|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
4-327 |
1.01e-106 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 314.83 E-value: 1.01e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 4 QKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEFA 83
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 84 YHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL----SSNIPFVSIDRTYENKAIPCVSS 158
Cdd:COG1609 81 RGIEEAARERGYQLLLANSDEdPEREREALRLLLSRRVDGLILAGSRLDDARLerlaEAGIPVVLIDRPLPDPGVPSVGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 159 DNQAGAELAADTLIAKGGRHFAFIGGHNkTINETKKRRLYFEKRIVEAGFPCQ---VLDLEEPYDDFVGQVEEFLINNPQ 235
Cdd:COG1609 161 DNRAGARLATEHLIELGHRRIAFIGGPA-DSSSARERLAGYREALAEAGLPPDpelVVEGDFSAESGYEAARRLLARGPR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 236 VDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKRER-PLQV 314
Cdd:COG1609 240 PTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDApPERV 319
|
330
....*....|...
gi 1239654491 315 TLPISYVDGKTTK 327
Cdd:COG1609 320 LLPPELVVRESTA 332
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
66-325 |
2.51e-100 |
|
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: 295.97 E-value: 2.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSP-IDDYLSSNIPFVS 143
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEdEEKEKEYLEMLKRNKVDGIILGSHSLdIEEYKKLNIPIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 144 IDRtYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKtINETKKRRLYFEKRIVEAGFPCQVLDLEEP---YD 220
Cdd:cd06291 81 IDR-YLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSN-NSPANERYRGFEDALKEAGIEYEIIEIDENdfsEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 221 DFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVAC 300
Cdd:cd06291 159 DAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAVEL 238
|
250 260
....*....|....*....|....*.
gi 1239654491 301 LVDVIEKRER-PLQVTLPISYVDGKT 325
Cdd:cd06291 239 LLKLIEGEEIeESRIVLPVELIERET 264
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
66-317 |
9.16e-68 |
|
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: 212.76 E-value: 9.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL----SSNIP 140
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEdPEREREYLRLLLSRRVDGIILAPSSLDDELLeellAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFP-CQVLDLEEPY 219
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGG-PLDLSTSRERLEGYRDALAEAGLPvDPELVVEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 220 DDFVGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEA 297
Cdd:cd06267 160 SEESGYeaARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAA 239
|
250 260
....*....|....*....|.
gi 1239654491 298 VACLVDVIEKRER-PLQVTLP 317
Cdd:cd06267 240 AELLLERIEGEEEpPRRIVLP 260
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-321 |
8.32e-57 |
|
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: 184.66 E-value: 8.32e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISGPKRELDYLTMLQQNKVDGIIAITYSP----IDDYLSSNIPF 141
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDALRQLLQYRVDGVIVTSATLsselAEECARRGIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 142 VSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGH--NKTINEtkkRRLYFEKRIVEAGFPCQVLDLEEP- 218
Cdd:cd06278 81 VLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPegTSTSRE---RERGFRAALAELGLPPPAVEAGDYs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 219 YDDFVGQVEEFLINNPQVDAIFTIND---FTALDTLAvlEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQ 295
Cdd:cd06278 158 YEGGYEAARRLLAAPDRPDAIFCANDlmaLGALDAAR--QEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAE 235
|
250 260
....*....|....*....|....*..
gi 1239654491 296 EAVACLVDVIEKRERPLQ-VTLPISYV 321
Cdd:cd06278 236 AAVDLLLERIENPETPPErRVLPGELV 262
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
8-311 |
9.69e-54 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 179.15 E-value: 9.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 8 TMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEFAYHVE 87
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 88 VALSKKNYKLLLCNI-SGPKRELDYLTMLQQNKVDGIIAITYSPIDDYLS-----SNIPFVSIDRTYENKAIPCVSSDNQ 161
Cdd:PRK10703 83 KNCYQKGYTLILCNAwNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAmleeyRHIPMVVMDWGEAKADFTDAIIDNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 162 -AGAELAADTLIAKGGRHFAFIGGHnKTINETKKRRLYFEKRIVEAGFPCQ----VLDLEEPYDDFvGQVEEFLINNPQV 236
Cdd:PRK10703 163 fEGGYLAGRYLIERGHRDIGVIPGP-LERNTGAGRLAGFMKAMEEANIKVPeewiVQGDFEPESGY-EAMQQILSQKHRP 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239654491 237 DAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVI-EKRERP 311
Cdd:PRK10703 241 TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIvNKREEP 316
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
9-314 |
1.50e-51 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 173.35 E-value: 1.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 9 MKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEFAYHVEV 88
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 89 ALSKKNYKLLLCNISGPKRELDY-LTMLQQNKVDGIIAI---TYSPIDDYLSS--NIPFVSIDRT---YENKAIpcvsSD 159
Cdd:PRK10423 81 SCFERGYSLVLCNTEGDEQRMNRnLETLMQKRVDGLLLLcteTHQPSREIMQRypSVPTVMMDWApfdGDSDLI----QD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 160 NQ-AGAELAADTLIAKGGRHFAFIGG-HNKTineTKKRRLY-FEKRIVEAGFPcqVLDLEEPYDDF-----VGQVEEFLI 231
Cdd:PRK10423 157 NSlLGGDLATQYLIDKGYTRIACITGpLDKT---PARLRLEgYRAAMKRAGLN--IPDGYEVTGDFefnggFDAMQQLLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 232 NNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKRERP 311
Cdd:PRK10423 232 LPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQ 311
|
...
gi 1239654491 312 LQV 314
Cdd:PRK10423 312 QQR 314
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-317 |
1.72e-51 |
|
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: 171.30 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNiSG--PKRELDYLTMLQQNKVDGIIAITYSPIDDYLSS----NI 139
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCN-SGrdPERERRYLEMLESQRVRGLIVTPSDDDLSHLARlrarGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 140 PFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKtINETKKRRLYFEKRIVEAGFPCQVLDLEEPY 219
Cdd:cd06293 80 AVVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLR-TRQVAERLAGARAAVAEAGLDPDEVVRELSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 220 DDF---VGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMA 294
Cdd:cd06293 159 PDAnaeLGRaaAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELG 238
|
250 260
....*....|....*....|....
gi 1239654491 295 QEAVACLVDVIE-KRERPLQVTLP 317
Cdd:cd06293 239 RAAADLLLDEIEgPGHPHEHVVFQ 262
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-317 |
1.36e-50 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 168.94 E-value: 1.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYLS----SNIP 140
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDdPERELAALDSLLSRRVDGLIITPARDDAPDLQelaaRGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETkkRRLY-FEKRIVEAGFPCQVLDLEEPY 219
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGR--DRLRgYRRALAEAGLPVPDERIVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 220 DDFVG---QVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQE 296
Cdd:cd06285 159 FTIEAgreAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRR 238
|
250 260
....*....|....*....|..
gi 1239654491 297 AVACLVDVIE-KRERPLQVTLP 317
Cdd:cd06285 239 AAELLLQLIEgGGRPPRSITLP 260
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
66-317 |
9.47e-49 |
|
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: 163.85 E-value: 9.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNiSG--PKRELDYLTMLQQNKVDGIIAITYSPIDDYLS----SNI 139
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCN-TDedPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEklvkSGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 140 PFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINeTKKRRLYFEKRIVEAGfpcqvLDLEEPY 219
Cdd:cd19977 80 PVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELST-RQERLEGYKAALADHG-----LPVDEEL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 220 ---DDFVGQVE----EFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEA 292
Cdd:cd19977 154 ikhVDRQDDVRkaisELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYE 233
|
250 260
....*....|....*....|....*..
