
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGPPR-VSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 85 IAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPYVLFDQPHDDYDGAAID 164
Cdd:COG1609 80 LRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 165 FDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASKKSGASAMKDYqrgqel 244
Cdd:COG1609 160 VDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRL------ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 245 gsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLMECL 324
Cdd:COG1609 234 ----LARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRI 309
|
330 340
....*....|....*....|....
gi 493831315 325 DGVHTWKKRVMLEPVLVERESIRK 348
Cdd:COG1609 310 EGPDAPPERVLLPPELVVRESTAP 333
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
69-341 |
1.26e-91 |
|
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: 274.78 E-value: 1.26e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASK 228
Cdd:cd06267 82 VLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 229 KSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQS 308
Cdd:cd06267 162 ESGYEAARE----------LLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQP 231
|
250 260 270
....*....|....*....|....*....|...
gi 493831315 309 AYRTGELAAKLLMECLDGVHTWKKRVMLEPVLV 341
Cdd:cd06267 232 AYEMGRAAAELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
68-345 |
2.97e-67 |
|
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: 212.40 E-value: 2.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGV-LLSLIHWDESINSA------ 140
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGViLLSGRLDAELLSELskrypi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 141 ------LDEAGIPYVLFDqphdDYDGAaidfdfyssgRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHM 214
Cdd:cd06284 81 vqcceyIPDSGVPSVSID----NEAAA----------YDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 215 ELKEDNIFVSTASKKSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEF 294
Cdd:cd06284 147 PVDEDLIIEGDFSFEAGYAAARAL----------LALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEF 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 493831315 295 GEMIVPALTTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06284 217 AEMFSPSLTTIRQPRYEIGETAAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
69-345 |
3.00e-67 |
|
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: 212.49 E-value: 3.00e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLL--SLIHwDESINSALDEAGI 146
Cdd:cd19976 2 IGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIasSNIS-DEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTA 226
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 227 SKKSGASAMKDyqrgqelgsmVLERKRiPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTIS 306
Cdd:cd19976 161 SLEGGYKAAEE----------LLKSKN-PTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIA 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 493831315 307 QSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd19976 230 QPIFEMGQEAAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
69-345 |
4.04e-66 |
|
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: 209.72 E-value: 4.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPM-DRPSRKKLFEGFQDALTDHHMELKEDNIFVSTAS 227
Cdd:cd19975 82 VLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLdDPNAGYPRYEGYKKALKDAGLPIKENLIVEGDFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 228 KKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQ 307
Cdd:cd19975 162 FKSGYQAMKR----------LLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQ 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 493831315 308 SAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd19975 232 PFYEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-345 |
6.05e-66 |
|
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: 209.39 E-value: 6.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGP------MDRpsrkklFEGFQDALTDHHMELKEDNIF 222
Cdd:cd06285 82 VLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPlnastgRDR------LRGYRRALAEAGLPVPDERIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 223 VSTASKKSGASAMKdyqrgqelgsMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPAL 302
Cdd:cd06285 156 PGGFTIEAGREAAY----------RLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 493831315 303 TTISQSAYRTGELAAKLLmecLDGVHTWKKRVM---LEPVLVERES 345
Cdd:cd06285 226 TTVRQPKYEMGRRAAELL---LQLIEGGGRPPRsitLPPELVVRES 268
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
8-347 |
1.15e-65 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 210.74 E-value: 1.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 8 ATIKDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQLIAA 87
Cdd:PRK10703 2 ATIKDVAKRAGVSTTTVSHVINKTRF-VAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 88 VQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHW-DESINSALDEAGIPYVLFD--QPHDDYDGAAID 164
Cdd:PRK10703 81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYpEPLLAMLEEYRHIPMVVMDwgEAKADFTDAIID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 165 FDFySSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASKKSGASAMKDyqrgqel 244
Cdd:PRK10703 161 NAF-EGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQ------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 245 gsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLMECL 324
Cdd:PRK10703 233 ---ILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRI 309
|
330 340
....*....|....*....|...
gi 493831315 325 DGVHTWKKRVMLEPVLVERESIR 347
Cdd:PRK10703 310 VNKREEPQTIEVHPRLVERRSVA 332
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
69-345 |
1.22e-64 |
|
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: 205.83 E-value: 1.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLslIHWDESINSaLDEAGIPY 148
Cdd:cd06291 2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIIL--GSHSLDIEE-YKKLNIPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFD-QPHDDYDgaAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHmeLKEDNIFVStas 227
Cdd:cd06291 79 VSIDrYLSEGIP--SVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAG--IEYEIIEID--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 228 kksgaSAMKDYQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQ 307
Cdd:cd06291 152 -----ENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQ 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 493831315 308 SAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06291 227 PIEEMAKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
69-345 |
8.10e-64 |
|
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: 203.64 E-value: 8.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDE-AGIP 147
Cdd:cd06275 2 IGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAAlRSIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTAS 227
Cdd:cd06275 82 VVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGDFE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 228 KKSGASAMkdyqrgQELgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQ 307
Cdd:cd06275 162 PEGGYEAM------QRL----LSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQ 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 493831315 308 SAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06275 232 PKDELGELAVELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-345 |
3.67e-62 |
|
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: 199.42 E-value: 3.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06293 2 IGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHhmELKEDNIFVSTASK 228
Cdd:cd06293 82 VLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEA--GLDPDEVVRELSAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 229 KSGASAmkdyqrGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQS 308
Cdd:cd06293 160 DANAEL------GRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQP 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 493831315 309 AYRTGELAAKLLM-ECLDGVHTwKKRVMLEPVLVERES 345
Cdd:cd06293 234 SYELGRAAADLLLdEIEGPGHP-HEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-345 |
9.11e-61 |
|
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: 195.91 E-value: 9.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEaGIPY 148
Cdd:cd06290 2 IGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAE-GIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASK 228
Cdd:cd06290 81 VLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 229 KSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQS 308
Cdd:cd06290 161 ESGYEAMKKL----------LKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQP 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 493831315 309 AYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06290 231 LYEMGKTAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
69-341 |
5.50e-60 |
|
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: 193.51 E-value: 5.50e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFvsTASK 228
Cdd:cd19977 82 VFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIK--HVDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 229 KSGasamkdyqrGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQS 308
Cdd:cd19977 160 QDD---------VRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQP 230
|
250 260 270
....*....|....*....|....*....|....
gi 493831315 309 AYRTGELAAKLLMECLDGVHTWKKR-VMLEPVLV 341
Cdd:cd19977 231 TYEIGRKAAELLLDRIENKPKGPPRqIVLPTELI 264
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
69-344 |
4.64e-59 |
|
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: 191.19 E-value: 4.64e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06270 2 IGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPPL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASK 228
Cdd:cd06270 82 VVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDFTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 229 KSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQS 308
Cdd:cd06270 162 EGGYAAAKQL----------LARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYP 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 493831315 309 AYRTGELAAKLLMECLDGvHTWKKRVMLEPVLVERE 344
Cdd:cd06270 232 IEEMAQAAAELALNLAYG-EPLPISHEFTPTLIERD 266
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
69-344 |
1.73e-57 |
|
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: 187.39 E-value: 1.73e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLS-LIHWDESINSALDEAGIP 147
Cdd:cd06289 2 VGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSpAAGTTAELLRRLKAWGIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLF--DQPHDDYDGAAIDFDFysSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVST 225
Cdd:cd06289 82 VVLAlrDVPGSDLDYVGIDNRL--GAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 226 ASKKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTI 305
Cdd:cd06289 160 ATREAGAEAARE----------LLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTV 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 493831315 306 SQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERE 344
Cdd:cd06289 230 SVHPREIGRRAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-345 |
2.78e-56 |
|
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: 184.25 E-value: 2.78e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLS-LIHwDESINSALDEAGIP 147
Cdd:cd06273 2 IGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVgSDH-DPELFELLEQRQVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPM---DRpSRKKLfEGFQDALTDHHMELKEDNIFVS 224
Cdd:cd06273 81 YVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTagnDR-ARARL-AGIRDALAERGLELPEERVVEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 225 TASKKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTT 304
Cdd:cd06273 159 PYSIEEGREALRR----------LLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493831315 305 ISQSAYRTGELAAKLLMECLDGvHTWKKRVMLEPVLVERES 345
Cdd:cd06273 229 VRVPAREIGELAARYLLALLEG-GPPPKSVELETELIVRES 268
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
69-345 |
1.06e-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: 180.05 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSI-TNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALDEAGIP 147
Cdd:cd06288 2 IGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMH-HREVTLPPELTDIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTAS 227
Cdd:cd06288 81 LVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDWG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 228 KKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQ 307
Cdd:cd06288 161 RESGYEAAKR----------LLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVAL 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 493831315 308 SAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06288 231 PYYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
69-343 |
3.39e-54 |
|
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: 178.99 E-value: 3.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLL-SLIHWDESINSaLDEAGIP 147
Cdd:cd06280 2 IGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILaPSAGPSRELKR-LLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTAS 227
Cdd:cd06280 81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 228 KKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQ 307
Cdd:cd06280 161 IEGGYEAVKA----------LLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQ 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 493831315 308 SAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVER 343
Cdd:cd06280 231 PAYEIGRIAAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
68-345 |
8.30e-54 |
|
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: 178.07 E-value: 8.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLS-LIHWDESINsALDEAGI 146
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTgTEHTPATRK-LLRAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYV-LFDQPHDDYDgAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSR-KKLFEGFQDALTDHHMELKEDNIFVS 224
Cdd:cd01575 80 PVVeTWDLPDDPID-MAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRaRQRLEGFRDALAEAGLPLPLVLLVEL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 225 TASKKSGASAMkdyqrgqelgSMVLERKRIPDALFTVNDMMAIGIMkqLETHQ--IHIPRDMSILGFDNVEFGEMIVPAL 302
Cdd:cd01575 159 PSSFALGREAL----------AELLARHPDLDAIFCSNDDLALGAL--FECQRrgIRVPGDIAIAGFGDLDIAAALPPAL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 493831315 303 TTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd01575 227 TTVRVPRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
4-345 |
7.38e-53 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 177.88 E-value: 7.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 4 KKKKATIKDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQ 83
Cdd:PRK09526 2 KSKPVTLYDVARYAGVSYQTVSRVLNQASH-VSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 84 LIAAVQKECMDNDY-VPILYSSHNQVQTERSCINMLIQAQVAGVLLSL-IHWDESINSALDEAGIPYVLFDQPhDDYDGA 161
Cdd:PRK09526 81 IAAAIKSRADQLGYsVVISMVERSGVEACQAAVNELLAQRVSGVIINVpLEDADAEKIVADCADVPCLFLDVS-PQSPVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 162 AIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHhmELKEDNIFVSTASKKSGasamkdYQRG 241
Cdd:PRK09526 160 SVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDY--QLQPIAVREGDWSAMSG------YQQT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 242 QELgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLM 321
Cdd:PRK09526 232 LQM----LREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLL 307
|
330 340
....*....|....*....|....
