|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
3-320 |
4.93e-108 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 317.91 E-value: 4.93e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 3 AKLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIERL 82
Cdd:COG1609 4 VTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 83 EDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA---PIVAFDRNLA-PKIPIVSSDNF 158
Cdd:COG1609 84 EEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEagiPVVLIDRPLPdPGVPSVGVDNR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 159 EGGKLAARALVKAGCQRIVMITGyDNSDSPTGLRQLGFNYELDKKGIICP----VPNDLSLMRRELEIKSIISR-EKPDG 233
Cdd:COG1609 164 AGARLATEHLIELGHRRIAFIGG-PADSSSARERLAGYREALAEAGLPPDpelvVEGDFSAESGYEAARRLLARgPRPTA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 234 IFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGKTV-NRDYVLP 312
Cdd:COG1609 243 IFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDApPERVLLP 322
|
....*...
gi 504447938 313 VNLIAGGS 320
Cdd:COG1609 323 PELVVRES 330
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
62-320 |
1.45e-107 |
|
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: 314.07 E-value: 1.45e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEAPIVA 141
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYKKLNIPIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 142 FDRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSdSPTGLRQLGFNYELDKKGIICPV----PNDLSLMR 217
Cdd:cd06291 81 IDRYLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNN-SPANERYRGFEDALKEAGIEYEIieidENDFSEED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 218 RELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEIL 296
Cdd:cd06291 160 AYELAKELLEKyPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAVELL 239
|
250 260
....*....|....*....|....*
gi 504447938 297 LKKIKGKTV-NRDYVLPVNLIAGGS 320
Cdd:cd06291 240 LKLIEGEEIeESRIVLPVELIERET 264
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
62-316 |
4.94e-69 |
|
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: 215.84 E-value: 4.94e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA---P 138
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAagiP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLA-PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSdSPTGLRQLGFNYELDKKGIicPVPNDL---- 213
Cdd:cd06267 81 VVLIDRRLDgLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDL-STSRERLEGYRDALAEAGL--PVDPELvveg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 214 --------SLMRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPL 285
Cdd:cd06267 158 dfseesgyEAARELLA-----LPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPA 232
|
250 260 270
....*....|....*....|....*....|..
gi 504447938 286 DEIAKLCVEILLKKIKGKTV-NRDYVLPVNLI 316
Cdd:cd06267 233 YEMGRAAAELLLERIEGEEEpPRRIVLPTELV 264
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
63-316 |
2.99e-62 |
|
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: 198.52 E-value: 2.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII--SSSHNLgiEDYEKVEA--- 137
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIiaPTGGNE--DLIEKLVKsgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLaP--KIPIVSSDNFEGGKLAARALVKAGCQRIVMITgYDNSDSPTGLRQLGFNYELDKKGIicpvPNDLSL 215
Cdd:cd19977 80 PVVFVDRYI-PglDVDTVVVDNFKGAYQATEHLIELGHKRIAFIT-YPLELSTRQERLEGYKAALADHGL----PVDEEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 MR---RELEIKSIISR-----EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDE 287
Cdd:cd19977 154 IKhvdRQDDVRKAISEllkleKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYE 233
|
250 260 270
....*....|....*....|....*....|.
gi 504447938 288 IAKLCVEILLKKI--KGKTVNRDYVLPVNLI 316
Cdd:cd19977 234 IGRKAAELLLDRIenKPKGPPRQIVLPTELI 264
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
66-320 |
2.35e-58 |
|
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: 188.52 E-value: 2.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 66 IFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA--PIV-AF 142
Cdd:cd06284 5 LVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSKryPIVqCC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 143 DRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSpTGLRQLGFNYELDKKGIICP----VPNDLSLMRR 218
Cdd:cd06284 85 EYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVY-ARERLEGYRRALAEAGLPVDedliIEGDFSFEAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 219 ELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILL 297
Cdd:cd06284 164 YAAARALLALpERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAAELLL 243
|
250 260
....*....|....*....|....
gi 504447938 298 KKIKGKTV-NRDYVLPVNLIAGGS 320
Cdd:cd06284 244 EKIEGEGVpPEHIILPHELIVRES 267
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
3-303 |
4.04e-55 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 182.62 E-value: 4.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 3 AKLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIERL 82
Cdd:PRK10703 2 ATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 83 EDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII-------SSSHNLgIEDYEKVeaPIVAFD--RNLAPKIPIV 153
Cdd:PRK10703 82 EKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLvmcseypEPLLAM-LEEYRHI--PMVVMDwgEAKADFTDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 154 SSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGlRQLGFNYELDKKGIicPVPNDLsLMRRELEIKS-------II 226
Cdd:PRK10703 159 IDNAFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAG-RLAGFMKAMEEANI--KVPEEW-IVQGDFEPESgyeamqqIL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504447938 227 SREK-PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGK 303
Cdd:PRK10703 235 SQKHrPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNK 312
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-320 |
1.42e-54 |
|
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: 178.96 E-value: 1.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA---PI 139
Cdd:cd06285 2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAArgvPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 140 VAFDRNLA-PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGlRQLGFNYELDKKGI------ICPVPND 212
Cdd:cd06285 82 VLVDRRIGdTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRD-RLRGYRRALAEAGLpvpderIVPGGFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRELeiKSIISREK-PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKL 291
Cdd:cd06285 161 IEAGREAA--YRLLSRPErPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRR 238
|
250 260 270
....*....|....*....|....*....|
gi 504447938 292 CVEILLKKIKGKTV-NRDYVLPVNLIAGGS 320
Cdd:cd06285 239 AAELLLQLIEGGGRpPRSITLPPELVVRES 268
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
63-316 |
1.61e-54 |
|
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: 178.99 E-value: 1.61e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA----P 138
Cdd:cd06275 2 IGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAAlrsiP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLA-PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTGLRQL-GFNYELDKKGIICP----VPND 212
Cdd:cd06275 82 VVVLDREIAgDNADAVLDDSFQGGYLATRHLIELGHRRIGCITG--PLEHSVSRERLaGFRRALAEAGIEVPpswiVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRELEIKSIISRE-KPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKL 291
Cdd:cd06275 160 FEPEGGYEAMQRLLSQPpRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
|
250 260
....*....|....*....|....*.
gi 504447938 292 CVEILLKKIKGK-TVNRDYVLPVNLI 316
Cdd:cd06275 240 AVELLLDRIENKrEEPQSIVLEPELI 265
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
7-321 |
1.03e-53 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 178.74 E-value: 1.03e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 7 DVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIERLEDEL 86
Cdd:PRK10423 3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 87 FKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII---SSSHNLGIEDYEKVEA-PIVAFDrnLAP---KIPIVSSDNFE 159
Cdd:PRK10423 83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLllcTETHQPSREIMQRYPSvPTVMMD--WAPfdgDSDLIQDNSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 160 GGKLAARALVKAGCQRIVMITGYDNSdSPTGLRQLGFNYELDKKGIicPVPND------------LSLMRRELEIksiis 227
Cdd:PRK10423 161 GGDLATQYLIDKGYTRIACITGPLDK-TPARLRLEGYRAAMKRAGL--NIPDGyevtgdfefnggFDAMQQLLAL----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 228 REKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGKTVNR 307
Cdd:PRK10423 233 PLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQ 312
|
330
....*....|....*
gi 504447938 308 D-YVLPVNLIAGGSI 321
Cdd:PRK10423 313 QrLQLTPELMERGSV 327
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-320 |
2.14e-53 |
|
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: 175.90 E-value: 2.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDG-IISSSHNLGIEDYEKVEA--- 137
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGiIIASSNISDEAIIKLLKEeki 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPK-IPIVSSDNFEGGKLAARALVKAGCQRIVMITGyDNSDSPTGLRQLGFNYELDKKGIICpVPNDLSLM 216
Cdd:cd19976 81 PVVVLDRYIEDNdSDSVGVDDYRGGYEATKYLIELGHTRIGCIVG-PPSTYNEHERIEGYKNALQDHNLPI-DESWIYSG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 217 RRELE-----IKSIISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKL 291
Cdd:cd19976 159 ESSLEggykaAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
|
250 260 270
....*....|....*....|....*....|
gi 504447938 292 CVEILLKKIKGKTVN-RDYVLPVNLIAGGS 320
Cdd:cd19976 239 AAKLLLKIIKNPAKKkEEIVLPPELIKRDS 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-320 |
1.07e-48 |
|
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: 163.88 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLG---IEDYEKVEAP 138
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTeenKQLLKNMNIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRN-LAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGyDNSDSPTGL-RQLGFNYELDKKGI-ICP---VPND 212
Cdd:cd19975 81 VVLVSTEsEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISG-PLDDPNAGYpRYEGYKKALKDAGLpIKEnliVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRELEIKSIISREK-PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKL 291
Cdd:cd19975 160 FSFKSGYQAMKRLLKNKKlPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKK 239
|
250 260 270
....*....|....*....|....*....|
gi 504447938 292 CVEILLKKIKGKTV-NRDYVLPVNLIAGGS 320
Cdd:cd19975 240 AVELLLDLIKNEKKeEKSIVLPHQIIERES 269
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
62-316 |
2.05e-48 |
|
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: 163.08 E-value: 2.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIED---YEKVEAP 138
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEElilIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLaPKIPI--VSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTG-LRQLGFNYELDKKGIicPVPNDL-- 213
Cdd:cd06270 81 LVVINRYI-PGLADrcVWLDNEQGGRLAAEHLLDLGHRRIACITG--PLDIPDArERLAGYRDALAEAGI--PLDPSLii 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 214 ----SLMRRELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEI 288
Cdd:cd06270 156 egdfTIEGGYAAAKQLLARgLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEM 235
|
250 260
....*....|....*....|....*...
gi 504447938 289 AKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06270 236 AQAAAELALNLAYGEPLPISHEFTPTLI 263
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-320 |
2.33e-47 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 160.14 E-value: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII----SSSHNLGIEDYEKVEA 137
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLIltvgDAQGSEALELLEEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIV-AFDRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGyDNSDSPTG-LRQLGFNYELDKKGI--ICPVPNDL 213
Cdd:cd06282 81 PYVlLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAG-DFSASDRArLRYQGYRDALKEAGLkpIPIVEVDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 214 SLMRRELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLC 292
Cdd:cd06282 160 PTNGLEEALTSLLSGpNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGRAA 239
|
250 260
....*....|....*....|....*...