gi 1239654491 293 MAQEAVACLVDVIE-KRER-PLQVTLP 317
Cdd:cd19977 234 IGRKAAELLLDRIEnKPKGpPRQIVLP 260
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
66-321 |
9.95e-47 |
|
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: 158.96 E-value: 9.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYLS-----SNI 139
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNdPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAEllaalRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 140 PFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhnKTINETKKRRLY-FEKRIVEAGfpcqvLDLEEP 218
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITG--PLEHSVSRERLAgFRRALAEAG-----IEVPPS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 219 Y---DDFVGQ-----VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPL 290
Cdd:cd06275 154 WiveGDFEPEggyeaMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPK 233
|
250 260 270
....*....|....*....|....*....|..
gi 1239654491 291 EAMAQEAVACLVDVIE-KRERPLQVTLPISYV 321
Cdd:cd06275 234 DELGELAVELLLDRIEnKREEPQSIVLEPELI 265
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-325 |
1.16e-45 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 155.90 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNIS-GPKRELDYLTMLQQNKVDGIIAITYSPIDDYL-----SSNI 139
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDyDPARELDAVETLLEQRVDGLILTVGDAQGSEAlelleEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 140 PFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRLYFEKRIVEAGF----PCQVlDL 215
Cdd:cd06282 81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRARLRYQGYRDALKEAGLkpipIVEV-DF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 216 EEPydDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQ 295
Cdd:cd06282 160 PTN--GLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGR 237
|
250 260 270
....*....|....*....|....*....|
gi 1239654491 296 EAVACLVDVIEKRERPLQVTLPISYVDGKT 325
Cdd:cd06282 238 AAADLLLAEIEGESPPTSIRLPHHLREGGS 267
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
66-325 |
1.11e-44 |
|
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: 153.48 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNI-SGPKRELDYLTMLQQNKVDGIIAITYSPIDDYL----SSNIP 140
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTgSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKqllkNMNIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRLYFEKRIVEAGFPcqvldLEEP-- 218
Cdd:cd19975 81 VVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPRYEGYKKALKDAGLP-----IKENli 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 219 ------YDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEA 292
Cdd:cd19975 156 vegdfsFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYE 235
|
250 260 270
....*....|....*....|....*....|....
gi 1239654491 293 MAQEAVACLVDVIEKRERPL-QVTLPISYVDGKT 325
Cdd:cd19975 236 MGKKAVELLLDLIKNEKKEEkSIVLPHQIIERES 269
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
66-317 |
2.08e-43 |
|
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: 150.00 E-value: 2.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL---SSNIPF 141
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSdPEREDDLLDMLRSRRVDGVILLSGRLDAELLselSKRYPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 142 VSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRLYFEkRIVEAGFPCQVLDLEEP--- 218
Cdd:cd06284 81 VQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRR-ALAEAGLPVDEDLIIEGdfs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 219 YDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAV 298
Cdd:cd06284 160 FEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAA 239
|
250 260
....*....|....*....|
gi 1239654491 299 ACLVDVIEKRERPLQ-VTLP 317
Cdd:cd06284 240 ELLLEKIEGEGVPPEhIILP 259
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
66-321 |
2.67e-43 |
|
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: 150.09 E-value: 2.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL-----SSNI 139
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNdFEREKKYIQELKERNVDGIIIASSNISDEAIikllkEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 140 PFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRLYFEKrIVEAGFPCQVLDLEEPY 219
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNA-LQDHNLPIDESWIYSGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 220 DDFVGQVEEF--LINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEA 297
Cdd:cd19976 160 SSLEGGYKAAeeLLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239
|
250 260
....*....|....*....|....*
gi 1239654491 298 VACLVDVI-EKRERPLQVTLPISYV 321
Cdd:cd19976 240 AKLLLKIIkNPAKKKEEIVLPPELI 264
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
66-298 |
1.02e-42 |
|
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: 148.44 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAIT-YSPIDD---YLSSNIP 140
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHdAEEEREAIEFLLDRRCDAIILHSrALSDEElilIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTIneTKKRRL-------------YFEKRIVEAG 207
Cdd:cd06270 81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIP--DARERLagyrdalaeagipLDPSLIIEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 208 FpcqvlDLEEPYDdfvgQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIR 287
Cdd:cd06270 159 F-----TIEGGYA----AAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVH 229
|
250
....*....|.
gi 1239654491 288 QPLEAMAQEAV 298
Cdd:cd06270 230 YPIEEMAQAAA 240
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
8-311 |
6.73e-42 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 148.37 E-value: 6.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 8 TMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEFAYHVE 87
Cdd:PRK10727 3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 88 -VALSKKNYKLLLCNISGPKRELDYLTMLQQNKVDGIIAITYSPIDDYLSS---NIP-FVSIDRT---YENKaipCVSSD 159
Cdd:PRK10727 83 qVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASlmkQIPgMVLINRIlpgFENR---CIALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 160 NQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFPC--QVLDLEEPyDDFVGQ--VEEFLINNPQ 235
Cdd:PRK10727 160 DRYGAWLATRHLIQQGHTRIGYLCS-NHSISDAEDRLQGYYDALAESGIPAndRLVTFGEP-DESGGEqaMTELLGRGRN 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239654491 236 VDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKRERP 311
Cdd:PRK10727 238 FTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLP 313
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
66-317 |
2.08e-41 |
|
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: 145.00 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGII----AITYSPIDDYLSSNiP 140
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYdKEKELRALELLKTKQIDGLIitsrENDWEVIEPYAKYG-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRtYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRL----YFEKRIVEAGFPCQVLDLE 216
Cdd:cd06286 80 IVLCEE-TDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSSASTQARLkayqDVLGEHGLSLREEWIFTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 217 EPYDDfvGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLAseRSLELSTIRQPLEAMA 294
Cdd:cd06286 159 HTIED--GYklAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPIS--ELLNLTTIDQPLEEMG 234
|
250 260
....*....|....*....|...
gi 1239654491 295 QEAVACLVDVIEKrERPLQVTLP 317
Cdd:cd06286 235 KEAFELLLSQLES-KEPTKKELP 256
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
66-316 |
4.31e-41 |
|
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: 144.33 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPT----VWHPFFGEFAYHVEVALSKKNYKLLLCNISGPKRELD-YLTMLQQNKVDGIIaITYSPIDD----YL- 135
Cdd:cd06292 1 LIGYVVPElpggFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDyYRDLVRSRRVDGFV-LASTRHDDprvrYLh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 136 SSNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhnktiNETKK----RRLYFEKRIVEAGFPCQ 211
Cdd:cd06292 80 EAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGG-----PEGSVpsddRLAGYRAALEEAGLPFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 212 V-LDLEEPYDDFVGQV--EEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQ 288
Cdd:cd06292 155 PgLVVEGENTEEGGYAaaARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQ 234
|
250 260 270
....*....|....*....|....*....|...
gi 1239654491 289 PLEAMAQEAVACLVDVIEK-----RERPLQVTL 316
Cdd:cd06292 235 PIDEIGRAVVDLLLAAIEGnpsepREILLQPEL 267
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-321 |
1.34e-40 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 143.03 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLcNISG--PKRELDYLTMLQQNKVDGIIAI--TYSP-IDDYL-SSNI 139
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLL-ATSEydPARELEQVRALIERGVDGLILVgsDHDPeLFELLeQRQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 140 PFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRLYFEKRIVEAG--FPcQVLDLEE 217
Cdd:cd06273 80 PYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIRDALAERGleLP-EERVVEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 218 PYDDFVGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQ 295
Cdd:cd06273 159 PYSIEEGReaLRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGE 238
|
250 260
....*....|....*....|....*.
