|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
8-342 |
2.42e-126 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 365.29 E-value: 2.42e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 8 RKRVTLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFT 87
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 88 MGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTsEADLQRYANSSTPLLITMRPLDwqQLPVDY 167
Cdd:COG1609 81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLD-DARLERLAEAGIPVVLIDRPLP--DPGVPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 168 VGVDSHAGVREATEYLIQQGHRDIVFIGGLTH----HMRYQGYLEAMNHHGLQPwsTDAFSLRAEPTQANGYQLMQQLLD 243
Cdd:COG1609 158 VGVDNRAGARLATEHLIELGHRRIAFIGGPADsssaRERLAGYREALAEAGLPP--DPELVVEGDFSAESGYEAARRLLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 244 MPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIAQPDAP 323
Cdd:COG1609 236 RGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAP 315
|
330
....*....|....*....
gi 447052526 324 LSHYIYRPTLQIRASTGKR 342
Cdd:COG1609 316 PERVLLPPELVVRESTAPA 334
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
70-337 |
6.47e-99 |
|
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: 293.32 E-value: 6.47e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSST 149
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPWSTDafSL 225
Cdd:cd06289 81 PVVLALRDVP--GSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSStrreRLAGFRAALAEAGLPLDESL--IV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLAL 305
Cdd:cd06289 157 PGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREI 236
|
250 260 270
....*....|....*....|....*....|..
gi 447052526 306 GKQAAQQILRRIAQPDAPLSHYIYRPTLQIRA 337
Cdd:cd06289 237 GRRAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
70-333 |
1.69e-84 |
|
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: 256.29 E-value: 1.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEaDLQRYANSST 149
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDE-LLEELLAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPwsTDAFSL 225
Cdd:cd06267 80 PVVLIDRRLD--GLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLStsreRLEGYRDALAEAGLPV--DPELVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLAL 305
Cdd:cd06267 156 EGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEM 235
|
250 260
....*....|....*....|....*...
gi 447052526 306 GKQAAQQILRRIAQPDAPLSHYIYRPTL 333
Cdd:cd06267 236 GRAAAELLLERIEGEEEPPRRIVLPTEL 263
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
9-337 |
1.05e-75 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 236.53 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 9 KRVTLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFTM 88
Cdd:PRK10014 5 KKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 89 GLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSSTPLLITMRP--LDwqqlPVD 166
Cdd:PRK10014 85 GLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEEKGIPVVFASRAsyLD----DVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 167 YVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLqPWSTDaFSLRAEPTQANGYQLMQQLL 242
Cdd:PRK10014 161 TVRPDNMQAAQLLTEHLIRNGHQRIAWLGGqsssLTRAERVGGYCATLLKFGL-PFHSE-WVLECTSSQKQAAEAITALL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 243 DMPSPPTAVICYNDLMAFGAESAL-------GERGL--FAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQI 313
Cdd:PRK10014 239 RHNPTISAVVCYNETIAMGAWFGLlragrqsGESGVdrYFEQQVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRM 318
|
330 340
....*....|....*....|....
gi 447052526 314 LRRIAQPDAPLSHYIYRPTLQIRA 337
Cdd:PRK10014 319 MQRITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-339 |
2.89e-73 |
|
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: 227.88 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEaDLQRYANSST 149
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAP-DLQELAARGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGL----THHMRYQGYLEAMNHHGLQPwsTDAFSL 225
Cdd:cd06285 80 PVVLVDRRIG--DTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPlnasTGRDRLRGYRRALAEAGLPV--PDERIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLAL 305
Cdd:cd06285 156 PGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEM 235
|
250 260 270
....*....|....*....|....*....|....
gi 447052526 306 GKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAST 339
Cdd:cd06285 236 GRRAAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
70-338 |
7.10e-64 |
|
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: 203.63 E-value: 7.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSST 149
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPWSTDAFSl 225
Cdd:cd19976 81 PVVVLDRYIE--DNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYneheRIEGYKNALQDHNLPIDESWIYS- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 rAEPTQANGYQLMQQLLDMpSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLAL 305
Cdd:cd19976 158 -GESSLEGGYKAAEELLKS-KNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEM 235
|
250 260 270
....*....|....*....|....*....|...
gi 447052526 306 GKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd19976 236 GQEAAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
70-338 |
5.07e-63 |
|
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: 201.33 E-value: 5.07e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAD--LQRYanS 147
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAelLAAL--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 STPLLItmrpLDW--QQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH----MRYQGYLEAMNHHGLQPwsTD 221
Cdd:cd06275 79 SIPVVV----LDReiAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHsvsrERLAGFRRALAEAGIEV--PP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVE 301
Cdd:cd06275 153 SWIVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQP 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 447052526 302 PLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06275 233 KDELGELAVELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
15-338 |
5.44e-63 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 203.39 E-value: 5.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 15 DVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFTMGLEMTL 94
Cdd:PRK10423 3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 95 AEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVL-CPVNSTSEAD-LQRYanSSTPlLITM--RPLDWQQlpvDYVGV 170
Cdd:PRK10423 83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLlCTETHQPSREiMQRY--PSVP-TVMMdwAPFDGDS---DLIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 171 DSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQpwSTDAFSLRAEPTQANGYQLMQQLLDMPS 246
Cdd:PRK10423 157 NSLLGGDLATQYLIDKGYTRIACITGpldkTPARLRLEGYRAAMKRAGLN--IPDGYEVTGDFEFNGGFDAMQQLLALPL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 247 PPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIAQPDAPLSH 326
Cdd:PRK10423 235 RPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQR 314
|
330
....*....|..
gi 447052526 327 YIYRPTLQIRAS 338
Cdd:PRK10423 315 LQLTPELMERGS 326
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
70-337 |
5.67e-63 |
|
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: 201.21 E-value: 5.67e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPvNSTSEADLQRYANSST 149
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHS-RALSDEELILIAEKIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH----HMRYQGYLEAMNHHGLQPwsTDAFSL 225
Cdd:cd06270 80 PLVVINRYIP--GLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDipdaRERLAGYRDALAEAGIPL--DPSLII 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVePLA- 304
Cdd:cd06270 156 EGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHY-PIEe 234
|
250 260 270
....*....|....*....|....*....|...
gi 447052526 305 LGKQAAQQILRRIAQPDAPLSHyIYRPTLQIRA 337
Cdd:cd06270 235 MAQAAAELALNLAYGEPLPISH-EFTPTLIERD 266
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
70-338 |
7.97e-63 |
|
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380507 [Multi-domain] Cd Length: 267 Bit Score: 200.84 E-value: 7.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLcpVNSTSEADLQRYANSST 149
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVIL--LSGRLDAELLSELSKRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDWQQLPvdYVGVDSHAGVREATEYLIQQGHRDIVFIGG-LTH---HMRYQGYLEAMNHHGLQPwsTDAFSL 225
Cdd:cd06284 79 PIVQCCEYIPDSGVP--SVSIDNEAAAYDATEYLISLGHRRIAHINGpLDNvyaRERLEGYRRALAEAGLPV--DEDLII 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLAL 305
Cdd:cd06284 155 EGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEI 234
|
250 260 270
....*....|....*....|....*....|...
gi 447052526 306 GKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06284 235 GETAAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
12-338 |
7.80e-61 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 198.41 E-value: 7.80e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 12 TLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFTMGLE 91
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 92 MTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGI-VLCpvnstSEadlqrYANSSTPLL-----ITMRPLDWQQLPV 165
Cdd:PRK10703 83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLlVMC-----SE-----YPEPLLAMLeeyrhIPMVVMDWGEAKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 166 DYVGV---DSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQP---WSTDAFslrAEPTqaNGY 235
Cdd:PRK10703 153 DFTDAiidNAFEGGYLAGRYLIERGHRDIGVIPGplerNTGAGRLAGFMKAMEEANIKVpeeWIVQGD---FEPE--SGY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 236 QLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILR 315
Cdd:PRK10703 228 EAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLD 307
|
330 340
....*....|....*....|...
gi 447052526 316 RIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:PRK10703 308 RIVNKREEPQTIEVHPRLVERRS 330
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
8-343 |
2.51e-60 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 196.75 E-value: 2.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 8 RKRVTLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFT 87
Cdd:PRK09526 3 SKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 88 MGLEMTLAEHGFITVMSnTSQRSDRQ--KQVLDTLLEHHVAGIVlcpVN---STSEADLQRYANSSTPLLItmrpLDWQ- 161
Cdd:PRK09526 83 AAIKSRADQLGYSVVIS-MVERSGVEacQAAVNELLAQRVSGVI---INvplEDADAEKIVADCADVPCLF----LDVSp 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 162 QLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQPWSTdafsLRAEPTQANGYQL 237
Cdd:PRK09526 155 QSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGpessVSARLRLAGWLEYLTDYQLQPIAV----REGDWSAMSGYQQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 238 MQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRi 317
Cdd:PRK09526 231 TLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLAL- 309
|
330 340
....*....|....*....|....*.