gi 504447938 293 VEILLKKIKGKTVNRDYVLPVNLIAGGS 320
Cdd:cd06282 240 ADLLLAEIEGESPPTSIRLPHHLREGGS 267
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-320 |
2.38e-47 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 160.01 E-value: 2.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNkEKDYLEMLAANQCDGIISSSHNLG---IEDYEKVEAP 138
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDGVIVTSATLSselAEECARRGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLA-PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTGL-RQLGFNYELDKKGIICPV--PNDLS 214
Cdd:cd06278 80 VVLFNRVVEdPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGG--PEGTSTSReRERGFRAALAELGLPPPAveAGDYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 215 ------LMRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQ-LELSIPDDLKIIGYDGT---AfiRHFYpELATIQQP 284
Cdd:cd06278 158 yeggyeAARRLLA-----APDRPDAIFCANDLMALGALDAARQeGGLVVPEDISVVGFDDIpmaA--WPSY-DLTTVRQP 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 504447938 285 LDEIAKLCVEILLKKIKGKTVN-RDYVLPVNLIAGGS 320
Cdd:cd06278 230 IEEMAEAAVDLLLERIENPETPpERRVLPGELVERGS 266
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-316 |
6.95e-47 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 158.93 E-value: 6.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII--SSSHNLGIEDYEKVEAPIV 140
Cdd:cd06290 2 IGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIvvGGFGDEELLKLLAEGIPVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 141 AFDRNLA-PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGlRQLGFNYELDKKGI-ICP---VPNDLSL 215
Cdd:cd06290 82 LVDRELEgLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQE-RYAGYRRALEDAGLeVDPrliVEGDFTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 MRRELEIKSIISREKP-DGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVE 294
Cdd:cd06290 161 ESGYEAMKKLLKRGGPfTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAAE 240
|
250 260
....*....|....*....|...
gi 504447938 295 ILLKKIKGK-TVNRDYVLPVNLI 316
Cdd:cd06290 241 ILLELIEGKgRPPRRIILPTELV 263
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-304 |
9.57e-47 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 158.59 E-value: 9.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA---P 138
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRArgtA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLAPK-IPIVSSDNFEGGKLAARALVKAGCQRIVMITGydnsdsPTGLRQLGFNYE----------LDKKGIIC 207
Cdd:cd06293 81 VVLLDRPAPGPaGCSVSVDDVQGGALAVDHLLELGHRRIAFVSG------PLRTRQVAERLAgaraavaeagLDPDEVVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 208 PVPNDLSLMR--RELEIKSIISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPL 285
Cdd:cd06293 155 ELSAPDANAElgRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPS 234
|
250
....*....|....*....
gi 504447938 286 DEIAKLCVEILLKKIKGKT 304
Cdd:cd06293 235 YELGRAAADLLLDEIEGPG 253
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
62-320 |
1.22e-45 |
|
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: 156.18 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII-----SSSHNLGIEDYEKVE 136
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIieptkSALPNPNLDLYEELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 137 A---PIVAFDRNLA-PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITgydNSDSPTG-LRQLGFNYELDKKGIicPVPN 211
Cdd:cd01541 81 KkgiPVVFINSYYPeLDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIF---KSDDLQGvERYQGFIKALREAGL--PIDD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 212 DLSLMRRELEIKSIISREK----------PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATI 281
Cdd:cd01541 156 DRILWYSTEDLEDRFFAEElreflrrlsrCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSV 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 504447938 282 QQPLDEIAKLCVEILLKKIKGKTVNRDYVLPVNLIAGGS 320
Cdd:cd01541 236 VHPKEELGRKAAELLLRMIEEGRKPESVIFPPELIERES 274
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
62-320 |
2.76e-45 |
|
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: 155.01 E-value: 2.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYA-ELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII--SSSHnlgiedyEKVEAP 138
Cdd:cd06288 1 TIGLITDDIATTPFAgDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIyaSMHH-------REVTLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNL--------APKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDsPTGLRQLGFNYELDKKGI----- 205
Cdd:cd06288 74 PELTDIPLvllncfddDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSL-ATRLRLAGYRAALAEAGIpydps 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 206 -ICPVPNDLSLMRRELeiKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQ 283
Cdd:cd06288 153 lVVHGDWGRESGYEAA--KRLLSApDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVAL 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 504447938 284 PLDEIAKLCVEILLKKIKGKTV-NRDYVLPVNLIAGGS 320
Cdd:cd06288 231 PYYEMGRRAAELLLDGIEGEPPePGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
62-318 |
2.11e-44 |
|
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: 152.41 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII---SSSHNLGIEDYEKVEAP 138
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIIlapSAGPSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNL-APKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSdSPTGLRQLGFNYELDKKGIicPVPNDLSL-- 215
Cdd:cd06280 81 IVLIDREVeGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEI-STTRERLAGYREALAEAGI--PVDESLIFeg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 -----MRRELeIKSIISREK-PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIA 289
Cdd:cd06280 158 dstieGGYEA-VKALLDLPPrPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIG 236
|
250 260 270
....*....|....*....|....*....|
gi 504447938 290 KLCVEILLKKIKGKTVN-RDYVLPVNLIAG 318
Cdd:cd06280 237 RIAAQLLLERIEGQGEEpRRIVLPTELIIR 266
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
3-316 |
7.22e-44 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 153.23 E-value: 7.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 3 AKLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNI-----SNVfyAE 77
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLalhapSQI--AA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 78 LIERLEDELfkqGYKTIICN-SEHDPNKEKDYLEMLAANQCDGIIsSSHNLGIEDYEKVEA-----PIVAFDRNLAPKIP 151
Cdd:PRK09526 84 AIKSRADQL---GYSVVISMvERSGVEACQAAVNELLAQRVSGVI-INVPLEDADAEKIVAdcadvPCLFLDVSPQSPVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 152 IVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSpTGLRQLGFNYELDKKGI-ICPVPN-DLSLM---RRELEIKSii 226
Cdd:PRK09526 160 SVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVS-ARLRLAGWLEYLTDYQLqPIAVREgDWSAMsgyQQTLQMLR-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 227 SREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGKTVN 306
Cdd:PRK09526 237 EGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQGQAVK 316
|
330
....*....|
gi 504447938 307 RDYVLPVNLI 316
Cdd:PRK09526 317 GSQLLPTSLV 326
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
62-316 |
2.84e-43 |
|
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: 149.62 E-value: 2.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII---SSSHNLGIEDYEKVEAP 138
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLIlqpTGNNNDAYLELAQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLAP-KIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGLRQLGF-----NYELDKKGIICPVPND 212
Cdd:cd06283 81 VVLVDRQIEPlNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRRERLQGFldalaRYNIEGDVYVIEIEDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRELEIKSIISREKPdGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLC 292
Cdd:cd06283 161 EDLQQALAAFLSQHDGGKT-AIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKAA 239
|
250 260
....*....|....*....|....*
gi 504447938 293 VEILLKKIKGKTVNRDYV-LPVNLI 316
Cdd:cd06283 240 AEILLERIEGDSGEPKEIeLPSELI 264
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
63-320 |
1.21e-42 |
|
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: 148.20 E-value: 1.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII---SSSHNLGIEDYEKVEAPI 139
Cdd:cd06299 2 IGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIavpTGENSEGLQALIAQGLPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 140 VAFDRNLA--PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTGL-RQLGFNYELDKKGIICPVPN----D 212
Cdd:cd06299 82 VFVDREVEglGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISG--PLSTSTGReRLAAFRAALTAAGIPIDEELvafgD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKL 291
Cdd:cd06299 160 FRQDSGAAAAHRLLSRgDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRR 239
|
250 260
....*....|....*....|....*....
gi 504447938 292 CVEILLKKIKGKTVNRDYVLPVNLIAGGS 320
Cdd:cd06299 240 AVELLLALIENGGRATSIRVPTELIPRES 268
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
63-316 |
5.79e-42 |
|
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: 146.15 E-value: 5.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLG---IEDYEKvEAPI 139
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDwevIEPYAK-YGPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 140 VAFDRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTG-LRQLGFNYELDKKGIicPVPNDLS---- 214
Cdd:cd06286 81 VLCEETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSSASTqARLKAYQDVLGEHGL--SLREEWIftnc 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 215 --------LMRRELEIKsiisrEKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRhfYPELATIQQPLD 286
Cdd:cd06286 159 htiedgykLAKKLLALK-----ERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISE--LLNLTTIDQPLE 231
|
250 260 270
....*....|....*....|....*....|
gi 504447938 287 EIAKLCVEILLKKIKGKTVNRdYVLPVNLI 316
Cdd:cd06286 232 EMGKEAFELLLSQLESKEPTK-KELPSKLI 260
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-320 |
1.34e-39 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 140.07 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSshnLGIED-------YEKV 135
Cdd:cd06281 2 VGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILT---PGDEDdpelaaaLARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 136 EAPIVAFDRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydNSDS-PTGLRQLGFNYELDKKGIicPVPNDL- 213
Cdd:cd06281 79 DIPVVLIDRDLPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTG--GPDIrPGRERIAGFKAAFAAAGL--PPDPDLv 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 214 ---------------SLMRREleiksiisrEKPDGIFVSDdlTAIL--VMKVVRQLELSIPDDLKIIGYDGTAFIRHFYP 276
Cdd:cd06281 155 rlgsfsadsgfreamALLRQP---------RPPTAIIALG--TQLLagVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDP 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 504447938 277 ELATIQQPLDEIAKLCVEILLKKIKGKTVN--RDYVLPVNLIAGGS 320
Cdd:cd06281 224 PITAIRWDLDAVGRAAAELLLDRIEGPPAGppRRIVVPTELILRDS 269
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
4-205 |
9.98e-38 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 136.93 E-value: 9.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 4 KLTDVAELAGVSPTTVSRVIN---KKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIE 80
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 81 RLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSShNLGIED--YEKVEA---PIVAFDRNL-APKIPIVS 154
Cdd:PRK11303 82 YLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVST-SLPPEHpfYQRLQNdglPIIALDRALdREHFTSVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504447938 155 SDNFEGGKLAARALVKAGCQRIVMITGY-DNSDSPtgLRQLGFNYELDKKGI 205
Cdd:PRK11303 161 SDDQDDAEMLAESLLKFPAESILLLGALpELSVSF--EREQGFRQALKDDPR 210
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
62-316 |
1.21e-37 |
|
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: 134.54 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYE---KVEAP 138
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKalkKLKIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLaPKIPIVSSDNFEGGKLAARALVKAGCQRIVMItGYDNSDSPTG-LRQLGFNYELDKKGIICP--VPNDLSL 215
Cdd:cd01542 81 VVVLGQEH-EGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYI-GVDEEDIAVGvARKQGYLDALKEHGIDEVeiVETDFSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 MRRELEIKSIISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEI 295
Cdd:cd01542 159 ESGYEAAKELLKENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAEL 238
|
250 260
....*....|....*....|.
