|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-335 |
3.06e-92 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 278.24 E-value: 3.06e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 1 MVTIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVFPpittsdRLSEPFF 80
Cdd:COG1609 3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVP------DLSNPFF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 81 MEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLMTNNLPFVIVGAPQGDTNkT 160
Cdd:COG1609 77 AELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPG-V 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 161 TYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPMLLFD-RKDPVSVEILMETI-- 237
Cdd:COG1609 156 PSVGVDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEgDFSAESGYEAARRLla 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 238 SSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSFKQLLDIINsNEQN 317
Cdd:COG1609 236 RGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIE-GPDA 314
|
330
....*....|....*...
gi 489079658 318 LSQTIFVPFSLKQRESVR 335
Cdd:COG1609 315 PPERVLLPPELVVRESTA 332
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
61-329 |
2.27e-82 |
|
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: 250.96 E-value: 2.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPPiTTSDRLSEPFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYL 140
Cdd:cd06294 1 TIGLVLPS-SAEELFQNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDPLIEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 141 MTNNLPFVIVGAPQgDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPML 220
Cdd:cd06294 80 KEEGFPFVVIGKPL-DDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 221 LF--DRKDPVSVEILMETISSFKA-TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVE 297
Cdd:cd06294 159 ILllDFSEEDGYDALQELLSKPPPpTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPY 238
|
250 260 270
....*....|....*....|....*....|..
gi 489079658 298 NLGKMSFKQLLDIINsNEQNLSQTIFVPFSLK 329
Cdd:cd06294 239 ELGREAAKLLINLLE-GPESLPKNVIVPHELI 269
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
61-328 |
5.26e-47 |
|
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: 159.60 E-value: 5.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIA-TGISLDDLIEQVKLMhLQKRVDGFIILYSDQDDPVKKY 139
Cdd:cd06267 1 TIGLIVPDISN------PFFAELLRGIEDAARERGYSLLLCnTDEDPEREREYLRLL-LSRRVDGIILAPSSLDDELLEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 140 LMTNNLPFVIVGAPqGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPM 219
Cdd:cd06267 74 LLAAGIPVVLIDRR-LDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 220 LLFDRKDPVS-----VEILMEtiSSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDI 294
Cdd:cd06267 153 LVVEGDFSEEsgyeaARELLA--LPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQ 230
|
250 260 270
....*....|....*....|....*....|....
gi 489079658 295 NVENLGKMSFKQLLDIINsNEQNLSQTIFVPFSL 328
Cdd:cd06267 231 PAYEMGRAAAELLLERIE-GEEEPPRRIVLPTEL 263
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
1-336 |
6.45e-42 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 148.72 E-value: 6.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 1 MVTIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVfppITTSDrlsEPFF 80
Cdd:PRK10703 1 MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLL---ATSSE---APYF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 81 MEILstitnEAKESHftvSIATGISL-----DDLIEQVKL---MHLQKRVDGFIILYSDQDDPVKKYLMTN-NLPFVIV- 150
Cdd:PRK10703 75 AEII-----EAVEKN---CYQKGYTLilcnaWNNLEKQRAylsMLAQKRVDGLLVMCSEYPEPLLAMLEEYrHIPMVVMd 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 151 -GAPQGDTNKTTyIDN--DNQLMAKtavEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPMLLFDRK-D 226
Cdd:PRK10703 147 wGEAKADFTDAI-IDNafEGGYLAG---RYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDfE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 227 PVSVEILMETISSFK--ATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSF 304
Cdd:PRK10703 223 PESGYEAMQQILSQKhrPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAF 302
|
330 340 350
....*....|....*....|....*....|...
gi 489079658 305 KQLLD-IINSNEQnlSQTIFVPFSLKQRESVRD 336
Cdd:PRK10703 303 NMLLDrIVNKREE--PQTIEVHPRLVERRSVAD 333
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
62-333 |
5.80e-37 |
|
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: 133.93 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPIttSDRLSEPFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLM 141
Cdd:cd06292 2 IGYVVPEL--PGGFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPRVRYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 142 TNNLPFVIVGAPQGDtNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPML- 220
Cdd:cd06292 80 EAGVPFVAFGRANPD-LDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 221 ----------------LFDRKDPVsveilmetissfkaTALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKL 284
Cdd:cd06292 159 vegenteeggyaaaarLLDLGPPP--------------TAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAF 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489079658 285 IHPYLTTFDINVENLGKMSFKQLLDIINSNEQNLSQTIFVPfSLKQRES 333
Cdd:cd06292 225 THPPLTTVRQPIDEIGRAVVDLLLAAIEGNPSEPREILLQP-ELVVRES 272
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
2-334 |
1.09e-36 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 134.74 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 2 VTIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVfppiTTSDRLSEPffM 81
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLA----TTSLALHAP--S 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 82 EILSTITNEAKESHFTVSIAT---------GISLDDLIEQvklmhlqkRVDGFIILYSDQDDPVKKYLMTN-NLPFVIVG 151
Cdd:PRK09526 80 QIAAAIKSRADQLGYSVVISMversgveacQAAVNELLAQ--------RVSGVIINVPLEDADAEKIVADCaDVPCLFLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 152 A-PQGDTNKTTYidnDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKtkpmllfdrkdPVSV 230
Cdd:PRK09526 152 VsPQSPVNSVSF---DPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQ-----------PIAV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 231 ---------------EILMETIssfKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDIN 295
Cdd:PRK09526 218 regdwsamsgyqqtlQMLREGP---VPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQD 294
|
330 340 350
....*....|....*....|....*....|....*....
gi 489079658 296 VENLGKMSFKQLLDIINSNEQNLSQTIfvPFSLKQRESV 334
Cdd:PRK09526 295 FRLLGKEAVDRLLALSQGQAVKGSQLL--PTSLVVRKST 331
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
61-333 |
5.79e-35 |
|
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: 128.44 E-value: 5.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIA-TGISLDDLIEQVKLMhLQKRVDGFIIlysdqdDPVK-- 137
Cdd:cd01541 1 TIGVITT------YIDDYIFPSIIQGIESVLSENGYSLLLAlTNNDVEKEREILESL-LDQNVDGLII------EPTKsa 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 ---------KYLMTNNLPFVIVGA--PQGDTNkttYIDNDNQLMAKTAVEHLYQKGHHNILFI--TDDLLSEvtsERYLG 204
Cdd:cd01541 68 lpnpnldlyEELQKKGIPVVFINSyyPELDAP---SVSLDDEKGGYLATKHLIDLGHRRIAGIfkSDDLQGV---ERYQG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 205 YLKGCFKRSLKTKP--MLLF---DRKDPVSVEILMETISSFK-ATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNN 278
Cdd:cd01541 142 FIKALREAGLPIDDdrILWYsteDLEDRFFAEELREFLRRLSrCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDD 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489079658 279 SNYAKLIHPYLTTFDINVENLGKMSFKQLLDIINSNEQNLSQtIFVPfSLKQRES 333
Cdd:cd01541 222 SYLASLSEPPLTSVVHPKEELGRKAAELLLRMIEEGRKPESV-IFPP-ELIERES 274
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-315 |
6.26e-35 |
|
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: 128.44 E-value: 6.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPPITTSDrlsEPFFMEILSTITNEAKESHFTVSIaTGISlDDLIEQVKLMHL--QKRVDGFIILySDQDDPVKK 138
Cdd:cd19974 1 NIAVLIPERFFGD---NSFYGKIYQGIEKELSELGYNLVL-EIIS-DEDEEELNLPSIisEEKVDGIIIL-GEISKEYLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YLMTNNLPFVIVGAPqGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLK--T 216
Cdd:cd19974 75 KLKELGIPVVLVDHY-DEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDINYTSSFMDRYLGYRKALLEAGLPpeK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 217 KPMLLFDRKDpvsVEILMETISSFKA----TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTF 292
Cdd:cd19974 154 EEWLLEDRDD---GYGLTEEIELPLKlmlpTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTV 230
|
250 260
....*....|....*....|...
