|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-331 |
5.76e-130 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 374.54 E-value: 5.76e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 1 MATMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEG 80
Cdd:COG1609 3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 81 IEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSED-LNEVEKTGLKYVLINRKPSFYDKNFVGVNN 159
Cdd:COG1609 83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDArLERLAEAGIPVVLIDRPLPDPGVPSVGVDN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 160 PLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQvKVLPE 239
Cdd:COG1609 163 RAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLAR-GPRPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 240 AICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIkEKDETRARQII 319
Cdd:COG1609 242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRI-EGPDAPPERVL 320
|
330
....*....|..
gi 1267416536 320 LTPSLVVRESCG 331
Cdd:COG1609 321 LPPELVVRESTA 332
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
61-325 |
5.59e-93 |
|
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: 277.86 E-value: 5.59e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSED-LNEVEKTGLK 139
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDElLEELLAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYS 219
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 220 LESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLS 299
Cdd:cd06267 161 EESGYEAARELLAL-PPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAA 239
|
250 260
....*....|....*....|....*.
gi 1267416536 300 MEFLLEMIkEKDETRARQIILTPSLV 325
Cdd:cd06267 240 AELLLERI-EGEEEPPRRIVLPTELV 264
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
4-329 |
1.59e-77 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 240.76 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 4 MKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEGIED 83
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 84 VSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEVEK--TGLKYVLINRKPSFYDKNFVGVNNPL 161
Cdd:PRK10423 81 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQryPSVPTVMMDWAPFDGDSDLIQDNSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 162 SSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIeQVKVLPEAI 241
Cdd:PRK10423 161 GGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLL-ALPLRPQAV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 242 CTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIkEKDETRARQIILT 321
Cdd:PRK10423 240 FTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRM-AQPTLQQQRLQLT 318
|
....*...
gi 1267416536 322 PSLVVRES 329
Cdd:PRK10423 319 PELMERGS 326
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
1-329 |
3.19e-76 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 237.70 E-value: 3.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 1 MATMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEG 80
Cdd:PRK10703 1 MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 81 IEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEV--EKTGLKYVLINRKPSFYDKNFVGVN 158
Cdd:PRK10703 81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMleEYRHIPMVVMDWGEAKADFTDAIID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 159 NPLS-SELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQvKVL 237
Cdd:PRK10703 161 NAFEgGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQ-KHR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 238 PEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIKEKDETRARq 317
Cdd:PRK10703 240 PTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQT- 318
|
330
....*....|..
gi 1267416536 318 IILTPSLVVRES 329
Cdd:PRK10703 319 IEVHPRLVERRS 330
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
61-329 |
8.72e-75 |
|
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: 231.66 E-value: 8.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGL-LLANIANSEDLNEVEKTgLK 139
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGViLLSGRLDAELLSELSKR-YP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYS 219
Cdd:cd06284 80 IVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 220 LESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLS 299
Cdd:cd06284 160 FEAGYAAARALLAL-PERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETA 238
|
250 260 270
....*....|....*....|....*....|
gi 1267416536 300 MEFLLEMIkEKDETRARQIILTPSLVVRES 329
Cdd:cd06284 239 AELLLEKI-EGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-329 |
1.72e-74 |
|
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: 230.91 E-value: 1.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSED-LNEVEKTGLK 139
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEEnKQLLKNMNIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDP-DINTARERKAGFISCMTQTGLDIDPMLIYDGEY 218
Cdd:cd19975 81 VVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLdDPNAGYPRYEGYKKALKDAGLPIKENLIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQVKvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd19975 161 SFKSGYQAMKRLLKNKK-LPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKK 239
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 299 SMEFLLEMIKEKDEtRARQIILTPSLVVRES 329
Cdd:cd19975 240 AVELLLDLIKNEKK-EEKSIVLPHQIIERES 269
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-329 |
7.39e-73 |
|
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: 226.75 E-value: 7.39e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLA--NIANSEDLNEVEKTGL 138
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIAssNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 139 KYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEY 218
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQVKvlPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd19976 161 SLEGGYKAAEELLKSKN--PTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 299 SMEFLLEMIKEKdETRARQIILTPSLVVRES 329
Cdd:cd19976 239 AAKLLLKIIKNP-AKKKEEIVLPPELIKRDS 268
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
61-325 |
4.66e-72 |
|
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: 224.33 E-value: 4.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDL-NEVEKTGLK 139
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLiEKLVKSGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYdGEYS 219
Cdd:cd19977 81 VVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIK-HVDR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 220 LESGYTNVKKMIEQVKvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLS 299
Cdd:cd19977 160 QDDVRKAISELLKLEK-PPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRKA 238
|
250 260
....*....|....*....|....*.
gi 1267416536 300 MEFLLEMIKEKDETRARQIILTPSLV 325
Cdd:cd19977 239 AELLLDRIENKPKGPPRQIVLPTELI 264
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-330 |
1.89e-70 |
|
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: 220.56 E-value: 1.89e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIAN-SEDLNEVEKTGLK 139
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDdAPDLQELAARGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYS 219
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 220 LESGYTNVKKMIeQVKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLS 299
Cdd:cd06285 161 IEAGREAAYRLL-SRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRA 239
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 300 MEFLLEMIKEKDETRaRQIILTPSLVVRESC 330
Cdd:cd06285 240 AELLLQLIEGGGRPP-RSITLPPELVVREST 269
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
61-329 |
3.91e-70 |
|
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: 219.82 E-value: 3.91e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEV--EKTGL 138
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELlaALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 139 KYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEY 218
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQVKvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd06275 161 EPEGGYEAMQRLLSQPP-RPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 299 SMEFLLEMIKEKDEtRARQIILTPSLVVRES 329
Cdd:cd06275 240 AVELLLDRIENKRE-EPQSIVLEPELIERES 269
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
61-328 |
2.46e-68 |
|
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: 215.12 E-value: 2.46e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANS--EDLNEVEKTGL 138
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTtaELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 139 KYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEY 218
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd06289 161 TREAGAEAARELLDA-APPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRR 239
|
250 260 270
....*....|....*....|....*....|
gi 1267416536 299 SMEFLLEMIkEKDETRARQIILTPSLVVRE 328
Cdd:cd06289 240 AARLLLRRI-EGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
61-329 |
1.94e-66 |
|
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: 210.07 E-value: 1.94e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLanIANSEDLNEVEKTGLKY 140
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIIL--GSHSLDIEEYKKLNIPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 141 VLINRKPSfYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSL 220
Cdd:cd06291 79 VSIDRYLS-EGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFSE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 221 ESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSM 300
Cdd:cd06291 158 EDAYELAKELLEK-YPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAV 236
|
250 260
....*....|....*....|....*....
gi 1267416536 301 EFLLEMIkEKDETRARQIILTPSLVVRES 329
Cdd:cd06291 237 ELLLKLI-EGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
61-327 |
2.00e-66 |
|
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: 210.19 E-value: 2.00e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIAN-SEDLNEVEKTGLK 139
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGpSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYS 219
Cdd:cd06280 81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 220 LESGYTNVKKMIEQVKVlPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLS 299
Cdd:cd06280 161 IEGGYEAVKALLDLPPR-PTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIA 239
|
250 260
....*....|....*....|....*...
gi 1267416536 300 MEFLLEMIKEKDETRaRQIILTPSLVVR 327
Cdd:cd06280 240 AQLLLERIEGQGEEP-RRIVLPTELIIR 266
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
61-329 |
6.14e-63 |
|
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: 201.24 E-value: 6.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNL-SNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEVEKTGLK 139
Cdd:cd06288 1 TIGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPPELTDIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSfyDKNFVGV--NNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGE 217
Cdd:cd06288 81 LVLLNCFDD--DPSLPSVvpDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 218 YSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGK 297
Cdd:cd06288 159 WGRESGYEAAKRLLSA-PDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGR 237
|
250 260 270
....*....|....*....|....*....|..