gi 504447938 296 LLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd01542 239 LLDMIEGEKVPKKQKLPYELI 259
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
62-320 |
2.67e-36 |
|
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: 131.46 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII--SSSH---------NLGIe 130
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLIltGTEHtpatrkllrAAGI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 131 dyekveaPIV---AFDRNlapkiPI---VSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGLRQLGFNYELDKKG 204
Cdd:cd01575 80 -------PVVetwDLPDD-----PIdmaVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFRDALAEAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 205 ------IICPVPNDLSLMRRELEikSIISREK-PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPE 277
Cdd:cd01575 148 lplplvLLVELPSSFALGREALA--ELLARHPdLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 504447938 278 LATIQQPLDEIAKLCVEILLKKIKGKTVN-RDYVLPVNLIAGGS 320
Cdd:cd01575 226 LTTVRVPRYEIGRKAAELLLARLEGEEPEpRVVDLGFELVRRES 269
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-316 |
8.18e-35 |
|
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: 127.68 E-value: 8.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDG-IISSSHNLGIEDYEKVEA--- 137
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGlILSPAAGTTAELLRRLKAwgi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAP-KIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTGLRQL-GFNYELDKKGI------ICPV 209
Cdd:cd06289 81 PVVLALRDVPGsDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGG--LSDSSTRRERLaGFRAALAEAGLpldeslIVPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 210 PNDlslmRRE--LEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLD 286
Cdd:cd06289 159 PAT----REAgaEAARELLDAaPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPR 234
|
250 260 270
....*....|....*....|....*....|.
gi 504447938 287 EIAKLCVEILLKKIKG-KTVNRDYVLPVNLI 316
Cdd:cd06289 235 EIGRRAARLLLRRIEGpDTPPERIIIEPRLV 265
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-320 |
1.84e-33 |
|
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: 123.77 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII--SSSHNLGIEDY-EKVEAPI 139
Cdd:cd06273 2 IGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLIlvGSDHDPELFELlEQRQVPY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 140 V---AFDRnlAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGLRQLGFNYELDKKGI------ICPVP 210
Cdd:cd06273 82 VltwSYDE--DSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIRDALAERGLelpeerVVEAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 211 NDLS----LMRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLD 286
Cdd:cd06273 160 YSIEegreALRRLLA-----RPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAR 234
|
250 260 270
....*....|....*....|....*....|....
gi 504447938 287 EIAKLCVEILLKKIKGKTVNRDYVLPVNLIAGGS 320
Cdd:cd06273 235 EIGELAARYLLALLEGGPPPKSVELETELIVRES 268
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
3-72 |
2.20e-33 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 117.69 E-value: 2.20e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 3 AKLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISN 72
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
70-320 |
2.94e-33 |
|
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: 123.51 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 70 ISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAAnqcDGII---SSSHNLGIEDYEKVEAPIVAFDRNL 146
Cdd:cd06295 20 ITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLDSGRA---DGLIvlgQGLDHDALRELAQQGLPMVVWGAPE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 147 APKIPI-VSSDNFEGGKLAARALVKAGCQRIVMITgyDNSDSPTGLRQLGFNYELDKKGIicPVPNDLSLMR-------R 218
Cdd:cd06295 97 DGQSYCsVGSDNVKGGALATEHLIEIGRRRIAFLG--DPPHPEVADRLQGYRDALAEAGL--EADPSLLLSCdfteesgY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 219 ELEIKSIISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLK 298
Cdd:cd06295 173 AAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTVRQDLALAGRLLVEKLLA 252
|
250 260
....*....|....*....|..
gi 504447938 299 KIKGKTVNRDyVLPVNLIAGGS 320
Cdd:cd06295 253 LIAGEPVTSS-MLPVELVVRES 273
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
30-307 |
7.14e-33 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 123.57 E-value: 7.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 30 SQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYL 109
Cdd:PRK11041 5 SQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 110 EMLAANQCDGIISSSHNLGIeDYEKVEapivafDRNLAP-----------KIPIVSSDNFEGGKLAARALVKAGCQRIVM 178
Cdd:PRK11041 85 NLIITKQIDGMLLLGSRLPF-DASKEE------QRNLPPmvmanefapelELPTVHIDNLTAAFEAVNYLHELGHKRIAC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 179 ITGYDnsDSP-TGLRQLGFNYELDKKGI-ICP---VPNDLSLMRRELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQL 252
Cdd:PRK11041 158 IAGPE--EMPlCHYRLQGYVQALRRCGItVDPqyiARGDFTFEAGAKALKQLLDLpQPPTAVFCHSDVMALGALSQAKRM 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 504447938 253 ELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGKTVNR 307
Cdd:PRK11041 236 GLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSS 290
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
62-320 |
3.27e-32 |
|
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: 120.38 E-value: 3.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICN-SEHDPNKEKDYLEMLAANQCDGII-SSSHNLGIEDYEKVEA-- 137
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATvDEDDPASVREALDRLLSQRVDGIIvIAPDEAVLEALRRLPPgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGlRQLGFNYELDKKGI--ICPVPNDLSL 215
Cdd:cd01574 81 PVVIVGSGPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARA-RLRGWREALEEAGLppPPVVEGDWSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 MRRELEIKSIISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEI 295
Cdd:cd01574 160 ASGYRAGRRLLDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRAVEL 239
|
250 260
....*....|....*....|....*.
gi 504447938 296 LLKKIKGKTVNRD-YVLPVNLIAGGS 320
Cdd:cd01574 240 LLALIEGPAPPPEsVLLPPELVVRES 265
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
62-316 |
8.38e-32 |
|
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor
Pssm-ID: 380498 [Multi-domain] Cd Length: 264 Bit Score: 119.62 E-value: 8.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYE---KVEAP 138
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYlcqAAGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNLAP-KIPIVSSDNFEGGKLAARALVKAGCQRIVMITGyDNSDSPTGLRQLGFNYELDKKGIICPVPNDLS--- 214
Cdd:cd06274 81 VVFLDRPFSGsDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGG-RPELPSTAERIRGFRAALAEAGITEGDDWILAegy 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 215 -------LMRRELEiksiISREKPDGIFVSDdlTAIL--VMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPL 285
Cdd:cd06274 160 dresgyqLMAELLA----RLGGLPQALFTSS--LTLLegVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDH 233
|
250 260 270
....*....|....*....|....*....|.
gi 504447938 286 DEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06274 234 DEIAEHAFELLDALIEGQPEPGVIIIPPELI 264
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
5-321 |
1.28e-31 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 120.52 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 5 LTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIERLED 84
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 85 ELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA---PIVAFDRNLAPKIPI-VSSDNFEG 160
Cdd:PRK14987 88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVagiPVVELMDSQSPCLDIaVGFDNFEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 161 GKLAARALVKAGCQRIVMITGydNSDSPTGLRQLGFNYELDKKGII--CPVPNDLSLMRRELEIKSIISREKP--DGIFV 236
Cdd:PRK14987 168 ARQMTTAIIARGHRHIAYLGA--RLDERTIIKQKGYEQAMLDAGLVpySVMVEQSSSYSSGIELIRQARREYPqlDGVFC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 237 SDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGKTVNRDYV-LPVNL 315
Cdd:PRK14987 246 TNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKMLdLGFTL 325
|
....*.
gi 504447938 316 IAGGSI 321
Cdd:PRK14987 326 SPGGSI 331
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
1-195 |
7.35e-31 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 118.66 E-value: 7.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 1 MVAK---LTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAE 77
Cdd:PRK10014 2 ATAKkitIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 78 LIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII------SSSHNLgiedyEKVEA---PIVAFDR-NLA 147
Cdd:PRK10014 82 LTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVViagaagSSDDLR-----EMAEEkgiPVVFASRaSYL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504447938 148 PKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTGLRQLG 195
Cdd:PRK10014 157 DDVDTVRPDNMQAAQLLTEHLIRNGHQRIAWLGG--QSSSLTRAERVG 202
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-320 |
1.07e-30 |
|
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: 116.50 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNI---SNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISsshnLGI--EDY-EKVE 136
Cdd:cd19974 2 IAVLIPERffgDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIII----LGEisKEYlEKLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 137 A---PIVAFDrNLAPKIPI--VSSDNFEGGKLAARALVKAGCQRIVMItGYDNSDSPTGLRQLGFN--------YELDKK 203
Cdd:cd19974 78 ElgiPVVLVD-HYDEELNAdsVLSDNYYGAYKLTSYLIEKGHKKIGFV-GDINYTSSFMDRYLGYRkalleaglPPEKEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 204 GIICPVPNDLSLMrreLEIKSIISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQ 283
Cdd:cd19974 156 WLLEDRDDGYGLT---EEIELPLKLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEV 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 504447938 284 PLDEIAKLCVEILLKKIKGK-TVNRDYVLPVNLIAGGS 320
Cdd:cd19974 233 DKEAMGRRAVEQLLWRIENPdRPFEKILVSGKLIERDS 270
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
62-320 |
2.08e-30 |
|
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: 115.83 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNI----SNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYE---K 134
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPRVRylhE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 135 VEAPIVAFDR-NLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTGL-RQLGFNYELDKKGIicPVPND 212
Cdd:cd06292 81 AGVPFVAFGRaNPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGG--PEGSVPSDdRLAGYRAALEEAGL--PFDPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 L------------SLMRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELAT 280
Cdd:cd06292 157 LvvegenteeggyAAAARLLD-----LGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTT 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 504447938 281 IQQPLDEIAKLCVEILLKKIKGKTVN-RDYVLPVNLIAGGS 320
Cdd:cd06292 232 VRQPIDEIGRAVVDLLLAAIEGNPSEpREILLQPELVVRES 272
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
63-320 |
1.05e-29 |
|
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: 113.92 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA---PI 139
Cdd:cd06298 2 VGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRspvPV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 140 V-AFDRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGLRQLGFNYELDKKGIICPVP----NDLS 214
Cdd:cd06298 82 VlAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLQGYKRALEEAGLEFNEPlifeGDYD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 215 LMRRELEIKSIISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVE 294
Cdd:cd06298 162 YDSGYELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVAMR 241
|
250 260
....*....|....*....|....*..