gi 489079658 293 DINVENLGKMSFKQLLDIINSNE 315
Cdd:cd19974 231 EVDKEAMGRRAVEQLLWRIENPD 253
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
61-333 |
9.08e-35 |
|
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: 128.02 E-value: 9.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPpITTSDRLSEPFFMEILSTITNEAKESHFTVSIATGISLDDlieqvklMHLQKRVDGFIIL--YSDQDDpvkK 138
Cdd:cd01544 1 TIGIIQW-YSEEEELEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDL-------ESLLEKVDGIIAIgkFSKEEI---E 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YLMTNNLPFVIVGAPqGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFI-----TDDLLSEVTSERYLGYLKGCFKRS 213
Cdd:cd01544 70 KLKKLNPNIVFVDSN-PDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIggkeyTSDDGEEIEDPRLRAFREYMKEKG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 214 LKTKPMLLFDRKDPVS-VEILMETISSFK-ATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTT 291
Cdd:cd01544 149 LYNEEYIYIGEFSVESgYEAMKELLKEGDlPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489079658 292 FDINVENLGKMSFKQLLDIINsNEQNLSQTIFVPFSLKQRES 333
Cdd:cd01544 229 VHIPTEEMGRTAVRLLLERIN-GGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
62-333 |
1.35e-34 |
|
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: 127.25 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATgiSLDDL-IEQVKLMHL-QKRVDGfIILYSDQDDPvkKY 139
Cdd:cd06291 2 IGLIVPDISN------PFFAELAKYIEKELFKKGYKMILCN--SNEDEeKEKEYLEMLkRNKVDG-IILGSHSLDI--EE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 140 LMTNNLPFVIVGapQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPM 219
Cdd:cd06291 71 YKKLNIPIVSID--RYLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 220 LLfdRKDPVSVEILMETISSF-----KATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDI 294
Cdd:cd06291 149 EI--DENDFSEEDAYELAKELlekypDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQ 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 489079658 295 NVENLGKMSFKQLLDIINSNEQNLSQTIFvPFSLKQRES 333
Cdd:cd06291 227 PIEEMAKEAVELLLKLIEGEEIEESRIVL-PVELIERET 264
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-333 |
9.79e-33 |
|
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: 122.67 E-value: 9.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIA-TGISLDDLIEQVKLMhLQKRVDGFIILYSDQDDPVKKYL 140
Cdd:cd19975 2 IGVIIPDISN------SFFAEILKGIEDEARENGYSVILCnTGSDEEREKKYLQLL-KEKRVDGIIFASGTLTEENKQLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 141 MTNNLPFVIVGApQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVT-SERYLGYlkgcfKRSLKtkpm 219
Cdd:cd19975 75 KNMNIPVVLVST-ESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAgYPRYEGY-----KKALK---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 220 llfDRKDPVSVEILMETISSFK---------------ATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKL 284
Cdd:cd19975 145 ---DAGLPIKENLIVEGDFSFKsgyqamkrllknkklPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEM 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489079658 285 IHPYLTTFDINVENLGKMSFKQLLDIINSNEQNLSQtIFVPFSLKQRES 333
Cdd:cd19975 222 SIPPLTTVSQPFYEMGKKAVELLLDLIKNEKKEEKS-IVLPHQIIERES 269
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-333 |
1.12e-32 |
|
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: 122.36 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPPIttsdrlSEPFFMEILSTITNEAKESHFTVSIATgiSLDDL---IEQVKLMhLQKRVDGFIILYSD-QDDPV 136
Cdd:cd19976 1 TIGLIVPDI------SNPFFSELVRGIEDTLNELGYNIILCN--TYNDFereKKYIQEL-KERNVDGIIIASSNiSDEAI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 137 KKYLMTNNLPFVIVGaPQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKT 216
Cdd:cd19976 72 IKLLKEEKIPVVVLD-RYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 217 KPMLLFDRKDPVS--VEILMETISSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDI 294
Cdd:cd19976 151 DESWIYSGESSLEggYKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQ 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 489079658 295 NVENLGKMSFKQLLDIINSNEQNLSQTIFVPfSLKQRES 333
Cdd:cd19976 231 PIFEMGQEAAKLLLKIIKNPAKKKEEIVLPP-ELIKRDS 268
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
62-329 |
4.67e-32 |
|
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: 120.29 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIA-TGISLDDLIEQVKLMHlQKRVDGFIILYSDQDDPVKKYL 140
Cdd:cd01542 2 IGVIVP------RLDSYSTSRVLEGIDEVLKENGYQPLIAnTNLDEEREIEYLETLA-RQKVDGIILFATEITDEHRKAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 141 MTNNLPFVIVGapQgDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFIT---DDLlsEVTSERYLGYLKGCFKRSLKTK 217
Cdd:cd01542 75 KKLKIPVVVLG--Q-EHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGvdeEDI--AVGVARKQGYLDALKEHGIDEV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 218 PMLL--FDRKDpvSVEILMETISSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDIN 295
Cdd:cd01542 150 EIVEtdFSMES--GYEAAKELLKENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFD 227
|
250 260 270
....*....|....*....|....*....|....
gi 489079658 296 VENLGKMSFKQLLDIINSNEqnLSQTIFVPFSLK 329
Cdd:cd01542 228 YEEAGEKAAELLLDMIEGEK--VPKKQKLPYELI 259
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
75-333 |
3.58e-31 |
|
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: 118.41 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 75 LSEPFFMEILSTITNEAKESHFTVSIA----TGISLDDLIEQVKlmhlQKRVDGfIILYSDQDDPVKKYLMTNNLPFVIV 150
Cdd:cd06284 9 ISNPFYSEILRGIEDAAAEAGYDVLLGdtdsDPEREDDLLDMLR----SRRVDG-VILLSGRLDAELLSELSKRYPIVQC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 151 GAPQGDTNkTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPMLL----FDRKD 226
Cdd:cd06284 84 CEYIPDSG-VPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIiegdFSFEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 227 PVS-VEILMEtiSSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSFK 305
Cdd:cd06284 163 GYAaARALLA--LPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAAE 240
|
250 260
....*....|....*....|....*...