gi 1267416536 298 LSMEFLLEMIkEKDETRARQIILTPSLVVRES 329
Cdd:cd06288 238 RAAELLLDGI-EGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
3.67e-62 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 198.99 E-value: 3.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEVEKTGLKY 140
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAEGIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 141 VLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSL 220
Cdd:cd06290 81 VLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 221 ESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSM 300
Cdd:cd06290 161 ESGYEAMKKLLKR-GGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAA 239
|
250 260
....*....|....*....|....*....
gi 1267416536 301 EFLLEMIKEKDETrARQIILTPSLVVRES 329
Cdd:cd06290 240 EILLELIEGKGRP-PRRIILPTELVIRES 267
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
61-328 |
3.44e-60 |
|
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: 193.89 E-value: 3.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANS-EDLNEVEKTGLK 139
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSdEELILIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRK-PSFYDKNfVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEY 218
Cdd:cd06270 81 LVVINRYiPGLADRC-VWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd06270 160 TIEGGYAAAKQLLAR-GLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQA 238
|
250 260 270
....*....|....*....|....*....|
gi 1267416536 299 SMEFLLEMIKEKDETRARQiiLTPSLVVRE 328
Cdd:cd06270 239 AAELALNLAYGEPLPISHE--FTPTLIERD 266
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
61-327 |
1.27e-56 |
|
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: 184.67 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNvSNGHKKI-LTYLELMLEKQVDGLLLANIANSEDL--------- 130
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQ-TNYDKEKeLRALELLKTKQIDGLIITSRENDWEViepyakygp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 131 ----NEVEKTGLKYVLINRKPSFYDknfvgvnnplsselAVNHLVRQGYKRIAFFGGDPDI--NTARERKAGFISCMTQT 204
Cdd:cd06286 80 ivlcEETDSPDIPSVYIDRYEAYLE--------------ALEYLKEKGHRKIGYCLGRPESssASTQARLKAYQDVLGEH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 205 GLDIDPMLIYDGEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSEnfLVP 284
Cdd:cd06286 146 GLSLREEWIFTNCHTIEDGYKLAKKLLAL-KERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISE--LLN 222
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1267416536 285 LSSIDHSTYDMGKLSMEFLLEMIKEKdetRARQIILTPSLVVR 327
Cdd:cd06286 223 LTTIDQPLEEMGKEAFELLLSQLESK---EPTKKELPSKLIER 262
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
1.76e-56 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380516 [Multi-domain] Cd Length: 270 Bit Score: 184.78 E-value: 1.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLA-NIANSEDLNEVEKTGLK 139
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTpSDDDLSHLARLRARGTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYD--GE 217
Cdd:cd06293 81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVRELsaPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 218 YSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGK 297
Cdd:cd06293 161 ANAELGRAAAAQLLAM-PPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGR 239
|
250 260 270
....*....|....*....|....*....|..
gi 1267416536 298 LSMEFLLEMIKEKDETrARQIILTPSLVVRES 329
Cdd:cd06293 240 AAADLLLDEIEGPGHP-HEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
61-329 |
2.97e-55 |
|
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: 181.32 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLA-NIANSEDLNEVEKTGLK 139
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVpTGENSEGLQALIAQGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDK-NFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEY 218
Cdd:cd06299 81 VVFVDREVEGLGGvPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQVKVlPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd06299 161 RQDSGAAAAHRLLSRGDP-PTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRR 239
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 299 SMEFLLEMIkeKDETRARQIILTPSLVVRES 329
Cdd:cd06299 240 AVELLLALI--ENGGRATSIRVPTELIPRES 268
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
1.80e-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: 380501 [Multi-domain] Cd Length: 266 Bit Score: 179.27 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKkILTYLELMLEKQVDGL-LLANIANSEDLNEVEKTGLK 139
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDGViVTSATLSSELAEECARRGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLdiDPMLIYDGEYS 219
Cdd:cd06278 80 VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGL--PPPAVEAGDYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 220 LESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGI-RVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd06278 158 YEGGYEAARRLLAA-PDRPDAIFCANDLMALGALDAARQEGGlVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAEA 236
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 299 SMEFLLEMIkEKDETRARQIILTPSLVVRES 329
Cdd:cd06278 237 AVDLLLERI-ENPETPPERRVLPGELVERGS 266
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
61-329 |
3.82e-51 |
|
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: 170.78 E-value: 3.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVS-----NLSNPFYPPLIEGIEDVSFNNNFNVilcnvsnghKKILTYLELM--LEKQVDGLLLANIANSEDLNEV 133
Cdd:cd01544 1 TIGIIQWyseeeELEDPYYLSIRLGIEKEAKKLGYEI---------KTIFRDDEDLesLLEKVDGIIAIGKFSKEEIEKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 134 EKTGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARE-----RKAGFISCMTQTGLdI 208
Cdd:cd01544 72 KKLNPNIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEeiedpRLRAFREYMKEKGL-Y 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 209 DPMLIYDGEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSEnFLVP-LSS 287
Cdd:cd01544 151 NEEYIYIGEFSVESGYEAMKELLKE-GDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAK-YVTPpLTT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1267416536 288 IDHSTYDMGKLSMEFLLEMIKEKDETrARQIILTPSLVVRES 329
Cdd:cd01544 229 VHIPTEEMGRTAVRLLLERINGGRTI-PKKVLLPTKLIERES 269
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
61-329 |
9.87e-51 |
|
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: 169.66 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLL-------LANIaNSEDLNEV 133
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIieptksaLPNP-NLDLYEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 134 EKTGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAF-FGGDpDInTARERKAGFISCMTQTGLDIDP-- 210
Cdd:cd01541 80 QKKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGiFKSD-DL-QGVERYQGFIKALREAGLPIDDdr 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 211 MLIYD-GEYSLESGYTNVKKMIEQVKVlpeaiCTA----SDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPL 285
Cdd:cd01541 158 ILWYStEDLEDRFFAEELREFLRRLSR-----CTAivcyNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1267416536 286 SSIDHSTYDMGKLSMEFLLEMIKEKDEtrARQIILTPSLVVRES 329
Cdd:cd01541 233 TSVVHPKEELGRKAAELLLRMIEEGRK--PESVIFPPELIERES 274
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
28-329 |
5.52e-50 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 169.02 E-value: 5.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 28 VSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTY 107
Cdd:PRK11041 4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 108 LELMLEKQVDGLLLANIANSEDLNEVEKTGLK-YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPD 186
Cdd:PRK11041 84 VNLIITKQIDGMLLLGSRLPFDASKEEQRNLPpMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGPEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 187 INTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQVKVlPEAICTASDIIAFGVIKGLRDSGIRVPED 266
Cdd:PRK11041 164 MPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQP-PTAVFCHSDVMALGALSQAKRMGLRVPQD 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267416536 267 ISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIKEKDETRARQiILTPSLVVRES 329
Cdd:PRK11041 243 LSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSR-LLDCELIIRGS 304
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
61-329 |
3.39e-49 |
|
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: 165.45 E-value: 3.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSnpFYPP--LIEGIEDVSFNNNFNVILCNVSNG-HKKILTYLELMLEKQVDGLLLanIANSEDLNEVEKT- 136
Cdd:cd01574 1 TIGVIATGLS--LYGPasTLAGIERAARERGYSVSIATVDEDdPASVREALDRLLSQRVDGIIV--IAPDEAVLEALRRl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 --GLKYVLINRKPSfYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIy 214
Cdd:cd01574 77 ppGLPVVIVGSGPS-PGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPPVVE- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 215 dGEYSLESGYTNVKKMIEQVkvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYD 294
Cdd:cd01574 155 -GDWSAASGYRAGRRLLDDG--PVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAE 231
|
250 260 270
....*....|....*....|....*....|....*
gi 1267416536 295 MGKLSMEFLLEMIkEKDETRARQIILTPSLVVRES 329
Cdd:cd01574 232 LGRRAVELLLALI-EGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
61-319 |
5.39e-49 |
|
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: 165.06 E-value: 5.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVI-----VSNLSNPFYPPLIEGIEDVSFNNNFNVILcNVSNGHKKIL-TYLELMLEKQVDGL-LLANIANSEDLNEV 133
Cdd:cd06294 1 TIGLVlpssaEELFQNPFFSEVLRGISQVANENGYSLLL-ATGNTEEELLeEVKRMVRGRRVDGFiLLYSKEDDPLIEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 134 EKTGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLI 213
Cdd:cd06294 80 KEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 214 YDGEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTY 293
Cdd:cd06294 160 LLLDFSEEDGYDALQELLSK-PPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPY 238
|
250 260
....*....|....*....|....*.