gi 1239654491 296 EAVACLVDVIEKRERPLQVTLPISYV 321
Cdd:cd06273 239 LAARYLLALLEGGPPPKSVELETELI 264
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
4-326 |
1.69e-40 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 144.75 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 4 QKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALI-IPTVWH-PffGE 81
Cdd:PRK09526 3 SKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLAtTSLALHaP--SQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 82 FAYHVEVALSKKNYKLLLCNISGP-----KRELDYLtmLQQnKVDGIIaITYsPIDD-------YLSSNIPFVSIDrTYE 149
Cdd:PRK09526 81 IAAAIKSRADQLGYSVVISMVERSgveacQAAVNEL--LAQ-RVSGVI-INV-PLEDadaekivADCADVPCLFLD-VSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 150 NKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINEtkkrRLYFE---KRIVEAGF-PCQVldLEEPYDDFVG- 224
Cdd:PRK09526 155 QSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSA----RLRLAgwlEYLTDYQLqPIAV--REGDWSAMSGy 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 225 -QVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVD 303
Cdd:PRK09526 229 qQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLA 308
|
330 340
....*....|....*....|...
gi 1239654491 304 VIEKRERPLQVTLPISYVDGKTT 326
Cdd:PRK09526 309 LSQGQAVKGSQLLPTSLVVRKST 331
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
66-322 |
1.31e-39 |
|
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: 140.49 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNIS-GPKRELDYLTMLQQNKVDGIIAITYSPIDDYLSS----NIP 140
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDeDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQAliaqGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYE-NKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGG--HNKTINEtkkRRLYFEKRIVEAGFPCQVLDLEE 217
Cdd:cd06299 81 VVFVDREVEgLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGplSTSTGRE---RLAAFRAALTAAGIPIDEELVAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 218 ---PYDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMA 294
Cdd:cd06299 158 gdfRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIG 237
|
250 260
....*....|....*....|....*...
gi 1239654491 295 QEAVACLVDVIEKRERPLQVTLPISYVD 322
Cdd:cd06299 238 RRAVELLLALIENGGRATSIRVPTELIP 265
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-311 |
1.70e-39 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380513 [Multi-domain] Cd Length: 267 Bit Score: 140.06 E-value: 1.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDY---LSSNIPF 141
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWnADRELEILRLLLARKVDGIIVVGGFGDEELlklLAEGIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 142 VSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFP-CQVLdleEPYD 220
Cdd:cd06290 81 VLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISG-PEDHPDAQERYAGYRRALEDAGLEvDPRL---IVEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 221 DFVGQ-----VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQ 295
Cdd:cd06290 157 DFTEEsgyeaMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGK 236
|
250
....*....|....*.
gi 1239654491 296 EAVACLVDVIEKRERP 311
Cdd:cd06290 237 TAAEILLELIEGKGRP 252
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
66-317 |
4.30e-39 |
|
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: 138.84 E-value: 4.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWH-PFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYS------PIDDYlss 137
Cdd:cd06288 1 TIGLITDDIATtPFAGDIIRGAQDAAEEHGYLLLLANTGGdPELEAEAIRELLSRRVDGIIYASMHhrevtlPPELT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 138 NIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFPCQ---VLD 214
Cdd:cd06288 78 DIPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGG-PEDSLATRLRLAGYRAALAEAGIPYDpslVVH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 215 LEEPYDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMA 294
Cdd:cd06288 157 GDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMG 236
|
250 260
....*....|....*....|....
gi 1239654491 295 QEAVACLVDVIEKRER-PLQVTLP 317
Cdd:cd06288 237 RRAAELLLDGIEGEPPePGVIRVP 260
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
62-317 |
2.56e-38 |
|
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: 137.00 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 62 NKTETIALIIPTVWH-------PFFGEFAYHVEVALSKKNYKLLLCNISGPKRELDYLtmLQQNKVDGIIAITYSPIDDY 134
Cdd:cd06295 1 QRSRTIAVVVPMDPHgdqsitdPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARL--LDSGRADGLIVLGQGLDHDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 135 L----SSNIPFV----SIDRTyenkAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTinETKKRRLYFEKRIVEA 206
Cdd:cd06295 79 LrelaQQGLPMVvwgaPEDGQ----SYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHP--EVADRLQGYRDALAEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 207 GFPCQVLDLEEPYDDFVG---QVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLEL 283
Cdd:cd06295 153 GLEADPSLLLSCDFTEESgyaAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPL 232
|
250 260 270
....*....|....*....|....*....|....
gi 1239654491 284 STIRQPLEAMAQEAVACLVDVIEkRERPLQVTLP 317
Cdd:cd06295 233 TTVRQDLALAGRLLVEKLLALIA-GEPVTSSMLP 265
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
66-317 |
4.53e-38 |
|
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: 136.23 E-value: 4.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNIS-GPKRELDYLTMLQQNKVDGII----AITYSPIDDYLSSNIP 140
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDeDPEKEKRYLDSLLSKQVDGIIlapsAGPSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFP-CQVLDLEEPY 219
Cdd:cd06280 81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITG-PLEISTTRERLAGYREALAEAGIPvDESLIFEGDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 220 DDFVGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEA 297
Cdd:cd06280 160 TIEGGYeaVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIA 239
|
250 260
....*....|....*....|.
gi 1239654491 298 VACLVDVIE-KRERPLQVTLP 317
Cdd:cd06280 240 AQLLLERIEgQGEEPRRIVLP 260
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
66-317 |
1.50e-37 |
|
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: 134.99 E-value: 1.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYL-TMLQQNkVDGII------AITYSPIDDYL-- 135
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNdVEKEREILeSLLDQN-VDGLIieptksALPNPNLDLYEel 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 136 -SSNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIgghNKTINET-KKRRLYFEKRIVEAGFP---- 209
Cdd:cd01541 80 qKKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGI---FKSDDLQgVERYQGFIKALREAGLPiddd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 210 ----CQVLDLEEPydDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELST 285
Cdd:cd01541 157 rilwYSTEDLEDR--FFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTS 234
|
250 260 270
....*....|....*....|....*....|..
gi 1239654491 286 IRQPLEAMAQEAVACLVDVIEKRERPLQVTLP 317
Cdd:cd01541 235 VVHPKEELGRKAAELLLRMIEEGRKPESVIFP 266
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-324 |
2.14e-35 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380629 [Multi-domain] Cd Length: 270 Bit Score: 129.21 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTvwHP-----FFGEFAYHVEVALSKKNYKLLLCNISgPKRE--LDYLTMLQQNKVDGIIAItySPID-DYL-- 135
Cdd:cd19974 1 NIAVLIPE--RFfgdnsFYGKIYQGIEKELSELGYNLVLEIIS-DEDEeeLNLPSIISEEKVDGIIIL--GEISkEYLek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 136 --SSNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIG--GHNKTINEtkkRRLYFEKRIVEAGFP-- 209
Cdd:cd19974 76 lkELGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGdiNYTSSFMD---RYLGYRKALLEAGLPpe 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 210 ---CQVLDLEEPYDDFvGQVEEFLiNNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTI 286
Cdd:cd19974 153 keeWLLEDRDDGYGLT-EEIELPL-KLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTV 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1239654491 287 RQPLEAMAQEAVACLVDVIEKRERPLQvtlpISYVDGK 324
Cdd:cd19974 231 EVDKEAMGRRAVEQLLWRIENPDRPFE----KILVSGK 264
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
7-297 |
2.18e-35 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 131.05 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 7 ITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEFAYHV 86
Cdd:PRK10401 2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 87 E-VALSKKNYKLLLCNISGPKRELDYLTMLQQNKVDGIIAITYSPIDDYLSS---NIP-FVSIDRTYENKAIPCVSSDNQ 161
Cdd:PRK10401 82 DlVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQfmdQIPgMVLINRVVPGYAHRCVCLDNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 162 AGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFpcqvldleEPYDDFVGQVE-----------EFL 230
Cdd:PRK10401 162 SGARMATRMLLNNGHQRIGYLSS-SHGIEDDAMRRAGWMSALKEQGI--------IPPESWIGTGTpdmqggeaamvELL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239654491 231 INNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEA 297
Cdd:PRK10401 233 GRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLA 299
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
66-317 |
2.03e-34 |
|
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: 126.54 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIP----TVW-HPFFGEFAYHVEVALSKKNYKLLLCNISGPKRELD-YLTMLQQNKVDGIIaITYS----PIDDYL 135
Cdd:cd06294 1 TIGLVLPssaeELFqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEeVKRMVRGRRVDGFI-LLYSkeddPLIEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 136 -SSNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFPC---Q 211
Cdd:cd06294 80 kEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGG-DKNLVVSIDRLQGYKQALKEAGLPLdddY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 212 VLDLEEPYDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLE 291
Cdd:cd06294 159 ILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPY 238
|
250 260
....*....|....*....|....*..