gi 447052526 318 AQPDAPLSHYIYRPTLQIRASTGKRG 343
Cdd:PRK09526 310 SQGQAVKGSQLLPTSLVVRKSTAPPN 335
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-338 |
6.25e-60 |
|
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: 193.64 E-value: 6.25e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVnSTSEADLQRYANSST 149
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPS-DDDLSHLARLRARGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDWQQLPVdyVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH----HMRYQGYLEAMNHHGLQP----WSTD 221
Cdd:cd06293 80 AVVLLDRPAPGPAGCS--VSVDDVQGGALAVDHLLELGHRRIAFVSGPLRtrqvAERLAGARAAVAEAGLDPdevvRELS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AFSLRAEptqaNGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAvE 301
Cdd:cd06293 158 APDANAE----LGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVR-Q 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 447052526 302 PL-ALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06293 233 PSyELGRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
70-338 |
6.91e-59 |
|
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: 190.81 E-value: 6.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEadlqRYANSST 149
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIE----EYKKLNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDWQqlpVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPwSTDAFSL 225
Cdd:cd06291 77 PIVSIDRYLSEG---IPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSpaneRYRGFEDALKEAGIEY-EIIEIDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RaEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIaVEPLA- 304
Cdd:cd06291 153 N-DFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTI-RQPIEe 230
|
250 260 270
....*....|....*....|....*....|....
gi 447052526 305 LGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06291 231 MAKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
70-339 |
9.00e-57 |
|
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: 185.55 E-value: 9.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDL----INPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLcpvnSTSEADLQRYA 145
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVL----ASTRHDDPRVR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 146 ---NSSTPLLITMRPldWQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLqPW 218
Cdd:cd06292 77 ylhEAGVPFVAFGRA--NPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGpegsVPSDDRLAGYRAALEEAGL-PF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 219 STDAFsLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTI 298
Cdd:cd06292 154 DPGLV-VEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 447052526 299 AVEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAST 339
Cdd:cd06292 233 RQPIDEIGRAVVDLLLAAIEGNPSEPREILLQPELVVRESS 273
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
70-333 |
6.46e-56 |
|
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: 183.11 E-value: 6.46e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNStSEADLQRYANSST 149
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGG-NEDLIEKLVKSGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PL-LITMRPLDwqqLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG---LTH-HMRYQGYLEAMNHHGLQPwstDAFS 224
Cdd:cd19977 80 PVvFVDRYIPG---LDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYpleLSTrQERLEGYKAALADHGLPV---DEEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 225 LRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLA 304
Cdd:cd19977 154 IKHVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYE 233
|
250 260 270
....*....|....*....|....*....|
gi 447052526 305 LGKQAAQQILRRI-AQPDAPLSHYIYRPTL 333
Cdd:cd19977 234 IGRKAAELLLDRIeNKPKGPPRQIVLPTEL 263
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
70-338 |
1.53e-55 |
|
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: 182.37 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVV---IDDLINPFFAEftmGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNST----SEADLQ 142
Cdd:cd01541 1 TIGVIttyIDDYIFPSIIQ---GIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSAlpnpNLDLYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 143 RYANSSTPLLITMRplDWQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFI---GGLTHHMRYQGYLEAMNHHGLQPWS 219
Cdd:cd01541 78 ELQKKGIPVVFINS--YYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIfksDDLQGVERYQGFIKALREAGLPIDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 220 TDAFSLRAEP-TQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTI 298
Cdd:cd01541 156 DRILWYSTEDlEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447052526 299 AVEPLALGKQAAQQILRRIAQPDAPLShYIYRPTLQIRAS 338
Cdd:cd01541 236 VHPKEELGRKAAELLLRMIEEGRKPES-VIFPPELIERES 274
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-338 |
2.68e-55 |
|
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: 181.66 E-value: 2.68e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGF-ITVMSNTSqRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEadLQRYANSS 148
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYtLIVSTSHW-NADRELEILRLLLARKVDGIIVVGGFGDEE--LLKLLAEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQpwSTDAFS 224
Cdd:cd06290 78 IPVVLVDRELE--GLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPdaqeRYAGYRRALEDAGLE--VDPRLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 225 LRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLA 304
Cdd:cd06290 154 VEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYE 233
|
250 260 270
....*....|....*....|....*....|....
gi 447052526 305 LGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06290 234 MGKTAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
70-338 |
3.22e-55 |
|
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: 181.21 E-value: 3.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLI-NPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVnSTSEADLQRYANSs 148
Cdd:cd06288 1 TIGLITDDIAtTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASM-HHREVTLPPELTD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQLPvdYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPWSTDAFS 224
Cdd:cd06288 79 IPLVLLNCFDDDPSLP--SVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLatrlRLAGYRAALAEAGIPYDPSLVVH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 225 lrAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLA 304
Cdd:cd06288 157 --GDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYE 234
|
250 260 270
....*....|....*....|....*....|....
gi 447052526 305 LGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06288 235 MGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
70-333 |
5.14e-55 |
|
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: 180.82 E-value: 5.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVI----DDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQkQVLDTLLE-HHVAGIVlcpVNSTSEAD--LQ 142
Cdd:cd20010 1 AIGLVLpldpGDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDEL-ATYRRLVErGRVDGFI---LARTRVNDprIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 143 RYANSSTPLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH----HMRYQGYLEAMNHHGLQPw 218
Cdd:cd20010 77 YLLERGIPFVVHGRSES--GAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEElnfaHQRRDGYRAALAEAGLPV- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 219 sTDAFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACA-YSNPPLTT 297
Cdd:cd20010 154 -DPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALeYFSPPLTT 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 447052526 298 IAVEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTL 333
Cdd:cd20010 233 TRSSLRDAGRRLAEMLLALIDGEPAAELQELWPPEL 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
70-336 |
1.65e-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: 179.38 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSsT 149
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHG-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH----HMRYQGYLEAMNHHGLQPwsTDAFSL 225
Cdd:cd06280 80 PIVLIDREVE--GLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEisttRERLAGYREALAEAGIPV--DESLIF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLAL 305
Cdd:cd06280 156 EGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEI 235
|
250 260 270
....*....|....*....|....*....|.
gi 447052526 306 GKQAAQQILRRIAQPDAPLSHYIYRPTLQIR 336
Cdd:cd06280 236 GRIAAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
70-338 |
7.70e-53 |
|
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: 175.08 E-value: 7.70e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGF---ITVMSNTSQRSDRQkqVLDTLLEHHVAGIVLCpVNSTSEADLQRYAN 146
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYsvsIATVDEDDPASVRE--ALDRLLSQRVDGIIVI-APDEAVLEALRRLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 147 SSTPLLITMRPldwQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQP----- 217
Cdd:cd01574 78 PGLPVVIVGSG---PSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGpldwVDARARLRGWREALEEAGLPPppvve 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 218 --WSTDAfslraeptqanGYQLMQQLLDMPsPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPL 295
Cdd:cd01574 155 gdWSAAS-----------GYRAGRRLLDDG-PVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 447052526 296 TTIAVEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd01574 223 TTVRQDFAELGRRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
70-338 |
1.24e-52 |
|
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: 174.77 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAdLQRYANSST 149
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEG-LQALIAQGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQPWSTDAFSL 225
Cdd:cd06299 80 PVVFVDREVE-GLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGplstSTGRERLAAFRAALTAAGIPIDEELVAFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RAepTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLAL 305
Cdd:cd06299 159 DF--RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERI 236
|
250 260 270
....*....|....*....|....*....|...