gi 1267416536 294 DMGKLSMEFLLEMIKEKDETRARQII 319
Cdd:cd06294 239 ELGREAAKLLINLLEGPESLPKNVIV 264
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
6.93e-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: 380497 [Multi-domain] Cd Length: 268 Bit Score: 159.60 E-value: 6.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNE-VEKTGLK 139
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFElLEQRQVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLI------NRKPSfydknfVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDIN-TARERKAGFISCMTQTGLDIDPML 212
Cdd:cd06273 81 YVLTwsydedSPHPS------IGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNdRARARLAGIRDALAERGLELPEER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 213 IYDGEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHST 292
Cdd:cd06273 155 VVEAPYSIEEGREALRRLLAR-PPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 1267416536 293 YDMGKLSMEFLLEMIKEKDEtrARQIILTPSLVVRES 329
Cdd:cd06273 234 REIGELAARYLLALLEGGPP--PKSVELETELIVRES 268
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
57-329 |
4.00e-46 |
|
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: 157.80 E-value: 4.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 57 KRTNTVGVIV-------SNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLElmlEKQVDGL-LLANIANSE 128
Cdd:cd06295 1 QRSRTIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLD---SGRADGLiVLGQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 129 DLNEVEKTGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTArERKAGFISCMTQTGLDI 208
Cdd:cd06295 78 ALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVA-DRLQGYRDALAEAGLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 209 DPMLIYDGEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSI 288
Cdd:cd06295 157 DPSLLLSCDFTEESGYAAMRALLDS-GTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1267416536 289 DHSTYDMGKLSMEFLLEMIKEKDETRArqiILTPSLVVRES 329
Cdd:cd06295 236 RQDLALAGRLLVEKLLALIAGEPVTSS---MLPVELVVRES 273
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
61-327 |
8.14e-46 |
|
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: 156.94 E-value: 8.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLL-ANIANSEDLNEVEKTGLK 139
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILqPTGNNNDAYLELAQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTAR-ERKAGFISCMTQTGLDIDPMLI-YDGE 217
Cdd:cd06283 81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRrERLQGFLDALARYNIEGDVYVIeIEDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 218 YSLESGYTNVKKMIEQVKVlpeAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGK 297
Cdd:cd06283 161 EDLQQALAAFLSQHDGGKT---AIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGK 237
|
250 260 270
....*....|....*....|....*....|
gi 1267416536 298 LSMEFLLEMIKEKDETrARQIILTPSLVVR 327
Cdd:cd06283 238 AAAEILLERIEGDSGE-PKEIELPSELIIR 266
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-330 |
1.64e-44 |
|
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: 153.55 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLAniANSEDLNEV----EKT 136
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILT--PGDEDDPELaaalARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLINR-KPSFYDKnfVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYD 215
Cdd:cd06281 79 DIPVVLIDRdLPGDIDS--VLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 216 GEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDM 295
Cdd:cd06281 157 GSFSADSGFREAMALLRQ-PRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAV 235
|
250 260 270
....*....|....*....|....*....|....*
gi 1267416536 296 GKLSMEFLLEMIKEKDETRARQIILTPSLVVRESC 330
Cdd:cd06281 236 GRAAAELLLDRIEGPPAGPPRRIVVPTELILRDSC 270
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
2-331 |
6.40e-44 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 154.00 E-value: 6.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 2 ATMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSnpFYPP--LIE 79
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLA--LHAPsqIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 80 GIEDVSFNNNFNVILCNVS-NGHKKILTYLELMLEKQVDGLLLaNIANSEDlnEVEKTGLKY----VLINRKPSFYDKNF 154
Cdd:PRK09526 84 AIKSRADQLGYSVVISMVErSGVEACQAAVNELLAQRVSGVII-NVPLEDA--DAEKIVADCadvpCLFLDVSPQSPVNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 155 VGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDidPMLIYDGEYSLESGYTNVKKMIEQv 234
Cdd:PRK09526 161 VSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQ--PIAVREGDWSAMSGYQQTLQMLRE- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 235 KVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEmIKEKDETR 314
Cdd:PRK09526 238 GPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLA-LSQGQAVK 316
|
330
....*....|....*..
gi 1267416536 315 ARQIILTpSLVVRESCG 331
Cdd:PRK09526 317 GSQLLPT-SLVVRKSTA 332
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
61-329 |
2.07e-43 |
|
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 150.78 E-value: 2.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKIL-TYLELMLEKQVDGLLLAN-IANSEDLNE-VEKTG 137
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCDSDDEDLAdRLRRFLSRSRPDGVILTPpLSDDPALLDaLDELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 138 LKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGE 217
Cdd:cd01545 81 IPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVVQGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 218 YSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGK 297
Cdd:cd01545 161 FTFESGLEAAEALLDL-PDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMAR 239
|
250 260 270
....*....|....*....|....*....|..
gi 1267416536 298 LSMEFLLEMIKEKDETRARQiILTPSLVVRES 329
Cdd:cd01545 240 RAVELLIAAIRGAPAGPERE-TLPHELVIRES 270
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
1-341 |
2.37e-43 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 152.60 E-value: 2.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 1 MATMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEG 80
Cdd:PRK10727 1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 81 IEDVSFNN-NFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEVEKTGLKYVLINRKPSFYDKNFVGVNN 159
Cdd:PRK10727 81 VEQVAYHTgNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIPGMVLINRILPGFENRCIALDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 160 PLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQVKVLPE 239
Cdd:PRK10727 161 RYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFTA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 240 AICTaSDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSEnFLVP-LSSIDHSTYDMGKLSMEFLLEMIKEKDETRARQi 318
Cdd:PRK10727 241 VACY-NDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSR-YVRPrLTTVRYPIVTMATQAAELALALADNRPLPEITN- 317
|
330 340
....*....|....*....|...
gi 1267416536 319 ILTPSLVVRESCGYKRNKIDNLS 341
Cdd:PRK10727 318 VFSPTLVRRHSVSTPSLEASHHA 340
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
72-329 |
5.36e-43 |
|
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: 149.70 E-value: 5.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 72 PFYPPLIEGIEDVSFNNNFNVILCNVSNGHKkILTYLELMLEKQVDG-LLLANIANSEDLNEVEKTGLKYVLINRKPSFY 150
Cdd:cd06277 19 PFFSELIDGIEREARKYGYNLLISSVDIGDD-FDEILKELTDDQSSGiILLGTELEEKQIKLFQDVSIPVVVVDNYFEDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 151 DKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKM 230
Cdd:cd06277 98 NFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMKAL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 231 IEQVKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIKEK 310
Cdd:cd06277 178 LDTGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDP 257
|
250
....*....|....*....