gi 489079658 306 QLLDIINSNEQNlSQTIFVPFSLKQRES 333
Cdd:cd06284 241 LLLEKIEGEGVP-PEHIILPHELIVRES 267
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
59-333 |
2.16e-29 |
|
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: 113.50 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 59 THNIGLVFPPITTSDR-LSEPFFMEILSTITNEAKESHFTVSIATgisLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVK 137
Cdd:cd06295 3 SRTIAVVVPMDPHGDQsITDPFFLELLGGISEALTDRGYDMLLST---QDEDANQLARLLDSGRADGLIVLGQGLDHDAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 KYLMTNNLPFVIVGAPQGDTNKTTyIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVtSERYLGYLKGCFKRSLKTK 217
Cdd:cd06295 80 RELAQQGLPMVVWGAPEDGQSYCS-VGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEV-ADRLQGYRDALAEAGLEAD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 218 PMLLFDRKDPV-----SVEILMETISSFKAtaLVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTF 292
Cdd:cd06295 158 PSLLLSCDFTEesgyaAMRALLDSGTAFDA--IFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489079658 293 DINVENLGKMSFKQLLDIINSNEQNLSQtifVPFSLKQRES 333
Cdd:cd06295 236 RQDLALAGRLLVEKLLALIAGEPVTSSM---LPVELVVRES 273
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-333 |
2.40e-29 |
|
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: 113.53 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIATGiSLDDLIEQVKL-MHLQKRVDGFIILYSD-QDDPVKK 138
Cdd:cd06282 1 TIGVLIP------SLNNPVFAEAAQGIQRAARAAGYSLLIATT-DYDPARELDAVeTLLEQRVDGLILTVGDaQGSEALE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YLMTNNLPFVIVGAPQGDTNKTTyIDNDNQLMAKTAVEHLYQKGHHNILFITDDL-LSEVTSERYLGYLKGCFKRSLKTK 217
Cdd:cd06282 74 LLEEEGVPYVLLFNQTENSSHPF-VSVDNRLASYDVAEYLIALGHRRIAMVAGDFsASDRARLRYQGYRDALKEAGLKPI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 218 PMLLFDRKDPVSVEILMETISSFKA-TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINV 296
Cdd:cd06282 153 PIVEVDFPTNGLEEALTSLLSGPNPpTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPS 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 489079658 297 ENLGKMSFKQLLDIINSNEQNlsQTIFVPFSLKQRES 333
Cdd:cd06282 233 RDMGRAAADLLLAEIEGESPP--TSIRLPHHLREGGS 267
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-333 |
3.88e-29 |
|
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: 112.71 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATGI-SLDDLIEQVKLMhLQKRVDGFIILYSDQDDPVKKyL 140
Cdd:cd06290 2 IGVLVPDIDS------PFYSEILNGIEEVLAESGYTLIVSTSHwNADRELEILRLL-LARKVDGIIVVGGFGDEELLK-L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 141 MTNNLPFVIVGAPQGDTNkTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYlkgcfKRSLKTKPMl 220
Cdd:cd06290 74 LAEGIPVVLVDRELEGLN-LPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGY-----RRALEDAGL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 221 lfdRKDPVSVEI----------LMETI----SSFkaTALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIH 286
Cdd:cd06290 147 ---EVDPRLIVEgdfteesgyeAMKKLlkrgGPF--TAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTT 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489079658 287 PYLTTFDINVENLGKMSFKQLLDIINSNEQNLSQTIfVPFSLKQRES 333
Cdd:cd06290 222 PPLTTVRQPLYEMGKTAAEILLELIEGKGRPPRRII-LPTELVIRES 267
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
62-333 |
2.72e-27 |
|
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: 108.11 E-value: 2.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVfppITTSdrlSEPFFMEILSTITNEAKESHFTVSIATGislDDLIEQVKL---MHLQKRVDGFIILYSDQDDPVKK 138
Cdd:cd06275 2 IGLL---VTSS---ENPFFAEVVRGVEDACFRAGYSLILCNS---DNDPEKQRAyldMLAEKRVDGLLLMCSEMTDDDAE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YL-MTNNLPFVIVGAPQGDTNkTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTK 217
Cdd:cd06275 73 LLaALRSIPVVVLDREIAGDN-ADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 218 PMLLFDRK-DPVSVEILMETISSF--KATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDI 294
Cdd:cd06275 152 PSWIVEGDfEPEGGYEAMQRLLSQppRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQ 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 489079658 295 NVENLGKMSFKQLLDIINSNEQNlSQTIFVPFSLKQRES 333
Cdd:cd06275 232 PKDELGELAVELLLDRIENKREE-PQSIVLEPELIERES 269
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
2-70 |
3.50e-27 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 101.51 E-value: 3.50e-27
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489079658 2 VTIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVFPPIT 70
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDIT 69
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-334 |
1.38e-26 |
|
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: 106.16 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIATgiSLDDLIEQVKLMH--LQKRVDGFIILYSDQDDPVKKY 139
Cdd:cd06285 2 IGVLVS------DLSNPFYAELVEGIEDAARERGYTVLLAD--TGDDPERELAALDslLSRRVDGLIITPARDDAPDLQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 140 LMTNNLPFVIVGAPQGDTNKTTYIdNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKP- 218
Cdd:cd06285 74 LAARGVPVVLVDRRIGDTALPSVT-VDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 219 MLLFDRKDPVSVEILMETI--SSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINV 296
Cdd:cd06285 153 RIVPGGFTIEAGREAAYRLlsRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPK 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 489079658 297 ENLGKMSFKQLLDIINSNEQNLSQTIFVPfSLKQRESV 334
Cdd:cd06285 233 YEMGRRAAELLLQLIEGGGRPPRSITLPP-ELVVREST 269
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
62-325 |
1.57e-26 |
|
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: 105.69 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPIttsdrlSEPFFMEILSTITNEAKESHFTVSIAtgiSLDD-------LIEqvklMHLQKRVDGFIILYSDQDD 134
Cdd:cd19977 2 IGLIVADI------LNPFFTSVVRGIEDEAYKNGYHVILC---NTDEdpekekkYIE----MLRAKQVDGIIIAPTGGNE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 135 PVKKYLMTNNLPFVIVG--APQGDTNkttYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKR 212
Cdd:cd19977 69 DLIEKLVKSGIPVVFVDryIPGLDVD---TVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 213 SLKTKPMLLFDRKDPVSVEILMETI--SSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLT 290
Cdd:cd19977 146 GLPVDEELIKHVDRQDDVRKAISELlkLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLT 225
|
250 260 270
....*....|....*....|....*....|....*
gi 489079658 291 TFDINVENLGKMSFKQLLDIINSNEQNLSQTIFVP 325
Cdd:cd19977 226 VIAQPTYEIGRKAAELLLDRIENKPKGPPRQIVLP 260
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
62-301 |
6.28e-26 |
|
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: 104.17 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpiTTSDRLSEPFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLM 141
Cdd:cd20010 2 IGLVLP--LDPGDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 142 TNNLPFVIVGAPQGDTNkTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPMLL 221
Cdd:cd20010 80 ERGIPFVVHGRSESGAP-YAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 222 F-DRKDPVSVEILMETISSFKA--TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITF-NNSNYAKLIHPYLTTFDINVE 297
Cdd:cd20010 159 ReGPLTEEGGYQAARRLLALPPppTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHdDLLPALEYFSPPLTTTRSSLR 238
|
....
gi 489079658 298 NLGK 301
Cdd:cd20010 239 DAGR 242
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
62-333 |
4.73e-25 |
|
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: 101.80 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTSdrlsepFFMEILSTITNEAKESHFTVSIA-TGISLDDLIEQVKLMhLQKRVDGFIILYSDQDDPVKKYL 140
Cdd:cd01575 2 VAVVVPSLSNS------VFAETLQGLSDVLEPAGYQLLLGnTGYSPEREEELIRAL-LSRRPAGLILTGTEHTPATRKLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 141 MTNNLPFV----IVGAPqgdtnkttyIDN----DNQLMAKTAVEHLYQKGHHNILFI-TDDLLSEVTSERYLGYLKGCFK 211
Cdd:cd01575 75 RAAGIPVVetwdLPDDP---------IDMavgfSNFAAGRAMARHLIERGYRRIAFVgARLDGDSRARQRLEGFRDALAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 212 RSLKTKPMLLFDRkdPVSVE---ILMETI--SSFKATALVVVGDVLAI-------RMvqllsfyDIKVPDDMSIITFNNS 279
Cdd:cd01575 146 AGLPLPLVLLVEL--PSSFAlgrEALAELlaRHPDLDAIFCSNDDLALgalfecqRR-------GIRVPGDIAIAGFGDL 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 489079658 280 NYAKLIHPYLTTFDINVENLGKMSFKQLLDIINsNEQNLSQTIFVPFSLKQRES 333
Cdd:cd01575 217 DIAAALPPALTTVRVPRYEIGRKAAELLLARLE-GEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
76-333 |
5.96e-25 |
|
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: 101.55 E-value: 5.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 76 SEPFFMEILSTITNEAKESHFTVSIATgISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLMTNNLPFVIVGApQG 155
Cdd:cd06277 17 ETPFFSELIDGIEREARKYGYNLLISS-VDIGDDFDEILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDN-YF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 156 DTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKT--KPMLLFDRKDPVSVEIL 233
Cdd:cd06277 95 EDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEdpEPEFVVSVGPEGAYKDM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 234 METISSFKA--TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSFKQLLDII 311
Cdd:cd06277 175 KALLDTGPKlpTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKI 254
|
250 260
....*....|....*....|..