gi 1239654491 292 AMAQEAVACLVDVIEKRER-PLQVTLP 317
Cdd:cd06294 239 ELGREAAKLLINLLEGPESlPKNVIVP 265
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
66-316 |
9.29e-33 |
|
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: 122.29 E-value: 9.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNI--SGPK--RELDylTMLQQNkVDGII---AI--TYSPIDDYLS 136
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTgeDPERqrRFLR--RMLEQG-VDGLIlspAAgtTAELLRRLKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 137 SNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTIneTKKRRLY-FEKRIVEAGFPCQ---V 212
Cdd:cd06289 78 WGIPVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSS--TRRERLAgFRAALAEAGLPLDeslI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 213 LDLEEPYDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEA 292
Cdd:cd06289 156 VPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPRE 235
|
250 260
....*....|....*....|....
gi 1239654491 293 MAQEAVACLVDVIEKRERPLQVTL 316
Cdd:cd06289 236 IGRRAARLLLRRIEGPDTPPERII 259
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
66-316 |
2.27e-32 |
|
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: 121.12 E-value: 2.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL----SSNIP 140
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNdPEKERDYIESLLSQRVDGLILQPTGNNNDAYlelaQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINeTKKRRLY-FEKRIVEAGFPCQVLDLE-EP 218
Cdd:cd06283 81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGIS-TRRERLQgFLDALARYNIEGDVYVIEiED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 219 YDDFVGQVEEFL-INNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEA 297
Cdd:cd06283 160 TEDLQQALAAFLsQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKAA 239
|
250
....*....|....*....
gi 1239654491 298 VACLVDVIEKRERPLQVTL 316
Cdd:cd06283 240 AEILLERIEGDSGEPKEIE 258
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
86-317 |
1.14e-31 |
|
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: 119.22 E-value: 1.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 86 VEVALSKKNYKLLLCNISG--PKRELDYLTMLQQNKVDGIIAITYSPIDD----YLSSNIPFVSIDRTyENKAIPCVSSD 159
Cdd:cd01574 21 IERAARERGYSVSIATVDEddPASVREALDRLLSQRVDGIIVIAPDEAVLealrRLPPGLPVVIVGSG-PSPGVPTVSID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 160 NQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFPCQVL-----DLEEPYDdfVGQVeefLINNP 234
Cdd:cd01574 100 QEEGARLATRHLLELGHRRIAHIAG-PLDWVDARARLRGWREALEEAGLPPPPVvegdwSAASGYR--AGRR---LLDDG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 235 QVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKRERPLQV 314
Cdd:cd01574 174 PVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRAVELLLALIEGPAPPPES 253
|
...
gi 1239654491 315 TLP 317
Cdd:cd01574 254 VLL 256
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
1-317 |
4.54e-31 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 119.43 E-value: 4.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 1 MEEQKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFG 80
Cdd:PRK10014 1 MATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 81 EFAYHVEVALSKKNYKLLL--CNISGPKRELDYLTMLQQNkVDGII-----AITYSPIDDYLSSNIPFVSIDRTYENKAI 153
Cdd:PRK10014 81 ELTAGLTEALEAQGRMVFLlqGGKDGEQLAQRFSTLLNQG-VDGVViagaaGSSDDLREMAEEKGIPVVFASRASYLDDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 154 PCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTIneTKKRRL-YFEKRIVEAGFPCQ---VLDLEEPYDDFVGQVEEF 229
Cdd:PRK10014 160 DTVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSL--TRAERVgGYCATLLKFGLPFHsewVLECTSSQKQAAEAITAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 230 LINNPQVDAIFTINDFTALDTLAVLEKLGRRVPED---------VQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVAC 300
Cdd:PRK10014 238 LRHNPTISAVVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADR 317
|
330
....*....|....*...
gi 1239654491 301 LVDVIEKRERPLQ-VTLP 317
Cdd:PRK10014 318 MMQRITHEETHSRnLIIP 335
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
66-317 |
8.68e-31 |
|
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: 116.88 E-value: 8.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWH----PFFGEFAYHVEVALSKKNYKLLLCNISGPKRELDYLT-MLQQNKVDGIIaITYSPIDD----YLS 136
Cdd:cd20010 1 AIGLVLPLDPGdlgdPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRrLVERGRVDGFI-LARTRVNDpriaYLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 137 -SNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFP-CQVLD 214
Cdd:cd20010 80 eRGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNG-PEELNFAHQRRDGYRAALAEAGLPvDPALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 215 LEEPYDDFVGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGI-QLASERSLELSTIRQPLE 291
Cdd:cd20010 159 REGPLTEEGGYqaARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLTTTRSSLR 238
|
250 260
....*....|....*....|....*..
gi 1239654491 292 AMAQEAVACLVDVIEKRE-RPLQVTLP 317
Cdd:cd20010 239 DAGRRLAEMLLALIDGEPaAELQELWP 265
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
66-317 |
9.04e-31 |
|
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: 116.89 E-value: 9.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLL--CNISGPKRELDYLTMLQQNKVDGIIAItySPIDD------YLSS 137
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSDDEDLADRLRRFLSRSRPDGVILT--PPLSDdpalldALDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 138 -NIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHnKTINETKKRRLYFEKRIVEAGFPcqvldle 216
Cdd:cd01545 79 lGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGP-PDHGASAERLEGFRDALAEAGLP------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 217 ePYDDFVGQ-----------VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELST 285
Cdd:cd01545 151 -LDPDLVVQgdftfesgleaAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTT 229
|
250 260 270
....*....|....*....|....*....|...
gi 1239654491 286 IRQPLEAMAQEAVACLVDVIEKRE-RPLQVTLP 317
Cdd:cd01545 230 VRQPIAEMARRAVELLIAAIRGAPaGPERETLP 262
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
9-267 |
6.29e-30 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 116.13 E-value: 6.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 9 MK--DVARLAGVSVGTVSRVIN---KEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEFA 83
Cdd:PRK11303 1 MKldEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 84 YHVEVALSKKNYKLLL-CNISGPKRELDYLTMLQQNKVDGIIAITYSPIDD--YL---SSNIPFVSIDRTYENKAIPCVS 157
Cdd:PRK11303 81 KYLERQARQRGYQLLIaCSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEHpfYQrlqNDGLPIIALDRALDREHFTSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 158 SDNQAGAELAADTLIAKGGRHFAFIGGHNKtINETKKRRLYFEKRIveAGFPCQVLDLE-EPYDDFVGQ--VEEFLINNP 234
Cdd:PRK11303 161 SDDQDDAEMLAESLLKFPAESILLLGALPE-LSVSFEREQGFRQAL--KDDPREVHYLYaNSFEREAGAqlFEKWLETHP 237
|
250 260 270
....*....|....*....|....*....|....
gi 1239654491 235 QVDAIFTINdFTALD-TLAVLEKLGRRVPEDVQV 267
Cdd:PRK11303 238 MPDALFTTS-YTLLQgVLDVLLERPGELPSDLAI 270
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
7-74 |
2.60e-29 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 106.90 E-value: 2.60e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1239654491 7 ITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTV 74
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDI 68
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
66-315 |
5.23e-29 |
|
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: 112.20 E-value: 5.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNiSG--PKRELDYL-TMLQQNkVDGIIaITYSPIDDYL-----SS 137
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGN-TGysPEREEELIrALLSRR-PAGLI-LTGTEHTPATrkllrAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 138 NIPFVSI-DrtYENKAIP-CVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRLYFEKRIVEAGFPCQ-VLD 214
Cdd:cd01575 78 GIPVVETwD--LPDDPIDmAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFRDALAEAGLPLPlVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 215 LEEPYDDFVGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEA 292
Cdd:cd01575 156 VELPSSFALGReaLAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYE 235
|
250 260
....*....|....*....|...