gi 504447938 295 ILLKKIKGKTV-NRDYVLPVNLIAGGS 320
Cdd:cd06298 242 LLTKLMNKEEVeETIVKLPHSIIWRQS 268
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
7-304 |
2.07e-29 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 114.87 E-value: 2.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 7 DVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIERLEDEL 86
Cdd:PRK10401 6 DVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDLVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 87 FKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIE---DYEKVEAPIVAFDRNLAP-KIPIVSSDNFEGGK 162
Cdd:PRK10401 86 QQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDelaQFMDQIPGMVLINRVVPGyAHRCVCLDNVSGAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 163 LAARALVKAGCQRIvmitGYDNSDSP---TGLRQLGFNYELDKKGIICP-------VPnDLS--------LMRRELEIKS 224
Cdd:PRK10401 166 MATRMLLNNGHQRI----GYLSSSHGiedDAMRRAGWMSALKEQGIIPPeswigtgTP-DMQggeaamveLLGRNLQLTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 225 iisrekpdgIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGKT 304
Cdd:PRK10401 241 ---------VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNL 311
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
62-320 |
5.17e-29 |
|
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: 111.98 E-value: 5.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA---P 138
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSagiP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFD--RNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDsPTGLRQLGFNYELDKKGIicPVPNDLSL- 215
Cdd:cd06296 81 FVLIDpvGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSV-SGRARLAGYRAALAEAGI--AVDPDLVRe 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 -----------MRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQP 284
Cdd:cd06296 158 gdftyeagyraARELLE-----LPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQP 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 504447938 285 LDEIAKLCVEILLKKIKGKTV-NRDYVLPVNLIAGGS 320
Cdd:cd06296 233 LREMGAVAVRLLLRLLEGGPPdARRIELATELVVRGS 269
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
62-320 |
8.96e-29 |
|
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: 111.49 E-value: 8.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTII--CNSeHDPNKEKDYLEMLAANQCDGII-----SSSHNLgIEDYEK 134
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDS-DDEDLADRLRRFLSRSRPDGVIltpplSDDPAL-LDALDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 135 VEAPIVAfdrnLAPK-----IPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSdSPTGLRQLGFNYELDKKGIicPV 209
Cdd:cd01545 79 LGIPYVR----IAPGtdddrSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDH-GASAERLEGFRDALAEAGL--PL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 210 PNDLSL------------MRRELEIKsiisrEKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPE 277
Cdd:cd01545 152 DPDLVVqgdftfesgleaAEALLDLP-----DRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPP 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 504447938 278 LATIQQPLDEIAKLCVEILLKKIKGK-TVNRDYVLPVNLIAGGS 320
Cdd:cd01545 227 LTTVRQPIAEMARRAVELLIAAIRGApAGPERETLPHELVIRES 270
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
3-297 |
3.24e-28 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 111.77 E-value: 3.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 3 AKLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPNISNVFYAELIERL 82
Cdd:PRK10727 2 ATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 83 EDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEAPI---VAFDRNLaPKIP--IVSSDN 157
Cdd:PRK10727 82 EQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIpgmVLINRIL-PGFEnrCIALDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 158 FEGGKLAARALVKAGCQRIVMI-TGYDNSDSPTGLRqlGFNYELDKKGIICpvpNDLSLMRRELE-------IKSIISRE 229
Cdd:PRK10727 161 RYGAWLATRHLIQQGHTRIGYLcSNHSISDAEDRLQ--GYYDALAESGIPA---NDRLVTFGEPDesggeqaMTELLGRG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504447938 230 KP-DGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILL 297
Cdd:PRK10727 236 RNfTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELAL 304
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
56-316 |
2.16e-27 |
|
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: 108.47 E-value: 2.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 56 QGKSAKLVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISS--SHNLGIEDYE 133
Cdd:COG1879 29 AAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSpvDPDALAPALK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 134 KVEA---PIVAFDRNLAPKIPI--VSSDNFEGGKLAARALVKA--GCQRIVMITGyDNSDSPTGLRQLGFNYELDKKG-- 204
Cdd:COG1879 109 KAKAagiPVVTVDSDVDGSDRVayVGSDNYAAGRLAAEYLAKAlgGKGKVAILTG-SPGAPAANERTDGFKEALKEYPgi 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 205 -IICPVP--NDLSLMRRELEikSIISRE-KPDGIFVSDDLTAILVMKVVRQLELsiPDDLKIIGYDGTAFIRhfypEL-- 278
Cdd:COG1879 188 kVVAEQYadWDREKALEVME--DLLQAHpDIDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDGSPEAL----QAik 259
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 504447938 279 -----ATIQQPLDEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:COG1879 260 dgtidATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLV 302
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
168-320 |
2.29e-27 |
|
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: 104.73 E-value: 2.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 168 LVKAGCQRIVMIT-GYDNSDSPTGLRQLGFNYELDKKGIicPVPNDLSLMRRELEIKSIISR-----EKPDGIFVSDDLT 241
Cdd:pfam13377 2 LAELGHRRIALIGpEGDRDDPYSDLRERGFREAARELGL--DVEPTLYAGDDEAEAAAARERlrwlgALPTAVFVANDEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 242 AILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIKG-KTVNRDYVLPVNLIAGGS 320
Cdd:pfam13377 80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGePAPPERVLLPPELVERES 159
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
74-306 |
3.15e-27 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 107.33 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 74 FYAELIERLEDELFKQGYKTIICNSEHDPNKEKDyLEMLAANQCDGIISSSHNLGIEDYEK---VEAPIVAFDrNLAPKI 150
Cdd:cd06277 20 FFSELIDGIEREARKYGYNLLISSVDIGDDFDEI-LKELTDDQSSGIILLGTELEEKQIKLfqdVSIPVVVVD-NYFEDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 151 PI--VSSDNFEGGKLAARALVKAGCQRIVMI-------------TGYDNSdsptgLRQLGFNYELDKKGIICPVPNDLSL 215
Cdd:cd06277 98 NFdcVVIDNEDGAYEAVKYLVELGHTRIGYLassyriknfeerrRGFRKA-----MRELGLSEDPEPEFVVSVGPEGAYK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 -MRRELEIKsiisREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVE 294
Cdd:cd06277 173 dMKALLDTG----PKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVR 248
|
250
....*....|..
gi 504447938 295 ILLKKIKGKTVN 306
Cdd:cd06277 249 RLIEKIKDPDGG 260
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
62-303 |
3.91e-27 |
|
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: 107.17 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIIcNSEHDPNKEKDYLE-MLAANQCDGIISSSHNLG---IEDYEKVEA 137
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAI-FPLLSEYRLEKYLRnSTLAYQCDGLVMASLDLTelfEEVIVPTEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNlAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGL---RQLGFNYELDKKGIICPVPN--- 211
Cdd:cd06297 80 PVVLIDAN-SMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTETVfreREQGFLEALNKAGRPISSSRmfr 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 212 -DLSLMRRELEIKSII-SREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHfyPELATIQQPLDEIA 289
Cdd:cd06297 159 iDNSSKKAECLARELLkKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTTVRQPVEEMG 236
|
250
....*....|....
gi 504447938 290 KLCVEILLKKIKGK 303
Cdd:cd06297 237 EAAAKLLLKRLNEY 250
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
62-315 |
6.66e-27 |
|
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: 106.56 E-value: 6.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII----SSSHNLGIEDYEKVEA 137
Cdd:cd01537 1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAinlvDPAAAGVAEKARGQNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPKIPI--VSSDNFEGGKLAARALVKAGCQRIVMITGydNSDSPTG-LRQLGFNYELDKKGIICP----VP 210
Cdd:cd01537 81 PVVFFDKEPSRYDKAyyVITDSKEGGIIQGDLLAKHGHIQIVLLKG--PLGHPDAeARLAGVIKELNDKGIKTEqlqlDT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 211 NDLSLMRRELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIA 289
Cdd:cd01537 159 GDWDTASGKDKMDQWLSGpNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLG 238
|
250 260
....*....|....*....|....*..
gi 504447938 290 KLCVEILLKKI-KGKTVNRDYVLPVNL 315
Cdd:cd01537 239 KTTFDLLLNLAdNWKIDNKVVRVPYVL 265
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
70-316 |
1.97e-24 |
|
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: 99.90 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 70 ISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDylemlaaNQCDGIISsshnLG------IEDYEKVEAPIVAFD 143
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLESLL-------EKVDGIIA----IGkfskeeIEKLKKLNPNIVFVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 144 RNLAP-KIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGL----RQLGFNYELDKKGIICP---------V 209
Cdd:cd01544 83 SNPDPdGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEEiedpRLRAFREYMKEKGLYNEeyiyigefsV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 210 PNDLSLMRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIA 289
Cdd:cd01544 163 ESGYEAMKELLK-----EGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMG 237
|
250 260
....*....|....*....|....*...
gi 504447938 290 KLCVEILLKKIKGK-TVNRDYVLPVNLI 316
Cdd:cd01544 238 RTAVRLLLERINGGrTIPKKVLLPTKLI 265
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
63-313 |
6.36e-23 |
|
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: 95.71 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNL-GIEDYEK--VEA-- 137
Cdd:cd01536 2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSeALVPAVKkaNAAgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPKIPIVS---SDNFEGGKLAARALVKA--GCQRIVMITGyDNSDSPTGLRQLGFNYELDKKG---IICPV 209
Cdd:cd01536 82 PVVAVDTDIDGGGDVVAfvgTDNYEAGKLAGEYLAEAlgGKGKVAILEG-PPGSSTAIDRTKGFKEALKKYPdieIVAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 210 PND------LSLMrreleiKSIISR-EKPDGIFVSDDLTAILVMKVVRQleLSIPDDLKIIGYDGTafirhfyPE----- 277
Cdd:cd01536 161 PANwdrakaLTVT------ENLLQAnPDIDAVFAANDDMALGAAEALKA--AGRTGDIKIVGVDGT-------PEalkai 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 504447938 278 -----LATIQQPLDEIAKLCVEILLKKIKGKTVNRDYVLPV 313
Cdd:cd01536 226 kdgelDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPV 266
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
62-316 |
1.05e-22 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 95.15 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNL-----GIEDYEKVE 136
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVkalvpAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 137 APIVAFDRNL--APKIPIVSSDNFEGGKLAARALVK--AGCQRIVMITGYDNSdSPTGLRQLGFNYELDKKGIICPVPND 212
Cdd:cd19968 81 IPVVTVDRRAegAAPVPHVGADNVAGGREVAKFVVDklPNGAKVIELTGTPGS-SPAIDRTKGFHEELAAGPKIKVVFEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRELE---IKSIIS--REKPDGIFVSDDLTAILVMKVVRQLELSIpDDLKIIGYDGT--AFIRHFYPEL-ATIQQP 284
Cdd:cd19968 160 TGNFERDEGltvMENILTslPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFDAVpdALQAIKDGELyATVEQP 238
|
250 260 270
....*....|....*....|....*....|..