gi 447052526 306 GKQAAQQILRRIAQPDAPLSHYIyRPTLQIRAS 338
Cdd:cd06299 237 GRRAVELLLALIENGGRATSIRV-PTELIPRES 268
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
70-338 |
3.49e-51 |
|
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380489 [Multi-domain] Cd Length: 269 Bit Score: 170.75 E-value: 3.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAdLQRYANSST 149
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPAT-RKLLRAAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMrplDWQQLPVDY-VGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH-----MRYQGYLEAMNHHGLQPwsTDAF 223
Cdd:cd01575 80 PVVETW---DLPDDPIDMaVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGdsrarQRLEGFRDALAEAGLPL--PLVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 224 SLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPL 303
Cdd:cd01575 155 LVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRY 234
|
250 260 270
....*....|....*....|....*....|....*
gi 447052526 304 ALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd01575 235 EIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
70-338 |
6.70e-51 |
|
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: 170.04 E-value: 6.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCpvNSTSEADLQRYANS-S 148
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFA--SGTLTEENKQLLKNmN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQLPvdYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM-----RYQGYLEAMNHHGL---QPWST 220
Cdd:cd19975 79 IPVVLVSTESEDPDIP--SVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPnagypRYEGYKKALKDAGLpikENLIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 221 D-AFSLraeptqANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIA 299
Cdd:cd19975 157 EgDFSF------KSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVS 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 447052526 300 VEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd19975 231 QPFYEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
70-338 |
2.50e-50 |
|
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: 168.85 E-value: 2.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVI-----DDLINPFFAEFTMGLEMTLAEHGFITVmsntsqRSDRQKQVLDTLLEHhVAGIVLcpVNSTSEADLQRY 144
Cdd:cd01544 1 TIGIIQwyseeEELEDPYYLSIRLGIEKEAKKLGYEIK------TIFRDDEDLESLLEK-VDGIIA--IGKFSKEEIEKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 145 ANSSTPL-LITMRPLDwqqLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM---------RYQGYLEAMNHHG 214
Cdd:cd01544 72 KKLNPNIvFVDSNPDP---DGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSddgeeiedpRLRAFREYMKEKG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 215 LQpwsTDAFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPP 294
Cdd:cd01544 149 LY---NEEYIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPP 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447052526 295 LTTIAVEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd01544 226 LTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-338 |
2.25e-49 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 166.17 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFtmgLEM---TLAEHGFITVMSNTSQRSDRQkQVLDTLLEHHVAGIVLCPVNSTSEAdLQRYAN 146
Cdd:cd06278 1 LVGVVVGDLSNPFYAEL---LEElsrALQARGLRPLLFNVDDEDDVD-DALRQLLQYRVDGVIVTSATLSSEL-AEECAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 147 SSTPLLITMRplDWQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQPWSTDA 222
Cdd:cd06278 76 RGIPVVLFNR--VVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGpegtSTSRERERGFRAALAELGLPPPAVEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 223 fslrAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESAL-GERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVE 301
Cdd:cd06278 154 ----GDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQP 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 447052526 302 PLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06278 230 IEEMAEAAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-338 |
2.84e-49 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 165.76 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLcpVNSTSEADLQRY-ANSS 148
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLIL--VGSDHDPELFELlEQRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITmrpldWQQLPVDY---VGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH-----MRYQGYLEAMNHHGL----- 215
Cdd:cd06273 79 VPYVLT-----WSYDEDSPhpsIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGndrarARLAGIRDALAERGLelpee 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 216 ----QPWSTDAfslraeptqanGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYS 291
Cdd:cd06273 154 rvveAPYSIEE-----------GREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447052526 292 NPPLTTIAVEPLALGKQAAQQILRRIAQPDAPLSHyIYRPTLQIRAS 338
Cdd:cd06273 223 SPPLTTVRVPAREIGELAARYLLALLEGGPPPKSV-ELETELIVRES 268
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
41-339 |
6.24e-49 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 166.33 E-value: 6.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 41 TQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTL 120
Cdd:PRK11041 8 TRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 121 LEHHVAGIVLC----PVNSTSEAdlQR------YANSSTPLLitmrpldwqQLPVdyVGVDSHAGVREATEYLIQQGHRD 190
Cdd:PRK11041 88 ITKQIDGMLLLgsrlPFDASKEE--QRnlppmvMANEFAPEL---------ELPT--VHIDNLTAAFEAVNYLHELGHKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 191 IVFIGGLTH----HMRYQGYLEAMNHHGLqpwSTD-AFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESA 265
Cdd:PRK11041 155 IACIAGPEEmplcHYRLQGYVQALRRCGI---TVDpQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQ 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447052526 266 LGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAST 339
Cdd:PRK11041 232 AKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-338 |
7.80e-48 |
|
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: 162.33 E-value: 7.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDD---LINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAG-IVLCPVNSTSeadLQRYA 145
Cdd:cd19974 1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGiIILGEISKEY---LEKLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 146 NSSTPLLItmrpLD--WQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH---HM-RYQGYLEAMNHHGLQPws 219
Cdd:cd19974 78 ELGIPVVL----VDhyDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDINYtssFMdRYLGYRKALLEAGLPP-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 220 tdafsLRAE---PTQANGYQLMQQL---LDMpSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNP 293
Cdd:cd19974 152 -----EKEEwllEDRDDGYGLTEEIelpLKL-MLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTP 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447052526 294 PLTTIAVEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd19974 226 PLTTVEVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
11-343 |
1.05e-46 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 161.48 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 11 VTLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFTMGL 90
Cdd:PRK10401 2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 91 EMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLcPVNSTSEADLQRYANSSTPLLITMRPLDwqqlpvDY--- 167
Cdd:PRK10401 82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIV-HSKALSDDELAQFMDQIPGMVLINRVVP------GYahr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 168 -VGVDSHAGVREATEYLIQQGHRDIVFIGGlTHH-----MRYQGYLEAMNHHGLQPwsTDAFSLRAEPTQANGYQLMQQL 241
Cdd:PRK10401 155 cVCLDNVSGARMATRMLLNNGHQRIGYLSS-SHGieddaMRRAGWMSALKEQGIIP--PESWIGTGTPDMQGGEAAMVEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 242 LDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIAQPD 321
Cdd:PRK10401 232 LGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNL 311
|
330 340
....*....|....*....|..
gi 447052526 322 APLSHYIYRPTLQIRASTGKRG 343
Cdd:PRK10401 312 DPRASHCFMPTLVRRHSVATRQ 333
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
12-340 |
1.75e-46 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 161.08 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 12 TLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFTMGLE 91
Cdd:PRK10727 3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 92 MTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLcPVNSTSEADLQRYANSSTPLLITMRPL-DWQQlpvDYVGV 170
Cdd:PRK10727 83 QVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVV-HAKMIPDAELASLMKQIPGMVLINRILpGFEN---RCIAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 171 DSHAGVREATEYLIQQGHRDIVFIGGlTHHM-----RYQGYLEAMNHHGLQpwSTDAFSLRAEPTQANGYQLMQQLLDMP 245
Cdd:PRK10727 159 DDRYGAWLATRHLIQQGHTRIGYLCS-NHSIsdaedRLQGYYDALAESGIP--ANDRLVTFGEPDESGGEQAMTELLGRG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 246 SPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIAQPDAPLS 325
Cdd:PRK10727 236 RNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLPEI 315
|
330
....*....|....*
gi 447052526 326 HYIYRPTLQIRASTG 340
Cdd:PRK10727 316 TNVFSPTLVRRHSVS 330
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-338 |
1.64e-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: 156.24 E-value: 1.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSST 149
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELAAALARLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqqLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH----HMRYQGYLEAMNHHGLQPwstDAFSL 225
Cdd:cd06281 81 PVVLIDRDLP---GDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDirpgRERIAGFKAAFAAAGLPP---DPDLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 226 RA-EPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLA 304
Cdd:cd06281 155 RLgSFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDA 234
|
250 260 270
....*....|....*....|....*....|....*
gi 447052526 305 LGKQAAQQILRRIAQPDAPLSHYIYRPT-LQIRAS 338
Cdd:cd06281 235 VGRAAAELLLDRIEGPPAGPPRRIVVPTeLILRDS 269
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
70-339 |
2.25e-45 |
|
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: 155.90 E-value: 2.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEaDLQRYANSST 149
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSR-QLRLLRSAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLItmrpLDWQQLPVD---YVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPwstDA 222
Cdd:cd06296 80 PFVL----IDPVGEPDPdlpSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVsgraRLAGYRAALAEAGIAV---DP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 223 FSLRAEP-TQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAvE 301
Cdd:cd06296 153 DLVREGDfTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVH-Q 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 447052526 302 PL-ALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAST 339
Cdd:cd06296 232 PLrEMGAVAVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
70-332 |
8.04e-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: 380505 [Multi-domain] Cd Length: 267 Bit Score: 154.36 E-value: 8.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSST 149
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALELLEEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDWQQLPvdYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH-----HMRYQGYLEAMNHHGLQPWSTDAFS 224
Cdd:cd06282 81 PYVLLFNQTENSSHP--FVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSasdraRLRYQGYRDALKEAGLKPIPIVEVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 225 LRAEPTQAngyqLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLA 304
Cdd:cd06282 159 FPTNGLEE----ALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRD 234
|
250 260 270
....*....|....*....|....*....|.