gi 1239654491 293 MAQEAVACLVDVIEKRERPLQVT 315
Cdd:cd01575 236 IGRKAAELLLARLEGEEPEPRVV 258
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
76-317 |
1.36e-28 |
|
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: 111.08 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 76 HPFFGEFAYHVEVALSKKNYKLLLCnisgpkRELDYLTMLQQNKVDGIIAI-TYSP--IDDYLSSNIPFVSIDRTYENKA 152
Cdd:cd01544 16 DPYYLSIRLGIEKEAKKLGYEIKTI------FRDDEDLESLLEKVDGIIAIgKFSKeeIEKLKKLNPNIVFVDSNPDPDG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 153 IPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETK----KRRLYFEKRiveagfpCQVLDLEEPYDDFVG---- 224
Cdd:cd01544 90 FDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEeiedPRLRAFREY-------MKEKGLYNEEYIYIGefsv 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 225 -----QVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVA 299
Cdd:cd01544 163 esgyeAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVR 242
|
250
....*....|....*....
gi 1239654491 300 CLVDVIEK-RERPLQVTLP 317
Cdd:cd01544 243 LLLERINGgRTIPKKVLLP 261
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
66-311 |
1.70e-28 |
|
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: 110.83 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLcnISGPKRELDYLTMLQQ---NKVDGIIAITYSPIDDYL----SSN 138
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVV--TATRAGRAPVDDWVRRavaRGSAGVVLVTSDPTSRQLrllrSAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 139 IPFVSID-RTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINeTKKRRLYFEKRIVEAGFP-------- 209
Cdd:cd06296 79 IPFVLIDpVGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVS-GRARLAGYRAALAEAGIAvdpdlvre 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 210 ------------CQVLDLEEPyddfvgqveeflinnPQvdAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLAS 277
Cdd:cd06296 158 gdftyeagyraaRELLELPDP---------------PT--AVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPAR 220
|
250 260 270
....*....|....*....|....*....|....
gi 1239654491 278 ERSLELSTIRQPLEAMAQEAVACLVDVIEKRERP 311
Cdd:cd06296 221 WTSPPLTTVHQPLREMGAVAVRLLLRLLEGGPPD 254
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
112-316 |
7.98e-28 |
|
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: 108.83 E-value: 7.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 112 LTMLQQNKVDGIIAITYSP--IDDYLSSNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTI 189
Cdd:cd01543 43 LDLLKGWKGDGIIARLDDPelAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAW 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 190 NEtkKRRLYFEKRIVEAGFPCQVLDLEEP-----YDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPED 264
Cdd:cd01543 123 SR--ERGEGFREALREAGYECHVYESPPSgssrsWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEE 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1239654491 265 VQVIGYDG---IQLASerSLELSTIRQPLEAMAQEAVACLVDVIEKRERPLQVTL 316
Cdd:cd01543 201 VAVLGVDNdelICELS--SPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPIL 253
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
77-316 |
3.73e-27 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 107.33 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 77 PFFGEFAYHVEVALSKKNYKLLLCNISGPKRELDYLTMLQQNKVDGIIAI-TYSPIDDY---LSSNIPFVSIDRTYENKA 152
Cdd:cd06277 19 PFFSELIDGIEREARKYGYNLLISSVDIGDDFDEILKELTDDQSSGIILLgTELEEKQIklfQDVSIPVVVVDNYFEDLN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 153 IPCVSSDNQAGAELAADTLIAKGGRHFAFIGGhNKTINETKKRRLYFEKRIVEAGF-----PCQVLDL--EEPYDDFVgq 225
Cdd:cd06277 99 FDCVVIDNEDGAYEAVKYLVELGHTRIGYLAS-SYRIKNFEERRRGFRKAMRELGLsedpePEFVVSVgpEGAYKDMK-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 226 vEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVI 305
Cdd:cd06277 176 -ALLDTGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKI 254
|
250
....*....|.
gi 1239654491 306 EKRERPLQVTL 316
Cdd:cd06277 255 KDPDGGTLKIL 265
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
66-303 |
6.23e-27 |
|
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380520 [Multi-domain] Cd Length: 268 Bit Score: 106.78 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISGPKRELDYL---TMLQQnkVDGIIAITYSPID----DYLSSN 138
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLrnsTLAYQ--CDGLVMASLDLTElfeeVIVPTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 139 IPFVSIDRtyENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINET---KKRRLYFEKRIVEAGFPcqvLDL 215
Cdd:cd06297 79 KPVVLIDA--NSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTEtvfREREQGFLEALNKAGRP---ISS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 216 EEPYDDFVGQ------VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSleLSTIRQP 289
Cdd:cd06297 154 SRMFRIDNSSkkaeclARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAASPG--LTTVRQP 231
|
250
....*....|....
gi 1239654491 290 LEAMAQEAVACLVD 303
Cdd:cd06297 232 VEEMGEAAAKLLLK 245
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
89-317 |
1.83e-26 |
|
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: 105.27 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 89 ALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL----SSNIPFVSIDRTYENkaIPCVSSDNQAG 163
Cdd:cd01542 24 VLKENGYQPLIANTNLdEEREIEYLETLARQKVDGIILFATEITDEHRkalkKLKIPVVVLGQEHEG--FSCVYHDDYGA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 164 AELAADTLIAKGGRHFAFIGghnktINET-----KKRRLYFEK----------RIVEAGFpcqvlDLEEPYDdfvgQVEE 228
Cdd:cd01542 102 GKLLGEYLLKKGHKNIAYIG-----VDEEdiavgVARKQGYLDalkehgidevEIVETDF-----SMESGYE----AAKE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 229 FLINNPqVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKR 308
Cdd:cd01542 168 LLKENK-PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAELLLDMIEGE 246
|
....*....
gi 1239654491 309 ERPLQVTLP 317
Cdd:cd01542 247 KVPKKQKLP 255
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
66-317 |
2.61e-26 |
|
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: 104.98 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLL-LCNISGPKRELDYLTMLQQNKVDGIIAIT-YSPIDDY---LSSNIP 140
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLiACSDDDPEQERRLVENLIARQVDGLIVAPsTPPDDIYylcQAAGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGH--NKTINEtkkRRLYFEKRIVEAGFPCQVLDLEEP 218
Cdd:cd06274 81 VVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRpeLPSTAE---RIRGFRAALAEAGITEGDDWILAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 219 -YDDFVGQ--VEEFL-INNPQVDAIFTiNDFTALD-TLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAM 293
Cdd:cd06274 158 gYDRESGYqlMAELLaRLGGLPQALFT-SSLTLLEgVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEI 236
|
250 260
....*....|....*....|....