gi 493831315 322 ECLDGvHTWKKRVMLEPVLVERES 345
Cdd:PRK09526 308 ALSQG-QAVKGSQLLPTSLVVRKS 330
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
69-345 |
1.32e-51 |
|
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: 172.45 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSI----TNPFYSQLIAAVQKECMDNDYVPILySSHNQVQTERSCINMLIQA-QVAG-VLLSLIHWDESINSaLD 142
Cdd:cd06292 2 IGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLL-FTASGDEDEIDYYRDLVRSrRVDGfVLASTRHDDPRVRY-LH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 EAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMD-RPSRKKLfEGFQDALTDHHMELKEDNI 221
Cdd:cd06292 80 EAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGsVPSDDRL-AGYRAALEEAGLPFDPGLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 222 FVSTASKKSGASAMkdyqrgQELgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPA 301
Cdd:cd06292 159 VEGENTEEGGYAAA------ARL----LDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 493831315 302 LTTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06292 229 LTTVRQPIDEIGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
10-346 |
1.39e-51 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 174.12 E-value: 1.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 10 IKDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQLIAAVQ 89
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRF-VSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 90 KECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDE-AGIPYVLFDQPHDDYDGAAIDFDFY 168
Cdd:PRK10423 80 RSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRyPSVPTVMMDWAPFDGDSDLIQDNSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 169 SSGRLAAEYLIENGHRELAFASGPMDR-PSRKKLfEGFQDALTDHHMELKEDNIFVSTASKKSGASAMKdyqrgqelgsM 247
Cdd:PRK10423 160 LGGDLATQYLIDKGYTRIACITGPLDKtPARLRL-EGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQ----------Q 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 248 VLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLMECLDGV 327
Cdd:PRK10423 229 LLALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQP 308
|
330
....*....|....*....
gi 493831315 328 HTWKKRVMLEPVLVERESI 346
Cdd:PRK10423 309 TLQQQRLQLTPELMERGSV 327
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
69-341 |
1.42e-51 |
|
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: 172.00 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSIT-----NPFYSQLIAAVQKECMDNDYVpILYSSHNQVQTE-RSCINMLIQAQVAGVLLSLIHWDESINSALD 142
Cdd:cd06294 2 IGLVLPSSAeelfqNPFFSEVLRGISQVANENGYS-LLLATGNTEEELlEEVKRMVRGRRVDGFILLYSKEDDPLIEYLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 EAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIF 222
Cdd:cd06294 81 EEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDYIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 223 VSTASKKSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPAL 302
Cdd:cd06294 161 LLDFSEEDGYDALQEL----------LSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPL 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 493831315 303 TTISQSAYRTGELAAKLLMECLDGvhtwkKRVMLEPVLV 341
Cdd:cd06294 231 TSVDINPYELGREAAKLLINLLEG-----PESLPKNVIV 264
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-326 |
1.12e-50 |
|
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: 169.77 E-value: 1.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSA-LDEAGIP 147
Cdd:cd06282 2 IGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALElLEEEGVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKL-FEGFQDALTDH---HMELKEdnifV 223
Cdd:cd06282 82 YVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRARLrYQGYRDALKEAglkPIPIVE----V 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 224 STASKKSGASAMKDYQRGQElgsmvlerkriPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALT 303
Cdd:cd06282 158 DFPTNGLEEALTSLLSGPNP-----------PTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLA 226
|
250 260
....*....|....*....|...
gi 493831315 304 TISQSAYRTGELAAKLLMECLDG 326
Cdd:cd06282 227 TVVQPSRDMGRAAADLLLAEIEG 249
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
68-345 |
4.32e-50 |
|
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: 168.51 E-value: 4.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLslihwdESINSA------- 140
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLII------EPTKSAlpnpnld 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 141 ----LDEAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELA--FASgpmDRPSRKKLFEGFQDALTDHHM 214
Cdd:cd01541 75 lyeeLQKKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAgiFKS---DDLQGVERYQGFIKALREAGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 215 ELKEDNIF-VSTASKKSgasamkdyQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVE 293
Cdd:cd01541 152 PIDDDRILwYSTEDLED--------RFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSY 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 493831315 294 FGEMIVPALTTISQSAYRTGELAAKLLMECLDGVHTwKKRVMLEPVLVERES 345
Cdd:cd01541 224 LASLSEPPLTSVVHPKEELGRKAAELLLRMIEEGRK-PESVIFPPELIERES 274
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
76-345 |
4.59e-49 |
|
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: 165.77 E-value: 4.59e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 76 ITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTErscinmlIQAQVAGVLL------SLIHWDESINsaldeagiPYV 149
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAigkfskEEIEKLKKLN--------PNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 150 LF-DQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKL-----FEGFQDALTDHHMeLKEDNIFV 223
Cdd:cd01544 79 VFvDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEEiedprLRAFREYMKEKGL-YNEEYIYI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 224 STASKKSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALT 303
Cdd:cd01544 158 GEFSVESGYEAMKEL----------LKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 493831315 304 TISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd01544 228 TVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
69-345 |
9.11e-48 |
|
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: 162.06 E-value: 9.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06299 2 IGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGA-AIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTAS 227
Cdd:cd06299 82 VFVDREVEGLGGVpVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDFR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 228 KKSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQ 307
Cdd:cd06299 162 QDSGAAAAHRL----------LSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQ 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 493831315 308 SAYRTGELAAKLLMECLDGVHTwKKRVMLEPVLVERES 345
Cdd:cd06299 232 PVERIGRRAVELLLALIENGGR-ATSIRVPTELIPRES 268
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-345 |
3.28e-47 |
|
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: 160.78 E-value: 3.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERScINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06278 2 VGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDA-LRQLLQYRVDGVIVTSATLSSELAEECARRGIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFdqpHDDYDGAAIDF---DFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELkeDNIFVST 225
Cdd:cd06278 81 VLF---NRVVEDPGVDSvscDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPP--PAVEAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 226 ASKKSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQL-ETHQIHIPRDMSILGFDNVEFGEMIVPALTT 304
Cdd:cd06278 156 YSYEGGYEAARRL----------LAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAAWPSYDLTT 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493831315 305 ISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06278 226 VRQPIEEMAEAAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
69-345 |
8.45e-47 |
|
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: 159.64 E-value: 8.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDY--VPILYSSHNQVQTERScINMLIQAQVAGVLLS--LIHwDESINSALDEA 144
Cdd:cd01545 2 IGLLYDNPSASYVSALQVGALRACREAGYhlVVEPCDSDDEDLADRL-RRFLSRSRPDGVILTppLSD-DPALLDALDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 145 GIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVS 224
Cdd:cd01545 80 GIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVVQG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 225 TASKKSGASAmkdyqrGQELgsmvLERKRIPDALFTVNDMMAIGIMKqlETHQ--IHIPRDMSILGFDNVEFGEMIVPAL 302
Cdd:cd01545 160 DFTFESGLEA------AEAL----LDLPDRPTAIFASNDEMAAGVLA--AAHRlgLRVPDDLSVAGFDDSPIARLVWPPL 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 493831315 303 TTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd01545 228 TTVRQPIAEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
69-343 |
1.12e-46 |
|
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: 159.25 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLslihwdESINSALDEAgIPY 148
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLII------TSRENDWEVI-EPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 -----VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASG--PMDRPSRKKLFEGFQDALTDHHMELKEDNI 221
Cdd:cd06286 75 akygpIVLCEETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGrpESSSASTQARLKAYQDVLGEHGLSLREEWI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 222 FvstaskkSGASAMKDyqrGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEmiVPA 301
Cdd:cd06286 155 F-------TNCHTIED---GYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISE--LLN 222
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 493831315 302 LTTISQSAYRTGELAAKLLMECLDGVHTwkKRVMLEPVLVER 343
Cdd:cd06286 223 LTTIDQPLEEMGKEAFELLLSQLESKEP--TKKELPSKLIER 262
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
68-335 |
3.58e-46 |
|
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: 157.66 E-value: 3.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIP 147
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDQPHDDYdgAAIDFDFYSSGRLAAEYLIENGHRELAFAS-GPMDRPSRKKLFEGFQDALTDHHMElkEDNIFVSTA 226
Cdd:cd01542 81 VVVLGQEHEGF--SCVYHDDYGAGKLLGEYLLKKGHKNIAYIGvDEEDIAVGVARKQGYLDALKEHGID--EVEIVETDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 227 SKKSGASAMKDyqrgqelgsmVLERKRiPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTIS 306
Cdd:cd01542 157 SMESGYEAAKE----------LLKENK-PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVK 225
|
250 260
....*....|....*....|....*....