gi 447052526 305 LGKQAAQQILRRIAQPDAPLSH---YIYRPT 332
Cdd:cd06282 235 MGRAAADLLLAEIEGESPPTSIrlpHHLREG 265
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
70-338 |
1.59e-44 |
|
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: 153.48 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSN-TSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSS 148
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVEPcDSDDEDLADRLRRFLSRSRPDGVILTPPLSDDPALLDALDELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TP--LLITMRPLDwqqlPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQPwsTDA 222
Cdd:cd01545 81 IPyvRIAPGTDDD----RSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGppdhGASAERLEGFRDALAEAGLPL--DPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 223 FSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAvEP 302
Cdd:cd01545 155 LVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVR-QP 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 447052526 303 L-ALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd01545 234 IaEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
70-328 |
2.89e-43 |
|
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: 149.95 E-value: 2.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEaDLQRYANSST 149
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDE-HRKALKKLKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMrpldwQQLPvDYVGV---DSHAGvREATEYLIQQGHRDIVFIG--------GLThhmRYQGYLEAMNHHGLQPw 218
Cdd:cd01542 80 PVVVLG-----QEHE-GFSCVyhdDYGAG-KLLGEYLLKKGHKNIAYIGvdeediavGVA---RKQGYLDALKEHGIDE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 219 stdAFSLRAEPTQANGYQLMQQLLDmPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTI 298
Cdd:cd01542 149 ---VEIVETDFSMESGYEAAKELLK-ENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTV 224
|
250 260 270
....*....|....*....|....*....|
gi 447052526 299 AVEPLALGKQAAQQILRRIAQPDAPLSHYI 328
Cdd:cd01542 225 KFDYEEAGEKAAELLLDMIEGEKVPKKQKL 254
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
70-328 |
6.03e-43 |
|
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: 149.66 E-value: 6.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVI----DDLI-NPFFAEFTMGLEMTLAEHGFiTVMSNTSQRSDRQK-QVLDTLLEHHVAGIVLCpvNSTSEADLQR 143
Cdd:cd06294 1 TIGLVLpssaEELFqNPFFSEVLRGISQVANENGY-SLLLATGNTEEELLeEVKRMVRGRRVDGFILL--YSKEDDPLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 144 YAN-SSTPLLITMRPLDWQQLPvdYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPw 218
Cdd:cd06294 78 YLKeEGFPFVVIGKPLDDNDVL--YVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVvsidRLQGYKQALKEAGLPL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 219 sTDAFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTI 298
Cdd:cd06294 155 -DDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSV 233
|
250 260 270
....*....|....*....|....*....|
gi 447052526 299 AVEPLALGKQAAQQILRRIAQPDAPLSHYI 328
Cdd:cd06294 234 DINPYELGREAAKLLINLLEGPESLPKNVI 263
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
66-338 |
1.28e-40 |
|
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: 143.55 E-value: 1.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 66 QKSLTIGVVID-------DLINPFFAEFTMGLEMTLAEHGFITVMSntsqRSDRQKQVLDTLLEHHVA-GIVLcpVNSTS 137
Cdd:cd06295 1 QRSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLS----TQDEDANQLARLLDSGRAdGLIV--LGQGL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 138 EAD-LQRYANSSTPLLITMRPLDWQQLPVdyVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH---MRYQGYLEAMNHH 213
Cdd:cd06295 75 DHDaLRELAQQGLPMVVWGAPEDGQSYCS--VGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPevaDRLQGYRDALAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 214 GLQPwsTDAFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNP 293
Cdd:cd06295 153 GLEA--DPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447052526 294 PLTTIAvEPLAL-GKQAAQQILRRIAQPDAPLSHYiyrPT-LQIRAS 338
Cdd:cd06295 231 PLTTVR-QDLALaGRLLVEKLLALIAGEPVTSSML---PVeLVVRES 273
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
81-325 |
5.78e-37 |
|
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: 133.90 E-value: 5.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 81 PFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCpvNSTSEADLQRYANSSTPLLItmrpLD- 159
Cdd:cd06277 19 PFFSELIDGIEREARKYGYNLLISSVDIGDDFDEILKELTDDQSSGIILLG--TELEEKQIKLFQDVSIPVVV----VDn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 160 -WQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH----HMRYQGYLEAMNHHGLQPWSTDAFSLRAEPTQAng 234
Cdd:cd06277 93 yFEDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRiknfEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGA-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 235 YQLMQQLLD-MPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQI 313
Cdd:cd06277 171 YKDMKALLDtGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRL 250
|
250
....*....|..
gi 447052526 314 LRRIAQPDAPLS 325
Cdd:cd06277 251 IEKIKDPDGGTL 262
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
182-339 |
1.55e-36 |
|
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: 129.38 E-value: 1.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 182 YLIQQGHRDIVFIGGLTHH------MRYQGYLEAMNHHGLQPwsTDAFSLRAEPTQANGYQlmQQLLDMPSPPTAVICYN 255
Cdd:pfam13377 1 HLAELGHRRIALIGPEGDRddpysdLRERGFREAARELGLDV--EPTLYAGDDEAEAAAAR--ERLRWLGALPTAVFVAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 256 DLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQI 335
Cdd:pfam13377 77 DEVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVE 156
|
....
gi 447052526 336 RAST 339
Cdd:pfam13377 157 REST 160
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
70-336 |
1.45e-35 |
|
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: 129.98 E-value: 1.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVnSTSEADLQRYANSST 149
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPT-GNNNDAYLELAQKGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVF----IGGL-THHMRYQGYLEAMNHHGLQPwstDAFS 224
Cdd:cd06283 80 PVVLVDRQIE--PLNWDTVVTDNYDATYEATEHLKEQGYERIVFvtepIKGIsTRRERLQGFLDALARYNIEG---DVYV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 225 LRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLA 304
Cdd:cd06283 155 IEIEDTEDLQQALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYE 234
|
250 260 270
....*....|....*....|....*....|..
gi 447052526 305 LGKQAAQQILRRIAQPDAPLSHYIYRPTLQIR 336
Cdd:cd06283 235 IGKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
70-336 |
1.02e-34 |
|
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: 127.66 E-value: 1.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPV-NSTSE-ADLQRYAns 147
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSReNDWEViEPYAKYG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 stPLLITMRPldwQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFI------GGLTHHMRYQGYLEAMNHHGLQP---W 218
Cdd:cd06286 79 --PIVLCEET---DSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYClgrpesSSASTQARLKAYQDVLGEHGLSLreeW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 219 S-TDAFSLraeptqANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDgvaacaysN----- 292
Cdd:cd06286 154 IfTNCHTI------EDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFD--------Nqpise 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 447052526 293 -PPLTTIAVEPLALGKQAAQQILRRIaqPDAPLSHYIYRPTLQIR 336
Cdd:cd06286 220 lLNLTTIDQPLEEMGKEAFELLLSQL--ESKEPTKKELPSKLIER 262
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
70-338 |
6.25e-32 |
|
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: 120.78 E-value: 6.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDD-----LINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLlehhVAGIVL--CPVNSTSEADLQ 142
Cdd:cd06279 1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAA----VDGFIVygLSDDDPAVAALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 143 RyanSSTPLLITMRPLDWQqlpVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTH---------------------HM 201
Cdd:cd06279 77 R---RGLPLVVVDGPAPPG---IPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDrgrergpvsaerlaaatnsvaRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 202 RYQGYLEAMNHHGLQP-----WSTDAFslraepTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGED 276
Cdd:cd06279 151 RLAGYRDALEEAGLDLddvpvVEAPGN------TEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPED 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447052526 277 ISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIaqPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06279 225 LSVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLL--PGAPPRPVILPTELVVRAS 284
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
71-317 |
1.48e-31 |
|
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: 119.27 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 71 IGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAG-IVLCPVNSTSE-ADLQRYANss 148
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGlAINLVDPAAAGvAEKARGQN-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 tpllITMRPLDWQQL---PVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH----MRYQGYLEAMNHHGLQpwsTD 221
Cdd:cd01537 80 ----VPVVFFDKEPSrydKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHpdaeARLAGVIKELNDKGIK---TE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AFSLR-AEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAV 300
Cdd:cd01537 153 QLQLDtGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQ 232
|
250
....*....|....*..
gi 447052526 301 EPLALGKQAAQQILRRI 317
Cdd:cd01537 233 DANNLGKTTFDLLLNLA 249
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
70-299 |
5.00e-31 |
|
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: 118.16 E-value: 5.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPvNSTSEADLQRYANSST 149
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMG-DELTEEIREEFKRSPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITMRPLDWQQLPVdyVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH-----MRYQGYLEAMNHHGLQ---PWSTD 221
Cdd:cd06298 80 PVVLAGTVDSDHEIPS--VNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEyinndKKLQGYKRALEEAGLEfnePLIFE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447052526 222 AFSlraepTQANGYQLMQQLLDMpSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIA 299
Cdd:cd06298 158 GDY-----DYDSGYELYEELLES-GEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSIN 229
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
70-338 |
6.16e-30 |
|
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: 115.26 E-value: 6.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTsEADLQRYANSST 149
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLT-ELFEEVIVPTEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLItmrpLDWQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM--------RYQGYLEAMNHHGLQPWSTD 221
Cdd:cd06297 80 PVVL----IDANSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVftetvfreREQGFLEALNKAGRPISSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AFslRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAysNPPLTTIAVE 301
Cdd:cd06297 156 MF--RIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQP 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 447052526 302 PLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRAS 338
Cdd:cd06297 232 VEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
167-333 |
1.21e-29 |
|
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: 114.44 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 167 YVGVDSHAGVREATEYLIQQGHRDIVFIG-----GLTHHMRyQGYLEAMNHHGLQPwstdaFSLRAEPTQANGYQLMQQL 241
Cdd:cd06271 97 WVDIDNEAGAYEAVERLAGLGHRRIAFIVpparySPHDRRL-QGYVRA*RDAGLTG-----YPLDADTTLEAGRAAAQRL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 242 LDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAAC-AYSNPPLTTIAVEPLALGKQAAQQILRRIAQP 320
Cdd:cd06271 171 LALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFLgAMITPPLTTVHAPIAEAGRELAKALLARIDGE 250
|
170
....*....|...