gi 1239654491 294 AQEAVACLVDVIEKRERPLQVTLP 317
Cdd:cd06274 237 AEHAFELLDALIEGQPEPGVIIIP 260
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
120-325 |
4.66e-26 |
|
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: 104.60 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 120 VDGIIAITYSP----IDDYLSSNIPFVSIDRTYENkAIPCVSSDNQAGAELAADTLIAKGGRHFAFIG---GHNKTINET 192
Cdd:cd06279 57 VDGFIVYGLSDddpaVAALRRRGLPLVVVDGPAPP-GIPSVGIDDRAAARAAARHLLDLGHRRIAILSlrlDRGRERGPV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 193 KKRRLY-------------FEKRIVEAGF-PCQVLDLEEPYDDFVG---QVEEFLINNPQVDAIFTINDFTALDTLAVLE 255
Cdd:cd06279 136 SAERLAaatnsvarerlagYRDALEEAGLdLDDVPVVEAPGNTEEAgraAARALLALDPRPTAILCMSDVLALGALRAAR 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 256 KLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKRERPlQVTLPISYVDGKT 325
Cdd:cd06279 216 ERGLRVPEDLSVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPR-PVILPTELVVRAS 284
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
171-326 |
1.14e-25 |
|
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: 100.49 E-value: 1.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 171 LIAKGGRHFAFIGGHNKTINET-KKRRLYFEKRIVEAGFPCQ-VLDLEEPYDDFVGQVEEFLINNPQVDAIFTINDFTAL 248
Cdd:pfam13377 2 LAELGHRRIALIGPEGDRDDPYsDLRERGFREAARELGLDVEpTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEVAL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239654491 249 DTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKRERPLQ-VTLPISYVDGKTT 326
Cdd:pfam13377 82 GVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPErVLLPPELVEREST 160
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
66-310 |
3.89e-25 |
|
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: 101.73 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIP---TVWHPFFGEFAYHVEVALSKKNYKLLLCNISGPKRELDYLTMLQQNKVDGIIAITYSPID---DYLS-SN 138
Cdd:cd06271 1 VIALVFPvteTELNGTVSE*VSGITEEAGTTGYHLLVWPFEEAES*VPIRDLVETGSADGVILSEIEPNDprvQFLTkQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 139 IPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIgGHNKTINETKKRRLYFEKRIVEAGFPCQVLDLEEP 218
Cdd:cd06271 81 FPFVAHGRSD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFI-VPPARYSPHDRRLQGYVRA*RDAGLTGYPLDADTT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 219 YDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSL-ELSTIRQPLEAMAQEA 297
Cdd:cd06271 160 LEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFLGAMITpPLTTVHAPIAEAGREL 239
|
250
....*....|...
gi 1239654491 298 VACLVDVIEKRER 310
Cdd:cd06271 240 AKALLARIDGEDP 252
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
66-321 |
9.78e-24 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 98.08 E-value: 9.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL-----SSNI 139
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNdEERELELLSLFQRRRVDGLILTPGDEDDPELaaalaRLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 140 PFVSIDRTYENKaIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHnKTINETKKRRLYFEKRIVEAG--FPCQVLDLEE 217
Cdd:cd06281 81 PVVLIDRDLPGD-IDSVLVDHRSGVRQATEYLLSLGHRRIALLTGG-PDIRPGRERIAGFKAAFAAAGlpPDPDLVRLGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 218 PYDDFVGQVEEFLINNPQ-VDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQE 296
Cdd:cd06281 159 FSADSGFREAMALLRQPRpPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRA 238
|
250 260
....*....|....*....|....*..
gi 1239654491 297 AVACLVDVIE--KRERPLQVTLPISYV 321
Cdd:cd06281 239 AAELLLDRIEgpPAGPPRRIVVPTELI 265
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
66-290 |
1.62e-23 |
|
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: 97.36 E-value: 1.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSPIDDYL----SSNIP 140
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNnVDKELDLLNTMLSKQVDGIIFMGDELTEEIReefkRSPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 141 FVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGG-HNKTINETKKRRLYfEKRIVEAGF---PCQVLDLE 216
Cdd:cd06298 81 VVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGpLKEYINNDKKLQGY-KRALEEAGLefnEPLIFEGD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1239654491 217 EPYDDFVGQVEEFLiNNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPL 290
Cdd:cd06298 160 YDYDSGYELYEELL-ESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPL 232
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
61-322 |
2.14e-22 |
|
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: 94.99 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 61 KNKTETIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAITYSP------IDD 133
Cdd:COG1879 30 AAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGdAAKQISQIEDLIAQGVDAIIVSPVDPdalapaLKK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 134 YLSSNIPFVSIDR-TYENKAIPCVSSDNQAGAELAADTLIAK--GGRHFAFIGGHNKTINeTKKRRLYFEKRIveAGFP- 209
Cdd:COG1879 110 AKAAGIPVVTVDSdVDGSDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPA-ANERTDGFKEAL--KEYPg 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 210 CQVLDLEEPYDDFVG---QVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRrvPEDVQVIGYDGIQLAsersLEL--- 283
Cdd:COG1879 187 IKVVAEQYADWDREKaleVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDGSPEA----LQAikd 260
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1239654491 284 ----STIRQPLEAMAQEAVACLVDVIEKRERPLQVTLPISYVD 322
Cdd:COG1879 261 gtidATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVT 303
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
64-320 |
5.92e-22 |
|
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: 93.34 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 64 TETIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNI-SGPKRELDYLTMLQQNKVDGIIAITYSPIDDYL-----SS 137
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVgDGEDTLTNAIDLLLASGADGIIITTPAPSGDDItakaeGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 138 NIPFVSIDRTYEN-KAIPCVSSDNQAGAELAADTLIAKG-GRHFAFIGGhNKTINETKKRRLYFEKRIVEAGFPCQVLDL 215
Cdd:pfam00532 81 GIPVIAADDAFDNpDGVPCVMPDDTQAGYESTQYLIAEGhKRPIAVMAG-PASALTARERVQGFMAALAAAGREVKIYHV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 216 EEPYDDFVGQ---VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGR-RVPEDV-----QVIGYDGIQLASERSLELS-- 284
Cdd:pfam00532 160 ATGDNDIPDAalaANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRvKIPDIVgiginSVVGFDGLSKAQDTGLYLSpl 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1239654491 285 -TIRQPLEAMAQEAVACLVDVIEK-RERPLQVTLPISY 320
Cdd:pfam00532 240 tVIQLPRQLLGIKASDMVYQWIPKfREHPRVLLIPRDF 277
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
36-306 |
2.15e-21 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 92.37 E-value: 2.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 36 STLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNIS-GPKRELDYLTM 114
Cdd:PRK11041 7 ATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAhQNQQEKTFVNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 115 LQQNKVDGIIaityspiddYLSSNIPF-VSIDrtyENK---------------AIPCVSSDNQAGAELAADTLIAKGGRH 178
Cdd:PRK11041 87 IITKQIDGML---------LLGSRLPFdASKE---EQRnlppmvmanefapelELPTVHIDNLTAAFEAVNYLHELGHKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 179 FAFIGGhNKTINETKKRRLYFEKRIVEAGfpcqvLDLEEPY---DDFV----GQVEEFLINNPQV-DAIFTINDFTALDT 250
Cdd:PRK11041 155 IACIAG-PEEMPLCHYRLQGYVQALRRCG-----ITVDPQYiarGDFTfeagAKALKQLLDLPQPpTAVFCHSDVMALGA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239654491 251 LAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVIE 306
Cdd:PRK11041 229 LSQAKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQ 284
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
3-295 |
1.12e-20 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 90.86 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 3 EQKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPTVWHPFFGEF 82
Cdd:PRK14987 2 KKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 83 AYHVEVALSKKNYKLLLCNIS-GPKRELDYLTMLQQNKVDGIIAI--TYSP--IDDYLSSNIPFVSIdrtyENKAIPC-- 155
Cdd:PRK14987 82 LRGIESVTDAHGYQTMLAHYGyKPEMEQERLESMLSWNIDGLILTerTHTPrtLKMIEVAGIPVVEL----MDSQSPCld 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 156 --VSSDNQAGAELAADTLIAKGGRHFAFIGGH--NKTINETKKrrlyFEKRIVEAGF-PCQVL-DLEEPYDDFVGQVEEF 229
Cdd:PRK14987 158 iaVGFDNFEAARQMTTAIIARGHRHIAYLGARldERTIIKQKG----YEQAMLDAGLvPYSVMvEQSSSYSSGIELIRQA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239654491 230 LINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQ 295
Cdd:PRK14987 234 RREYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGS 299
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
10-61 |
3.75e-20 |
|
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.