gi 1267416536 311 DETRARQIILTpSLVVRES 329
Cdd:cd06277 258 DGGTLKILVST-KLVERGS 275
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
61-329 |
3.16e-42 |
|
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: 147.42 E-value: 3.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIA-NSEDLNEVEKTGLK 139
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDpTSRQLRLLRSAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLIN-------RKPSfydknfVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPML 212
Cdd:cd06296 81 FVLIDpvgepdpDLPS------VGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 213 IYDGEYSLESGYTNVKKMIEQVKvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHST 292
Cdd:cd06296 155 VREGDFTYEAGYRAARELLELPD-PPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPL 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 1267416536 293 YDMGKLSMEFLLEMIKEKDETrARQIILTPSLVVRES 329
Cdd:cd06296 234 REMGAVAVRLLLRLLEGGPPD-ARRIELATELVVRGS 269
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
61-320 |
4.46e-42 |
|
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: 146.87 E-value: 4.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDG-LLLANIANSEDLNEVEKTGLK 139
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGiILFATEITDEHRKALKKLKIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKpsFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDP-DINTARERKAGFISCMTQTGldIDPMLIYDGEY 218
Cdd:cd01542 81 VVVLGQE--HEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEeDIAVGVARKQGYLDALKEHG--IDEVEIVETDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQVKvlPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd01542 157 SMESGYEAAKELLKENK--PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEK 234
|
250 260
....*....|....*....|..
gi 1267416536 299 SMEFLLEMIKEKDEtrARQIIL 320
Cdd:cd01542 235 AAELLLDMIEGEKV--PKKQKL 254
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
61-329 |
6.84e-42 |
|
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: 146.64 E-value: 6.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNL----SNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSED-LNEVEK 135
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPrVRYLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 136 TGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYD 215
Cdd:cd06292 81 AGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLVVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 216 GEYSLESGYTNVKKMIEQVKVlPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDM 295
Cdd:cd06292 161 GENTEEGGYAAAARLLDLGPP-PTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEI 239
|
250 260 270
....*....|....*....|....*....|....
gi 1267416536 296 GKLSMEFLLEMIkEKDETRARQIILTPSLVVRES 329
Cdd:cd06292 240 GRAVVDLLLAAI-EGNPSEPREILLQPELVVRES 272
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
1-335 |
7.64e-42 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 148.77 E-value: 7.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 1 MATMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEG 80
Cdd:PRK10401 1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 81 IEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLllanIANSEDLNEVEKTGL-----KYVLINRKPSFYDKNFV 155
Cdd:PRK10401 81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNAL----IVHSKALSDDELAQFmdqipGMVLINRVVPGYAHRCV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 156 GVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYtnvKKMIEQV- 234
Cdd:PRK10401 157 CLDNVSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGE---AAMVELLg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 235 -KVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIKEKDET 313
Cdd:PRK10401 234 rNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNLDP 313
|
330 340
....*....|....*....|..
gi 1267416536 314 RARQIILtPSLVVRESCGYKRN 335
Cdd:PRK10401 314 RASHCFM-PTLVRRHSVATRQN 334
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
61-329 |
1.01e-41 |
|
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: 146.28 E-value: 1.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLL-LANIANSEDLNEVEKTGLK 139
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIfMGDELTEEIREEFKRSPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLIN------RKPSfydknfVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERK-AGFISCMTQTGLDIDPML 212
Cdd:cd06298 81 VVLAGtvdsdhEIPS------VNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKlQGYKRALEEAGLEFNEPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 213 IYDGEYSLESGYTNVKKMIEqvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHST 292
Cdd:cd06298 155 IFEGDYDYDSGYELYEELLE--SGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPL 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 1267416536 293 YDMGKLSMEfLLEMIKEKDETRARQIILTPSLVVRES 329
Cdd:cd06298 233 YDIGAVAMR-LLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-327 |
1.13e-41 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 148.32 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 2 ATMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEGI 81
Cdd:PRK10014 7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 82 EDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSED--LNEVEKTGLKYVLINRKPSFYDKNFVGVNN 159
Cdd:PRK10014 87 TEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDdlREMAEEKGIPVVFASRASYLDDVDTVRPDN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 160 PLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQVKVLPE 239
Cdd:PRK10014 167 MQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHNPTISA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 240 AICTaSDIIAFGVIKGLRDSGIRVPED---------ISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIkEK 310
Cdd:PRK10014 247 VVCY-NETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQRI-TH 324
|
330
....*....|....*..
gi 1267416536 311 DETRARQIILTPSLVVR 327
Cdd:PRK10014 325 EETHSRNLIIPPRLIAR 341
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
61-329 |
1.62e-41 |
|
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: 145.72 E-value: 1.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILcnvSNGHkkiltY--------LELMLEKQVDGLLLANIANSEDLNE 132
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLL---GNTG-----YspereeelIRALLSRRPAGLILTGTEHTPATRK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 133 -VEKTGLKYVLI-NRKPSFYDKNfVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINT-ARERKAGFISCMTQTGLDID 209
Cdd:cd01575 73 lLRAAGIPVVETwDLPDDPIDMA-VGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 210 PMLIYDGEYSLESGYTNVKKMIEQVKvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSID 289
Cdd:cd01575 152 LVLLVELPSSFALGREALAELLARHP-DLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVR 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1267416536 290 HSTYDMGKLSMEFLLEMIKEKDETrARQIILTPSLVVRES 329
Cdd:cd01575 231 VPRYEIGRKAAELLLARLEGEEPE-PRVVDLGFELVRRES 269
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
2.64e-41 |
|
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: 145.00 E-value: 2.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSN---LSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEVEKTG 137
Cdd:cd19974 1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGEISKEYLEKLKELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 138 LKYVLINrkpsFYDKNF----VGVNNPLSSELAVNHLVRQGYKRIAFFGgdpDINTAR---ERKAGFISCMTQTGLDIDP 210
Cdd:cd19974 81 IPVVLVD----HYDEELnadsVLSDNYYGAYKLTSYLIEKGHKKIGFVG---DINYTSsfmDRYLGYRKALLEAGLPPEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 211 -MLIYDGEYSLESGYTNVKKMIEqvKVLPEA-ICtASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSI 288
Cdd:cd19974 154 eEWLLEDRDDGYGLTEEIELPLK--LMLPTAfVC-ANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1267416536 289 DHSTYDMGKLSMEFLLEMIKEKDETRARQIILTPsLVVRES 329
Cdd:cd19974 231 EVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGK-LIERDS 270
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
61-325 |
1.94e-39 |
|
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: 140.38 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVS----NLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIA-NSEDLNEVEK 135
Cdd:cd20010 1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRvNDPRIAYLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 136 TGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYD 215
Cdd:cd20010 81 RGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALVRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 216 GEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNN-SFSENFLVPLSSIDHSTYD 294
Cdd:cd20010 161 GPLTEEGGYQAARRLLAL-PPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLTTTRSSLRD 239
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 295 MGKLSMEFLLEMIKEKDETRaRQIILTPSLV 325
Cdd:cd20010 240 AGRRLAEMLLALIDGEPAAE-LQELWPPELI 269
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
169-330 |
2.52e-39 |
|
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: 136.70 E-value: 2.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 169 HLVRQGYKRIAFFGGDPDIN--TARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNvkkMIEQVKVLPEAICTASD 246
Cdd:pfam13377 1 HLAELGHRRIALIGPEGDRDdpYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARE---RLRWLGALPTAVFVAND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 247 IIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIkEKDETRARQIILTPSLVV 326
Cdd:pfam13377 78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLL-NGEPAPPERVLLPPELVE 156
|
....