gi 493831315 307 QSAYRTGELAAKLLMECLDGVHTWKKRVM 335
Cdd:cd01542 226 FDYEEAGEKAAELLLDMIEGEKVPKKQKL 254
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
69-345 |
1.69e-45 |
|
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: 156.20 E-value: 1.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQvqTERSC---INMLIQAQVAGVLLslIHWDESINSALDE-- 143
Cdd:cd01574 2 IGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDED--DPASVreaLDRLLSQRVDGIIV--IAPDEAVLEALRRlp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 144 AGIPYVLFDQPHDDyDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHhmELKEDNIFV 223
Cdd:cd01574 78 PGLPVVIVGSGPSP-GVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEA--GLPPPPVVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 224 STASKKSGasamkdYQRGQELGsmvleRKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALT 303
Cdd:cd01574 155 GDWSAASG------YRAGRRLL-----DDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLT 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 493831315 304 TISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd01574 224 TVRQDFAELGRRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-345 |
6.87e-45 |
|
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: 154.70 E-value: 6.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHW-DESINSALDEAGIP 147
Cdd:cd06281 2 VGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEdDPELAAALARLDIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDQ-PHDDYDgaAIDFDFYSSGRLAAEYLIENGHRELAFASGPMD-RPSRKKLfEGFQDALTDHHMELKEDNIFVST 225
Cdd:cd06281 82 VVLIDRdLPGDID--SVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDiRPGRERI-AGFKAAFAAAGLPPDPDLVRLGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 226 ASKKSGASAMkdyqrgqelgSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTI 305
Cdd:cd06281 159 FSADSGFREA----------MALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493831315 306 SQSAYRTGELAAKLLMECLDGVHTWK-KRVMLEPVLVERES 345
Cdd:cd06281 229 RWDLDAVGRAAAELLLDRIEGPPAGPpRRIVVPTELILRDS 269
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
45-347 |
2.47e-43 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 152.07 E-value: 2.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 45 DAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVA 124
Cdd:PRK11041 14 QAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLIITKQID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 125 GVLL--SLIHWDESI------------NSALDEAGIPYVlfdqpHDDYDGAAIDfdfyssgrlAAEYLIENGHRELAFAS 190
Cdd:PRK11041 94 GMLLlgSRLPFDASKeeqrnlppmvmaNEFAPELELPTV-----HIDNLTAAFE---------AVNYLHELGHKRIACIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 191 GPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASKKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIM 270
Cdd:PRK11041 160 GPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQ----------LLDLPQPPTAVFCHSDVMALGAL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493831315 271 KQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERESIR 347
Cdd:PRK11041 230 SQAKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGSTA 306
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
68-345 |
1.46e-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: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSI---TNPFYSQLIAAVQKECMDNDYVPILYSShnQVQTERSCI--NMLIQAQVAGV-LLSLIhwDESINSAL 141
Cdd:cd19974 1 NIAVLIPERffgDNSFYGKIYQGIEKELSELGYNLVLEII--SDEDEEELNlpSIISEEKVDGIiILGEI--SKEYLEKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 142 DEAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAF------ASGPMDRpsrkklFEGFQDALTDHHME 215
Cdd:cd19974 77 KELGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFvgdinyTSSFMDR------YLGYRKALLEAGLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 216 LKEDNIFVSTaskksgasamKDYQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFG 295
Cdd:cd19974 151 PEKEEWLLED----------RDDGYGLTEEIELPLKLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 493831315 296 EMIVPALTTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd19974 221 ELSTPPLTTVEVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
69-345 |
1.43e-39 |
|
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: 141.19 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVP-----SITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERScinmLIQAQVAG-VLLSLIHWDESInSALD 142
Cdd:cd06279 2 IGVLLPddlsyAFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAA----VRNAAVDGfIVYGLSDDDPAV-AALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 EAGIPYVLFDQPHDDyDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRP------------------SRKKLfEG 204
Cdd:cd06279 77 RRGLPLVVVDGPAPP-GIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGrergpvsaerlaaatnsvARERL-AG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 205 FQDALTDHHMELKEDNIFVSTASkksgasamkDYQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDM 284
Cdd:cd06279 155 YRDALEEAGLDLDDVPVVEAPGN---------TEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493831315 285 SILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLMECLDGVHTwkKRVMLEPVLVERES 345
Cdd:cd06279 226 SVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPP--RPVILPTELVVRAS 284
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
69-343 |
9.36e-39 |
|
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: 138.45 E-value: 9.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLL--SLIHWDESInsALDEAGI 146
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILqpTGNNNDAYL--ELAQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPS-RKKLFEGFQDALTDHHMELKEdnIFVST 225
Cdd:cd06283 80 PVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGIStRRERLQGFLDALARYNIEGDV--YVIEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 226 ASKKSGASAMKDYqrgqeLGSMVLERKripdALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTI 305
Cdd:cd06283 158 EDTEDLQQALAAF-----LSQHDGGKT----AIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTI 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 493831315 306 SQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVER 343
Cdd:cd06283 229 RQPTYEIGKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
68-345 |
2.42e-38 |
|
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: 137.79 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIP 147
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 148 YVLFDqPHDDYDGA--AIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVST 225
Cdd:cd06296 81 FVLID-PVGEPDPDlpSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 226 ASKKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTI 305
Cdd:cd06296 160 FTYEAGYRAARE----------LLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 493831315 306 SQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06296 230 HQPLREMGAVAVRLLLRLLEGGPPDARRIELATELVVRGS 269
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
79-345 |
1.50e-36 |
|
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: 133.13 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 79 PFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERScINMLIQAQVAGVLLSLIHWDESINSALDEAGIPYVLFDQPHDDY 158
Cdd:cd06277 19 PFFSELIDGIEREARKYGYNLLISSVDIGDDFDEI-LKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 159 DGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASKKSGASAMKDY 238
Cdd:cd06277 98 NFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMKAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 239 QRgqelgsmvlERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAK 318
Cdd:cd06277 178 LD---------TGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVR 248
|
250 260
....*....|....*....|....*..
gi 493831315 319 LLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06277 249 RLIEKIKDPDGGTLKILVSTKLVERGS 275
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
64-345 |
3.50e-36 |
|
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: 131.99 E-value: 3.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 64 GRNRQIGVVVP-------SITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERScinmLIQAQVA-GVLLSLIHWDE 135
Cdd:cd06295 1 QRSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLAR----LLDSGRAdGLIVLGQGLDH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 136 SINSALDEAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFAsGPMDRPSRKKLFEGFQDALTDHHME 215
Cdd:cd06295 77 DALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFL-GDPPHPEVADRLQGYRDALAEAGLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 216 LKEDNIFVSTASKKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFG 295
Cdd:cd06295 156 ADPSLLLSCDFTEESGYAAMRA----------LLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 493831315 296 EMIVPALTTISQSayrtGELAAKLLMECLDGVHTWK--KRVMLEPVLVERES 345
Cdd:cd06295 226 AYFRPPLTTVRQD----LALAGRLLVEKLLALIAGEpvTSSMLPVELVVRES 273
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
69-320 |
5.97e-36 |
|
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: 131.26 E-value: 5.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQL------IAAVQKecmdndYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALD 142
Cdd:cd06298 2 VGVIIPDISNLYYAELargiddIATMYK------YNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 EAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFE-GFQDALTDHHMELKEDNI 221
Cdd:cd06298 76 RSPVPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLqGYKRALEEAGLEFNEPLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 222 FVSTaskksgasamKDYQRGQELGSMVLERKRiPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPA 301
Cdd:cd06298 156 FEGD----------YDYDSGYELYEELLESGE-PDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQ 224
|
250
....*....|....*....