Pssm-ID: 143331 [Multi-domain] Cd Length: 52 Bit Score: 82.07 E-value: 3.75e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1239654491 10 KDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPDVYARGMKK 61
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 ... |
66-318 |
7.25e-18 |
|
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: 81.84 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLllcNISGPKreLDYLTMLQQ------NKVDGIIAITYSP------IDD 133
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVEL---VVLDAQ--GDVAKQISQiedliaQGVDAIIIAPVDSealvpaVKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 134 YLSSNIPFVSIDR--TYENKAIPCVSSDNQAGAELAADTLIAK--GGRHFAFIGGhNKTINETKKRRLYFEKrIVEAGFP 209
Cdd:cd01536 76 ANAAGIPVVAVDTdiDGGGDVVAFVGTDNYEAGKLAGEYLAEAlgGKGKVAILEG-PPGSSTAIDRTKGFKE-ALKKYPD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 210 CQVLDleEPYDDFVGQ-----VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRrvPEDVQVIGYDGIQLASERSLE-- 282
Cdd:cd01536 154 IEIVA--EQPANWDRAkaltvTENLLQANPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTPEALKAIKDge 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 1239654491 283 -LSTIRQPLEAMAQEAVACLVDVIEKRERPLQVTLPI 318
Cdd:cd01536 230 lDATVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPV 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
66-318 |
2.59e-17 |
|
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: 80.37 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKN-YKLLlcnISGPKRELDYLTMLQ------QNKVDGI-IAITYS-----PID 132
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEANgYELL---VKGIKQETDIEQQIAivenliAQKVDAIvIAPADSkalvpVLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 133 DYLSSNIPFVSIDRTYENKA-------IPCVSSDNQAGAELAADTLIAK--GGRHFAFIGGHNKTINeTKKRRLYFEKRI 203
Cdd:cd19970 78 KAVDAGIAVINIDNRLDADAlkegginVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGADN-AQQRKAGFLKAF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 204 VEAGFpcQVLDLEEPY---DDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDGIQLASErS 280
Cdd:cd19970 157 EEAGM--KIVASQSANweiDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNIPAVRP-L 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1239654491 281 LE----LSTIRQPLEAMAQEAVACLVDVIEKRERPLQVTLPI 318
Cdd:cd19970 232 LKdgkmLATIDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPV 273
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
8-53 |
2.66e-17 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 74.21 E-value: 2.66e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1239654491 8 TMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAIQELNYIPD 53
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
78-319 |
1.22e-16 |
|
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: 78.44 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 78 FFGEFAYHVEVALSKKNYKLLLCNI--SGPKRElDYLTMLQQNKVDGIIAITYSPIDDYLS-----SNIPFVSIDRTyEN 150
Cdd:cd01537 13 FMSVIRKAIEQDAKQPGVQLLMNDSqnDQEKQN-DQIDVLLAKRVKGLAINLVDPAAAGVAekargQNVPVVFFDKE-PS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 151 KAIPC--VSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTiNETKKRRLYFEKRIVEAGFPCQVLDLEEP-YDDFVG--Q 225
Cdd:cd01537 91 RYDKAyyVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGH-PDAEARLAGVIKELNDKGIKTEQLQLDTGdWDTASGkdK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 226 VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVI 305
Cdd:cd01537 170 MDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKTTFDLLLNLA 249
|
250
....*....|....*
gi 1239654491 306 E-KRERPLQVTLPIS 319
Cdd:cd01537 250 DnWKIDNKVVRVPYV 264
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
114-314 |
9.04e-16 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 75.92 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 114 MLQQNKVDGIIAI---TYSPIDDYLSS-NIPFVSIDRT-YENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKT 188
Cdd:cd06287 51 MLDALDVDGAIVVeptVEDPILARLRQrGVPVVSIGRApGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 189 INETKKRRLYfEKRIVEAGFPCQVLDLEEPYDDFVGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQ 266
Cdd:cd06287 131 NSSLESEAAY-LRFAQEYGTTPVVYKVPESEGERAGYeaAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLM 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1239654491 267 VIG-YDGIQlASERSLELSTIRQPLEAMAQEAVACLVDVIEKRERPLQV 314
Cdd:cd06287 210 VVTrYDGIR-ARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEV 257
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
66-314 |
2.62e-15 |
|
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: 74.72 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHP-FFGEFAYHVEVALSKKNYKLLLcnISGPKRELDYLT---MLQQNKVDGIIAITYSPID-DYLSSN-- 138
Cdd:cd06272 1 TIGLYWPSVGERvALTRLLSGINEAISKQGYNINL--SICPYKVGHLCTakgLFSENRFDGVIVFGISDSDiEYLNKNkp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 139 -IPFVSIDRtyENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINETKKRRlYFEKRIVEAG--FPCQVLDL 215
Cdd:cd06272 79 kIPIVLYNR--ESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGK-GFIETCEKHGihLSDSIIDS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 216 EEPYD-DFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMA 294
Cdd:cd06272 156 RGLSIeGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIA 235
|
250 260
....*....|....*....|
gi 1239654491 295 QEAVACLVDVIEKRERPLQV 314
Cdd:cd06272 236 EESLRLILKLIEGRENEIQQ 255
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
8-327 |
8.33e-15 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 74.02 E-value: 8.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 8 TMKDVARLAGVSVGTVSRVINKEP--GIKESTLEKVQTAIQELNYIPDVYARGMKKNKTETIALIIPT------VWHPFF 79
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIYSyqqeleINDPYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 80 GEFAYHVEVALSKKNYKLLLCNISGPKRELdyltmlqqNKVDGIIAITYSPID-----DYLSSNIPFvsIDRTYENKAIP 154
Cdd:PRK10339 83 LAIRHGIETQCEKLGIELTNCYEHSGLPDI--------KNVTGILIVGKPTPAlraaaSALTDNICF--IDFHEPGSGYD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 155 CVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTiNETKKRRLYFekriVEAGFPCQVLDLEEPY-DDFVGQ-----VEE 228
Cdd:PRK10339 153 AVDIDLARISKEIIDFYINQGVNRIGFIGGEDEP-GKADIREVAF----AEYGRLKQVVREEDIWrGGFSSSsgyelAKQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 229 FLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAMAQEAVACLVDVI-EK 307
Cdd:PRK10339 228 MLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKArDG 307
|
330 340
....*....|....*....|
gi 1239654491 308 RERPLQVTLPISYVDGKTTK 327
Cdd:PRK10339 308 RALPLLVFVPSKLKLRGTTR 327
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
66-322 |
3.54e-14 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 71.54 E-value: 3.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISGP-KRELDYLTMLQQNKVDGIIAITYSP------IDDYLSSN 138
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDlAKQLSQIEDFIQQGVDAIILAPVDSggivpaIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 139 IPFVSID-RTYENKAIPCVSSDNQAGAELAADTL---IAKGGRHFAFIGghNKTINETKKRRLYFeKRIVEAGFPCQVLD 214
Cdd:cd06322 81 IPVFTVDvKADGAKVVTHVGTDNYAGGKLAGEYAlkaLLGGGGKIAIID--YPEVESVVLRVNGF-KEAIKKYPNIEIVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 215 lEEPYDD----FVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRrvPEDVQVIGYDG----IQLASERSLELSTI 286
Cdd:cd06322 158 -EQPGDGrreeALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGK--EDKIKVIGFDGnpeaIKAIAKGGKIKADI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1239654491 287 RQPLEAMAQEAVACLVDVIEKRERPLQVTLPISYVD 322
Cdd:cd06322 235 AQQPDKIGQETVEAIVKYLAGETVEKEILIPPKLYT 270
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
67-306 |
6.86e-13 |
|
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: 67.56 E-value: 6.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 67 IALIIPTvwHPFFGEFA----YHVEVALSKKNYKLLLCNISGPKRELDYL-TMLQQNKVDGIIaITYSPIDD----YL-S 136
Cdd:cd20009 2 IALVLPT--EDEIDGFTsqliSGISEALRGTPYHLVVTPEFPGDDPLEPVrYIVENRLADGII-ISHTEPQDprvrYLlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 137 SNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIAKGGRHFAFIGGHNKTINeTKKRRLYFEKRIVEAGFPCQVL--- 213
Cdd:cd20009 79 RGFPFVTHGRTELSTPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTY-AQHRLRGFRRALAEAGLEVEPLliv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 214 DLEEPYDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYDGIQLASERSLELSTIRQPLEAM 293
Cdd:cd20009 158 TLDSSAEAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEA 237
|
250
....*....|...