gi 447052526 321 DAPLSHYIYRPTL 333
Cdd:cd06271 251 DPETLQVLVQPSL 263
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
8-317 |
4.99e-29 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 114.35 E-value: 4.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 8 RKRVTLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFT 87
Cdd:PRK14987 3 KKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 88 MGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAdLQRYANSSTPLLITMrplDWQQLPVDY 167
Cdd:PRK14987 83 RGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRT-LKMIEVAGIPVVELM---DSQSPCLDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 168 -VGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH---MRYQGYLEAMNHHGLQPWSTdafSLRAEPTQANGYQLMQQLLD 243
Cdd:PRK14987 159 aVGFDNFEAARQMTTAIIARGHRHIAYLGARLDErtiIKQKGYEQAMLDAGLVPYSV---MVEQSSSYSSGIELIRQARR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447052526 244 MPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQILRRI 317
Cdd:PRK14987 236 EYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARI 309
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
167-333 |
3.17e-27 |
|
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: 107.62 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 167 YVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM----RYQGYLEAMNHHGLQPWSTDAFSLraEPTQANGYQLMQQLL 242
Cdd:cd20009 97 YFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTyaqhRLRGFRRALAEAGLEVEPLLIVTL--DSSAEAIRAAARRLL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 243 DMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIaVEPLAL-GKQAAQQILRRIAQPD 321
Cdd:cd20009 175 RQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTL-YEDIEEaGRFLAEALLRRIEGEP 253
|
170
....*....|..
gi 447052526 322 APLSHYIYRPTL 333
Cdd:cd20009 254 AEPLQTLERPEL 265
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
11-80 |
7.53e-27 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 100.74 E-value: 7.53e-27
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 11 VTLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLIN 80
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
70-337 |
1.06e-23 |
|
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: 98.21 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVV-IDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVlcpVNSTSEADLQrYANSS 148
Cdd:cd06272 1 TIGLYwPSVGERVALTRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVI---VFGISDSDIE-YLNKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 T---PLLITMRPldwqQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH----MRYQGYLEAMNHHGLQpwSTD 221
Cdd:cd06272 77 KpkiPIVLYNRE----SPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNrnqtLRGKGFIETCEKHGIH--LSD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVE 301
Cdd:cd06272 151 SIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVP 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 447052526 302 PLALGKQAAQQILRRIAQPDAPLSHYIYRPTLQIRA 337
Cdd:cd06272 231 IEKIAEESLRLILKLIEGRENEIQQLILYPELIFRE 266
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
12-252 |
2.03e-23 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 98.80 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 12 TLTDVARAAGVSKSTVSLVLN---DSSLIKKETQQKVQQAIEQLGYVYNRFAANLRSQKSLTIGVVIDDLINPFFAEFTM 88
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 89 GLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVlcpVNSTSEAD---LQRYANSSTPLLITMRPLDWQQLpV 165
Cdd:PRK11303 82 YLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALI---VSTSLPPEhpfYQRLQNDGLPIIALDRALDREHF-T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 166 DYVGVDSHAGvREATEYLIQQGHRDIVFIGGL----THHMRYQGYLEAMNHHGLQP--WSTDAFSlraeptQANGYQLMQ 239
Cdd:PRK11303 158 SVVSDDQDDA-EMLAESLLKFPAESILLLGALpelsVSFEREQGFRQALKDDPREVhyLYANSFE------REAGAQLFE 230
|
250
....*....|...
gi 447052526 240 QLLDMPSPPTAVI 252
Cdd:PRK11303 231 KWLETHPMPDALF 243
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
70-279 |
1.33e-22 |
|
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: 94.97 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPvnSTSEADLQRYANSS- 148
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAP--STPPDDIYYLCQAAg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQLPVdyVGVDSHAGVREATEYLIQQGHRDIVFIGGL----THHMRYQGYLEAMNHHGLQPWSTDAFS 224
Cdd:cd06274 79 LPVVFLDRPFSGSDAPS--VVSDNRAGARALTEKLLAAGPGEIYFLGGRpelpSTAERIRGFRAALAEAGITEGDDWILA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 447052526 225 LRAEPTQanGYQLMQQLLD-MPSPPTAVICyNDLMAF-GAESALGERGLFAGEDISL 279
Cdd:cd06274 157 EGYDRES--GYQLMAELLArLGGLPQALFT-SSLTLLeGVLRFLRERLGAIPSDLVL 210
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
70-323 |
1.49e-22 |
|
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: 94.94 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSS- 148
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQLPVDYVGVDSHAGVREATEYLIQQ--GHRDIVFIGGLTHH----MRYQGYLEAMNHHglqPWSTDA 222
Cdd:cd01536 81 IPVVAVDTDIDGGGDVVAFVGTDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSstaiDRTKGFKEALKKY---PDIEIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 223 FSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDGVAAC--AYSNPPLT-TIA 299
Cdd:cd01536 158 AEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTPEAlkAIKDGELDaTVA 235
|
250 260
....*....|....*....|....
gi 447052526 300 VEPLALGKQAAQQILRRIAQPDAP 323
Cdd:cd01536 236 QDPYLQGYLAVEAAVKLLNGEKVP 259
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
68-317 |
5.31e-21 |
|
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: 91.03 E-value: 5.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 68 SLTIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVnSTSEADLQRYANS 147
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTP-APSGDDITAKAEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 ST-PLLITMRPLDWQQLPVDYVGVDSHAGvREATEYLIQQGH-RDIVFIGG----LTHHMRYQGYLEAMNHHGLQPWSTD 221
Cdd:pfam00532 80 YGiPVIAADDAFDNPDGVPCVMPDDTQAG-YESTQYLIAEGHkRPIAVMAGpasaLTARERVQGFMAALAAAGREVKIYH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AfsLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAacAYSN--------- 292
Cdd:pfam00532 159 V--ATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVKIPDIVGIGINSVV--GFDGlskaqdtgl 234
|
250 260
....*....|....*....|....*..
gi 447052526 293 --PPLTTIAVEPLALGKQAAQQILRRI 317
Cdd:pfam00532 235 ylSPLTVIQLPRQLLGIKASDMVYQWI 261
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
15-65 |
1.92e-20 |
|
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: 83.23 E-value: 1.92e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 447052526 15 DVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYNRFAANLRS 65
Cdd:cd01392 2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
60-318 |
5.72e-20 |
|
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];
Pssm-ID: 441483 [Multi-domain] Cd Length: 307 Bit Score: 88.83 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 60 AANLRSQKSLTIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEA 139
Cdd:COG1879 25 EAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 140 D-LQRYANSSTPLLITMRPLDWQQlPVDYVGVDSHAGVREATEYLIQQ--GHRDIVFIGGL----THHMRYQGYLEAMNH 212
Cdd:COG1879 105 PaLKKAKAAGIPVVTVDSDVDGSD-RVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSpgapAANERTDGFKEALKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 213 HG----LQPWSTDAfslraepTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDGVA-A 287
Cdd:COG1879 184 YPgikvVAEQYADW-------DREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDGSPeA 254
|
250 260 270
....*....|....*....|....*....|...
gi 447052526 288 CAY-SNPPLT-TIAVEPLALGKQAAQQILRRIA 318
Cdd:COG1879 255 LQAiKDGTIDaTVAQDPYLQGYLAVDAALKLLK 287
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
12-339 |
3.34e-19 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 86.74 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 12 TLTDVARAAGVSKSTVSLVLN-DSSL-IKKETQQKVQQAIEQLGY-VYNRFAANLRSQKSLTI--------GVVIDDlin 80
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNdDPTLnVKEETKHRILEIAEKLEYkTSSARKLQTGAVNQHHIlaiysyqqELEIND--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 81 PFFAEFTMGLEMTLAEHGfITVMSNTSQRSDRQKQvldtllehHVAGIVLcpVNSTSEADLQRYANSSTPLLItmrpLDW 160
Cdd:PRK10339 80 PYYLAIRHGIETQCEKLG-IELTNCYEHSGLPDIK--------NVTGILI--VGKPTPALRAAASALTDNICF----IDF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 161 --QQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQPwSTDAFslRAEPTQANG 234
Cdd:PRK10339 145 hePGSGYDAVDIDLARISKEIIDFYINQGVNRIGFIGGedepGKADIREVAFAEYGRLKQVVR-EEDIW--RGGFSSSSG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 235 YQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGVAACAYSNPPLTTIAVEPLALGKQAAQQIL 314
Cdd:PRK10339 222 YELAKQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLY 301
|
330 340
....*....|....*....|....*..