gi 504447938 285 LDEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd19968 239 PGGQARTALRILVDYLKDKKAPKKVNLKPKLI 270
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
63-316 |
5.67e-22 |
|
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: 93.00 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFP----NISNVFYAELIERLEDELFKQGYKTII--CNSEHDPnkEKDYLEMLAANQCDGIISSS-----------H 125
Cdd:cd20010 2 IGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLapAPSGEDE--LATYRRLVERGRVDGFILARtrvndpriaylL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 126 NLGIedyekveaPIVAFDR-NLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGydnsdsPTGL-----RQLGFNYE 199
Cdd:cd20010 80 ERGI--------PFVVHGRsESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNG------PEELnfahqRRDGYRAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 200 LDKKGIICP----VPNDLS------LMRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGT- 268
Cdd:cd20010 146 LAEAGLPVDpalvREGPLTeeggyqAARRLLA-----LPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLl 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504447938 269 AFIRHFYPELATIQQPLDEIAKLCVEILLKKIKGK-TVNRDYVLPVNLI 316
Cdd:cd20010 221 PALEYFSPPLTTTRSSLRDAGRRLAEMLLALIDGEpAAELQELWPPELI 269
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
63-311 |
1.65e-20 |
|
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: 89.18 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNIS-----NVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII--SSSHNLGIEDYEKV 135
Cdd:cd06294 2 IGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFIllYSKEDDPLIEYLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 136 EA-PIVAFDRNLAPK-IPIVSSDNFEGGKLAARALVKAGCQRIVMITGydnsdsPTGL-----RQLGFNYELDKKGIicP 208
Cdd:cd06294 82 EGfPFVVIGKPLDDNdVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGG------DKNLvvsidRLQGYKQALKEAGL--P 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 209 VPNDLSLMRRELE------IKSIISREK-PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATI 281
Cdd:cd06294 154 LDDDYILLLDFSEedgydaLQELLSKPPpPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSV 233
|
250 260 270
....*....|....*....|....*....|
gi 504447938 282 QQPLDEIAKLCVEILLKKIKGKTVNRDYVL 311
Cdd:cd06294 234 DINPYELGREAAKLLINLLEGPESLPKNVI 263
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
7-55 |
2.75e-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: 2.75e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 504447938 7 DVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPNNLARGL 55
Cdd:cd01392 2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSL 50
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
62-305 |
2.84e-20 |
|
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380496 [Multi-domain] Cd Length: 266 Bit Score: 88.20 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNI-SNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSshNLGIEDYE-----KV 135
Cdd:cd06272 1 TIGLYWPSVgERVALTRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVF--GISDSDIEylnknKP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 136 EAPIVAFDRnLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMItGYDNSDSPTGLRQLGFNYELDKKGIICpvpNDLSL 215
Cdd:cd06272 79 KIPIVLYNR-ESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYI-GNPNSNRNQTLRGKGFIETCEKHGIHL---SDSII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 216 MRRELEI-------KSIISREK-PDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDE 287
Cdd:cd06272 154 DSRGLSIeggdnaaKKLLKKKTlPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEK 233
|
250
....*....|....*...
gi 504447938 288 IAKLCVEILLKKIKGKTV 305
Cdd:cd06272 234 IAEESLRLILKLIEGREN 251
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
4-49 |
1.58e-19 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 80.37 E-value: 1.58e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 504447938 4 KLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQELNYKPN 49
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
138-320 |
2.15e-18 |
|
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: 83.41 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMIT---GYDNSDSPTGLRQL-------------------- 194
Cdd:cd06279 81 PLVVVDGPAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSlrlDRGRERGPVSAERLaaatnsvarerlagyrdale 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 195 GFNYELDKKGIICPVPNDLS----LMRRELEiksiiSREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAF 270
Cdd:cd06279 161 EAGLDLDDVPVVEAPGNTEEagraAARALLA-----LDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDIPE 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504447938 271 IRHFYPELATIQQPLDEIAKLCVEILLKKIKGkTVNRDYVLPVNLIAGGS 320
Cdd:cd06279 236 AAAADPGLTTVRQPAVEKGRAAARLLLGLLPG-APPRPVILPTELVVRAS 284
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
62-304 |
3.57e-17 |
|
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380622 [Multi-domain] Cd Length: 272 Bit Score: 79.67 E-value: 3.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNL--GIEDYEKVEA-- 137
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADAdaSIAAVKKAKDag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 -PIVAFDRNLAPKIPIVS---SDNFEGGKLAARALVK--AGCQRIVMITGYDnSDSPTGLRQLGFNYELDKKGIICPVPN 211
Cdd:cd19967 81 iPVFLIDREINAEGVAVAqivSDNYQGAVLLAQYFVKlmGEKGLYVELLGKE-SDTNAQLRSQGFHSVIDQYPELKMVAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 212 ---DLSLMRRELEIKSII-SREKPDGIFVSDDLTAILVMKVVRQleLSIPDDLKIIGYDGTAFIRHFYPE---LATIQQP 284
Cdd:cd19967 160 qsaDWDRTEAFEKMESILqANPDIKGVICGNDEMALGAIAALKA--AGRAGDVIIVGFDGSNDVRDAIKEgkiSATVLQP 237
|
250 260
....*....|....*....|
gi 504447938 285 LDEIAKLCVEILLKKIKGKT 304
Cdd:cd19967 238 AKLIARLAVEQADQYLKGGS 257
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
109-288 |
2.94e-16 |
|
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380485 [Multi-domain] Cd Length: 265 Bit Score: 77.24 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 109 LEMLAANQCDGIISSSHNLgiEDYEKVEA---PIVAFD-RNLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMItGYDN 184
Cdd:cd01543 43 LDLLKGWKGDGIIARLDDP--ELAEALRRlgiPVVNVSgSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFC-GFRN 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 185 ---SDsptgLRQLGFNYELDKKGIICPV---PNDLSLMRRELEIKSII----SREKPDGIFVSDDLTAILVMKVVRQLEL 254
Cdd:cd01543 120 aawSR----ERGEGFREALREAGYECHVyesPPSGSSRSWEEEREELAdwlkSLPKPVGIFACNDDRARQVLEACREAGI 195
|
170 180 190
....*....|....*....|....*....|....*
gi 504447938 255 SIPDDLKIIGYDGTAFIRHF-YPELATIQQPLDEI 288
Cdd:cd01543 196 RVPEEVAVLGVDNDELICELsSPPLSSIALDAEQI 230
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
63-316 |
7.56e-16 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 76.16 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII-----SSSHNLGIEDYEKVEA 137
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIIlapvdSGGIVPAIEAANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPKIPI--VSSDNFEGGKLAARALVKA---GCQRIVMITgYDNSDSpTGLRQLGFNYELDKKGIICPVPND 212
Cdd:cd06322 82 PVFTVDVKADGAKVVthVGTDNYAGGKLAGEYALKAllgGGGKIAIID-YPEVES-VVLRVNGFKEAIKKYPNIEIVAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRELEIKS----IISREKPDGIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGTafirhfyPE----------- 277
Cdd:cd06322 160 PGDGRREEALAAtedmLQANPDLDGIFAIGDPAALGALTAIESAGKE--DKIKVIGFDGN-------PEaikaiakggki 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 504447938 278 LATIQQPLDEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06322 231 KADIAQQPDKIGQETVEAIVKYLAGETVEKEILIPPKLY 269
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
63-304 |
2.92e-15 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 74.27 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIIC-NSEHDPNKEKDYLEMLAANQCDGII---SSSHNLG--IEDYEKVE 136
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVgPAEADAAEQVAQIEDAIAQGVDAIIvapVDPTALApvLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 137 APIVAFDRNL--APKIPIVSSDNFEGGKLAARALVKA--GCQRIVMITGydNSDSP-TGLRQLGFNYELDKK-------G 204
Cdd:pfam13407 81 IPVVTFDSDApsSPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSG--SPGDPnANERIDGFKKVLKEKypgikvvA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 205 IICPVPNDLSLMRRELEikSIIS--REKPDGIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGTAFIRHFYPE---LA 279
Cdd:pfam13407 159 EVEGTNWDPEKAQQQME--ALLTayPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEALEAIKDgtiDA 234
|
250 260
....*....|....*....|....*
gi 504447938 280 TIQQPLDEIAKLCVEILLKKIKGKT 304
Cdd:pfam13407 235 TVLQDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
138-302 |
2.42e-14 |
|
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: 71.80 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRN-LAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGyDNSDSPTGLRQLGFNYELDKKGIICPVPNDLSLM 216
Cdd:cd20009 82 PFVTHGRTeLSTPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAP-PRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 217 RRELEIKSII-----SREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKL 291
Cdd:cd20009 161 SSAEAIRAAArrllrQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRF 240
|
170
....*....|.
gi 504447938 292 CVEILLKKIKG 302
Cdd:cd20009 241 LAEALLRRIEG 251
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
63-315 |
4.24e-14 |
|
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380546 [Multi-domain] Cd Length: 268 Bit Score: 71.17 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII-----SSSHNLGIEDYEKVEA 137
Cdd:cd06323 2 IGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLinptdSDAVSPAVEEANEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPK--IPIVSSDNFEGGKLAARALVKA--GCQRIVMITGYDNSdSPTGLRQLGFNYELDKKG---IICPVP 210
Cdd:cd06323 82 PVITVDRSVTGGkvVSHIASDNVAGGEMAAEYIAKKlgGKGKVVELQGIPGT-SAARERGKGFHNAIAKYPkinVVASQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 211 ND------LSLMRRELEIKSIIsrekpDGIFVSDDLTAIlvmKVVRQLELSIPDDLKIIGYDGTafirhfyPE------- 277
Cdd:cd06323 161 ADfdrtkgLNVMENLLQAHPDI-----DAVFAHNDEMAL---GAIQALKAAGRKDVIVVGFDGT-------PDavkavkd 225
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 504447938 278 ---LATI-QQPlDEIAKLCVEILLKKIKGKTVnrDYVLPVNL 315
Cdd:cd06323 226 gklAATVaQQP-EEMGAKAVETADKYLKGEKV--PKKIPVPL 264
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
63-317 |
2.39e-13 |
|
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).