gi 489079658 312 NsNEQNLSQTIFVPFSLKQRES 333
Cdd:cd06277 255 K-DPDGGTLKILVSTKLVERGS 275
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
61-313 |
8.22e-25 |
|
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: 101.18 E-value: 8.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATgiSLDDLIEQVKL--MHLQKRVDGFIILYSDQDDPVKK 138
Cdd:cd06280 1 TIGLIVPDITN------PFFTTIARGIEDAAEKHGYQVILAN--TDEDPEKEKRYldSLLSKQVDGIILAPSAGPSRELK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YLMTNNLPFVIVGApQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKP 218
Cdd:cd06280 73 RLLKHGIPIVLIDR-EVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 219 MLLF-----DRKDPVSVEILMETISSfkATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFD 293
Cdd:cd06280 152 SLIFegdstIEGGYEAVKALLDLPPR--PTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVA 229
|
250 260
....*....|....*....|
gi 489079658 294 INVENLGKMSFKQLLDIINS 313
Cdd:cd06280 230 QPAYEIGRIAAQLLLERIEG 249
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
62-333 |
1.43e-24 |
|
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: 100.70 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTSdrlsePFFMEILSTITNEAKESHFTVSIA-TGISLDDLIEQVKLMhLQKRVDGFII--LYSDQDDPVKK 138
Cdd:cd06288 2 IGLITDDIATT-----PFAGDIIRGAQDAAEEHGYLLLLAnTGGDPELEAEAIREL-LSRRVDGIIYasMHHREVTLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 ylmTNNLPFVIVGApQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKP 218
Cdd:cd06288 76 ---LTDIPLVLLNC-FDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 219 MLLFDRKDPVSV--EILMETISS-FKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDIN 295
Cdd:cd06288 152 SLVVHGDWGRESgyEAAKRLLSApDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALP 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 489079658 296 VENLGKMSFKQLLDIINSNEQnLSQTIFVPFSLKQRES 333
Cdd:cd06288 232 YYEMGRRAAELLLDGIEGEPP-EPGVIRVPCPLIERES 268
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
61-331 |
7.79e-24 |
|
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: 98.39 E-value: 7.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIATgiSLDDLIEQVKLMHL--QKRVDGFIILYSDQD-DPVK 137
Cdd:cd06286 1 TIGVVVP------YIDHPYFSQLINGIAEAAFKKGYQVLLLQ--TNYDKEKELRALELlkTKQIDGLIITSRENDwEVIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 KYLMTNnlPFVIVGAPQGDTNKTTYIDNDNQLMAktAVEHLYQKGHHNILFITD--DLLSEVTSERYLGYLKGCFKRSLK 215
Cdd:cd06286 73 PYAKYG--PIVLCEETDSPDIPSVYIDRYEAYLE--ALEYLKEKGHRKIGYCLGrpESSSASTQARLKAYQDVLGEHGLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 216 TKPMLLFDR----KDpvSVEILMETI-SSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHpyLT 290
Cdd:cd06286 149 LREEWIFTNchtiED--GYKLAKKLLaLKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELLN--LT 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489079658 291 TFDINVENLGKMSFKQLLDIINSNEQNlsqTIFVPFSLKQR 331
Cdd:cd06286 225 TIDQPLEEMGKEAFELLLSQLESKEPT---KKELPSKLIER 262
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-333 |
9.92e-24 |
|
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: 98.35 E-value: 9.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIAT-GISLDDLIEQVKLMhLQKRVDGFIILYSDQDDPVKKYL 140
Cdd:cd06273 2 IGAIVP------TLDNAIFARAIQALQQTLAEAGYTLLLATsEYDPARELEQVRAL-IERGVDGLILVGSDHDPELFELL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 141 MTNNLPFVIVGAPQGDTNKTTyIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLS-EVTSERYLGYLKGCFKRSLKTKPM 219
Cdd:cd06273 75 EQRQVPYVLTWSYDEDSPHPS-IGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGnDRARARLAGIRDALAERGLELPEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 220 LLFDRkdPVSVEilmETISSFKA--------TALVVVGDVLAI-------RMvqllsfyDIKVPDDMSIITFNNSNYAKL 284
Cdd:cd06273 154 RVVEA--PYSIE---EGREALRRllarpprpTAIICGNDVLALgalaecrRL-------GISVPEDLSITGFDDLELAAH 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489079658 285 IHPYLTTFDINVENLGKMSFKQLLDIINSNEQNLSQTIfvPFSLKQRES 333
Cdd:cd06273 222 LSPPLTTVRVPAREIGELAARYLLALLEGGPPPKSVEL--ETELIVRES 268
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
4-334 |
1.22e-23 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 99.39 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 4 IKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVfppITTSdrlSEPFFMEI 83
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGML---ITAS---TNPFYSEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 84 L-----------------STITNEAKESHftvsiatgiSLDDLieqvklmhLQKRVDGFIILYSDQDDPVKKYLMT-NNL 145
Cdd:PRK10423 75 VrgverscfergyslvlcNTEGDEQRMNR---------NLETL--------MQKRVDGLLLLCTETHQPSREIMQRyPSV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 146 PFVIVG-AP-QGDTNkttyIDNDNQLM-AKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTkpmllf 222
Cdd:PRK10423 138 PTVMMDwAPfDGDSD----LIQDNSLLgGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNI------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 223 drkdPVSVEIL--METISSFKAT-----------ALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYL 289
Cdd:PRK10423 208 ----PDGYEVTgdFEFNGGFDAMqqllalplrpqAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPL 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 489079658 290 TTFDINVENLGKMSFKQLLDIINSNEQNLSQTIFVPfSLKQRESV 334
Cdd:PRK10423 284 TTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTP-ELMERGSV 327
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
62-332 |
3.20e-23 |
|
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: 96.82 E-value: 3.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIATGISLDDLiEQVKLMHL-QKRVDGfIILYSD--QDDPVKK 138
Cdd:cd06270 2 IGLVVP------DLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEE-EREAIEFLlDRRCDA-IILHSRalSDEELIL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YlMTNNLPFVIVgapqgdtNKttYIDN--------DNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCF 210
Cdd:cd06270 74 I-AEKIPPLVVI-------NR--YIPGladrcvwlDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 211 KRSLKTKPML-----------------LFDRKDPVsveilmetissfkaTALVVVGDVLAIRMVQLLSFYDIKVPDDMSI 273
Cdd:cd06270 144 EAGIPLDPSLiiegdftieggyaaakqLLARGLPF--------------TALFAYNDDMAIGALAALHEAGIKVPEDVSV 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 489079658 274 ITFNNSNYAKLIHPYLTTFDINVENLGKMSFKQLLDIINsNEQNLSQTIFVPfSLKQRE 332
Cdd:cd06270 210 IGFDDVPLARYLSPKLTTVHYPIEEMAQAAAELALNLAY-GEPLPISHEFTP-TLIERD 266
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
62-333 |
6.42e-23 |
|
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: 96.19 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPIttsdrlSEPFFMEILSTITNEAKESHFTVSIATgiSLDDLIEQVKLMH--LQKRVDGFIILYSDQDDPVKKY 139
Cdd:cd06299 2 IGLLVPDI------RNPFFAELASGIEDEARAHGYSVILGN--SDEDPEREDESLEmlLSQRVDGIIAVPTGENSEGLQA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 140 LMTNNLPFVIVGAPQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPM 219
Cdd:cd06299 74 LIAQGLPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 220 LLF--DRKDPVSVEILMETIS-SFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINV 296
Cdd:cd06299 154 LVAfgDFRQDSGAAAAHRLLSrGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPV 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 489079658 297 ENLGKMSFKQLLDIINSNEQNLSQTIfvPFSLKQRES 333
Cdd:cd06299 234 ERIGRRAVELLLALIENGGRATSIRV--PTELIPRES 268
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
61-333 |
1.43e-22 |
|
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: 95.05 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 61 NIGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIAtgISLDDLIEQVKLMH--LQKRVDGFIILYSDQDDPVKK 138
Cdd:cd06298 1 TVGVIIPDISN------LYYAELARGIDDIATMYKYNIILS--NSDNNVDKELDLLNtmLSKQVDGIIFMGDELTEEIRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YLMTNNLPFVIVGAPQGDtNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSE-VTSERYLGYLKGCFKRSLKTK 217
Cdd:cd06298 73 EFKRSPVPVVLAGTVDSD-HEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYiNNDKKLQGYKRALEEAGLEFN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 218 PMLLFDRKDPV--SVEILMETISSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDIN 295
Cdd:cd06298 152 EPLIFEGDYDYdsGYELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQP 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 489079658 296 VENLGKMSFKQLLDIINsNEQNLSQTIFVPFSLKQRES 333
Cdd:cd06298 232 LYDIGAVAMRLLTKLMN-KEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
62-312 |
3.07e-22 |
|
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: 94.15 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATgiSLDDlIEQvKLMHLQK----RVDGFIILYSDQDDPVK 137
Cdd:cd06283 2 IGVIVADITN------PFSSLLLKGIEDVCREAGYQLLICN--SNND-PEK-ERDYIESllsqRVDGLILQPTGNNNDAY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 KYLMTNNLPFVIV----GAPQGDTNKTtyidnDNQLMAKTAVEHLYQKGHHNILFITDDLlSEVTS--ERYLGYLKGCfK 211
Cdd:cd06283 72 LELAQKGLPVVLVdrqiEPLNWDTVVT-----DNYDATYEATEHLKEQGYERIVFVTEPI-KGISTrrERLQGFLDAL-A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 212 RSLKTKPMLLFDRKDPvsvEILMETISSF------KATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLI 285
Cdd:cd06283 145 RYNIEGDVYVIEIEDT---EDLQQALAAFlsqhdgGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLI 221
|
250 260
....*....|....*....|....*..