gi 447052526 315 RRIAQPDA-PLShyIYRPT-LQIRAST 339
Cdd:PRK10339 302 EKARDGRAlPLL--VFVPSkLKLRGTT 326
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
167-339 |
4.28e-16 |
|
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: 76.86 E-value: 4.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 167 YVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHH---MRYQGYLEAMNHHGLQPWSTDAFSLRAEPTQANGYQ-LMQQLL 242
Cdd:cd01543 88 RVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAwsrERGEGFREALREAGYECHVYESPPSGSSRSWEEEREeLADWLK 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 243 DMPsPPTAVICYNDLMAFGAESALGERGLFAGEDISLIG--NDgVAACAYSNPPLTTIAVEPLALGKQAAQQILRRIAQP 320
Cdd:cd01543 168 SLP-KPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGvdND-ELICELSSPPLSSIALDAEQIGYEAAELLDRLMRGE 245
|
170 180
....*....|....*....|
gi 447052526 321 DAPLSHYIYRPT-LQIRAST 339
Cdd:cd01543 246 RVPPEPILIPPLgVVTRQST 265
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
71-315 |
1.48e-15 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 75.42 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 71 IGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSD-RQKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYANSS 148
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAaEQVAQIEDAIAQGVDAIIVAPVDPTALAPvLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDwQQLPVDYVGVDSHAGVREATEYLIQQ--GHRDIVFIGG----LTHHMRYQGYLEAMNHHGLQpWSTDA 222
Cdd:pfam13407 81 IPVVTFDSDAP-SSPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGspgdPNANERIDGFKKVLKEKYPG-IKVVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 223 FSLRAEPTQANGYQLMQQLL-DMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDGVAACAYSnppL------ 295
Cdd:pfam13407 159 EVEGTNWDPEKAQQQMEALLtAYPNPLDGIISPNDGMAGGAAQALEAAGL--AGKVVVTGFDATPEALEA---Ikdgtid 233
|
250 260
....*....|....*....|
gi 447052526 296 TTIAVEPLALGKQAAQQILR 315
Cdd:pfam13407 234 ATVLQDPYGQGYAAVELAAA 253
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
12-57 |
2.55e-15 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 69.20 E-value: 2.55e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 447052526 12 TLTDVARAAGVSKSTVSLVLNDSSLIKKETQQKVQQAIEQLGYVYN 57
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
70-335 |
7.91e-15 |
|
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: 73.55 E-value: 7.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVmsNTSQRSDRQKQV--LDTLLEHHVAGIVLCPVNSTSEADLQRYANS 147
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFV--TYDQKNSANEQVtnANDLIAQGVDGIIISPTNSSAAPTVLDLANE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 -STPLLITmrplDWQQLPVDYVGV---DSHAGVREATEYLIQ-------QGHRdivfIGGLTHHM-------RYQGYLEA 209
Cdd:cd06319 79 aKIPVVIA----DIGTGGGDYVSYiisDNYDGGYQAGEYLAEalkengwGGGS----VGIIAIPQsrvngqaRTAGFEDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 210 MNHHGLQpwsTDAFSLRAEPTQANGYQLMQQLL----DMpsppTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDGv 285
Cdd:cd06319 151 LEEAGVE---EVALRQTPNSTVEETYSAAQDLLaanpDI----KGIFAQNDQMAQGALQAIEEAGR--TGDILVVGFDG- 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 286 aacaysNPP----------LTTIAVEPLALGKQAAQQILRRIaQPDAPLSHYIYRPTLQI 335
Cdd:cd06319 221 ------DPEaldlikdgklDGTVAQQPFGMGARAVELAIQAL-NGDNTVEKEIYLPVLLV 273
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
70-318 |
2.23e-14 |
|
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: 72.31 E-value: 2.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSS- 148
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQlPVDYVGVDSHAGVREATEYLIQQ---GHRDIVFIGGLTHH---MRYQGYLEAMNHH-GLQPWSTD 221
Cdd:cd06322 81 IPVFTVDVKADGAK-VVTHVGTDNYAGGKLAGEYALKAllgGGGKIAIIDYPEVEsvvLRVNGFKEAIKKYpNIEIVAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AFSLRAEptqaNGYQLMQQLL----DMpsppTAVICYNDLMAFGAESALGERGlfAGEDISLIGNDG----VAACAYSNP 293
Cdd:cd06322 160 PGDGRRE----EALAATEDMLqanpDL----DGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDGnpeaIKAIAKGGK 229
|
250 260
....*....|....*....|....*
gi 447052526 294 PLTTIAVEPLALGKQAAQQILRRIA 318
Cdd:cd06322 230 IKADIAQQPDKIGQETVEAIVKYLA 254
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
71-319 |
3.91e-14 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 71.53 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 71 IGVVIDDLI---NPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANS 147
Cdd:cd01391 2 IGVVTSSLHqirEQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 STPLL-----ITMRPLDWQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM---RYQGYLEAMNHHGLQPWS 219
Cdd:cd01391 82 DIPQLaldatSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSgelRMAGFKELAKQEGICIVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 220 TD-AFSLRAEptqaNGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAgeDISLIGNDGVA---ACAYS--NP 293
Cdd:cd01391 162 SDkADWNAGE----KGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVG--DVSVIGSDGWAdrdEVGYEveAN 235
|
250 260
....*....|....*....|....*.
gi 447052526 294 PLTTIAVEPLALGkqaaQQILRRIAQ 319
Cdd:cd01391 236 GLTTIKQQKMGFG----ITAIKAMAD 257
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
70-321 |
7.98e-14 |
|
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: 70.40 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANSST 149
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 150 PLLITM-RPLDwQQLPVDYVGVDSHAGVREATEYLIQ--QGHRDIVFIGGL----THHMRYQGYLEAM-NHHGLQPWSTD 221
Cdd:cd06323 81 IPVITVdRSVT-GGKVVSHIASDNVAGGEMAAEYIAKklGGKGKVVELQGIpgtsAARERGKGFHNAIaKYPKINVVASQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AfslrAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGlfaGEDISLIG----NDGVAACAySNPPLTT 297
Cdd:cd06323 160 T----ADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGfdgtPDAVKAVK-DGKLAAT 231
|
250 260
....*....|....*....|....*..
gi 447052526 298 IAVEPL---ALGKQAAQQILRRIAQPD 321
Cdd:cd06323 232 VAQQPEemgAKAVETADKYLKGEKVPK 258
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
70-285 |
1.10e-13 |
|
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: 70.33 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQrsDRQKQVLD--TLLEHHVAGIVLCPVNSTS-EADLQRYAN 146
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQ--DQEKQINDirDLIAQGVDAILISPIDATGwDPVLKEAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 147 SSTPLLITMRPLD--WQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLTHHM-------RYQGYLEAM-NHHGLQ 216
Cdd:cd06309 79 AGIPVILVDRTIDgeDGSLYVTFIGSDFVEEGRRAAEWLVKNYKGGKGNVVELQGTAgssvaidRSKGFREVIkKHPNIK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 217 PwstdAFSLRAEPTQANGYQLMQQLLDM-PSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDGV 285
Cdd:cd06309 159 I----VASQSGNFTREKGQKVMENLLQAgPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQ 224
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
70-287 |
9.33e-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: 380625 [Multi-domain] Cd Length: 275 Bit Score: 67.66 E-value: 9.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRS---DRQKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYA 145
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEANGYELLVKGIKQEtdiEQQIAIVENLIAQKVDAIVIAPADSKALVPvLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 146 NSSTPLL-ITMRpLDWQQL-----PVDYVGVDSHAGVREATEYLIQQ--GHRDIVFIGGLTHH----MRYQGYLEAMNHH 213
Cdd:cd19970 81 DAGIAVInIDNR-LDADALkeggiNVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGAdnaqQRKAGFLKAFEEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 214 GLQ-------PWSTDafslraeptqaNGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDGVA 286
Cdd:cd19970 160 GMKivasqsaNWEID-----------EANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGK--AGKVLVVGFDNIP 226
|
.
gi 447052526 287 A 287
Cdd:cd19970 227 A 227
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
70-284 |
9.24e-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: 64.49 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVM-SNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYANS 147
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNVELIvTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPvVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 STPLLITMRPLDwqQLPVD-YVGVDSHAGVREATEYLIQQ--GHRDIVFIGGL----THHMRYQGYLEAMNHHglqPWST 220
Cdd:cd06308 81 GIPVIVLDRKVS--GDDYTaFIGADNVEIGRQAGEYIAELlnGKGNVVEIQGLpgssPAIDRHKGFLEAIAKY---PGIK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447052526 221 DAFSLRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDG 284
Cdd:cd06308 156 IVASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGR--EKEIKIIGVDG 217
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
70-312 |
1.10e-11 |
|
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: 64.27 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNST-SEADLQRYANSS 148
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADaSIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFI------GGLTHHMRYQGYLEAM-NHHGLQPWSTD 221
Cdd:cd19967 81 IPVFLIDREINAEGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVellgkeSDTNAQLRSQGFHSVIdQYPELKMVAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 222 AfslrAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDG---VAACAYSNPPLTTI 298
Cdd:cd19967 161 S----ADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDGsndVRDAIKEGKISATV 234
|
250
....*....|....