Pssm-ID: 395423 [Multi-domain] Cd Length: 281 Bit Score: 69.08 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLGIEDYEKVEA----P 138
Cdd:pfam00532 4 LGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEgygiP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDR--NLAPKIPIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTGLRQLGFNYELDKKGI------ICPVP 210
Cdd:pfam00532 84 VIAADDafDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGRevkiyhVATGD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 211 NDL--------SLMRRELEIKSIISrekpdgifVSDDLTAILVMKVVRQLELSIPDD-----LKIIGYDG--TAFIRHFY 275
Cdd:pfam00532 164 NDIpdaalaanAMLVSHPTIDAIVA--------MNDEAAMGAVRALLKQGRVKIPDIvgigiNSVVGFDGlsKAQDTGLY 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 504447938 276 -PELATIQQPLDEIAKLCVEILLKKI-KGKTVNRDYVLPVNLIA 317
Cdd:pfam00532 236 lSPLTVIQLPRQLLGIKASDMVYQWIpKFREHPRVLLIPRDFFK 279
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
63-316 |
9.21e-13 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 67.31 E-value: 9.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFK--QGYKTIICNSEHDPNKEKDYLEMLAANQCD----------GI---ISSSHNL 127
Cdd:cd06321 2 IGVTVQDLGNPFFVAMVRGAEEAAAEinPGAKVTVVDARYDLAKQFSQIDDFIAQGVDlillnaadsaGIepaIKRAKDA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 128 GIedyekveaPIVAFDRNLAPKIPIVSSDNFEGGKLAARALVKA--GCQRIVMITGYDNsdSPTGLRQLGFNYELDK-KG 204
Cdd:cd06321 82 GI--------IVVAVDVAAEGADATVTTDNVQAGYLACEYLVEQlgGKGKVAIIDGPPV--SAVIDRVNGCKEALAEyPG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 205 IICPVPND--------LSLMRReleiksIISREKP-DGIFVSDDLTAILVMKVVRQLELsipDDLKIIGYDGT-----AF 270
Cdd:cd06321 152 IKLVDDQNgkgsraggLSVMTR------MLTAHPDvDGVFAINDPGAIGALLAAQQAGR---DDIVITSVDGSpeavaAL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 504447938 271 IRHFYPELATIQQPLDEIAKLCVEILLKKIKGKTVNRDYVL-PVNLI 316
Cdd:cd06321 223 KREGSPFIATAAQDPYDMARKAVELALKILNGQEPAPELVLiPSTLV 269
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
63-303 |
3.10e-12 |
|
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: 65.52 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNIS---NVFYAELIERLEDELFKQGYKTIICNSEHDpNKEKDYLEMLAANQCDGIISSSHNLG---IEDYEKVE 136
Cdd:cd06271 2 IALVFPVTEtelNGTVSE*VSGITEEAGTTGYHLLVWPFEEA-ES*VPIRDLVETGSADGVILSEIEPNdprVQFLTKQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 137 APIVAFDRNLAPK-IPIVSSDNFEGGKLAARALVKAGCQRIVMItGYDNSDSPTGLRQLGFNYELDKKGI---------I 206
Cdd:cd06271 81 FPFVAHGRSD*PIgHAWVDIDNEAGAYEAVERLAGLGHRRIAFI-VPPARYSPHDRRLQGYVRA*RDAGLtgypldadtT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 207 CPVPNDLSLMRRELEiksiisrEKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHF-YPELATIQQPL 285
Cdd:cd06271 160 LEAGRAAAQRLLALS-------PRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFLGAMiTPPLTTVHAPI 232
|
250
....*....|....*...
gi 504447938 286 DEIAKLCVEILLKKIKGK 303
Cdd:cd06271 233 AEAGRELAKALLARIDGE 250
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
99-316 |
5.57e-12 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 64.95 E-value: 5.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 99 EHDPNKEKDYLEMLAANQCDGI-ISSSHNLGIEDYekVEA------PIVAFDRNLA--PKIPIVSSDNFEGGKLAARALV 169
Cdd:cd20004 40 EDDVEAQIQIIEYFIDQGVDGIvLAPLDRKALVAP--VERaraqgiPVVIIDSDLGgdAVISFVATDNYAAGRLAAKRMA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 170 KA--GCQRIVMITGYDNSDSpTGLRQLGFNYELDKKGIICPV------PNDLSLMRRELEikSIISREKP-DGIFVSDDL 240
Cdd:cd20004 118 KLlnGKGKVALLRLAKGSAS-TTDRERGFLEALKKLAPGLKVvddqyaGGTVGEARSSAE--NLLNQYPDvDGIFTPNES 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 241 TAILVMKVVRQLELSipDDLKIIGYDGTAF----IRHFYPELATIQQPLDeIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd20004 195 TTIGALRALRRLGLA--GKVKFIGFDASDLlldaLRAGEISALVVQDPYR-MGYLGVKTAVAALRGKPVPKRIDTGVVLV 271
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
62-316 |
3.88e-11 |
|
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.
Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 62.56 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFK-QGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISS---SHNLgIEDYEKVEA 137
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSpneADAL-TPVVKKAYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 ---PIVAFDRNLA--PKIPIVSSDNFEGGKLAARALVKA--GCQRIVMITGYDNSdSPTGLRQLGFNYELDKKG---IIC 207
Cdd:cd06308 80 agiPVIVLDRKVSgdDYTAFIGADNVEIGRQAGEYIAELlnGKGNVVEIQGLPGS-SPAIDRHKGFLEAIAKYPgikIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 208 PVPNDLSLMRRELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRqlELSIPDDLKIIGYDGT-----AFIRH--FYpelA 279
Cdd:cd06308 159 SQDGDWLRDKAIKVMEDLLQAhPDIDAVYAHNDEMALGAYQALK--KAGREKEIKIIGVDGLpeageKAVKDgiLA---A 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 504447938 280 TIQQPLdeIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06308 234 TFLYPT--GGKEAIEAALKILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
63-316 |
5.03e-11 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 61.97 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTII--CNSEHDPNKEKDYLEMLAANQCDGII----SSSHNLG-IEDYEKV 135
Cdd:cd06310 2 IGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFvgPESEEDVAGQNSLLEELINKKPDAIVvaplDSEDLVDpLKDAKDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 136 EAPIVAFDRNLAPKIPI--VSSDNFEGGKLAARALVKA--GCQRIVMITGyDNSDSPTGLRQLGFNYELDKK--GIIC-- 207
Cdd:cd06310 82 GIPVIVIDSGIKGDAYLsyIATDNYAAGRLAAQKLAEAlgGKGKVAVLSL-TAGNSTTDQREEGFKEYLKKHpgGIKVla 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 208 -PVPNDLSLMRRELEIKSIISREKPDGIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGT----AFIRHFYPELATIQ 282
Cdd:cd06310 161 sQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLS--GQIKIVGFDSQeellDALKNGKIDALVVQ 238
|
250 260 270
....*....|....*....|....*....|....
gi 504447938 283 QPLdEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06310 239 NPY-EIGYEGIKLALKLLKGEEVPKNIDTGAELI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
64-315 |
5.78e-11 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 61.83 E-value: 5.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 64 GLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIIssshnLGIEDYEKVEA------ 137
Cdd:cd19971 3 GFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIF-----LNPVDSEGIRPaleaak 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 ----PIVAFDRNLAPK---IPIVSSDNFEGGKLAARALVK--AGCQRIVMItgydnsDSPTGL----RQLGFNYELDKKG 204
Cdd:cd19971 78 eagiPVINVDTPVKDTdlvDSTIASDNYNAGKLCGEDMVKklPEGAKIAVL------DHPTAEscvdRIDGFLDAIKKNP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 205 II---------CPVPNDLSLMRRELEIKSIIsrekpDGIFVSDDLTAILVMKVVRqlELSIPDDLKIIGYDGTAFIRHFY 275
Cdd:cd19971 152 KFevvaqqdgkGQLEVAMPIMEDILQAHPDL-----DAVFALNDPSALGALAALK--AAGKLGDILVYGVDGSPDAKAAI 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 504447938 276 PE---LATIQQPLDEIAKLCVEILLKKIKGKTVNRDYVLPVNL 315
Cdd:cd19971 225 KDgkmTATAAQSPIEIGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
149-315 |
1.80e-10 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 60.73 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 149 KIPIVSSDNFEGGKLAARAL---VKAGCQRIVM--ITGYDNSDSptglRQLGFNYELDKKGI-ICPVPNDLSLMRRELEI 222
Cdd:cd19970 104 NVPFVGPDNRQGAYLAGDYLakkLGKGGKVAIIegIPGADNAQQ----RKAGFLKAFEEAGMkIVASQSANWEIDEANTV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 223 KSIISREKPD--GIFVSDDLTAILVMKVVRqlELSIPDDLKIIGYDGTAFIRHFYPE---LATIQQPLDEIAKLCVEILL 297
Cdd:cd19970 180 AANLLTAHPDirGILCANDNMALGAIKAVD--AAGKAGKVLVVGFDNIPAVRPLLKDgkmLATIDQHPAKQAVYGIEYAL 257
|
170
....*....|....*...
gi 504447938 298 KKIKGKTVNRDYVLPVNL 315
Cdd:cd19970 258 KMLNGEEVPGWVKTPVEL 275
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
65-316 |
2.45e-10 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 59.90 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 65 LIFPNISNVFYAELIERLEDELFKQGYKTI-ICNSEHDPNKEKDYLEMLAANQCDGI-ISSSHNLGIEDY-EKVEA---P 138
Cdd:cd06314 4 LVPKGLNNPFWDLAEAGAEKAAKELGVNVEfVGPQKSDAAEQVQLIEDLIARGVDGIaISPNDPEAVTPViNKAADkgiP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 139 IVAFDRNlAPK---IPIVSSDNFEGGKLAARALVKA--GCQRIVMITGYDNSDSPTgLRQLGFNYELDKKG---IICPVP 210
Cdd:cd06314 84 VITFDSD-APDskrLAYIGTDNYEAGREAGELMKKAlpGGGKVAIITGGLGADNLN-ERIQGFKDALKGSPgieIVDPLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 211 NDLSLMRRELEIKSIISR-EKPDGIFVSDDLTAILVMKVVRQLELsiPDDLKIIGYDGTA----FIRHFYPELATIQQPl 285
Cdd:cd06314 162 DNDDIAKAVQNVEDILKAnPDLDAIFGVGAYNGPAIAAALKDAGK--VGKVKIVGFDTLPetlqGIKDGVIAATVGQRP- 238
|
250 260 270
....*....|....*....|....*....|..