gi 489079658 286 HPYLTTFDINVENLGKMSFKQLLDIIN 312
Cdd:cd06283 222 GPGITTIRQPTYEIGKAAAEILLERIE 248
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-205 |
3.08e-22 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 95.55 E-value: 3.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 2 VTIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVFppittSDrLSEPFFM 81
Cdd:PRK10014 7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIV-----RD-LSAPFYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 82 EILSTITnEAKESHFTVSIAT--GISLDDLIEQVKLMhLQKRVDGFIIL-YSDQDDPVKKYLMTNNLPFVIVGapqgdtn 158
Cdd:PRK10014 81 ELTAGLT-EALEAQGRMVFLLqgGKDGEQLAQRFSTL-LNQGVDGVVIAgAAGSSDDLREMAEEKGIPVVFAS------- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489079658 159 KTTYIDN------DNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGY 205
Cdd:PRK10014 152 RASYLDDvdtvrpDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGY 204
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-332 |
5.43e-22 |
|
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: 93.40 E-value: 5.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATgiSLDDLIEQ---VKLMhLQKRVDGFIIL-YSDQDDPVK 137
Cdd:cd06289 2 VGLIVPDLSN------PFFAELLAGIEEALEEAGYLVFLAN--TGEDPERQrrfLRRM-LEQGVDGLILSpAAGTTAELL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 KYLMTNNLPFVIVGAPQGDTnKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTK 217
Cdd:cd06289 73 RRLKAWGIPVVLALRDVPGS-DLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 218 PML-----------------LFDRKDPVsveilmetissfkaTALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSN 280
Cdd:cd06289 152 ESLivpgpatreagaeaareLLDAAPPP--------------TAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVP 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489079658 281 YAKLIHPYLTTFDINVENLGKMSFKQLLDIINSNEQNlSQTIFVPFSLKQRE 332
Cdd:cd06289 218 EAALWTPPLTTVSVHPREIGRRAARLLLRRIEGPDTP-PERIIIEPRLVVRE 268
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
62-325 |
2.41e-21 |
|
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: 91.72 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpitTSDRLSEPFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHlQKRVDGFIILYSDQDDPVKKYLM 141
Cdd:cd06271 2 IALVFP---VTETELNGTVSE*VSGITEEAGTTGYHLLVWPFEEAES*VPIRDLVE-TGSADGVILSEIEPNDPRVQFLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 142 TNNLPFVIVGAPQGDTNKTtYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPmLL 221
Cdd:cd06271 78 KQNFPFVAHGRSD*PIGHA-WVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGLTGYP-LD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 222 FDRKDPVSVEILMETI-SSFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNY-AKLIHPYLTTFDINVENL 299
Cdd:cd06271 156 ADTTLEAGRAAAQRLLaLSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFlGAMITPPLTTVHAPIAEA 235
|
250 260
....*....|....*....|....*.
gi 489079658 300 GKMSFKQLLDIINSNEQNLSQTIFVP 325
Cdd:cd06271 236 GRELAKALLARIDGEDPETLQVLVQP 261
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
62-333 |
1.43e-20 |
|
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: 89.56 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVfppittSDRLSEPFFMEILSTITNEAKESHFTVSIAT--GISLDDLIEQVKLMhLQKRVDGFIILYSDQDDPVKKY 139
Cdd:cd01574 2 IGVI------ATGLSLYGPASTLAGIERAARERGYSVSIATvdEDDPASVREALDRL-LSQRVDGIIVIAPDEAVLEALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 140 LMTNNLPFVIVGAPQGDTnkTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLktkpm 219
Cdd:cd01574 75 RLPPGLPVVIVGSGPSPG--VPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGL----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 220 llfdrkDPVSV-----------EILMETISSFKATALVVVGDVLA---IRMVQLLsfyDIKVPDDMSIITFNNSNYAKLI 285
Cdd:cd01574 148 ------PPPPVvegdwsaasgyRAGRRLLDDGPVTAVFAANDQMAlgaLRALHER---GLRVPEDVSVVGFDDIPEAAYF 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 489079658 286 HPYLTTFDINVENLGKMSFKQLLDIINSNEQnLSQTIFVPFSLKQRES 333
Cdd:cd01574 219 VPPLTTVRQDFAELGRRAVELLLALIEGPAP-PPESVLLPPELVVRES 265
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
5-56 |
3.79e-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: 82.46 E-value: 3.79e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489079658 5 KDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILAS 56
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
177-334 |
1.36e-19 |
|
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: 84.31 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 177 HLYQKGHHNILFIT--DDLLSEVTSERYLGYLKGCFKRSLKTKPML-LFDRKDPVSVEILMETISSFKATALVVVGDVLA 253
Cdd:pfam13377 1 HLAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGLDVEPTLyAGDDEAEAAAARERLRWLGALPTAVFVANDEVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 254 IRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSFKQLLDIINsNEQNLSQTIFVPFSLKQRES 333
Cdd:pfam13377 81 LGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLN-GEPAPPERVLLPPELVERES 159
|
.
gi 489079658 334 V 334
Cdd:pfam13377 160 T 160
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
1-291 |
2.41e-19 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 87.50 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 1 MVTIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVfppitTSDrLSEPFF 80
Cdd:PRK10727 1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLV-----VGD-VSDPFF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 81 MEILSTITNEAKESHFTVSIATGISLDD----LIEQVklmhLQKRVDGFIILYSDQDDPVKKYLMTNNLPFVIVgapqgd 156
Cdd:PRK10727 75 GAMVKAVEQVAYHTGNFLLIGNGYHNEQkerqAIEQL----IRHRCAALVVHAKMIPDAELASLMKQIPGMVLI------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 157 tNK------TTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPMLL-FDRKDPVS 229
Cdd:PRK10727 145 -NRilpgfeNRCIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVtFGEPDESG 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489079658 230 VEILM-ETISSFKA-TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTT 291
Cdd:PRK10727 224 GEQAMtELLGRGRNfTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTT 287
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
1-334 |
3.65e-18 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 84.06 E-value: 3.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 1 MVTIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVFPPIttsdrlSEPFF 80
Cdd:PRK10401 1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDV------SDAFF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 81 MEILSTITNEAKESHFTVSIATGI--------SLDDLIEQ---VKLMHLQKRVDGFIILYSDQDDPVkkYLMTNNLPfvi 149
Cdd:PRK10401 75 GALVKAVDLVAQQHQKYVLIGNSYheaekerhAIEVLIRQrcnALIVHSKALSDDELAQFMDQIPGM--VLINRVVP--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 150 vgapqGDTNKTTYIDNDNQlmAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLkTKPMLLFDRKDP-- 227
Cdd:PRK10401 150 -----GYAHRCVCLDNVSG--ARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGI-IPPESWIGTGTPdm 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 228 -----VSVEILMETIssfKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKM 302
Cdd:PRK10401 222 qggeaAMVELLGRNL---QLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKL 298
|
330 340 350
....*....|....*....|....*....|..