gi 447052526 299 AVEPLALGKQAAQQ 312
Cdd:cd19967 235 LQPAKLIARLAVEQ 248
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
70-286 |
2.37e-11 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 63.76 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQrSDRQKQV--LDTLLEHHVAGIVLCPVNST----------- 136
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGKIELEIYDAQ-NDQSTQNdqIDTMIAKGVDLLVVNLVDRTaaqtiidkaka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 137 ------------SEADLQRYANSstpllitmrpldWqqlpvdYVGVDSH-AGVREA---TEYLIQQGHRD---------I 191
Cdd:cd01539 81 anipviffnrepSREDLKSYDKA------------Y------YVGTDAEeSGIMQGeiiADYWKANPEIDkngdgkiqyV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 192 VFIGGLTHH---MRYQGYLEAMNHHG--LQPWSTDAfslrAEPTQANGYQLMQQLLDMPSPPT-AVICYNDLMAFGAESA 265
Cdd:cd01539 143 MLKGEPGHQdaiARTKYSVKTLNDAGikTEQLAEDT----ANWDRAQAKDKMDAWLSKYGDKIeLVIANNDDMALGAIEA 218
|
250 260
....*....|....*....|....
gi 447052526 266 LGERGLFAGE---DISLIGNDGVA 286
Cdd:cd01539 219 LKAAGYNTGDgdkYIPVFGVDATP 242
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
70-287 |
7.27e-11 |
|
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: 61.90 E-value: 7.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGF-ITVMSNtsqRSDRQKQV--LDTLLEHHVAGIVLCPVNSTSEAD-LQRYA 145
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVdLVVLDG---NGDVSTQInqVDTLIAQGVDAIIVVPVDADALAPaVEKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 146 NSSTPLLITMRPLDwQQLPVDYVGVDSHAGVREATEYLIQQ--GHRDIVFIGGLTHH----MRYQGYLEAMNHH------ 213
Cdd:cd06313 78 EAGIPLVGVNALIE-NEDLTAYVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQsaqiDRGKGIENVLKKYpdikvl 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447052526 214 GLQP--WStdafslRAEptqanGYQLMQQLLDM-PSPPTAVICYNDLMAFGAESALGERGLfagEDISLIGNDGVAA 287
Cdd:cd06313 157 AEQTanWS------RDE-----AMSLMENWLQAyGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDGIED 219
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
70-285 |
2.94e-10 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 60.09 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYANSS 148
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPaIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQlPVDYVGVDSHAGVREATEYLIQQ--GHRDIVFIGGL----THHMRYQGYleamnHHGLQPwsTDA 222
Cdd:cd19968 81 IPVVTVDRRAEGAA-PVPHVGADNVAGGREVAKFVVDKlpNGAKVIELTGTpgssPAIDRTKGF-----HEELAA--GPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447052526 223 FSLRAEPT----QANGYQLMQQLLD-MPSPPTAVICYNDLMAFGAESALGERGLFAGeDISLIGNDGV 285
Cdd:cd19968 153 IKVVFEQTgnfeRDEGLTVMENILTsLPGPPDAIICANDDMALGAIEAMRAAGLDLK-KVKVIGFDAV 219
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
70-283 |
1.18e-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: 58.12 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGF--ITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYAN 146
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVkiIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDpLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 147 SSTPLLITMRPLDwQQLPVDYVGVDSHAGVREATEYLIQQ--GHRDIVFIGGL----THHMRYQGYLEAMnhhglqpwST 220
Cdd:cd06310 81 KGIPVIVIDSGIK-GDAYLSYIATDNYAAGRLAAQKLAEAlgGKGKVAVLSLTagnsTTDQREEGFKEYL--------KK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447052526 221 DAFSLRAEPTQ------ANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGND 283
Cdd:cd06310 152 HPGGIKVLASQyagsdyAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKL--SGQIKIVGFD 218
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
69-284 |
3.86e-09 |
|
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: 56.86 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 69 LTIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQR-SDRQKQVLDTLLEHHVAGIVLCPVNSTSEADLQRYANS 147
Cdd:cd06301 1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEYPGVKLVIVDAQSdAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 S-TPLLITMRPLDWQQLPVDYVGVDSHAGVREATEYLIQQGHRD---IVFIGGLTHH---MRYQGYLEAMNHH-GLQ--- 216
Cdd:cd06301 81 AgIPLVYVNREPDSKPKGVAFVGSDDIESGELQMEYLAKLLGGKgniAILDGVLGHEaqiLRTEGNKDVLAKYpGMKiva 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447052526 217 ----PWStdafslRAEptqanGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDG 284
Cdd:cd06301 161 eqtaNWS------REK-----AMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGK--KDDILVAGIDA 219
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
70-315 |
7.64e-09 |
|
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: 55.76 E-value: 7.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQV--LDTLLEHHVAGIVLCPVNSTS-EADLQRYAN 146
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGAKVTVVDARYDLAKQFsqIDDFIAQGVDLILLNAADSAGiEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 147 SStpllITMRPLDWQQLPVD-YVGVDSHAGVREATEYLIQQ--GHRDIVFIGGL---THHMRYQGYLEAMNHHGLQPWST 220
Cdd:cd06321 81 AG----IIVVAVDVAAEGADaTVTTDNVQAGYLACEYLVEQlgGKGKVAIIDGPpvsAVIDRVNGCKEALAEYPGIKLVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 221 DAfslRAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfagEDISLIGNDG----VAACAYSNPPLT 296
Cdd:cd06321 157 DQ---NGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGR---DDIVITSVDGspeaVAALKREGSPFI 230
|
250 260
....*....|....*....|...
gi 447052526 297 -TIAVEPLALGKQA---AQQILR 315
Cdd:cd06321 231 aTAAQDPYDMARKAvelALKILN 253
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
171-281 |
2.51e-08 |
|
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: 54.53 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 171 DSHAGVREAtEYLIQQGHR-------DIVFIGGLTHHM----RYQGYLEAMNHHG----LQpwstdafSLRAEPTQANGY 235
Cdd:cd06324 118 NEQAGYLLA-KALIKAARKksddgkiRVLAISGDKSTPasilREQGLRDALAEHPdvtlLQ-------IVYANWSEDEAY 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 447052526 236 QLMQQLLDMpSPPTAVI-CYNDLMAFGAESALGERGLFAGEDIsLIG 281
Cdd:cd06324 190 QKTEKLLQR-YPDIDIVwAANDAMALGAIDALEEAGLKPGKDV-LVG 234
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
70-283 |
1.67e-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: 380659 [Multi-domain] Cd Length: 273 Bit Score: 51.85 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDR--QKQVLDTLLEHHVAGIVLCPVNSTS-EADLQRYAN 146
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPSREDDVeaQIQIIEYFIDQGVDGIVLAPLDRKAlVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 147 SSTPLLITMRPLDwQQLPVDYVGVDSHAGVREATEYLIQ--QGHRDIVFI----GGLTHHMRYQGYLEAMNHHGLQPW-S 219
Cdd:cd20004 81 QGIPVVIIDSDLG-GDAVISFVATDNYAAGRLAAKRMAKllNGKGKVALLrlakGSASTTDRERGFLEALKKLAPGLKvV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447052526 220 TDAFslrAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfAGeDISLIGND 283
Cdd:cd20004 160 DDQY---AGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGL-AG-KVKFIGFD 218
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
71-315 |
6.89e-07 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 49.95 E-value: 6.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 71 IGVVIDDLINPFFAEFTMGLEMTLAEHGF-ITVMS-NTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTS-EADLQRYANS 147
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVkVDVQAaPSETDTQGQLNLLETMLNKGYDAILVSPISDTNlIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 STPLLITMRPLDWQQLPVDYVGVDSHAGV------REATEYLIQQ--GHRDIVFIGGL----THHMRYQGYLEAMN-HHG 214
Cdd:cd06320 82 GIPVINLDDAVDADALKKAGGKVTSFIGTdnvaagALAAEYIAEKlpGGGKVAIIEGLpgnaAAEARTKGFKETFKkAPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 215 L-----QP--W-STDAFSLRAeptqangyQLMQQLLDMpsppTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDGV- 285
Cdd:cd06320 162 LklvasQPadWdRTKALDAAT--------AILQAHPDL----KGIYAANDTMALGAVEAVKAAGK--TGKVLVVGTDGIp 227
|
250 260 270
....*....|....*....|....*....|..