gi 504447938 286 DEIAKLCVEILLKKIK-GKTVNRDYVLPVNLI 316
Cdd:cd06314 239 YEMGYLSVKLLYKLLKgGKPVPDVIDTGVDVV 270
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
63-316 |
4.43e-10 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 59.58 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTII--CNSEHDPNKEKDYLEMLAANQCDGII---SSSHNL--GIEDYEKV 135
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVqaAPSETDTQGQLNLLETMLNKGYDAILvspISDTNLipPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 136 EAPIVAFDRNLAPK---------IPIVSSDNFEGGKLAARALVKA--GCQRIVMITGydNSDSPTG-LRQLGFNYELDKK 203
Cdd:cd06320 82 GIPVINLDDAVDADalkkaggkvTSFIGTDNVAAGALAAEYIAEKlpGGGKVAIIEG--LPGNAAAeARTKGFKETFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 204 G---IICPVPNDLSLMRRELEIKSIISREkPD--GIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGT----AFIRHf 274
Cdd:cd06320 160 PglkLVASQPADWDRTKALDAATAILQAH-PDlkGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDGIpeakKSIKA- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 504447938 275 yPEL-ATIQQPLDEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06320 236 -GELtATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALI 277
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
96-269 |
3.22e-09 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 56.87 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 96 CNSEHDPNKEKDYLEMLAANQCDGIIssshnLGIEDYEKVEA----------PIVAFDRNLAPKIPI--VSSDNFEGGKL 163
Cdd:cd20005 37 PDTESDVDKQIEMLDNAIAKKPDAIA-----LAALDTNALLPqlekakekgiPVVTFDSGVPSDLPLatVATDNYAAGAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 164 AARALVKA-GCQRIVMITGYDNSDSPTGLRQLGFNYELDKK--GI-ICPVPNDLSLMRRELEIKSIISREKPD--GIFVS 237
Cdd:cd20005 112 AADHLAELiGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKypDIkVVNVQYGVGDHAKAADIAKAILQANPDlkGIYAT 191
|
170 180 190
....*....|....*....|....*....|..
gi 504447938 238 DDLTAILVMKVVRQLELSipDDLKIIGYDGTA 269
Cdd:cd20005 192 NEGAAIGVANALKEMGKL--GKIKVVGFDSGE 221
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
138-312 |
6.96e-09 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 55.71 E-value: 6.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLA-PKIPI--VSSDNFEGGKLAARALVKA-GCQRIVMITGYDNSDSPTGLRQLGFNYELDKKGIICPVP--- 210
Cdd:cd20007 83 KVVTVDTTLGdPSFVLsqIASDNVAGGALAAEALAELiGGKGKVLVINSTPGVSTTDARVKGFAEEMKKYPGIKVLGvqy 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 211 --NDLSlmrRELEIKSIISREKPD--GIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGTAFIrhfYPEL------AT 280
Cdd:cd20007 163 seNDPA---KAASIVAAALQANPDlaGIFGTNTFSAEGAAAALRNAGKT--GKVKVVGFDASPAQ---VEQLkagtidAL 234
|
170 180 190
....*....|....*....|....*....|..
gi 504447938 281 IQQPLDEIAKLCVEILLKKIKGKTVNRDYVLP 312
Cdd:cd20007 235 IAQKPAEIGYLAVEQAVAALTGKPVPKDILTP 266
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
63-312 |
3.95e-08 |
|
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.
Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 53.76 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSshnlGIED------YEKVE 136
Cdd:cd06309 2 VGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILIS----PIDAtgwdpvLKEAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 137 A---PIVAFDRNLA--PKIPIVS---SDNFEGGKLAARALVKAGCQ---RIVMITGYDNSdSPTGLRQLGFNYELDKKG- 204
Cdd:cd06309 78 DagiPVILVDRTIDgeDGSLYVTfigSDFVEEGRRAAEWLVKNYKGgkgNVVELQGTAGS-SVAIDRSKGFREVIKKHPn 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 205 --IICPVPNDLSLMRRELEIKSIISREKP--DGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTafirhfyPE--- 277
Cdd:cd06309 157 ikIVASQSGNFTREKGQKVMENLLQAGPGdiDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQ-------KDale 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 504447938 278 -------LATIQ-QPLdeIAKLCVEILLKKIKGKTVNRDYVLP 312
Cdd:cd06309 230 aikagelNATVEcNPL--FGPTAFDTIAKLLAGEKVPKLIIVE 270
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
62-297 |
1.32e-07 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 51.89 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIF---PNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII---SSSHNLGIE-DYEK 134
Cdd:cd01391 1 IIGVVTsslHQIREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIgpgSSSVAIVIQnLAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 135 VEAPIVAFD------RNLAPKIPIVS--SDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPtgLRQLGFNyELDKKGII 206
Cdd:cd01391 81 FDIPQLALDatsqdlSDKTLYKYFLSvvFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGE--LRMAGFK-ELAKQEGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 207 CPV---PNDLSLMRRELEI--KSIISREKPDGIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGTAFIRHFY-----P 276
Cdd:cd01391 158 CIVasdKADWNAGEKGFDRalRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDEVGyeveaN 235
|
250 260
....*....|....*....|.
gi 504447938 277 ELATIQQPLDEIAKLCVEILL 297
Cdd:cd01391 236 GLTTIKQQKMGFGITAIKAMA 256
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
3-301 |
1.66e-07 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 52.07 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 3 AKLTDVAELAGVSPTTVSRVINKKGYLSQK--TIDKVHAAMQELNYKPNNLARGLQGKSAKLVGLIFPN------ISNVF 74
Cdd:PRK10339 2 ATLKDIAIEAGVSLATVSRVLNDDPTLNVKeeTKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIYSyqqeleINDPY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 75 YAELIERLEDELFKQGYKTIIC-NSEHDPNKEKdylemlaanqCDGI--ISSSHNLGIEDYEKVEAPIVAFD-RNLAPKI 150
Cdd:PRK10339 82 YLAIRHGIETQCEKLGIELTNCyEHSGLPDIKN----------VTGIliVGKPTPALRAAASALTDNICFIDfHEPGSGY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 151 PIVSSDNFEGGKLAARALVKAGCQRIVMITGYDNSDSPTgLRQLGFNYELDKKGIICpvPNDL------SLMRRELEIKS 224
Cdd:PRK10339 152 DAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKAD-IREVAFAEYGRLKQVVR--EEDIwrggfsSSSGYELAKQM 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504447938 225 IISREKPDGIFVSDDLTAILVMKVVRQLELSIPDDLKIIGYDGTAFIRHFYPELATIQQPLDEIAKLCVEILLKKIK 301
Cdd:PRK10339 229 LAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKAR 305
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
74-316 |
3.98e-07 |
|
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380528 [Multi-domain] Cd Length: 273 Bit Score: 50.37 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 74 FYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISsshNLGIEDY------EKVEA--PIVAFDRN 145
Cdd:cd06305 13 WDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIII---SHGDADAldpklkKALDAgiPVVTFDTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 146 LA-PKIPIVSSDNFEGGKLAARALVKA--GCQRIVMITGydNSDSPTGLRQLGF-NYELDKKGIICPVP--------NDL 213
Cdd:cd06305 90 SQvPGVNNITQDDYALGTLSLGQLVKDlnGEGNIAVFNV--FGVPPLDKRYDIYkAVLKANPGIKKIVAelgdvtpnTAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 214 SLMRRELEIKSIISREKPDGIFVSDDLTAIlvmKVVRQLELSIPDDLKIIGYDGT-----AFIRHFYPELATIQQPLDEI 288
Cdd:cd06305 168 DAQTQVEALLKKYPEGGIDAIWAAWDEPAK---GAVQALEEAGRTDIKVYGVDISnqdleLMADEGSPWVATAAQDPALI 244
|
250 260
....*....|....*....|....*...
gi 504447938 289 AKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06305 245 GTVAVRNVARKLAGEDLPDKYSLVPVLI 272
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
63-305 |
1.37e-06 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 48.95 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHN--LGIEDYEKVEA--- 137
Cdd:cd06318 2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDpeGLTPAVKAAKAagi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPKIPI---VSSDNFEGGKLAARALVKA-GCQR--IVMITGydNSDSPTGL-RQLGF-----NYELDKKGI 205
Cdd:cd06318 82 PVITVDSALDPSANVatqVGRDNKQNGVLVGKEAAKAlGGDPgkIIELSG--DKGNEVSRdRRDGFlagvnEYQLRKYGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 206 --ICPVPNDLSLMRRELEIKSI--ISREKPD--GIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGTAFIRHFYPE-- 277
Cdd:cd06318 160 snIKVVAQPYGNWIRSGAVAAMedLLQAHPDinVVYAENDDMALGAMKALKAAGML--DKVKVAGADGQKEALKLIKDgk 237
|
250 260
....*....|....*....|....*....