gi 1267416536 327 RESC 330
Cdd:pfam13377 157 REST 160
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
1.33e-38 |
|
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: 138.18 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLL--ANIANSEDLNEVEKTGL 138
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILtvGDAQGSEALELLEEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 139 KYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGD-PDINTARERKAGFISCMTQTGLDIDPMLiydgE 217
Cdd:cd06282 81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDfSASDRARLRYQGYRDALKEAGLKPIPIV----E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 218 YSLESGytnvkKMIEQVKVL------PEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHS 291
Cdd:cd06282 157 VDFPTN-----GLEEALTSLlsgpnpPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQP 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1267416536 292 TYDMGKLSMEFLLEMIkeKDETRARQIILtpSLVVRES 329
Cdd:cd06282 232 SRDMGRAAADLLLAEI--EGESPPTSIRL--PHHLREG 265
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
62-322 |
2.25e-37 |
|
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: 134.68 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 62 VGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDL--NEVEKTGLK 139
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGvaEKARGQNVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDK-NFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEY 218
Cdd:cd01537 82 VVFFDKEPSRYDKaYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 219 SLESGYTNVKKMIEQVKVlPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKL 298
Cdd:cd01537 162 DTASGKDKMDQWLSGPNK-PTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKT 240
|
250 260
....*....|....*....|....
gi 1267416536 299 SMEFLLEMIKEKDETraRQIILTP 322
Cdd:cd01537 241 TFDLLLNLADNWKID--NKVVRVP 262
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
61-329 |
2.31e-34 |
|
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: 126.81 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDLNEV-EKTGLK 139
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEViVPTEKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 140 YVLINRKPSFYDknFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTA----RERKAGFISCMTQTGLDIDPMLIYD 215
Cdd:cd06297 81 VVLIDANSMGYD--CVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTetvfREREQGFLEALNKAGRPISSSRMFR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 216 GEYSLESGYTNVKKMIEQVKvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENflVPLSSIDHSTYDM 295
Cdd:cd06297 159 IDNSSKKAECLARELLKKAD-NPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTTVRQPVEEM 235
|
250 260 270
....*....|....*....|....*....|....
gi 1267416536 296 GKLSMEFLLEMIKEkDETRARQIILTPSLVVRES 329
Cdd:cd06297 236 GEAAAKLLLKRLNE-YGGPPRSLKFEPELIVRES 268
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
89-328 |
1.27e-32 |
|
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: 122.10 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 89 NFNVILCNVSNGHkkILTYLELMLEKQVDGLLLANIANSEDL-NEVEKTGLKYVLINRKPSFYdkNFVGVNNPLSSELAV 167
Cdd:cd06272 32 NINLSICPYKVGH--LCTAKGLFSENRFDGVIVFGISDSDIEyLNKNKPKIPIVLYNRESPKY--STVNVDNEKAGRLAV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 168 NHLVRQGYKRIAFFGgDPDINTA-RERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQvKVLPEAICTASD 246
Cdd:cd06272 108 LLLIQKGHKSIAYIG-NPNSNRNqTLRGKGFIETCEKHGIHLSDSIIDSRGLSIEGGDNAAKKLLKK-KTLPKAIFCNSD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 247 IIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIkEKDETRARQIILTPSLVV 326
Cdd:cd06272 186 DIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLI-EGRENEIQQLILYPELIF 264
|
..
gi 1267416536 327 RE 328
Cdd:cd06272 265 RE 266
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
2-71 |
1.36e-29 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 108.06 E-value: 1.36e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 2 ATMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSN 71
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
1-323 |
4.00e-29 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 114.47 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 1 MATMKDISKKANVSLSTVSAVINQ--SAYVSPALTNRVMQAIEELNYKPNAvARSLKKKRTNTVGVIV-------SNLSN 71
Cdd:PRK10339 1 MATLKDIAIEAGVSLATVSRVLNDdpTLNVKEETKHRILEIAEKLEYKTSS-ARKLQTGAVNQHHILAiysyqqeLEIND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 72 PFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKIltylelmleKQVDGLLLANIANSEDLNEVEKTGLKYVLINRKPSFYD 151
Cdd:PRK10339 80 PYYLAIRHGIETQCEKLGIELTNCYEHSGLPDI---------KNVTGILIVGKPTPALRAAASALTDNICFIDFHEPGSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 152 KNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLdIDPMLIYDGEYSLESGYTNVKKMI 231
Cdd:PRK10339 151 YDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQV-VREEDIWRGGFSSSSGYELAKQML 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 232 EQVKvLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIG-ND--NNSFSenfLVPLSSIDHSTYDMGKLSMEFLLEmiK 308
Cdd:PRK10339 230 ARED-YPKALFVASDSIAIGVLRAIHERGLNIPQDISLISvNDipTARFT---FPPLSTVRIHSEMMGSQGVNLLYE--K 303
|
330
....*....|....*
gi 1267416536 309 EKDETRARQIILTPS 323
Cdd:PRK10339 304 ARDGRALPLLVFVPS 318
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
108-329 |
1.88e-27 |
|
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: 108.44 E-value: 1.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 108 LELMLEKQVDGLLlANIANSEDLNEVEKTGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGgDPDI 187
Cdd:cd01543 43 LDLLKGWKGDGII-ARLDDPELAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCG-FRNA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 188 NTARERKAGFISCMTQTGLDIDpmlIYDGEYSL--ESGYTNVKKMIEQVKVLPE--AICTASDIIAFGVIKGLRDSGIRV 263
Cdd:cd01543 121 AWSRERGEGFREALREAGYECH---VYESPPSGssRSWEEEREELADWLKSLPKpvGIFACNDDRARQVLEACREAGIRV 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1267416536 264 PEDISVIGNDNNSFSENFL-VPLSSIDHSTYDMGKLSMEFLLEMIKEkdETRARQIILTP--SLVVRES 329
Cdd:cd01543 198 PEEVAVLGVDNDELICELSsPPLSSIALDAEQIGYEAAELLDRLMRG--ERVPPEPILIPplGVVTRQS 264
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
107-325 |
1.97e-26 |
|
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: 105.58 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 107 YLELMLEKQVDGLLLANIaNSED--LNEVEKTGLKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGD 184
Cdd:cd06271 49 IRDLVETGSADGVILSEI-EPNDprVQFLTKQNFPFVAHGRSD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 185 PDINTARERKAGFISCMTQTGLdidPMLIYDGEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVP 264
Cdd:cd06271 128 ARYSPHDRRLQGYVRA*RDAGL---TGYPLDADTTLEAGRAAAQRLLAL-SPRPTAIVTMNDSATIGLVAGLQAAGLKIG 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267416536 265 EDISVIGNDNNSFSENFLVPLSSIDHST-YDMGKLSMEFLLEMIKEKDETRArQIILTPSLV 325
Cdd:cd06271 204 EDVSIIGKDSAPFLGAMITPPLTTVHAPiAEAGRELAKALLARIDGEDPETL-QVLVQPSLS 264
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
4-267 |
2.23e-26 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 106.89 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 4 MK--DISKKANVSLSTVSAVINQSA--Y-VSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLI 78
Cdd:PRK11303 1 MKldEIARLAGVSRTTASYVINGKAkqYrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 79 EGIEDVSFNNNFN-VILC---NVSNGHKKIltylELMLEKQVDGLLLANI--ANSEDLNEVEKTGLKYVLINRkpSFYDK 152
Cdd:PRK11303 81 KYLERQARQRGYQlLIACsddQPDNEMRCA----EHLLQRQVDALIVSTSlpPEHPFYQRLQNDGLPIIALDR--ALDRE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 153 NFVGV---NNPLSSELAvNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDpmLIYDGEYSLESGYTNVKK 229
Cdd:PRK11303 155 HFTSVvsdDQDDAEMLA-ESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREVH--YLYANSFEREAGAQLFEK 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1267416536 230 MIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDI 267
Cdd:PRK11303 232 WLET-HPMPDALFTTSYTLLQGVLDVLLERPGELPSDL 268
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
61-329 |
1.22e-23 |
|
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: 98.43 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVS-----NLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHkkilTYLELMLEKQVDGLLLANIanSEDLNEVE- 134
Cdd:cd06279 1 AIGVLLPddlsyAFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEG----SAAAAVRNAAVDGFIVYGL--SDDDPAVAa 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 135 --KTGLKYVLINRKPSfYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDIN-----------------TARERKA 195
Cdd:cd06279 75 lrRRGLPLVVVDGPAP-PGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGrergpvsaerlaaatnsVARERLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 196 GFISCMTQTGLDIDPMLIYDGEYSL-ESGYTNVKKMIEQVKVlPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGNDN 274
Cdd:cd06279 154 GYRDALEEAGLDLDDVPVVEAPGNTeEAGRAAARALLALDPR-PTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDD 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1267416536 275 NSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIkekDETRARQIILTPSLVVRES 329
Cdd:cd06279 233 IPEAAAADPGLTTVRQPAVEKGRAAARLLLGLL---PGAPPRPVILPTELVVRAS 284
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
61-325 |
1.99e-19 |
|
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: 86.49 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFN-VILCNVSN-GHKKILTylELMLEKQVDGLLLANIANSEDLNEV-EKTG 137
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQlLIACSDDDpEQERRLV--ENLIARQVDGLIVAPSTPPDDIYYLcQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 138 LKYVLINRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGE 217
Cdd:cd06274 79 LPVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 218 YSLESGYTNVKKMIEQVKVLPEAICTASdIIAF-GVIKGLRDSGIRVPEDIsVIGndnnSFSENFLV-----PLSSIDHS 291
Cdd:cd06274 159 YDRESGYQLMAELLARLGGLPQALFTSS-LTLLeGVLRFLRERLGAIPSDL-VLG----TFDDHPLLdflpnPVDSVRQD 232
|
250 260 270
....*....|....*....|....*....|....