gi 489079658 303 SFKQLLDIINSNEQNLSQTIFVPfSLKQRESV 334
Cdd:PRK10401 299 ATELALQGAAGNLDPRASHCFMP-TLVRRHSV 329
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-334 |
6.64e-18 |
|
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: 82.29 E-value: 6.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATgiSLDDLIEQVKLMHL--QKRVDGFIILYSDQDDP-VKK 138
Cdd:cd06281 2 VGCLVSDISN------PLYARIVKAAEARLRAAGYTLLLAS--TGNDEERELELLSLfqRRRVDGLILTPGDEDDPeLAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YLMTNNLPFVIVG-APQGDTNKttyIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTK 217
Cdd:cd06281 74 ALARLDIPVVLIDrDLPGDIDS---VLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 218 PMLLfdRKDPVSVEI-------LMETISsfKATALVVVG-----DVL-AIRMVQLlsfydiKVPDDMSIITFNNSNYAKL 284
Cdd:cd06281 151 PDLV--RLGSFSADSgfreamaLLRQPR--PPTAIIALGtqllaGVLrAVRAAGL------RIPGDLSVVSIGDSDLAEL 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489079658 285 IHPYLTTFDINVENLGKMSFKQLLDIINSNEQNLSQTIFVPFSLKQRESV 334
Cdd:cd06281 221 HDPPITAIRWDLDAVGRAAAELLLDRIEGPPAGPPRRIVVPTELILRDSC 270
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
71-328 |
9.71e-18 |
|
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: 81.52 E-value: 9.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 71 TSDRLSEPFFMEILSTITNEAKESHFTVSIatGISLDDLIEQVKLMH--LQKRVDGFIILYSDQDDP-VKKYLMTNNLPF 147
Cdd:cd01537 5 TIYSYDDNFMSVIRKAIEQDAKQPGVQLLM--NDSQNDQEKQNDQIDvlLAKRVKGLAINLVDPAAAgVAEKARGQNVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 148 VIVGAPQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPMLLFDRK-D 226
Cdd:cd01537 83 VFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGDwD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 227 PVSVEILMETISS--FKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSF 304
Cdd:cd01537 163 TASGKDKMDQWLSgpNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKTTF 242
|
250 260
....*....|....*....|....
gi 489079658 305 KQLLDIINsNEQNLSQTIFVPFSL 328
Cdd:cd01537 243 DLLLNLAD-NWKIDNKVVRVPYVL 265
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
62-334 |
2.66e-17 |
|
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: 80.40 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLM 141
Cdd:cd06296 2 IDLVLP------QLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 142 TNNLPFVIVGAPQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYlkgcfkRS-------L 214
Cdd:cd06296 76 SAGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGY------RAalaeagiA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 215 KTKPMLLFDRKDPVSV-EILMETISSFK-ATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTF 292
Cdd:cd06296 150 VDPDLVREGDFTYEAGyRAARELLELPDpPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489079658 293 DINVENLGKMSFKQLLDIINsNEQNLSQTIFVPFSLKQRESV 334
Cdd:cd06296 230 HQPLREMGAVAVRLLLRLLE-GGPPDARRIELATELVVRGST 270
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
3-48 |
7.14e-17 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 73.44 E-value: 7.14e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489079658 3 TIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPN 48
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-333 |
9.46e-16 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 76.16 E-value: 9.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATgiSLDDLIEQVKL--MHLQKRVDGFIILYSDQDDPVKKY 139
Cdd:cd06293 2 IGLVVPDVSN------PFFAEVARGVEDAARERGYAVVLCN--SGRDPERERRYleMLESQRVRGLIVTPSDDDLSHLAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 140 LMTNNLPFVIVGAPQGDTNKTTyIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPM 219
Cdd:cd06293 74 LRARGTAVVLLDRPAPGPAGCS-VSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 220 LLFDRKDPVSVEI---LMETISSFKA--TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDI 294
Cdd:cd06293 153 VRELSAPDANAELgraAAAQLLAMPPrpTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQ 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 489079658 295 NVENLGKMSFKQLLDIINSNEQNLSQTIFVPfSLKQRES 333
Cdd:cd06293 233 PSYELGRAAADLLLDEIEGPGHPHEHVVFQP-ELVVRSS 270
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
62-333 |
2.45e-14 |
|
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: 71.82 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFppittsDRLSEPFFMEILSTITNEAKES--HFTVSIATGISlDDLIEQVKLMHLQKRVDGFIIL--YSDqDDPVK 137
Cdd:cd01545 2 IGLLY------DNPSASYVSALQVGALRACREAgyHLVVEPCDSDD-EDLADRLRRFLSRSRPDGVILTppLSD-DPALL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 KYLMTNNLPFVIVgAPQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFIT--DDLLSevTSERYLGYLKGCFKRSLK 215
Cdd:cd01545 74 DALDELGIPYVRI-APGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAgpPDHGA--SAERLEGFRDALAEAGLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 216 TKPML-----------------LFDRKDPvsveilmetissfkATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNN 278
Cdd:cd01545 151 LDPDLvvqgdftfesgleaaeaLLDLPDR--------------PTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDD 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489079658 279 SNYAKLIHPYLTTFDINVENLGKMSFKQLLDIInSNEQNLSQTIFVPFSLKQRES 333
Cdd:cd01545 217 SPIARLVWPPLTTVRQPIAEMARRAVELLIAAI-RGAPAGPERETLPHELVIRES 270
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
4-308 |
2.56e-14 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 72.75 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 4 IKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVFPPITTSdrlsepFFMEI 83
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQ------VFAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 84 LSTITNeAKESHFTVSIATGISLDDLIEQVKLMH-LQKRVDGFIILYSDQDDPVKKYLMTNNLPFVIVGAPQGDTNKTTy 162
Cdd:PRK14987 82 LRGIES-VTDAHGYQTMLAHYGYKPEMEQERLESmLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 163 IDNDNQLMAKTAVEHLYQKGHHNILFITDDlLSEVTSERYLGYLKGCFKRSLKTKPMLLFDRKDPVS-VEILMETISSF- 240
Cdd:PRK14987 160 VGFDNFEAARQMTTAIIARGHRHIAYLGAR-LDERTIIKQKGYEQAMLDAGLVPYSVMVEQSSSYSSgIELIRQARREYp 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489079658 241 KATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSFKQLL 308
Cdd:PRK14987 239 QLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLL 306
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
62-291 |
2.60e-14 |
|
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: 72.24 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpittsDRLSE----PFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVklmhLQKRVDGFIILYSDQDDPVK 137
Cdd:cd06279 2 IGVLLP-----DDLSYafsdPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAV----RNAAVDGFIVYGLSDDDPAV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 KYLMTNNLPFVIVGAPQGDtnKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLL-----------------SEVTSE 200
Cdd:cd06279 73 AALRRRGLPLVVVDGPAPP--GIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDrgrergpvsaerlaaatNSVARE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 201 RYLGYLKGCFKRSLKTKPMLLFDrkdpVSVEILMETISSFKA--------TALVVVGDVLAIRMVQLLSFYDIKVPDDMS 272
Cdd:cd06279 151 RLAGYRDALEEAGLDLDDVPVVE----APGNTEEAGRAAARAllaldprpTAILCMSDVLALGALRAARERGLRVPEDLS 226
|
250
....*....|....*....