gi 493831315 302 LTTISQSAYRTGELAAKLL 320
Cdd:cd06298 225 LTSINQPLYDIGAVAMRLL 243
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
69-345 |
6.00e-36 |
|
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: 131.43 E-value: 6.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06297 2 ISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIVPTEKPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDgaAIDFDFYSSGRLAAEYLIENGHRELAF----ASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVS 224
Cdd:cd06297 82 VLIDANSMGYD--CVYVDNVKGGFMATEYLAGLGEREYVFfgieEDTVFTETVFREREQGFLEALNKAGRPISSSRMFRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 225 TASKKSGasamkdyqrgQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMivPALTT 304
Cdd:cd06297 160 DNSSKKA----------ECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493831315 305 ISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERES 345
Cdd:cd06297 228 VRQPVEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
69-340 |
7.33e-35 |
|
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: 128.52 E-value: 7.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESInSALDEAG--I 146
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAG-VAEKARGqnV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYVLFDQPHDDYDGA-AIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVST 225
Cdd:cd01537 81 PVVFFDKEPSRYDKAyYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 226 ASKKSGASAMKdyqrgqelgsMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTI 305
Cdd:cd01537 161 WDTASGKDKMD----------QWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 493831315 306 SQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVL 340
Cdd:cd01537 231 LQDANNLGKTTFDLLLNLADNWKIDNKVVRVPYVL 265
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
69-341 |
1.16e-34 |
|
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: 128.05 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPS----ITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLS--LIHwDESINSaLD 142
Cdd:cd20010 2 IGLVLPLdpgdLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILArtRVN-DPRIAY-LL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 EAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIF 222
Cdd:cd20010 80 ERGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 223 vstaskksgaSAMKDYQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFG-EMIVPA 301
Cdd:cd20010 160 ----------EGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPAlEYFSPP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 493831315 302 LTTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLV 341
Cdd:cd20010 230 LTTTRSSLRDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
6-343 |
8.65e-34 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 127.52 E-value: 8.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 6 KKATIKDVAARANTSITTVSRVLSGsdypvKEELKTAIID----AAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFY 81
Cdd:PRK10014 5 KKITIHDVALAAGVSVSTVSLVLSG-----KGRISTATGErvnqAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 82 SQLIAAVQKECMDNDYVPIL-YSSHNQVQTERsCINMLIQAQVAGVLLSLIHWDESINSA-LDEAGIPYVLFDQPH--DD 157
Cdd:PRK10014 80 AELTAGLTEALEAQGRMVFLlQGGKDGEQLAQ-RFSTLLNQGVDGVVIAGAAGSSDDLREmAEEKGIPVVFASRASylDD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 158 YDgaAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASKKSGASAMkd 237
Cdd:PRK10014 159 VD--TVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAI-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 238 yqrgqelgSMVLERKRIPDALFTVNDMMAIGIMKQLET--HQI-------HIPRDMSILGFDNVEFGEMIVPALTTISQS 308
Cdd:PRK10014 235 --------TALLRHNPTISAVVCYNETIAMGAWFGLLRagRQSgesgvdrYFEQQVALAAFTDVPEAELDDPPLTWASTP 306
|
330 340 350
....*....|....*....|....*....|....*
gi 493831315 309 AYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVER 343
Cdd:PRK10014 307 AREIGRTLADRMMQRITHEETHSRNLIIPPRLIAR 341
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
8-347 |
1.89e-32 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 123.71 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 8 ATIKDVAARANTSITTVSRVLSGSDyPVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQLIAA 87
Cdd:PRK10727 2 ATIKDVARLAGVSVATVSRVINNSP-KASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 88 VQKECMDN-DYVPILYSSHNQvQTERSCINMLIQAQVAGVLlslIHW----DESINSALDEagIP-YVLFDQPHDDYDGA 161
Cdd:PRK10727 81 VEQVAYHTgNFLLIGNGYHNE-QKERQAIEQLIRHRCAALV---VHAkmipDAELASLMKQ--IPgMVLINRILPGFENR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 162 AIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASKKSGASAMKDyqrg 241
Cdd:PRK10727 155 CIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTE---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 242 qelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLM 321
Cdd:PRK10727 231 ------LLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELAL 304
|
330 340
....*....|....*....|....*.
gi 493831315 322 ECLDGVHTWKKRVMLEPVLVERESIR 347
Cdd:PRK10727 305 ALADNRPLPEITNVFSPTLVRRHSVS 330
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
177-345 |
2.32e-32 |
|
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: 118.59 E-value: 2.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 177 YLIENGHRELAFASGPMDRPSRK--KLFEGFQDALTDHHMELkedNIFVSTASKKSGASAMKDyqrgqelgsMVLERKRI 254
Cdd:pfam13377 1 HLAELGHRRIALIGPEGDRDDPYsdLRERGFREAARELGLDV---EPTLYAGDDEAEAAAARE---------RLRWLGAL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 255 PDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLLMECLDGVHTWKKRV 334
Cdd:pfam13377 69 PTAVFVANDEVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERV 148
|
170
....*....|.
gi 493831315 335 MLEPVLVERES 345
Cdd:pfam13377 149 LLPPELVERES 159
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
9-350 |
3.17e-31 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 120.65 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 9 TIKDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQLIAAV 88
Cdd:PRK10401 3 TIRDVARQAGVSVATVSRVLNNSAL-VSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 89 -------QKecmdndYVPILYSSHnQVQTERSCINMLI-QAQVAGVLLSLIHWDESINSALDEagIP-YVLFDQPHDDYD 159
Cdd:PRK10401 82 dlvaqqhQK------YVLIGNSYH-EAEKERHAIEVLIrQRCNALIVHSKALSDDELAQFMDQ--IPgMVLINRVVPGYA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 160 GAAIDFDFYSSGRLAAEYLIENGHRELAF--ASGPM-DRPSRKklfEGFQDALTDHHMELKEDNIFVSTASKKSGASAMK 236
Cdd:PRK10401 153 HRCVCLDNVSGARMATRMLLNNGHQRIGYlsSSHGIeDDAMRR---AGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 237 DyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELA 316
Cdd:PRK10401 230 E----------LLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLA 299
|
330 340 350
....*....|....*....|....*....|....
gi 493831315 317 AKLLMECLDGVHTWKKRVMLEPVLVERESIRKTQ 350
Cdd:PRK10401 300 TELALQGAAGNLDPRASHCFMPTLVRRHSVATRQ 333
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
78-341 |
2.09e-28 |
|
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: 110.98 E-value: 2.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 78 NPFYSQLIAAVQKECMDNDY--VPILYSSHNQVQterSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPYVLFDQPH 155
Cdd:cd06271 14 NGTVSE*VSGITEEAGTTGYhlLVWPFEEAES*V---PIRDLVETGSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 156 DDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMD-RPSRKKLfEGFQDALTDHHME---LKEDNIFvstaskksg 231
Cdd:cd06271 91 *PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARySPHDRRL-QGYVRA*RDAGLTgypLDADTTL--------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 232 asamkdyQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEF-GEMIVPALTTISQSAY 310
Cdd:cd06271 161 -------EAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFlGAMITPPLTTVHAPIA 233
|
250 260 270
....*....|....*....|....*....|.
gi 493831315 311 RTGELAAKLLMECLDGVHTWKKRVMLEPVLV 341
Cdd:cd06271 234 EAGRELAKALLARIDGEDPETLQVLVQPSLS 264
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
69-290 |
4.37e-28 |
|
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: 110.37 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPY 148
Cdd:cd06274 2 IGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQAAGLPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 149 VLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVSTASK 228
Cdd:cd06274 82 VFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEGYDR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493831315 229 KSGASAMKDYqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFD 290
Cdd:cd06274 162 ESGYQLMAEL---------LARLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFD 214
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
69-326 |
2.95e-26 |
|
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: 105.08 E-value: 2.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKEC-MDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALDEA--- 144
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAkELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVD-PTALAPVLKKAkda 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 145 GIPYVLFDQPHDDYDGAA-IDFDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNI 221
Cdd:pfam13407 80 GIPVVTFDSDAPSSPRLAyVGFDNEAAGEAAGELLAEalGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 222 FVSTASKKSGAsamkdYQRGQELgsmvLERKRIP-DALFTVNDMMAIGIMKQLEthQIHIPRDMSILGFDN-VEFGEMIV 299
Cdd:pfam13407 160 VEGTNWDPEKA-----QQQMEAL----LTAYPNPlDGIISPNDGMAGGAAQALE--AAGLAGKVVVTGFDAtPEALEAIK 228
|
250 260
....*....|....*....|....*....
gi 493831315 300 PAL--TTISQSAYRTGELAAKLLMECLDG 326
Cdd:pfam13407 229 DGTidATVLQDPYGQGYAAVELAAALLKG 257
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
69-346 |
5.44e-26 |
|
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: 105.39 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDeSINSALD---EAG 145
Cdd:COG1879 36 IGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPD-ALAPALKkakAAG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFDQPHDDYDGAA-IDFDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDALTDHHmELKEDNIF 222
Cdd:COG1879 115 IPVVTVDSDVDGSDRVAyVGSDNYAAGRLAAEYLAKalGGKGKVAILTGSPGAPAANERTDGFKEALKEYP-GIKVVAEQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 223 VSTASKKSGASAMKDY-QRGQELgsmvlerkripDALFTVNDMMAIGIMKQLEthQIHIPRDMSILGFD----NVEF--- 294
Cdd:COG1879 194 YADWDREKALEVMEDLlQAHPDI-----------DGIFAANDGMALGAAQALK--AAGRKGDVKVVGFDgspeALQAikd 260
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 493831315 295 GEMIVpaltTISQSAYRTGELAAKLLMECLDGvHTWKKRVMLEPVLVERESI 346
Cdd:COG1879 261 GTIDA----TVAQDPYLQGYLAVDAALKLLKG-KEVPKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
69-326 |
3.20e-25 |
|
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: 102.64 E-value: 3.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALD---EAG 145
Cdd:cd01536 2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVD-SEALVPAVKkanAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFDQPHDDYDGAA--IDFDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDALTDHHmelkeDNI 221
Cdd:cd01536 81 IPVVAVDTDIDGGGDVVafVGTDNYEAGKLAGEYLAEalGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYP-----DIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 222 FVSTAS----KKSGASAMKDY-QRGQELgsmvlerkripDALFTVNDMMAIGIMKQLEthQIHIPRDMSILGFDNVEFGE 296
Cdd:cd01536 156 IVAEQPanwdRAKALTVTENLlQANPDI-----------DAVFAANDDMALGAAEALK--AAGRTGDIKIVGVDGTPEAL 222
|
250 260 270
....*....|....*....|....*....|...