gi 1267416536 292 TYDMGKLSMEFLLEmiKEKDETRARQIILTPSLV 325
Cdd:cd06274 233 HDEIAEHAFELLDA--LIEGQPEPGVIIIPPELI 264
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
4-308 |
2.37e-19 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 87.39 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 4 MKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKKKRTNTVGVIVSNLSNPFYPPLIEGIED 83
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 84 VSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANS-EDLNEVEKTGLKYV-LINRKPSFYDKNfVGVNNPL 161
Cdd:PRK14987 88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTpRTLKMIEVAGIPVVeLMDSQSPCLDIA-VGFDNFE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 162 SSELAVNHLVRQGYKRIAFFGGDPDINTARERKaGFISCMTQTGLDIDPMLIyDGEYSLESGYTNVKKMIEQVKVLPEAI 241
Cdd:PRK14987 167 AARQMTTAIIARGHRHIAYLGARLDERTIIKQK-GYEQAMLDAGLVPYSVMV-EQSSSYSSGIELIRQARREYPQLDGVF 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1267416536 242 CTASDiIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIK 308
Cdd:PRK14987 245 CTNDD-LAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIR 310
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
49-328 |
3.09e-19 |
|
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: 86.52 E-value: 3.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 49 AVARSLKKKRTNTVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLAniANSE 128
Cdd:COG1879 23 AAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVS--PVDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 129 D-----LNEVEKTGLKYVLINRKPSFYDKN-FVGVNNPLSSELAVNHLVRQ--GYKRIAFFGGDPDINTARERKAGFISC 200
Cdd:COG1879 101 DalapaLKKAKAAGIPVVTVDSDVDGSDRVaYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKEA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 201 MTQTGlDIDPMLIYDGEYSLESGYTNVKKMIEQvkvLPE--AICTASDIIAFGVIKGLRDSGIrvPEDISVIGNDNNSFS 278
Cdd:COG1879 181 LKEYP-GIKVVAEQYADWDREKALEVMEDLLQA---HPDidGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDGSPEA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1267416536 279 ENFLVP---LSSIDHSTYDMGKLSMEFLLEMIkeKDETRARQIILTPSLVVRE 328
Cdd:COG1879 255 LQAIKDgtiDATVAQDPYLQGYLAVDAALKLL--KGKEVPKEILTPPVLVTKE 305
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
5-56 |
3.57e-19 |
|
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: 79.76 E-value: 3.57e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1267416536 5 KDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPNAVARSLKK 56
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
61-311 |
4.28e-19 |
|
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: 85.31 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIaNSEDL----NEVEKT 136
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPV-DSEALvpavKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLINRKPSFYDKN--FVGVNNPLSSELAVNHLVRQ--GYKRIAFFGGDPDINTARERKAGFISCMTQTGlDIDPML 212
Cdd:cd01536 80 GIPVVAVDTDIDGGGDVvaFVGTDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKEALKKYP-DIEIVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 213 IYDGEYSLESGYTNVKKMIEQVKVLpEAICTASDIIAFGVIKGLRDSGIrvPEDISVIGNDNNSFSENFLVP---LSSID 289
Cdd:cd01536 159 EQPANWDRAKALTVTENLLQANPDI-DAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTPEALKAIKDgelDATVA 235
|
250 260
....*....|....*....|..
gi 1267416536 290 HSTYDMGKLSMEFLLEMIKEKD 311
Cdd:cd01536 236 QDPYLQGYLAVEAAVKLLNGEK 257
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
164-308 |
2.39e-18 |
|
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: 83.36 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 164 ELAVNHLVRQGYKRIAFFGGDPDINTARERKAGFISCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQVKvLPEAICT 243
Cdd:cd20009 107 YEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPP-RPDGIIC 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1267416536 244 ASDIIAFGVIKGLRDSGIRVPEDISVIGNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIK 308
Cdd:cd20009 186 ASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIE 250
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
62-311 |
3.65e-17 |
|
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: 80.05 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 62 VGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNG-HKKILTYLELMLEKQVDGLLLaNIANSEDLNEV----EKT 136
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEAdAAEQVAQIEDAIAQGVDAIIV-APVDPTALAPVlkkaKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLINR-KPSFYDKNFVGVNNPLSSELAVNHLVRQ--GYKRIAFFGGDPDINTARERKAGFISCMTQ--TGLDIDPm 211
Cdd:pfam13407 80 GIPVVTFDSdAPSSPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKEkyPGIKVVA- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 212 LIYDGEYSLESGYTNVKKMIEQVKVLPEAICTASDIIAFGVIKGLRDSGIRvpEDISVIGNDNNSFSENFL---VPLSSI 288
Cdd:pfam13407 159 EVEGTNWDPEKAQQQMEALLTAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEALEAIkdgTIDATV 236
|
250 260
....*....|....*....|...