gi 504447938 278 -LATIQQPLDEIAKLCVEILLKKIKGKTV 305
Cdd:cd06318 238 yVATGLNDPDLLGKTAVDTAAKVVKGEES 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
63-316 |
3.98e-06 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 47.44 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII-----SSSHNLGIEDYEKVEA 137
Cdd:cd19972 2 IGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIyipagATAAAVPVKAARAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNlAPKIP---IVSSDNFEGGKLAARALVK--AGCQRIVMITGyDNSDSPTGLRQLGFNYELDKkgiiCPvpnD 212
Cdd:cd19972 82 PVIAVDRN-PEDAPgdtFIATDSVAAAKELGEWVIKqtGGKGEIAILHG-QLGTTPEVDRTKGFQEALAE----AP---G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 213 LSLMRRE---------LEIKSIISREKPD--GIFVSDDLTAILVMKVVRqlELSIPDDLKIIGYDG--TAF--IRHFYPE 277
Cdd:cd19972 153 IKVVAEQtadwdqdegFKVAQDMLQANPNitVFFGQSDAMALGAAQAVK--VAGLDHKIWVVGFDGdvAGLkaVKDGVLD 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 504447938 278 lATIQQPLDEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd19972 231 -ATMTQQTQKMGRLAVDSAIDLLNGKAVPKEQLQDAVLT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
98-310 |
1.17e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 46.07 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 98 SEHDPNKEKDYLEMLAANQCDGII---SSSHNL--GIEDYEKvEAPIVAFDRNLAPK--IPIVSSDNFEGGKLAARALVK 170
Cdd:cd20008 39 TEADIAGQVNLVENAISRKPDAIVlapNDTAALvpAVEAADA-GIPVVLVDSGANTDdyDAFLATDNVAAGALAADELAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 171 A------GCQRIVMITGYDNSDSPTGlRQLGFNYELDKK--GIIC--PVPNDlSLMRRELEIKSIISREKPD--GIFVSD 238
Cdd:cd20008 118 LlkasggGKGKVAIISFQAGSQTLVD-REEGFRDYIKEKypDIEIvdVQYSD-GDIAKALNQTTDLLTANPDlvGIFGAN 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504447938 239 DLTAILVMKVVRQLELSipDDLKIIGYDGT----AFIRHFYPELATIQQPlDEIAKLCVEILLKKIKGKTVNRDYV 310
Cdd:cd20008 196 NPSAVGVAQALAEAGKA--GKIVLVGFDSSpdevALLKSGVIKALVVQDP-YQMGYEGVKTAVKALKGEEIVEKNV 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
63-316 |
1.74e-05 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 45.43 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII----SSSHNLGIEDYEKVEA- 137
Cdd:cd06319 2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIisptNSSAAPTVLDLANEAKi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFD--RNLAPKIPIVSSDNFEGGKLAARALVKA------GCQRIVMITGYDNSDSPTgLRQLGFNYELDKKGI---- 205
Cdd:cd06319 82 PVVIADigTGGGDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQ-ARTAGFEDALEEAGVeeva 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 206 ICPVPN-DLSLMRRELEiKSIISREKPDGIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGTafirhfyPE------- 277
Cdd:cd06319 161 LRQTPNsTVEETYSAAQ-DLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGD-------PEaldlikd 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 504447938 278 ---LATI-QQPLdEIAKLCVEILLKKIKGK-TVNRDYVLPVNLI 316
Cdd:cd06319 231 gklDGTVaQQPF-GMGARAVELAIQALNGDnTVEKEIYLPVLLV 273
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
62-306 |
3.02e-05 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 44.88 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLG----IEDYEKVEA 137
Cdd:cd19992 1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGaaanIVDKAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 -PIVAFDRnLAPKIPI---VSSDNFEGGKLAARALVKAGCQ-RIVMITGyDNSDSPTGLRQLGFNYELDK---KGII--- 206
Cdd:cd19992 81 vPVISYDR-LILNADVdlyVGRDNYKVGQLQAEYALEAVPKgNYVILSG-DPGDNNAQLITAGAMDVLQPaidSGDIkiv 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 207 --CPVPN---DLSLMrrelEIKSIISRE--KPDGIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGtafirhfypELA 279
Cdd:cd19992 159 ldQYVKGwspDEAMK----LVENALTANnnNIDAVLAPNDGMAGGAIQALKAQGLA--GKVFVTGQDA---------ELA 223
|
250 260 270
....*....|....*....|....*....|....*....
gi 504447938 280 ------------TIQQPLDEIAKLCVEILLKKIKGKTVN 306
Cdd:cd19992 224 alkrivegtqtmTVWKDLKELARAAADAAVKLAKGEKPQ 262
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
63-316 |
8.64e-05 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 43.52 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNL-----GIEDYEKVEA 137
Cdd:cd06317 2 IALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVngsipAIKRASEAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 138 PIVAFDRNLAPKIPI--VSSDNFEGGKLAARALVK-----AGCQRIVMITGYDNSdSPTGLRQLGFNYELDKKGIICPVP 210
Cdd:cd06317 82 PVIAYDAVIPSDFQAaqVGVDNLEGGKEIGKYAADyikaeLGGQAKIGVVGALSS-LIQNQRQKGFEEALKANPGVEIVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 211 NDLSLMRRELEIKS----IISREKPDGIFVSDDLTAILVMKVVRQLELSipDDLKIIGYDGTAFIRHFYPE----LATIQ 282
Cdd:cd06317 161 TVDGQNVQEKALSAaenlLTANPDLDAIYATGEPALLGAVAAVRSQGRQ--GKIKVFGWDLTKQAIFLGIDegvlQAVVQ 238
|
250 260 270
....*....|....*....|....*....|....
gi 504447938 283 QPLDEIAKLCVEILLKKIKGKTVNRDYVLPVNLI 316
Cdd:cd06317 239 QDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIV 272
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
232-320 |
9.88e-05 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 43.18 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 232 DGIFVSDDLTAILVMKVVRQLELSIPDDLKIIG-YDGtafIRHF--YPELATIQQPLDEIAKLCVEILLKKIKGKTVNRD 308
Cdd:cd06287 180 DAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTrYDG---IRARtaDPPLTAVDLHLDRVARTAIDLLFASLSGEERSVE 256
|
90
....*....|..
gi 504447938 309 YVLPVNLIAGGS 320
Cdd:cd06287 257 VGPAPELVVRAS 268
|
|
| PBP1_ABC_xylose_binding-like |
cd19995 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
63-314 |
2.52e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380650 [Multi-domain] Cd Length: 294 Bit Score: 41.89 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYaELIER--LEDELFKQ--GYKTIICNSEHDPNKEKDYLE-MLA------------ANQCDGIISSSH 125
Cdd:cd19995 2 VAFLLPDTTSARW-EQQDApgFEKAMKKLcpDCKVIYQNANGDASTQQQQAEaAITqgakvlvvdpvdSNAAAGIVAKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 126 NLGIedyekveaPIVAFDRnLAPKIPI---VSSDNFEGGKLAARALVKAGCQ------RIVMITGyDNSDSPTGLRQLGF 196
Cdd:cd19995 81 QAGV--------PVIAYDR-LILGGPAdyyVSFDNVAVGEAQAQSLVDHLKAigkkgvNIVMING-SPTDNNAGLFKKGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 197 NYELDKKG------IIC--PVPN-DLSLMRRELEikSIISR--EKPDGIFVSDDLTA---ILVMKvvRQ-LELSIPddlk 261
Cdd:cd19995 151 HEVLDPLGdsgelkLVCeyDTPDwDPANAQTAME--QALTKlgNNIDGVLSANDGLAggaIAALK--AQgLAGKVP---- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504447938 262 IIGYDGTafirhfypeLATIQQ------------PLDEIAKLCVEILLKKIKGKTVNRDYVLPVN 314
Cdd:cd19995 223 VTGQDAT---------VAGLQRilagdqymtvykPIKKEAAAAAKVAVALLKGETPPSDLVTGTV 278
|
|
| PBP1_ChvE |
cd19994 |
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ... |
62-170 |
4.71e-04 |
|
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380649 [Multi-domain] Cd Length: 304 Bit Score: 41.46 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHN---LG--IEDYEKVE 136
Cdd:cd19994 1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDgsaLGdvLEEAKDAG 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 504447938 137 APIVAFDRnLAPKIPIVSS----DNFEGGKLAARALVK 170
Cdd:cd19994 81 IPVIAYDR-LIMNTDAVDYyvtfDNEKVGELQGQYLVD 117
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
86-189 |
6.72e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 40.92 E-value: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 86 LFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGII-----SSSHNLGIEDYEKVEAPIVAFDRNLAPKIPI-VSSDNFE 159
Cdd:cd19993 25 LEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIvlaqdGDAILPAVEKAAAEGIPVIAYDRLIENPIAFyISFDNVE 104
|
90 100 110
....*....|....*....|....*....|.
gi 504447938 160 GGKLAARALVKA-GCQRIVMITGydnsdSPT 189
Cdd:cd19993 105 VGRMQARGVLKAkPEGNYVFIKG-----SPT 130
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
62-189 |
2.36e-03 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380480 [Multi-domain] Cd Length: 283 Bit Score: 38.94 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 62 LVGLIFPNISNVFYAELIERLEDELFKQGYKTIICNSEHDPNKEKDYLEMLAANQCDGIISSSHNLG-----IEDYEKVE 136
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQalspvVAEAKAEG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 504447938 137 APIVAFDR--NLAPKIPIVSSDNFEGGKLAARALVKA-GCQRIVMITGydnsdSPT 189
Cdd:cd01538 81 IKVIAYDRliLNADVDYYISFDNEKVGELQAQALLDAkPEGNYVLIGG-----SPT 131
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
4-42 |
2.46e-03 |
|
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: 35.61 E-value: 2.46e-03
10 20 30
....*....|....*....|....*....|....*....
gi 504447938 4 KLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQ 42
Cdd:cd00093 14 TQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALG 52
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
63-316 |
4.78e-03 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 37.93 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 63 VGLIFPNISNVFYAEL---IERLEDELFKQGYK-TIICNSEHDPNKEKDYLEMLAAnQCDGIISSSHNL-----GIEDYE 133
Cdd:cd06307 2 FGFLLPSPENPFYELLrraIEAAAAALRDRRVRlRIHFVDSLDPEALAAALRRLAA-GCDGVALVAPDHplvraAIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 134 KVEAPIVAFDRNLA--PKIPIVSSDNFEGGKLAARALVKAGCQR---IVMITGyDNSDSPTGLRQLGFnyeldkkgiicp 208
Cdd:cd06307 81 ARGIPVVTLVSDLPgsRRLAYVGIDNRAAGRTAAWLMGRFLGRRpgkVLVILG-SHRFRGHEEREAGF------------ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504447938 209 vpndLSLMRRE---LEI-KSIISREKPDGIF--VSD------DLTAILVM-----KVVRQL-ELSIPDDLKIIGYDGTAF 270
Cdd:cd06307 148 ----RSVLRERfpdLTVlEVLEGLDDDELAYelLREllarhpDLVGIYNAgggneGIARALrEAGRARRVVFIGHELTPE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 504447938 271 IRhfypEL-------ATIQQPLDEIAKLCVEILLKKIKGKTVNRDYV-LPVNLI 316
Cdd:cd06307 224 TR----RLlrdgtidAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPpIPIEII 273
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
4-42 |
5.25e-03 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 34.80 E-value: 5.25e-03
10 20 30
....*....|....*....|....*....|....*....
gi 504447938 4 KLTDVAELAGVSPTTVSRVINKKGYLSQKTIDKVHAAMQ 42
Cdd:smart00530 12 TQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALG 50
|
|
| |