gi 493831315 297 MIVPA--LT-TISQSAYRTGELAAKLLMECLDG 326
Cdd:cd01536 223 KAIKDgeLDaTVAQDPYLQGYLAVEAAVKLLNG 255
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
4-326 |
4.29e-25 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 103.57 E-value: 4.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 4 KKKKATIKDVAARANTSITTVSRVLSGSDyPVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFYSQ 83
Cdd:PRK14987 2 KKKRPVLQDVADRVGVTKMTVSRFLRNPE-QVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 84 LIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALDEAGIPYV-LFDQPHDDYDgAA 162
Cdd:PRK14987 81 VLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVeLMDSQSPCLD-IA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 163 IDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLfEGFQDALTDhhMELKEDNIFVSTASKksgasamkdYQRGQ 242
Cdd:PRK14987 160 VGFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQ-KGYEQAMLD--AGLVPYSVMVEQSSS---------YSSGI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 243 ELgsMVLERKRIP--DALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYRTGELAAKLL 320
Cdd:PRK14987 228 EL--IRQARREYPqlDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERL 305
|
....*.
gi 493831315 321 MECLDG 326
Cdd:PRK14987 306 LARIRG 311
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
8-78 |
3.07e-23 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 91.49 E-value: 3.07e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493831315 8 ATIKDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPSITN 78
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGR-VSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
134-345 |
6.27e-23 |
|
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: 96.12 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 134 DESINSALDEAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKlFEGFQDALTDHH 213
Cdd:cd01543 60 DPELAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAWSRER-GEGFREALREAG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 214 MELkedNIFvSTASKKSGASAMKDYQR-GQELGSmvLERkriPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNV 292
Cdd:cd01543 139 YEC---HVY-ESPPSGSSRSWEEEREElADWLKS--LPK---PVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDND 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493831315 293 E-FGEMIVPALTTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPV-LVERES 345
Cdd:cd01543 210 ElICELSSPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILIPPLgVVTRQS 264
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
69-344 |
2.91e-20 |
|
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: 88.97 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFY-SQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWD--ESINSALdeAG 145
Cdd:cd06272 2 IGLYWPSVGERVAlTRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVFGISDSdiEYLNKNK--PK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFDQPHDDYdgAAIDFDFYSSGRLAAEYLIENGHRELAFA--SGPMDRPSRKKlfEGFQDALTDHHMELKEDNIFV 223
Cdd:cd06272 80 IPIVLYNRESPKY--STVNVDNEKAGRLAVLLLIQKGHKSIAYIgnPNSNRNQTLRG--KGFIETCEKHGIHLSDSIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 224 STASKKSGASAMKdyqrgqelgsMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALT 303
Cdd:cd06272 156 RGLSIEGGDNAAK----------KLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLT 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493831315 304 TISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERE 344
Cdd:cd06272 226 VVGVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFRE 266
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
8-322 |
1.08e-19 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 88.28 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 8 ATIKDVAARANTSITTVSRVLSgsDYP---VKEELKTAIIDAAEALNYKPNLFGQLLRGGRNRQIGVVVPS------ITN 78
Cdd:PRK10339 2 ATLKDIAIEAGVSLATVSRVLN--DDPtlnVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIYSyqqeleIND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 79 PFYSQLIAAVQKECmdnDYVPI-LYSSHNqvqterSCINMLIQAqVAGVLLsLIHWDESINSALDE--AGIPYVLFDQPH 155
Cdd:PRK10339 80 PYYLAIRHGIETQC---EKLGIeLTNCYE------HSGLPDIKN-VTGILI-VGKPTPALRAAASAltDNICFIDFHEPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 156 DDYDgaAIDFDFYSSGRLAAEYLIENGHRELAFASGpMDRPSRKKLFEgfqDALTDHHmELK----EDNIFVSTASKKSG 231
Cdd:PRK10339 149 SGYD--AVDIDLARISKEIIDFYINQGVNRIGFIGG-EDEPGKADIRE---VAFAEYG-RLKqvvrEEDIWRGGFSSSSG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 232 asamkdYQRGQELgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIVPALTTISQSAYR 311
Cdd:PRK10339 222 ------YELAKQM----LAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEM 291
|
330
....*....|.
gi 493831315 312 TGELAAKLLME 322
Cdd:PRK10339 292 MGSQGVNLLYE 302
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
69-346 |
4.79e-18 |
|
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: 82.79 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALD---EAG 145
Cdd:cd06319 2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTN-SSAAPTVLDlanEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFD--QPHDDYDgAAIDFDFYSSGRLAAEYLIEN------GHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELK 217
Cdd:cd06319 81 IPVVIADigTGGGDYV-SYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 218 eDNIFVSTASKKSGASAMKDyqrgqelgsMVLERKRIpDALFTVNDMMAIGIMKQLETHQihipRDMSIL--GFD-NVEF 294
Cdd:cd06319 160 -ALRQTPNSTVEETYSAAQD---------LLAANPDI-KGIFAQNDQMAQGALQAIEEAG----RTGDILvvGFDgDPEA 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 493831315 295 GEMIVPA--LTTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLVERESI 346
Cdd:cd06319 225 LDLIKDGklDGTVAQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV 278
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
9-291 |
2.00e-17 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 81.85 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 9 TIKDVAARANTSITTVSRVLSG--SDYPVKEelKT-----AIIdaaEALNYKPNLFGQLLRGGRNRQIGVVVPSITNPFY 81
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINGkaKQYRVSD--KTvekvmAVV---REHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 82 SQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSlihwdesinSAL----------DEAGIPYVLF 151
Cdd:PRK11303 77 ARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVS---------TSLppehpfyqrlQNDGLPIIAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 152 DQP-HDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLfEGFQDALTDHHMELkeDNIFVSTASKKS 230
Cdd:PRK11303 148 DRAlDREHFTSVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFERE-QGFRQALKDDPREV--HYLYANSFEREA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493831315 231 GASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGF-DN 291
Cdd:PRK11303 225 GAQLFEKW----------LETHPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFgDN 276
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
141-326 |
1.99e-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: 77.96 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 141 LDEAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELK-ED 219
Cdd:cd20009 76 LLERGFPFVTHGRTELSTPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEpLL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 220 NIFVSTASkksgasamkdyQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFDNVEFGEMIV 299
Cdd:cd20009 156 IVTLDSSA-----------EAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFR 224
|
170 180
....*....|....*....|....*..
gi 493831315 300 PALTTISQSAYRTGELAAKLLMECLDG 326
Cdd:cd20009 225 PPIDTLYEDIEEAGRFLAEALLRRIEG 251
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
69-290 |
2.21e-16 |
|
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: 78.03 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALDEA---G 145
Cdd:cd06309 2 VGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPID-ATGWDPVLKEAkdaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFDQPHDDYDG----AAIDFDFYSSGRLAAEYLIEN---GHRELAFASGPMDRPSRKKLFEGFQDALTDHHmelke 218
Cdd:cd06309 81 IPVILVDRTIDGEDGslyvTFIGSDFVEEGRRAAEWLVKNykgGKGNVVELQGTAGSSVAIDRSKGFREVIKKHP----- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493831315 219 DNIFVSTaskKSGasamkDYQR--GQELGSMVL--ERKRIpDALFTVNDMMAIGIMKQLETHQIHIPRDMSILGFD 290
Cdd:cd06309 156 NIKIVAS---QSG-----NFTRekGQKVMENLLqaGPGDI-DVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGID 222
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
11-63 |
4.11e-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: 68.59 E-value: 4.11e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 493831315 11 KDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPNLFGQLLRG 63
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPR-VSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
69-326 |
1.76e-13 |
|
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: 69.54 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINS--ALDEAGI 146
Cdd:cd19971 2 FGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPAleAAKEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYVLFDQPHDDYDGAA--IDFDFYSSGRLAAEYLIE---NGHR----ELAFASGPMDRpsrkklFEGFQDALTDHhmelK 217
Cdd:cd19971 82 PVINVDTPVKDTDLVDstIASDNYNAGKLCGEDMVKklpEGAKiavlDHPTAESCVDR------IDGFLDAIKKN----P 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 218 EDNIFVSTASKKSGASAMKDYQRgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHqiHIPRDMSILGFDN------ 291
Cdd:cd19971 152 KFEVVAQQDGKGQLEVAMPIMED-------ILQAHPDLDAVFALNDPSALGALAALKAA--GKLGDILVYGVDGspdaka 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 493831315 292 -VEFGEMIvpalTTISQSAYRTGELAAKLLMECLDG 326
Cdd:cd19971 223 aIKDGKMT----ATAAQSPIEIGKKAVETAYKILNG 254
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
69-341 |
2.28e-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: 69.23 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALD---EAG 145
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVD-SGGIVPAIEaanEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFDQPHD--DYDgAAIDFDFYSSGRLAAEYLIE---NGHRELAFASGPMDRPSRKKLfEGFQDALTDHhmelkeDN 220
Cdd:cd06322 81 IPVFTVDVKADgaKVV-THVGTDNYAGGKLAGEYALKallGGGGKIAIIDYPEVESVVLRV-NGFKEAIKKY------PN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 221 I-FVSTASKKSGASamKDYQRGQELgsmvLERKRIPDALFTVNDMMAIGIMKQLEthQIHIPRDMSILGFD-------NV 292
Cdd:cd06322 153 IeIVAEQPGDGRRE--EALAATEDM----LQANPDLDGIFAIGDPAALGALTAIE--SAGKEDKIKVIGFDgnpeaikAI 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 493831315 293 EFGEMIVpalTTISQSAYRTGELAAKLLMECLDGvHTWKKRVMLEPVLV 341
Cdd:cd06322 225 AKGGKIK---ADIAQQPDKIGQETVEAIVKYLAG-ETVEKEILIPPKLY 269
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
69-350 |
2.64e-13 |
|
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: 69.46 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLL--SLIHWDeSINSALDEAGI 146
Cdd:pfam00532 4 LGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIIttPAPSGD-DITAKAEGYGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYVLFDQPHDDYDGA-AIDFDFYSSGRLAAEYLIENGH-RELAFASGPMDRPSRKKLFEGFQDALTDHHMELKEDNIFVS 224
Cdd:pfam00532 83 PVIAADDAFDNPDGVpCVMPDDTQAGYESTQYLIAEGHkRPIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVATG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 225 TASKKSGASAMkdyqrgQELgsmvLERKRIPDALFTVNDMMAIGIMKQLE---------THQIHIPRDMSILGFDNVEFG 295
Cdd:pfam00532 163 DNDIPDAALAA------NAM----LVSHPTIDAIVAMNDEAAMGAVRALLkqgrvkipdIVGIGINSVVGFDGLSKAQDT 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 493831315 296 EMIVPALTTISQSAYRTGELAAKLLMecldgvhtwkkrvmlEPVLVERESIRKTQ 350
Cdd:pfam00532 233 GLYLSPLTVIQLPRQLLGIKASDMVY---------------QWIPKFREHPRVLL 272
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
69-298 |
2.26e-12 |
|
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.
Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 66.42 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSS-HNQVQTERSCINMLIQAQVAGVLLSLIHWDeSINSALDEA--- 144
Cdd:cd06308 2 IGFSQCSLNDPWRAAMNEEIKAEAAKYPNVELIVTDaQGDAAKQIADIEDLIAQGVDLLIVSPNEAD-ALTPVVKKAyda 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 145 GIPYVLFDQ--PHDDYDgAAIDFDFYSSGRLAAEYLIE--NGH------RELAFASGPMDRPsrkklfEGFQDALTdhhm 214
Cdd:cd06308 81 GIPVIVLDRkvSGDDYT-AFIGADNVEIGRQAGEYIAEllNGKgnvveiQGLPGSSPAIDRH------KGFLEAIA---- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 215 elKEDNIFVstaskksGASAMKDYQRGQELGSM--VLERKRIPDALFTVNDMMAIGIMKQLETHQIHipRDMSILGFD-- 290
Cdd:cd06308 150 --KYPGIKI-------VASQDGDWLRDKAIKVMedLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVDgl 218
|
....*...
gi 493831315 291 NVEFGEMI 298
Cdd:cd06308 219 PEAGEKAV 226
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
68-341 |
3.45e-12 |
|
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: 65.77 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQ---KECMDNDYVpILYSSHNQVQTERSCINMLIQAQVAGVLLSL-----IHwdESINS 139
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEeaaAEINPGAKV-TVVDARYDLAKQFSQIDDFIAQGVDLILLNAadsagIE--PAIKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 140 ALDeAGIPYVLFDQPHDDYDgAAIDFDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLfEGFQDALtdhhmeLK 217
Cdd:cd06321 78 AKD-AGIIVVAVDVAAEGAD-ATVTTDNVQAGYLACEYLVEqlGGKGKVAIIDGPPVSAVIDRV-NGCKEAL------AE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 218 EDNIFVST-----ASKKSGASAMKDYqrgqelgsmvLERKRIPDALFTVNDMMAIGIMKQLETHQihiPRDMSILGFDNv 292
Cdd:cd06321 149 YPGIKLVDdqngkGSRAGGLSVMTRM----------LTAHPDVDGVFAINDPGAIGALLAAQQAG---RDDIVITSVDG- 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 493831315 293 efGEMIVPALT--------TISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPVLV 341
Cdd:cd06321 215 --SPEAVAALKregspfiaTAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLV 269
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
9-55 |
6.20e-12 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 59.57 E-value: 6.20e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 493831315 9 TIKDVAARANTSITTVSRVLSGSDYpVKEELKTAIIDAAEALNYKPN 55
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGR-VSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
69-307 |
8.15e-12 |
|
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: 64.62 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINS--ALDEAGI 146
Cdd:cd06323 2 IGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAveEANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYVLFDQPHDDYDGAA-IDFDFYSSGRLAAEYLIENGHRE--------LAFASGPMDRPsrkklfEGFQDALTDHHmelk 217
Cdd:cd06323 82 PVITVDRSVTGGKVVShIASDNVAGGEMAAEYIAKKLGGKgkvvelqgIPGTSAARERG------KGFHNAIAKYP---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 218 edNIFVStaskksgASAMKDYQRGQELGSM--VLERKRIPDALFTVNDMMAIGIMKQLETHQihiPRDMSILGFDN---- 291
Cdd:cd06323 152 --KINVV-------ASQTADFDRTKGLNVMenLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGtpda 219
|
250
....*....|....*....
gi 493831315 292 ---VEFGEMivpaLTTISQ 307
Cdd:cd06323 220 vkaVKDGKL----AATVAQ 234
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
69-274 |
4.25e-10 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 59.69 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITN------PFYSQliaAVQKECMDNDYVPILYSSHNQvqtERSCINMLIqAQVAGVLLSLIHWDESINSALD 142
Cdd:cd06311 2 IGISIPSADHgwtagvAYYAE---KQAKELADLEYKLVTSSNANE---QVSQLEDLI-AQKVDAIVILPQDSEELTVAAQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 ---EAGIPYVLFDQPHDDYDGAA-IDFDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDAltdhhMEL 216
Cdd:cd06311 75 kakDAGIPVVNFDRGLNVLIYDLyVAGDNPGMGVVSAEYIGKklGGKGNVVVLEVPSSGSVNEERVAGFKEV-----IKG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493831315 217 KEDNIFV-STASKKSGASAMKDYQrgqelgSMVLERKRIpDALFTVNDMMAIGIMKQLE 274
Cdd:cd06311 150 NPGIKILaMQAGDWTREDGLKVAQ------DILTKNKKI-DAVWAADDDMAIGVLQAIK 201
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
69-339 |
1.26e-09 |
|
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: 58.10 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINS--ALDEAGI 146
Cdd:cd19967 2 VAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAvkKAKDAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYVLFDQ--PHDDYDGAAIDFDFYSSGRLAAEYLIENGHRELAFAS--GPMDRPSRKKLFEGFQDALtDHHMELKednif 222
Cdd:cd19967 82 PVFLIDReiNAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVEllGKESDTNAQLRSQGFHSVI-DQYPELK----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 223 vSTASKksgaSAMKDYQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQihIPRDMSILGFDN-------VEFG 295
Cdd:cd19967 156 -MVAQQ----SADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAG--RAGDVIIVGFDGsndvrdaIKEG 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 493831315 296 EMIVpaltTISQSAYRTGELAAKLLMECLDGVHTWKKRVMLEPV 339
Cdd:cd19967 229 KISA----TVLQPAKLIARLAVEQADQYLKGGSTGKEEKQLFDC 268
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
69-328 |
3.05e-09 |
|
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: 57.28 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPS---ITNPFYSQLIAAVQKECMDN----DYVPIlySSHNQVQTERSciNMLIQAQVAGVLLSLIHWDE-SINSA 140
Cdd:cd01391 2 IGVVTSSlhqIREQFGIQRVEAIFHTADKLgasvEIRDS--CWHGSVALEQS--IEFIRDNIAGVIGPGSSSVAiVIQNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 141 LDEAGIPYVLFDQPHDDYDGAA-------IDFDFYSSGRLAAEYLIENGHRELAFASGPMDRPSRKKLfEGFQDALTdhh 213
Cdd:cd01391 78 AQLFDIPQLALDATSQDLSDKTlykyflsVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGELRM-AGFKELAK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 214 melKEDNIFVstASKKSGASAMkdyQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKqlETHQIHIPRDMSILGFDN-- 291
Cdd:cd01391 154 ---QEGICIV--ASDKADWNAG---EKGFDRALRKLREGLKARVIVCANDMTARGVLS--AMRRLGLVGDVSVIGSDGwa 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493831315 292 ----VEFGEMIVPaLTTISQSAYRTGELAAKLLMECLDGVH 328
Cdd:cd01391 224 drdeVGYEVEANG-LTTIKQQKMGFGITAIKAMADGSQNMH 263
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
69-326 |
4.25e-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: 380533 [Multi-domain] Cd Length: 272 Bit Score: 56.58 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDY-VPILYS-SHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINSALD--EA 144
Cdd:cd06310 2 IGVVLKGTTSAFWRTVREGAEAAAKDLGVkIIFVGPeSEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDakDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 145 GIPYVLFDQphDDYDGAAIDF---DFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDALTDHHMELKed 219
Cdd:cd06310 82 GIPVIVIDS--GIKGDAYLSYiatDNYAAGRLAAQKLAEalGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIK-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 220 niFVstaskksgASAMKDYQRGQELGSMVLERKRIPDA--LFTVNDMMAIGIMKQLetHQIHIPRDMSILGFD------- 290
Cdd:cd06310 158 --VL--------ASQYAGSDYAKAANETEDLLGKYPDIdgIFATNEITALGAAVAI--KSRKLSGQIKIVGFDsqeelld 225
|
250 260 270
....*....|....*....|....*....|....*.