gi 1267416536 289 DHSTYDMGKLSMEFLLEMIKEKD 311
Cdd:pfam13407 237 LQDPYGQGYAAVELAAALLKGKK 259
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
3-48 |
1.88e-16 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 72.28 E-value: 1.88e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1267416536 3 TMKDISKKANVSLSTVSAVINQSAYVSPALTNRVMQAIEELNYKPN 48
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
59-318 |
4.84e-16 |
|
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: 77.17 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 59 TNTVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVsNGHKKILT-YLELMLEKQVDGLLLANIANSED--LNEVEK 135
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAV-GDGEDTLTnAIDLLLASGADGIIITTPAPSGDdiTAKAEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 136 TGLKYVLINRkpSFYDKNFVGVNNPL---SSELAVNHLVRQGYKR-IAFFGGDPDINTARERKAGFISCMTQTGLDIDPM 211
Cdd:pfam00532 80 YGIPVIAADD--AFDNPDGVPCVMPDdtqAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGREVKIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 212 LIYDGEYSLESGYTNVKKMIEQVkvlPE--AICTASDIIAFGVIKGLRDSG-IRVPEDISVIGNDNNSFSE--------N 280
Cdd:pfam00532 158 HVATGDNDIPDAALAANAMLVSH---PTidAIVAMNDEAAMGAVRALLKQGrVKIPDIVGIGINSVVGFDGlskaqdtgL 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 1267416536 281 FLVPLSSIDHSTYDMGKLSMEFLLEMI-KEKDETRARQI 318
Cdd:pfam00532 235 YLSPLTVIQLPRQLLGIKASDMVYQWIpKFREHPRVLLI 273
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
116-329 |
2.23e-11 |
|
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: 63.21 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 116 VDG-LLLANIANSEDLNEVEKTGLKYVLINRKPSFY-DKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGDPDINTARER 193
Cdd:cd06287 57 VDGaIVVEPTVEDPILARLRQRGVPVVSIGRAPGTDePVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLES 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 194 KAGFISCMTQTGLDidPMLIYDGEYSLES-GYTNVKKMIEQvkvLP--EAICTASDIIAFGVIKGLRDSGIRVPEDISVI 270
Cdd:cd06287 137 EAAYLRFAQEYGTT--PVVYKVPESEGERaGYEAAAALLAA---HPdiDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVV 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1267416536 271 GNDNNSFSENFLVPLSSIDHSTYDMGKLSMEFLLEMIKEkdETRARQIILTPSLVVRES 329
Cdd:cd06287 212 TRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSG--EERSVEVGPAPELVVRAS 268
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
61-273 |
2.78e-11 |
|
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: 63.17 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANI---ANSEDLNEVEKTG 137
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIdvkALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 138 LKYVLINRK-----PSFYdknfVGVNNPLSSELAVNHLVRQ--GYKRIAFFGGDPDINTARERKAGFISCMtQTGLDIDP 210
Cdd:cd19968 81 IPVVTVDRRaegaaPVPH----VGADNVAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGFHEEL-AAGPKIKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1267416536 211 MLIYDGEYSLESGYTNVKKMIEQVKVLPEAICTASDIIAFGVIKGLRDSGIRVpEDISVIGND 273
Cdd:cd19968 156 VFEQTGNFERDEGLTVMENILTSLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFD 217
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
61-273 |
2.43e-10 |
|
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: 60.31 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANS---EDLNEVEKTG 137
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATgwdPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 138 LKYVLINRKPSFYDKN----FVGVNNPLSSELAVNHLVRQgYK----RIAFFGGDPDINTARERKAGFiscmtQTGLDID 209
Cdd:cd06309 81 IPVILVDRTIDGEDGSlyvtFIGSDFVEEGRRAAEWLVKN-YKggkgNVVELQGTAGSSVAIDRSKGF-----REVIKKH 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1267416536 210 PMLIY----DGEYSLESGYTNVKKMIEQVKVLPEAICTASDIIAFGVIKGLRDSGIRVPEDISVIGND 273
Cdd:cd06309 155 PNIKIvasqSGNFTREKGQKVMENLLQAGPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGID 222
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
62-273 |
1.01e-09 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 58.43 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 62 VGVIVSNL---SNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLANIANSEDL--NEVEKT 136
Cdd:cd01391 2 IGVVTSSLhqiREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIViqNLAQLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLI-------NRKPSFYDKNFVGVNNPLSSELAVNHLVRQGYKRIAFFGGdPDINTARERKAGFISCMTQTGLDID 209
Cdd:cd01391 82 DIPQLALdatsqdlSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHG-EGLNSGELRMAGFKELAKQEGICIV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1267416536 210 PMLIYDgEYSLESGYTNVKKMIEQvKVLPEAICTASDIIAFGVIKGLRDSGIRvpEDISVIGND 273
Cdd:cd01391 161 ASDKAD-WNAGEKGFDRALRKLRE-GLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSD 220
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-326 |
7.59e-08 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 52.68 E-value: 7.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDV--SFNNNFNVILcnVSNGH--KKILTYLELMLEKQVDgLLLANIANSEDLNE-VEK 135
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAaaEINPGAKVTV--VDARYdlAKQFSQIDDFIAQGVD-LILLNAADSAGIEPaIKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 136 T---GLKYVLINRKPSFYDKnFVGVNNPLSSELAVNHLVRQ--GYKRIAFFGGdPDINTARERKAGFISCMTQTGlDIDP 210
Cdd:cd06321 78 AkdaGIIVVAVDVAAEGADA-TVTTDNVQAGYLACEYLVEQlgGKGKVAIIDG-PPVSAVIDRVNGCKEALAEYP-GIKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 211 MLIYDGEYSLESGYTNVKKMIEQVKVLpEAICTASDIIAFGVIKGLRDSGIR---------VPEDISVIGNDNNSFSEnf 281
Cdd:cd06321 155 VDDQNGKGSRAGGLSVMTRMLTAHPDV-DGVFAINDPGAIGALLAAQQAGRDdivitsvdgSPEAVAALKREGSPFIA-- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1267416536 282 lvplsSIDHSTYDMGKLSMEFLLEMIkeKDETRARQIILTPSLVV 326
Cdd:cd06321 232 -----TAAQDPYDMARKAVELALKIL--NGQEPAPELVLIPSTLV 269
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
61-273 |
8.18e-08 |
|
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: 52.55 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIED-VSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLAniANSED-----LNEVE 134
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAeAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVS--PNEADaltpvVKKAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 135 KTGLKYVLINRKPSFYDKN-FVGVNNPLSSELAVNHLVRQ-GYK-RIAFFGGDPDINTARERKAGFISCMTQTGlDIDPM 211
Cdd:cd06308 79 DAGIPVIVLDRKVSGDDYTaFIGADNVEIGRQAGEYIAELlNGKgNVVEIQGLPGSSPAIDRHKGFLEAIAKYP-GIKIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1267416536 212 LIYDGEYSLESGYTNVKKMIEQVKVlPEAICTASDIIAFGVIKGLRDSGIRvpEDISVIGND 273
Cdd:cd06308 158 ASQDGDWLRDKAIKVMEDLLQAHPD-IDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVD 216
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
113-271 |
4.63e-06 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380547 [Multi-domain] Cd Length: 317 Bit Score: 47.60 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 113 EKQVDGLLLANIANSED--LNEVEKTGLKYVLINRKPSFYDKNFVGVN-----NPLSS----------ELAvNHLVRQGY 175
Cdd:cd06324 56 PPKPDYLILVNEKGVAPelLELAEQAKIPVFLINNDLTDEERALLGKPrekfkYWLGSivpdneqagyLLA-KALIKAAR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 176 K-------RIAFFGGDPDINTARERKAGFISCMTQTGlDIDPMLIYDGEYSLESGYTNVKKMIEQVkvlPE--AICTASD 246
Cdd:cd06324 135 KksddgkiRVLAISGDKSTPASILREQGLRDALAEHP-DVTLLQIVYANWSEDEAYQKTEKLLQRY---PDidIVWAAND 210
|
170 180
....*....|....*....|....*
gi 1267416536 247 IIAFGVIKGLRDSGIRVPEDISVIG 271
Cdd:cd06324 211 AMALGAIDALEEAGLKPGKDVLVGG 235
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
112-322 |
4.69e-06 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 47.24 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 112 LEKQVD-GLLLANIANSEDLNEVEKTGLKYvlinrkpsfydkNFVGVNNPLSSELAVNHLVRQGYK--RIAFFGGDPDIN 188
Cdd:cd19970 76 LKKAVDaGIAVINIDNRLDADALKEGGINV------------PFVGPDNRQGAYLAGDYLAKKLGKggKVAIIEGIPGAD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 189 TARERKAGFISCMTQTGLDIdpMLIYDGEYSLESGYTNVKKMIEQVKVLpEAICTASDIIAFGVIKGLRDSGIRvpEDIS 268
Cdd:cd19970 144 NAQQRKAGFLKAFEEAGMKI--VASQSANWEIDEANTVAANLLTAHPDI-RGILCANDNMALGAIKAVDAAGKA--GKVL 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1267416536 269 VIGNDNNSFSENFL---VPLSSIDHSTYDMGKLSMEFLLEMIKEKDetrARQIILTP 322
Cdd:cd19970 219 VVGFDNIPAVRPLLkdgKMLATIDQHPAKQAVYGIEYALKMLNGEE---VPGWVKTP 272
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
62-311 |
2.17e-05 |
|
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: 45.33 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 62 VGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKI--LTYLELMLEKQVDGLLLANIANS---EDLNEVEKT 136
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPSETDTQgqLNLLETMLNKGYDAILVSPISDTnliPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLINRKP--------SFYDKNFVGVNNPLSSELAVNHLVRQ--GYKRIAFFGGDPDINTARERKAGFISCMTQ-TG 205
Cdd:cd06320 82 GIPVINLDDAVdadalkkaGGKVTSFIGTDNVAAGALAAEYIAEKlpGGGKVAIIEGLPGNAAAEARTKGFKETFKKaPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 206 LDIDPMLiyDGEYSLESGYTNVKKMIEQVKVLpEAICTASDIIAFGVIKGLRDSGIRvpEDISVIGNDNN-----SFSEN 280
Cdd:cd06320 162 LKLVASQ--PADWDRTKALDAATAILQAHPDL-KGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDGIpeakkSIKAG 236
|
250 260 270
....*....|....*....|....*....|.