gi 447052526 286 -AACAYSNPPLT-TIAVEPLALGKQAAQQILR 315
Cdd:cd06320 228 eAKKSIKAGELTaTVAQYPYLEGAMAVEAALR 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
70-284 |
1.65e-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: 380627 [Multi-domain] Cd Length: 269 Bit Score: 48.98 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQ-KQVLDtLLEHHVAGIVLCPVNSTSEADLQRYANSS 148
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQvNQIQD-LITQNIDALIYIPAGATAAAVPVKAARAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITM--RPLDwqqLPVD-YVGVDSHAGVREATEYLIQQ--GHRDIVFI----GGLTHHMRYQGYLEAMNHHG----L 215
Cdd:cd19972 80 GIPVIAVdrNPED---APGDtFIATDSVAAAKELGEWVIKQtgGKGEIAILhgqlGTTPEVDRTKGFQEALAEAPgikvV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447052526 216 QPWSTDAFslraeptQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLfaGEDISLIGNDG 284
Cdd:cd19972 157 AEQTADWD-------QDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFDG 216
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
70-288 |
1.66e-06 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380480 [Multi-domain] Cd Length: 283 Bit Score: 48.96 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYANSS 148
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPvVAEAKAEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPL-----LITMRPLDWqqlpvdYVGVDS-HAGVREATEYLIQQGHRDIVFIGG--------LTH---HMRYQGYLEAMN 211
Cdd:cd01538 81 IKViaydrLILNADVDY------YISFDNeKVGELQAQALLDAKPEGNYVLIGGsptdnnakLFRdgqMKVLQPAIDSGK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447052526 212 HHGLQPWSTDAFSlraeptQANGYQLMQQLLDMPSPPT-AVICYNDLMAFGAESALGERGLFAGEDISliGNDG-VAAC 288
Cdd:cd01538 155 IKVVGDQWVDDWL------PANAQQIMENALTANGNNVdAVVASNDGTAGGAIAALKAQGLSGGVPVS--GQDAdLAAI 225
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
70-271 |
6.00e-06 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 47.02 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFiTVMSNTSQrSDRQKQVLDT--LLEHHVAGIVLCPVNSTSEADLQRYANS 147
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGV-ELVVTDAQ-NDLTKQISDVedLITRGVDVLILNPVDPEGLTPAVKAAKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 STPLLITM-RPLDWQQLPVDYVGVDSHAGVREATEYLIQQ-GHRDIVFI------GGLTHHMRYQGYLEAMNHHGLQPWS 219
Cdd:cd06318 79 AGIPVITVdSALDPSANVATQVGRDNKQNGVLVGKEAAKAlGGDPGKIIelsgdkGNEVSRDRRDGFLAGVNEYQLRKYG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 447052526 220 TDAFSLRAEP----TQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGL 271
Cdd:cd06318 159 KSNIKVVAQPygnwIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGM 214
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
164-338 |
7.85e-06 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 46.65 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 164 PVDYVGVDSHAGVREATEYLIQQGHRDIVFIGGLThhmRYQGYLEAMNHH--GLQPWSTDAFSLRAEPTQ--ANGYQLMQ 239
Cdd:cd06287 94 PVPYVDLQSAATARLLLEHLHGAGARQVALLTGSS---RRNSSLESEAAYlrFAQEYGTTPVVYKVPESEgeRAGYEAAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 240 QLLDMPSPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGN-DGVAAcAYSNPPLTTIAVEPLALGKQAAQQILRRIA 318
Cdd:cd06287 171 ALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRyDGIRA-RTADPPLTAVDLHLDRVARTAIDLLFASLS 249
|
170 180
....*....|....*....|
gi 447052526 319 QPDAPLsHYIYRPTLQIRAS 338
Cdd:cd06287 250 GEERSV-EVGPAPELVVRAS 268
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
70-336 |
8.35e-06 |
|
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: 46.81 E-value: 8.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDR-QKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYANS 147
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAeQVQLIEDLIARGVDGIAISPNDPEAVTPvINKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 148 STPLLITMRPLDwQQLPVDYVGVDSHAGVREATEYLIQQ---GHRDIVFIGGLT---HHMRYQGYLEAM-NHHGLQ---P 217
Cdd:cd06314 81 GIPVITFDSDAP-DSKRLAYIGTDNYEAGREAGELMKKAlpgGGKVAIITGGLGadnLNERIQGFKDALkGSPGIEivdP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 218 WSTDAFSLRAEptqangyQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGLFAgeDISLIG-----------NDGVA 286
Cdd:cd06314 160 LSDNDDIAKAV-------QNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVG--KVKIVGfdtlpetlqgiKDGVI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 447052526 287 AcaysnpplTTIAVEPLALGKQAAqQILRRIAQPDAPLSHYIYRPTLQIR 336
Cdd:cd06314 231 A--------ATVGQRPYEMGYLSV-KLLYKLLKGGKPVPDVIDTGVDVVT 271
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
70-315 |
1.18e-04 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 43.15 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGF-ITVMSNTSQRSDRQKQVLDtLLEHHVAGIVLCPVNSTSEADLQRYANSS 148
Cdd:PRK10653 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYnLVVLDSQNNPAKELANVQD-LTVRGTKILLINPTDSDAVGNAVKMANQA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDWQQLPVDYVGVDSHAGVREATEYLIQQGHRDIVFI------GGLTHHMRYQGYLEAMNHHGL-----QP 217
Cdd:PRK10653 107 NIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEGAKVIqlegiaGTSAARERGEGFKQAVAAHKFnvlasQP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 218 wstdafslrAEPTQANGYQLMQQLLDMPSPPTAVICYNDLMAFGAESALGERGlfaGEDISLIG----NDGVAACAySNP 293
Cdd:PRK10653 187 ---------ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGfdgtPDGIKAVN-RGK 253
|
250 260
....*....|....*....|....*
gi 447052526 294 PLTTIAVEPL---ALGKQAAQQILR 315
Cdd:PRK10653 254 LAATIAQQPDqigAIGVETADKVLK 278
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
113-332 |
1.45e-04 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 43.00 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 113 QKQVLDTLLEHHVAGIVLCPVNSTS-EADLQRYANSSTPLLITMRPLDWQQLPVDYVGVDSHAGVREATEYLIQQ--GHR 189
Cdd:cd20007 45 QTPIVNAVIAKKPDALLIAPTDPQAlIAPLKRAADAGIKVVTVDTTLGDPSFVLSQIASDNVAGGALAAEALAELigGKG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 190 DIVFIGGL----THHMRYQGYLEAMN-HHGLQPWSTDaFSlraEPTQANGYQLMQQLLdmPSPP--TAVICYNDLMAFGA 262
Cdd:cd20007 125 KVLVINSTpgvsTTDARVKGFAEEMKkYPGIKVLGVQ-YS---ENDPAKAASIVAAAL--QANPdlAGIFGTNTFSAEGA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 263 ESALGERGlfAGEDISLIGNDGvaacaysNPPL----------TTIAVEPLALGKQAAQQILRRIAqpDAPLSHYIYRPT 332
Cdd:cd20007 199 AAALRNAG--KTGKVKVVGFDA-------SPAQveqlkagtidALIAQKPAEIGYLAVEQAVAALT--GKPVPKDILTPF 267
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
94-323 |
1.78e-04 |
|
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: 42.62 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 94 LAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNSTSEAD-LQRYANSSTPL-----LITMRP-LDWqqlpvd 166
Cdd:cd19994 25 LEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDvLEEAKDAGIPViaydrLIMNTDaVDY------ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 167 YVGVDSHA-GVREAtEYLIQQ-------GHRDIVFIGG----LTHHMRYQGyleAMNHhgLQPWSTD-AFSLRAEPT--- 230
Cdd:cd19994 99 YVTFDNEKvGELQG-QYLVDKlglkdgkGPFNIELFAGspddNNAQLFFKG---AMEV--LQPYIDDgTLVVRSGQTtfe 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 231 --------QANGYQLMQQLLDMP----SPPTAVICYNDLMAFGAESALGERGLFAGEDISLIGNDG-VAACAY--SNPPL 295
Cdd:cd19994 173 qvatpdwdTETAQARMETLLSAYytggKKLDAVLSPNDGIARGVIEALKAAGYDTGPWPVVTGQDAeDASVKSilDGEQS 252
|
250 260
....*....|....*....|....*...
gi 447052526 296 TTIAVEPLALGKQAAqQILRRIAQPDAP 323
Cdd:cd19994 253 MTVFKDTRLLAKATV-ELVDALLEGEEV 279
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
70-323 |
6.75e-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: 37.74 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 70 TIGVVIDDLINPFFAEFTMGLEMTLAEHGFITVMSNTSQRSDRQKQVLDTLLEHHVAGIVLCPVNST-SEADLQRYANSS 148
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNgSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 149 TPLLITMRPLDwQQLPVDYVGVDSHAGVRE----ATEYLIQQ--GHRDIVFIGGLT---HHMRYQGYLEAMNHH-GLQPW 218
Cdd:cd06317 81 IPVIAYDAVIP-SDFQAAQVGVDNLEGGKEigkyAADYIKAElgGQAKIGVVGALSsliQNQRQKGFEEALKANpGVEIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052526 219 STDAFSLRAEPTQANGYQLMQQLLDMpsppTAVICYNDLMAFGAESALGERGlfAGEDISLIGNDGVAACAYS----NPP 294
Cdd:cd06317 160 ATVDGQNVQEKALSAAENLLTANPDL----DAIYATGEPALLGAVAAVRSQG--RQGKIKVFGWDLTKQAIFLgideGVL 233
|
250 260
....*....|....*....|....*....
gi 447052526 295 LTTIAVEPLALGKQAAQQILRRIAQPDAP 323
Cdd:cd06317 234 QAVVQQDPEKMGYEAVKAAVKAIKGEDVE 262
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
249-288 |
9.99e-03 |
|
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380646 [Multi-domain] Cd Length: 284 Bit Score: 37.22 E-value: 9.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 447052526 249 TAVICYNDLMAFGAESALGERGLfAGeDISLIGNDGV-AAC 288
Cdd:cd19991 187 DAVIASNDGTAGGAIQALAEQGL-AG-KVAVSGQDADlAAC 225
|
|
| |