gi 489079658 273 IITFNNSNYAKLIHPYLTT 291
Cdd:cd06279 227 VTGFDDIPEAAAADPGLTT 245
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-333 |
2.84e-14 |
|
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: 71.80 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVfppittSDRLSEPFFMEILSTITNEAKESHFTV---SIATGISLDDLIEQVklmhLQKRVDGFIILYSDQDDPVKK 138
Cdd:cd06278 2 VGVV------VGDLSNPFYAELLEELSRALQARGLRPllfNVDDEDDVDDALRQL----LQYRVDGVIVTSATLSSELAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 139 YLMTNNLPFVIVGaPQGDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCfKRSLKTKP 218
Cdd:cd06278 72 ECARRGIPVVLFN-RVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAAL-AELGLPPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 219 ML----------------LFDRKDPVsveilmetissfkaTALVVVGDVLAI----RMVQLLSfydIKVPDDMSIITFNN 278
Cdd:cd06278 150 AVeagdysyeggyeaarrLLAAPDRP--------------DAIFCANDLMALgaldAARQEGG---LVVPEDISVVGFDD 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489079658 279 ------SNYAklihpyLTTFDINVENLGKMSFKQLLDIINSNEQNlSQTIFVPFSLKQRES 333
Cdd:cd06278 213 ipmaawPSYD------LTTVRQPIEEMAEAAVDLLLERIENPETP-PERRVLPGELVERGS 266
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
62-332 |
3.47e-14 |
|
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: 71.64 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTSDRLSEpffmeILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLM 141
Cdd:cd06272 2 IGLYWPSVGERVALTR-----LLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVFGISDSDIEYLNKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 142 TNNLPFVIVGAPQGDTNkTTYIDNDnQLMAKtAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKRSLKTKPMLL 221
Cdd:cd06272 77 KPKIPIVLYNRESPKYS-TVNVDNE-KAGRL-AVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 222 FDRKDPVSV-EILMETISSFK--ATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVEN 298
Cdd:cd06272 154 DSRGLSIEGgDNAAKKLLKKKtlPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEK 233
|
250 260 270
....*....|....*....|....*....|....
gi 489079658 299 LGKMSFKQLLDIINSNEQNLSQTIFVPfSLKQRE 332
Cdd:cd06272 234 IAEESLRLILKLIEGRENEIQQLILYP-ELIFRE 266
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
62-333 |
6.27e-13 |
|
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: 67.88 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTsdrlsePFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLM 141
Cdd:cd06297 2 ISLLVPEVMT------PFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 142 TNNLPFVIVGApqgDTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFI----TDDLLSEVTSERYLGYLKGCFK--RSLK 215
Cdd:cd06297 76 PTEKPVVLIDA---NSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFgieeDTVFTETVFREREQGFLEALNKagRPIS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 216 TKPMLLFDRKDPVSVEILMETISSFKATALVVVG-DVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLihPYLTTFDI 294
Cdd:cd06297 153 SSRMFRIDNSSKKAECLARELLKKADNPAAFFAAaDLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTTVRQ 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 489079658 295 NVENLGKMSFKQLLDIINSNEQNlSQTIFVPFSLKQRES 333
Cdd:cd06297 231 PVEEMGEAAAKLLLKRLNEYGGP-PRSLKFEPELIVRES 268
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
28-335 |
1.19e-12 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 67.71 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 28 ISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVFPPIttsdrlSEPFFMEILSTITNEAKESHFTVSIAtgisld 107
Cdd:PRK11041 4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDI------CDPFFSEIIRGIEVTAAEHGYLVLIG------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 108 DLIEQ-------VKLMhLQKRVDGFIILYSDQDDPVKKYLMTNNLPFVIVG--APQGDTnKTTYIDNdnqLMAK-TAVEH 177
Cdd:PRK11041 72 DCAHQnqqektfVNLI-ITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANefAPELEL-PTVHIDN---LTAAfEAVNY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 178 LYQKGHHNILFIT---DDLLSEVtseRYLGYLKGCFKRSLKTKPMLLFdRKD------PVSVEILMETisSFKATALVVV 248
Cdd:PRK11041 147 LHELGHKRIACIAgpeEMPLCHY---RLQGYVQALRRCGITVDPQYIA-RGDftfeagAKALKQLLDL--PQPPTAVFCH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 249 GDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTT-----FDInvenlGKMSFKQLLDIINSNE-QNLSQti 322
Cdd:PRK11041 221 SDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTvaqprYEI-----GREAMLLLLEQLQGHHvSSGSR-- 293
|
330
....*....|...
gi 489079658 323 FVPFSLKQRESVR 335
Cdd:PRK11041 294 LLDCELIIRGSTA 306
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
79-319 |
2.71e-12 |
|
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: 65.91 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 79 FFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKlmhlqkrVDGFIILYSDQDDPVKKYLMTNNLPFVIVGAPQGDTN 158
Cdd:cd06287 21 FMMEVAAAAAEEALEHDLALVLVPPLHHVSMLDALD-------VDGAIVVEPTVEDPILARLRQRGVPVVSIGRAPGTDE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 159 KTTYIDNDNQLMAKTAVEHLYQKGHHNILFITDDLLSEVTSERYLGYLKGCFKR----SLKTKPMLLFDRKDPVSVEILM 234
Cdd:cd06287 94 PVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRFAQEYgttpVVYKVPESEGERAGYEAAAALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 235 ETISSFKatALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSFKQLLDIINSN 314
Cdd:cd06287 174 AAHPDID--AVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGE 251
|
....*
gi 489079658 315 EQNLS 319
Cdd:cd06287 252 ERSVE 256
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
1-335 |
3.45e-12 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 66.32 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 1 MVTIKDVAQKAGVNPSTVSRVLKDNRSISMK--TKEKVRKAMADLGYVPNVAAQIL-ASGLTHNIGLVFpPITTSDRLSE 77
Cdd:PRK10339 1 MATLKDIAIEAGVSLATVSRVLNDDPTLNVKeeTKHRILEIAEKLEYKTSSARKLQtGAVNQHHILAIY-SYQQELEIND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 78 PFFMEILSTITNEAKEshftvsiaTGISLDDLIEQVKLMHLQKrVDGfiILYSDQDDPVKKYL---MTNNLPFVIVGAPQ 154
Cdd:PRK10339 80 PYYLAIRHGIETQCEK--------LGIELTNCYEHSGLPDIKN-VTG--ILIVGKPTPALRAAasaLTDNICFIDFHEPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 155 GDTNKttyIDNDNQLMAKTAVEHLYQKGHHNILFI---TDDLLSEVTSERYLGYlkGCFKRSLKTKPMLLFDRKDPVSVE 231
Cdd:PRK10339 149 SGYDA---VDIDLARISKEIIDFYINQGVNRIGFIggeDEPGKADIREVAFAEY--GRLKQVVREEDIWRGGFSSSSGYE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 232 ILMETIS-SFKATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYLTTFDINVENLGKMSFKQLLDI 310
Cdd:PRK10339 224 LAKQMLArEDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEK 303
|
330 340
....*....|....*....|....*
gi 489079658 311 INsNEQNLSQTIFVPFSLKQRESVR 335
Cdd:PRK10339 304 AR-DGRALPLLVFVPSKLKLRGTTR 327
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
59-332 |
3.38e-11 |
|
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).
Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 62.91 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 59 THNIGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVS-IATGISLDDLIEQVKLMhLQKRVDGFIILYSDQDDP-V 136
Cdd:pfam00532 1 TLKLGALVP------QLDEPFFQDLVKGITKAAKDHGFDVFlLAVGDGEDTLTNAIDLL-LASGADGIIITTPAPSGDdI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 137 KKYLMTNNLPFVIVGApQGDTNKT--TYIDNDNQlMAKTAVEHLYQKGHHNILFITDDLLSEVTSER----YLGYLKGCf 210
Cdd:pfam00532 74 TAKAEGYGIPVIAADD-AFDNPDGvpCVMPDDTQ-AGYESTQYLIAEGHKRPIAVMAGPASALTARErvqgFMAALAAA- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 211 KRSLKTKPMLLFDRKDPVSVEILMETISS---FKA----TALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAK 283
Cdd:pfam00532 151 GREVKIYHVATGDNDIPDAALAANAMLVShptIDAivamNDEAAMGAVRALLKQGRVKIPDIVGIGINSVVGFDGLSKAQ 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489079658 284 LIHPY---LTTFDINVENLGKMSFKQLLDIINSNEQNlSQTIFVPFSLKQRE 332
Cdd:pfam00532 231 DTGLYlspLTVIQLPRQLLGIKASDMVYQWIPKFREH-PRVLLIPRDFFKET 281
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
62-325 |
8.47e-11 |
|
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: 61.40 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPPITTSDrlsePFFMEILSTITNEAKESHFTVSIATGISLDDLIEQVKLMHLQKRVDGFIILYSDQDDPVKKYLM 141
Cdd:cd20009 2 IALVLPTEDEID----GFTSQLISGISEALRGTPYHLVVTPEFPGDDPLEPVRYIVENRLADGIIISHTEPQDPRVRYLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 142 TNNLPFVIvgapQGDTNKTT---YIDNDNQLMAKTAVEHLYQKGHHNILFITDDllSEVTSERYLgyLKGcFKRSLKTKP 218
Cdd:cd20009 78 ERGFPFVT----HGRTELSTphaYFDFDNEAFAYEAVRRLAARGRRRIALVAPP--RELTYAQHR--LRG-FRRALAEAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 219 MLLFDRkDPVSVEILMETISSF---------KATALVVVGDVLAIRMVQLLSFYDIKVPDDMSIITFNNSNYAKLIHPYL 289
Cdd:cd20009 149 LEVEPL-LIVTLDSSAEAIRAAarrllrqppRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPI 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 489079658 290 TTFDINVENLGKMSFKQLLDIINSNEQNLSQTIFVP 325
Cdd:cd20009 228 DTLYEDIEEAGRFLAEALLRRIEGEPAEPLQTLERP 263
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
39-328 |
2.00e-07 |
|
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: 51.85 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 39 AMADLGYVPNVAAQILASGLTHNIGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIA-TGISLDDLIEQVKLMh 117
Cdd:COG1879 13 ALALAACGSAAAEAAAAAAKGKTIGFVVK------TLGNPFFVAVRKGAEAAAKELGVELIVVdAEGDAAKQISQIEDL- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 118 LQKRVDGFIILYSDQD---DPVKKyLMTNNLPFVIVGAPQGDTNKTTYIDNDNQLMAKTAVEHLYQ--KGHHNILFITDD 192
Cdd:COG1879 86 IAQGVDAIIVSPVDPDalaPALKK-AKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKalGGKGKVAILTGS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 193 LLSEVTSERYLGylkgcFKRSLKTKPML--------LFDRKDpvSVEILMETISSF-KATALVVVGDVLAIRMVQLLSfy 263
Cdd:COG1879 165 PGAPAANERTDG-----FKEALKEYPGIkvvaeqyaDWDREK--ALEVMEDLLQAHpDIDGIFAANDGMALGAAQALK-- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489079658 264 DIKVPDDMSIITFNNSNYA-KLIH--PYLTTFDINVENLGKMSFKQLLDIINSNEqnLSQTIFVPFSL 328
Cdd:COG1879 236 AAGRKGDVKVVGFDGSPEAlQAIKdgTIDATVAQDPYLQGYLAVDAALKLLKGKE--VPKEILTPPVL 301
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
75-218 |
1.10e-06 |
|
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: 49.10 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 75 LSEPFFMEILSTITNEAKESHFTVSIATGISldDLIEQVKLMH--LQKRVDGFIILYSDQD---DPVKKyLMTNNLPFVI 149
Cdd:cd01536 9 LTNPFWVAVKKGAEAAAKELGVELVVLDAQG--DVAKQISQIEdlIAQGVDAIIIAPVDSEalvPAVKK-ANAAGIPVVA 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489079658 150 VG-APQGDTNKTTYIDNDN----QLMAKTAVEHLYQKGhhNILFITDDLLSEVTSERYLGylkgcFKRSLKTKP 218
Cdd:cd01536 86 VDtDIDGGGDVVAFVGTDNyeagKLAGEYLAEALGGKG--KVAILEGPPGSSTAIDRTKG-----FKEALKKYP 152
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
3-218 |
9.52e-06 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 46.79 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 3 TIKDVAQKAGVNPSTVSRVLK---DNRSISMKTKEKVRKAMADLGYVPNVAAQILASGLTHNIGLVFPpittsDrLSEPF 79
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIP-----D-LENTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 80 FMEILSTITNEAKESHFTVSIAtgiSLDDLIE---QVKLMHLQKRVDGFIILYS-DQDDPVKKYLMTNNLPfVIVGAPQG 155
Cdd:PRK11303 76 YARIAKYLERQARQRGYQLLIA---CSDDQPDnemRCAEHLLQRQVDALIVSTSlPPEHPFYQRLQNDGLP-IIALDRAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489079658 156 DTNKTTYIDNDNQLMAKTAVEHLYQKGHHNILFItdDLLSE--VTSERYLGylkgcFKRSLKTKP 218
Cdd:PRK11303 152 DREHFTSVVSDDQDDAEMLAESLLKFPAESILLL--GALPElsVSFEREQG-----FRQALKDDP 209
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
62-312 |
4.69e-05 |
|
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: 44.22 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 62 IGLVFPpittsdRLSEPFFMEILSTITNEAKESHFTVSIaTGISLDDLIEQVKLMH--LQKRVDGFIILYSDQD--DPVK 137
Cdd:pfam13407 1 IGVVPK------STGNPFFQAAEEGAEEAAKELGGEVIV-VGPAEADAAEQVAQIEdaIAQGVDAIIVAPVDPTalAPVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 138 KYLMTNNLPFVIVGAPQGDTNKTTYIDNDNQLMAKTAVEHLYQ--KGHHNILFITDDLLSEVTSERYLG---YLKGCFKr 212
Cdd:pfam13407 74 KKAKDAGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEalGGKGKVAILSGSPGDPNANERIDGfkkVLKEKYP- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489079658 213 SLKTKPMLLFDRKDP-VSVEILMETISSFKAT--ALVVVGDVLAIRMVQLLSfyDIKVPDDMSIITFNNSN-YAKLIHP- 287
Cdd:pfam13407 153 GIKVVAEVEGTNWDPeKAQQQMEALLTAYPNPldGIISPNDGMAGGAAQALE--AAGLAGKVVVTGFDATPeALEAIKDg 230
|
250 260
....*....|....*....|....*.
gi 489079658 288 -YLTTFDINVENLGKMSFKQLLDIIN 312
Cdd:pfam13407 231 tIDATVLQDPYGQGYAAVELAAALLK 256
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
3-40 |
6.01e-04 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 37.53 E-value: 6.01e-04
10 20 30
....*....|....*....|....*....|....*...
gi 489079658 3 TIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKAM 40
Cdd:cd00093 14 TQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKAL 51
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
3-36 |
9.52e-04 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 36.73 E-value: 9.52e-04
10 20 30
....*....|....*....|....*....|....
gi 489079658 3 TIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKV 36
Cdd:smart00530 12 TQEELAEKLGVSRSTLSRIENGKRKPSLETLKKL 45
|
|
| HipB |
COG1396 |
Transcriptional regulator, contains XRE-family HTH domain [Transcription]; |
3-39 |
1.89e-03 |
|
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
Pssm-ID: 441006 [Multi-domain] Cd Length: 83 Bit Score: 36.90 E-value: 1.89e-03
10 20 30
....*....|....*....|....*....|....*..
gi 489079658 3 TIKDVAQKAGVNPSTVSRVLKDNRSISMKTKEKVRKA 39
Cdd:COG1396 22 TQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKA 58
|
|
| |