gi 1267416536 281 FLVplSSIDHSTYDMGKLSMEFLLEMIKEKD 311
Cdd:cd06320 237 ELT--ATVAQYPYLEGAMAVEAALRLLQGQK 265
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
61-326 |
2.36e-05 |
|
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: 45.48 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDgLLLANIANSEDL----NEVEKT 136
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVD-VLILNPVDPEGLtpavKAAKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLINR--KPSFYDKNFVG----VNNPLSSELAVNHLVRQGYKrIAFFGGDPDINTARERKAGFIScmtqtGLDiDP 210
Cdd:cd06318 80 GIPVITVDSalDPSANVATQVGrdnkQNGVLVGKEAAKALGGDPGK-IIELSGDKGNEVSRDRRDGFLA-----GVN-EY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 211 MLIYDGEYSLE---SGYTN------VKKMIEQVKVLPEA--ICTASDIIAFGVIKGLRDSGIRvpEDISVIGNDNNSFS- 278
Cdd:cd06318 153 QLRKYGKSNIKvvaQPYGNwirsgaVAAMEDLLQAHPDInvVYAENDDMALGAMKALKAAGML--DKVKVAGADGQKEAl 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1267416536 279 ----ENFLVPLSSIDHSTydMGKLSMEFLLEmiKEKDETRARQIILTPSLVV 326
Cdd:cd06318 231 klikDGKYVATGLNDPDL--LGKTAVDTAAK--VVKGEESFPEFTYTPTALI 278
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
108-277 |
7.53e-04 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 40.68 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 108 LELMLEKQVDGLLLANiANSEDLNE-VEKT---GLKYVLINRKPSFYDK-NFVGVNNPLSSELAVNHLVR--QGYKRIAF 180
Cdd:cd20004 50 IEYFIDQGVDGIVLAP-LDRKALVApVERAraqGIPVVIIDSDLGGDAViSFVATDNYAAGRLAAKRMAKllNGKGKVAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 181 FGGDPDINTARERKAGFISCMTQTGLDIDpmlIYDGEYsleSGYTNVKKMIEQVKVLPE-----AICTASDIIAFGVIKG 255
Cdd:cd20004 129 LRLAKGSASTTDRERGFLEALKKLAPGLK---VVDDQY---AGGTVGEARSSAENLLNQypdvdGIFTPNESTTIGALRA 202
|
170 180
....*....|....*....|..
gi 1267416536 256 LRDSGirVPEDISVIGNDNNSF 277
Cdd:cd20004 203 LRRLG--LAGKVKFIGFDASDL 222
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
61-312 |
1.79e-03 |
|
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: 39.59 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILCNVSNGHKKILTYLELMLEKQVDGLLLaNIANSEDL-NEVEKT--- 136
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLI-NPTDSDAVsPAVEEAnea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLINRKPSFYDK-NFVGVNNPLSSELAVNHLVR--QGYKRIAFFGGDPDINTARERKAGFISCMTQTGlDIDPMLI 213
Cdd:cd06323 80 GIPVITVDRSVTGGKVvSHIASDNVAGGEMAAEYIAKklGGKGKVVELQGIPGTSAARERGKGFHNAIAKYP-KINVVAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 214 YDGEYSLESGYTNVKKMIEQVKVLpEAICTASDIIAFGVIKGLRDSGirvPEDISVIGNDNN-----SFSENFLvpLSSI 288
Cdd:cd06323 159 QTADFDRTKGLNVMENLLQAHPDI-DAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTpdavkAVKDGKL--AATV 232
|
250 260
....*....|....*....|....
gi 1267416536 289 DHSTYDMGKLSMEFLLEMIKEKDE 312
Cdd:cd06323 233 AQQPEEMGAKAVETADKYLKGEKV 256
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-310 |
2.18e-03 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 39.25 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSFNNNFNVILC-----NVSNGHKKILtylELMLEKQVDGLLLANIaNSEDL----N 131
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVgpeseEDVAGQNSLL---EELINKKPDAIVVAPL-DSEDLvdplK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 132 EVEKTGLKYVLINR--KPSFYDkNFVGVNNPLSSELAVNHLVRQ--GYKRIAFFGGDPDINTARERKAGFISCMTQtgld 207
Cdd:cd06310 77 DAKDKGIPVIVIDSgiKGDAYL-SYIATDNYAAGRLAAQKLAEAlgGKGKVAVLSLTAGNSTTDQREEGFKEYLKK---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 208 iDPMliydGEYSLESGYTN------VKKMIEQVKVLPEA--ICTASDIIAFGVIKGLRDSGIRvpEDISVIGNDNNSFSE 279
Cdd:cd06310 152 -HPG----GIKVLASQYAGsdyakaANETEDLLGKYPDIdgIFATNEITALGAAVAIKSRKLS--GQIKIVGFDSQEELL 224
|
250 260 270
....*....|....*....|....*....|....
gi 1267416536 280 NFL---VPLSSIDHSTYDMGKLSMEFLLEMIKEK 310
Cdd:cd06310 225 DALkngKIDALVVQNPYEIGYEGIKLALKLLKGE 258
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
61-313 |
4.96e-03 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 38.33 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 61 TVGVIVSNLSNPFYPPLIEGIEDVSF-NNNFNVILCNVSNGHKKILTYLELMLEKQVDGLL--LANIANSEDLNE-VEKT 136
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKaGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVvnLVDRTAAQTIIDkAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 137 GLKYVLINRKPS-----FYDKN-FVGVNNPLS----SELAVNHLVRQ--------GYKRIAFFGGDPDINTARERKAGFI 198
Cdd:cd01539 82 NIPVIFFNREPSredlkSYDKAyYVGTDAEESgimqGEIIADYWKANpeidkngdGKIQYVMLKGEPGHQDAIARTKYSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1267416536 199 SCMTQTGLDIDPMLIYDGEYSLESGYTNVKKMIEQV--KVlpEAICTASDIIAFGVIKGLRDSG---IRVPEDISVIGND 273
Cdd:cd01539 162 KTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYgdKI--ELVIANNDDMALGAIEALKAAGyntGDGDKYIPVFGVD 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1267416536 274 NN-----SFSENFLvpLSSIDHSTYDMGKLSMEFLLEMIKEKDET 313
Cdd:cd01539 240 ATpealeAIKEGKM--LGTVLNDAKAQAKAIYELAKNLANGKEPL 282
|
|
| |