gi 493831315 291 NVEFGemIVPALttISQSAYRTGELAAKLLMECLDG 326
Cdd:cd06310 226 ALKNG--KIDAL--VVQNPYEIGYEGIKLALKLLKG 257
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
68-322 |
6.27e-09 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 56.05 E-value: 6.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDY-----VPILYSSHNQVQTerscINMLIQAQVAGVLLSLI---HWDESINS 139
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVnvefvGPQKSDAAEQVQL----IEDLIARGVDGIAISPNdpeAVTPVINK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 140 ALDeAGIPYVLFDQPHDD-----YDGAaidfDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDALTDH 212
Cdd:cd06314 77 AAD-KGIPVITFDSDAPDskrlaYIGT----DNYEAGREAGELMKKalPGGGKVAIITGGLGADNLNERIQGFKDALKGS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 213 -HMEL---KEDNIFVSTASKKSgASAMKDYqrgqelgsmvlerkriPD--ALFTVNDMMAIGIMKQLEthQIHIPRDMSI 286
Cdd:cd06314 152 pGIEIvdpLSDNDDIAKAVQNV-EDILKAN----------------PDldAIFGVGAYNGPAIAAALK--DAGKVGKVKI 212
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 493831315 287 LGFDNVEfgeMIVPAL------TTISQSAYRTGELAAKLLME 322
Cdd:cd06314 213 VGFDTLP---ETLQGIkdgviaATVGQRPYEMGYLSVKLLYK 251
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
69-342 |
6.20e-08 |
|
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: 53.07 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSL---IHWDESINSALDeAG 145
Cdd:cd06305 2 IAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHgdaDALDPKLKKALD-AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIE--NGHRELAFASG----PMDRpsRKKLFEGFQDALTDHHMELKE- 218
Cdd:cd06305 81 IPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKdlNGEGNIAVFNVfgvpPLDK--RYDIYKAVLKANPGIKKIVAEl 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 219 ----DNIFVSTASKksGASAMKDYQRGQelgsmvlerkriPDALFTVNDMMAIGIMKQL-ETHQIHIPrdmsILGFD-NV 292
Cdd:cd06305 159 gdvtPNTAADAQTQ--VEALLKKYPEGG------------IDAIWAAWDEPAKGAVQALeEAGRTDIK----VYGVDiSN 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 493831315 293 EFGEMIV----PALTTISQSAYRTGELAAKLLMECLDGVHTwKKRVMLEPVLVE 342
Cdd:cd06305 221 QDLELMAdegsPWVATAAQDPALIGTVAVRNVARKLAGEDL-PDKYSLVPVLIT 273
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
69-278 |
2.03e-07 |
|
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380649 [Multi-domain] Cd Length: 304 Bit Score: 51.86 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALDEA---G 145
Cdd:cd19994 2 IGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVD-GSALGDVLEEAkdaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 146 IPYVLFDQ-----PHDDYdgaAIDFDFYSSGRLAAEYLIE--NGHRE-----LAFASGPMDRPSRKKLFEGFQDALTdhh 213
Cdd:cd19994 81 IPVIAYDRlimntDAVDY---YVTFDNEKVGELQGQYLVDklGLKDGkgpfnIELFAGSPDDNNAQLFFKGAMEVLQ--- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493831315 214 mELKEDNIFVStaskKSGASAMKD-----------YQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQI 278
Cdd:cd19994 155 -PYIDDGTLVV----RSGQTTFEQvatpdwdtetaQARMETLLSAYYTGGKKLDAVLSPNDGIARGVIEALKAAGY 225
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
68-334 |
6.73e-07 |
|
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: 49.92 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTER--SCINMLIQAQVAGVLLSLIhwDESINSALDEA- 144
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATEADIAGqvNLVENAISRKPDAIVLAPN--DTAALVPAVEAa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 145 --GIPYVLFDQP--HDDYDgAAIDFDFYSSGRLAAEYLIE------NGHRELA---FASGP---MDRpsrkklFEGFQDA 208
Cdd:cd20008 79 daGIPVVLVDSGanTDDYD-AFLATDNVAAGALAADELAEllkasgGGKGKVAiisFQAGSqtlVDR------EEGFRDY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 209 LTDHHMELKEDNIFVSTASKKSGASAMKDyqrgqelgsmVLERKRIPDALFTVNDMMAIGIMKQLETHQihipRDMSIL- 287
Cdd:cd20008 152 IKEKYPDIEIVDVQYSDGDIAKALNQTTD----------LLTANPDLVGIFGANNPSAVGVAQALAEAG----KAGKIVl 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 493831315 288 -GFDnveFGEMIVPAL------TTISQSAYRTGELAAKLLMECLDGVHTWKKRV 334
Cdd:cd20008 218 vGFD---SSPDEVALLksgvikALVVQDPYQMGYEGVKTAVKALKGEEIVEKNV 268
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
68-343 |
1.45e-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: 380659 [Multi-domain] Cd Length: 273 Bit Score: 49.15 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKeCMDNDYVPILY---SSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINS--ALD 142
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEK-AAQELGVEIYWrgpSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPveRAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 EAGIPYVLFDQPHDDYD-GAAIDFDFYSSGRLAAEYLIE--NGHRELA---FASG---PMDRPsrkklfEGFQDALTDHH 213
Cdd:cd20004 80 AQGIPVVIIDSDLGGDAvISFVATDNYAAGRLAAKRMAKllNGKGKVAllrLAKGsasTTDRE------RGFLEALKKLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 214 MELK-EDNIFVSTASKKSGASAMKDYQRGQELgsmvlerkripDALFTVNDMMAIGI---MKQ--LETHQIHIprdmsil 287
Cdd:cd20004 154 PGLKvVDDQYAGGTVGEARSSAENLLNQYPDV-----------DGIFTPNESTTIGAlraLRRlgLAGKVKFI------- 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493831315 288 GFDnveFGEMIVPALT--TIS----QSAYRTGELAAKLLMECLDGvHTWKKRVMLEPVLVER 343
Cdd:cd20004 216 GFD---ASDLLLDALRagEISalvvQDPYRMGYLGVKTAVAALRG-KPVPKRIDTGVVLVTK 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
68-328 |
1.84e-06 |
|
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: 48.79 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIA-AVQKECMDNDYVPILysshNQVQTERScinmlIQAQVAGVllslihwDESINSALD---- 142
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKgARKHAKEANGYELLV----KGIKQETD-----IEQQIAIV-------ENLIAQKVDaivi 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 143 ----------------EAGIPYVLFDQPHDD--YDGAAIDFDFYSS-----GRLAAEYLIEN--GHRELAFASGP---MD 194
Cdd:cd19970 65 apadskalvpvlkkavDAGIAVINIDNRLDAdaLKEGGINVPFVGPdnrqgAYLAGDYLAKKlgKGGKVAIIEGIpgaDN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 195 RPSRKKlfeGFQDALTDHHMELkednifvsTASKksgaSAMKDYQRGQELGSMVLERKRIPDALFTVNDMMAIGIMKQLE 274
Cdd:cd19970 145 AQQRKA---GFLKAFEEAGMKI--------VASQ----SANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVD 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 275 THQihIPRDMSILGFDNVefgEMIVPALT------TISQSAYRTGELAAKLLMECLDGVH 328
Cdd:cd19970 210 AAG--KAGKVLVVGFDNI---PAVRPLLKdgkmlaTIDQHPAKQAVYGIEYALKMLNGEE 264
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
69-346 |
2.99e-06 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 48.04 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESIN--SALDEAGI 146
Cdd:cd06313 2 IGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPavEKAKEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 147 PYV-----LFDQPHDDYDGAaidfDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDALTDH-HMELKE 218
Cdd:cd06313 82 PLVgvnalIENEDLTAYVGS----DDVVAGELEGQAVADrlGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKVLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 219 DNifvsTA--SKKSGASAMKDY-QR-GQELgsmvlerkripDALFTVNDMMAIGIMKQLETHQIhipRDMSILGFD---- 290
Cdd:cd06313 158 EQ----TAnwSRDEAMSLMENWlQAyGDEI-----------DGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDgied 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 493831315 291 ---NVEFGEMIVpaltTISQSAYRTGELAAKLLMECLDGVhTWKKRVMLEPVLVERESI 346
Cdd:cd06313 220 alqAVKSGELIA----TVLQDAEAQGKGAVEVAVDAVKGE-GVEKKYYIPFVLVTKDNV 273
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
102-209 |
3.54e-06 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 47.72 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 102 YSSHNQVQTerscINMLIQAQVAGVLLSLIHWD---ESINSALDeAGIPYVLFDQphDDYDGAAIDF---DFYSSGRLAA 175
Cdd:cd19969 40 ADVNEQITA----IEQAIAKNPDGIAVSAIDPEaltPTINKAVD-AGIPVVTFDS--DAPESKRISYvgtDNYEAGYAAA 112
|
90 100 110
....*....|....*....|....*....|....*.
gi 493831315 176 EYLIE--NGHRELAFASGPmDRPSRKKLFEGFQDAL 209
Cdd:cd19969 113 EKLAEllGGKGKVAVLTGP-GQPNHEERVEGFKEAF 147
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
68-216 |
3.48e-05 |
|
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.
Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 44.88 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYS--SHNQVQTERSCINMLIQAQVAGVLLSLIHWDeSINSALDEA- 144
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEagGYTNLSKQISQLEDCVASGADAILLGAISFD-GLDPKVAEAa 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493831315 145 --GIPYV-LFDQPHDDYDGAAIDFDFYSSGRLAAEYLIENGHR---ELAFASGPMDRPSRKKLFEGFQDALTDHHMEL 216
Cdd:cd06306 80 aaGIPVIdLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHPGkpvKVAWFPGPAGAGWAEDREKGFKEALAGSNVEI 157
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
69-181 |
6.44e-05 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 44.15 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQ---KECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHwDESINSALDEA- 144
Cdd:cd19996 2 IGFSNAGLGNSWRVQMIAEFEaeaAKLKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNS-PTALLPAIEKAa 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 493831315 145 --GIPYVLFDQP--HDDYdGAAIDFDFYSSGRLAAEYLIEN 181
Cdd:cd19996 81 aaGIPVVLFDSGvgSDKY-TAFVGVDDAAFGRVGAEWLVKQ 120
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
69-329 |
7.56e-05 |
|
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.
Pssm-ID: 380524 [Multi-domain] Cd Length: 272 Bit Score: 43.76 E-value: 7.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSS-HNQVQTERSCINMLIQAQVAGVLLSLIHWDES---INSALDeA 144
Cdd:cd06301 3 IGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDaQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASapaVDAAAD-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 145 GIPYVLFDQ-PHDDYDGAA-IDFDFYSSGRLAAEYLIE--NGHRELAFASGPMDRPSRKKLFEGFQDALTDH-HMELked 219
Cdd:cd06301 82 GIPLVYVNRePDSKPKGVAfVGSDDIESGELQMEYLAKllGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpGMKI--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 220 nIFVSTAskksgasamkDYQR--GQELGSMVLERKRIPDALFTVNDMMAIGIMKQLETHQIHipRDMSILGFDnvefgeM 297
Cdd:cd06301 159 -VAEQTA----------NWSRekAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKK--DDILVAGID------A 219
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 493831315 298 IVPALT---------TISQSAYRTGELAAKLLMECLDGVHT 329
Cdd:cd06301 220 TPDALKamkagrldaTVFQDAAGQGETAVDVAVKAAKGEEV 260
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
69-317 |
1.05e-04 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 43.54 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIqaqVAGVLLSLIHWDES--INSAL---DE 143
Cdd:PRK10653 29 IALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGTKILLINPTDSdaVGNAVkmaNQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 144 AGIPYVLFDQphddydGAA-------IDFDFYSSGRLAAEYLIE---NGHR-----ELAFASGPMDRPsrkklfEGFQDA 208
Cdd:PRK10653 106 ANIPVITLDR------GATkgevvshIASDNVAGGKMAGDFIAKklgEGAKviqleGIAGTSAARERG------EGFKQA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 209 LTDHHMELKednifvstaskksgASAMKDYQRGQELGSM--VLERKRIPDALFTVNDMMAIGIMKQLETHQihiPRDMSI 286
Cdd:PRK10653 174 VAAHKFNVL--------------ASQPADFDRTKGLNVMqnLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMV 236
|
250 260 270
....*....|....*....|....*....|.
gi 493831315 287 LGFDNVEFGEmivpalttisqSAYRTGELAA 317
Cdd:PRK10653 237 VGFDGTPDGI-----------KAVNRGKLAA 256
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
69-180 |
9.90e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 40.26 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERS-CINMLiqAQVAGVLLSLIHWDESINSALDEA--- 144
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASqVENLL--AQGIDVLIIAPVDAGAAANIVDKAkaa 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 493831315 145 GIPYVLFDQ--PHDDYDgAAIDFDFYSSGRLAAEYLIE 180
Cdd:cd19992 80 GVPVISYDRliLNADVD-LYVGRDNYKVGQLQAEYALE 116
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
69-213 |
1.10e-03 |
|
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: 40.24 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPI-----LYSSHNQVQTERSCINMLiqAQVAGVLLSLIHwDESINSALDE 143
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVrlrihFVDSLDPEALAAALRRLA--AGCDGVALVAPD-HPLVRAAIDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 144 ---AGIPYVLF--DQPHDD---YDGAaidfDFYSSGRLAAE----YLIENGHRELAFASGPMDRPSRKKLfEGFQDALTD 211
Cdd:cd06307 79 laaRGIPVVTLvsDLPGSRrlaYVGI----DNRAAGRTAAWlmgrFLGRRPGKVLVILGSHRFRGHEERE-AGFRSVLRE 153
|
..
gi 493831315 212 HH 213
Cdd:cd06307 154 RF 155
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
68-299 |
2.07e-03 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380547 [Multi-domain] Cd Length: 317 Bit Score: 39.51 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 68 QIGVVVPSI-TNPFYSQLIAAVQKECMD-NDYVPILYSSHNQVQTERSCINMLIQA------------QVAGVLLSLihw 133
Cdd:cd06324 1 RVVFINPGKeDEPFWQNVTRFMQAAAKDlGIELEVLYANRNRFKMLELAEELLARPpkpdylilvnekGVAPELLEL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 134 desinsaLDEAGIPYVLFD------------QPHDDYDG--AAIDFDFYSSGRLAAEYLIENGHRE--------LAFaSG 191
Cdd:cd06324 78 -------AEQAKIPVFLINndltdeerallgKPREKFKYwlGSIVPDNEQAGYLLAKALIKAARKKsddgkirvLAI-SG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 192 PMDRPS---RKKlfeGFQDALTDHHmELKEDNIFVSTASKKSGASAMKD-YQRGQELgsmvlerkripDALFTVNDMMAI 267
Cdd:cd06324 150 DKSTPAsilREQ---GLRDALAEHP-DVTLLQIVYANWSEDEAYQKTEKlLQRYPDI-----------DIVWAANDAMAL 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 493831315 268 GIMKQLETHQIHIPRDMSILGFD-------NVEFGEMIV 299
Cdd:cd06324 215 GAIDALEEAGLKPGKDVLVGGIDwspealqAVKDGELTA 253
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
69-180 |
2.09e-03 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 39.60 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQ-------KECMDNDYvpILYSSHNQVQTERSCINMLIQAQVAGVLLslihwD----ESI 137
Cdd:cd19999 2 IGVSNGYVGNEWRAQMIADFEevaaeykEEGVISDL--IVQNADADATGQISQIRNMINEGVDAILI-----DpvsaTAL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 493831315 138 NSALDEA---GIPYVLFDQPHDDYDGAAIDFDFYSSGRLAAEYLIE 180
Cdd:cd19999 75 NPVIEKAqaaGILVVSFDQPVSSPDAINVVIDQYKWAAIQAQWLAE 120
|
|
| PBP1_ABC_sugar_binding-like |
cd19998 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
103-180 |
7.00e-03 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380653 [Multi-domain] Cd Length: 302 Bit Score: 37.65 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 103 SSHNQVQTERSCINMLIQAQVAGVLLslihwDESINSALD-------EAGIPYVLFDQPHDDYDGAAIDFDFYSSGRLAA 175
Cdd:cd19998 40 SSGTDVQAQISAIDNMIAAGYDAILI-----YAISPTALNpvikracDAGIVVVAFDNVVDEPCAYNVNTDQAKAGEQTA 114
|
....*
gi 493831315 176 EYLIE 180
Cdd:cd19998 115 QWLVD 119
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
115-326 |
9.07e-03 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 37.22 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 115 INMLIQA---QVAGVLLSLIHWDESINsALDEA---GIPYVLFD-QPHDDYDGAAIDFDFYSSGRLAAEYLIEN------ 181
Cdd:cd20005 47 IEMLDNAiakKPDAIALAALDTNALLP-QLEKAkekGIPVVTFDsGVPSDLPLATVATDNYAAGALAADHLAELiggkgk 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 182 ----GHRELAFASgpMDRPsrkklfEGFQDALTDHHMELKEDNIFVSTASKKSGASAMKDyqrgqelgsMVLERKRIpDA 257
Cdd:cd20005 126 vaivAHDATSETG--IDRR------DGFKDEIKEKYPDIKVVNVQYGVGDHAKAADIAKA---------ILQANPDL-KG 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493831315 258 LFTVNDMMAIGIMKQLEthQIHIPRDMSILGFD-------NVEFGEMivpaLTTISQSAYRTGELAAKLLMECLDG 326
Cdd:cd20005 188 IYATNEGAAIGVANALK--EMGKLGKIKVVGFDsgeaqidAIKNGVI----AGSVTQNPYGMGYKTVKAAVKALKG 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
69-211 |
9.40e-03 |
|
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: 37.36 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493831315 69 IGVVVPSITNPFYSQLIAAVQKECMDNDYVPILYSSHNQVQTERSCINMLIQAQVAGVLLSLIHWDESINS--ALDEAGI 146
Cdd:cd06317 2 IALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAikRASEAGI 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493831315 147 PYVLFDQPHD-DYDGAAIDFDFY----SSGRLAAEYLIENGHRE-----LAFASGPMDRPSRKklfeGFQDALTD 211
Cdd:cd06317 82 PVIAYDAVIPsDFQAAQVGVDNLeggkEIGKYAADYIKAELGGQakigvVGALSSLIQNQRQK----GFEEALKA 152
|
|
| |