gi 1239654491 294 AQEAVACLVDVIE 306
Cdd:cd20009 238 GRFLAEALLRRIE 250
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
67-309 |
3.79e-12 |
|
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: 65.41 E-value: 3.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 67 IALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG--PKRELDYLTMLQQNKVDGII------AITYSPIDDYLSSN 138
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEadAAEQVAQIEDAIAQGVDAIIvapvdpTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 139 IPFVSIDR-TYENKAIPCVSSDNQAGAELAADTLIAKGGRH--FAFIGGhNKTINETKKRRLYFEKRIVEAGFPCQVLDL 215
Cdd:pfam13407 81 IPVVTFDSdAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKgkVAILSG-SPGDPNANERIDGFKKVLKEKYPGIKVVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 216 EEP----YDDFVGQVEEFL-INNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDgiqlASERSLEL------- 283
Cdd:pfam13407 160 VEGtnwdPEKAQQQMEALLtAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFD----ATPEALEAikdgtid 233
|
250 260
....*....|....*....|....*.
gi 1239654491 284 STIRQPLEAMAQEAVACLVDVIEKRE 309
Cdd:pfam13407 234 ATVLQDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
66-318 |
3.96e-12 |
|
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: 65.49 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLL--CNISGPKRELDYLTMLQQnKVDGIIAitySPID---------DY 134
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVldAQNSSSKQASDLENAIAQ-GVDGIIV---SPIDvkalvpaieAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 135 LSSNIPFVSIDRTYENKA-IPCVSSDNQAGAELAADTLIAK---GGRHFAFIG--GHNKTINETKkrrlyfekriveaGF 208
Cdd:cd19968 77 IKAGIPVVTVDRRAEGAApVPHVGADNVAGGREVAKFVVDKlpnGAKVIELTGtpGSSPAIDRTK-------------GF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 209 PcQVLDLEEPYDDFVGQVEEFL-------------INNPQVDAIFTINDFTALDTLAVLEKLGRRVpEDVQVIGYDGI-- 273
Cdd:cd19968 144 H-EELAAGPKIKVVFEQTGNFErdegltvmeniltSLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFDAVpd 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1239654491 274 QLASERSLEL-STIRQPLEAMAQEAVACLVDVIEKRERPLQVTLPI 318
Cdd:cd19968 222 ALQAIKDGELyATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKP 267
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
104-322 |
4.49e-11 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 62.25 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 104 GPKRELDYLTMLQQ------NKVDGII-------AITySPIDDYLSSNIPFVSIDR-TYENKAIPCVSSDNQAGAELAAD 169
Cdd:cd20004 36 GPSREDDVEAQIQIieyfidQGVDGIVlapldrkALV-APVERARAQGIPVVIIDSdLGGDAVISFVATDNYAAGRLAAK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 170 TLIAK-GGRHFAFIGGHNKTINETKKRRLYFEKRIVEAGFPCQVLDleepyDDFVG--------QVEEFLINNPQVDAIF 240
Cdd:cd20004 115 RMAKLlNGKGKVALLRLAKGSASTTDRERGFLEALKKLAPGLKVVD-----DQYAGgtvgearsSAENLLNQYPDVDGIF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 241 TINDFTALDTLAVLEKLGRRVpeDVQVIGYDGIQ--LASERSLELS--TIRQPlEAMAQEAVACLVDVIEKRERPLQVTL 316
Cdd:cd20004 190 TPNESTTIGALRALRRLGLAG--KVKFIGFDASDllLDALRAGEISalVVQDP-YRMGYLGVKTAVAALRGKPVPKRIDT 266
|
....*.
gi 1239654491 317 PISYVD 322
Cdd:cd20004 267 GVVLVT 272
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
66-318 |
6.40e-11 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 61.87 E-value: 6.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLlcnISGPKrelDYLTMLQ--------QNKVDGI-IAIT-----YSPI 131
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELD---VQGPP---TFDPTLQtpivnaviAKKPDALlIAPTdpqalIAPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 132 DDYLSSNIPFVSIDRTYENKAIPC--VSSDNQAGAELAADTLI-AKGGRHFAFIGGHNKTINETKKRRLYFEKRIvEAGF 208
Cdd:cd20007 75 KRAADAGIKVVTVDTTLGDPSFVLsqIASDNVAGGALAAEALAeLIGGKGKVLVINSTPGVSTTDARVKGFAEEM-KKYP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 209 PCQVLDLEEPYDDFVG---QVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDGiQLASERSLELST 285
Cdd:cd20007 154 GIKVLGVQYSENDPAKaasIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKT--GKVKVVGFDA-SPAQVEQLKAGT 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 1239654491 286 I-----RQPLEaMAQEAVACLVDVIEKRERPLQVTLPI 318
Cdd:cd20007 231 IdaliaQKPAE-IGYLAVEQAVAALTGKPVPKDILTPF 267
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
100-309 |
1.37e-10 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 61.10 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 100 CNISGPKRELDY---LTMLQQ---NKVDGII--AITYSPIDDYL----SSNIPFVSIDRTYENKAIPC-VSSDNQAGAEL 166
Cdd:cd20005 32 ITFEGPDTESDVdkqIEMLDNaiaKKPDAIAlaALDTNALLPQLekakEKGIPVVTFDSGVPSDLPLAtVATDNYAAGAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 167 AADTLiakggrhFAFIGG--------HNKTINETKKRRLYFEKRIVEAGFPCQVLDLEEPYDDFV---GQVEEFLINNPQ 235
Cdd:cd20005 112 AADHL-------AELIGGkgkvaivaHDATSETGIDRRDGFKDEIKEKYPDIKVVNVQYGVGDHAkaaDIAKAILQANPD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1239654491 236 VDAIFTINDFTALDTLAVLEKLGrrVPEDVQVIGYDG---IQLASERSLELSTIRQPLEAMAQEAVACLVDVIEKRE 309
Cdd:cd20005 185 LKGIYATNEGAAIGVANALKEMG--KLGKIKVVGFDSgeaQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVKALKGEE 259
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
66-322 |
3.09e-10 |
|
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: 60.00 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAitySPID---------DYL 135
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNdPAKQLSQVEDLIVRKVDALLI---NPTDsdavspaveEAN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 136 SSNIPFVSIDR-TYENKAIPCVSSDNQAGAELAADtLIAKggrhfaFIGGHNKTI--------NETKKRRLYFEKRIVEA 206
Cdd:cd06323 78 EAGIPVITVDRsVTGGKVVSHIASDNVAGGEMAAE-YIAK------KLGGKGKVVelqgipgtSAARERGKGFHNAIAKY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 207 GFPCQVLDLEEPYDDFVGQ--VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRrvpEDVQVIGYDGI--QLASERSLE 282
Cdd:cd06323 151 PKINVVASQTADFDRTKGLnvMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGR---KDVIVVGFDGTpdAVKAVKDGK 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1239654491 283 LS-TIRQPLEAMAQEAVACLVDVIEKRERPLQVTLPISYVD 322
Cdd:cd06323 228 LAaTVAQQPEEMGAKAVETADKYLKGEKVPKKIPVPLKLVT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
66-271 |
3.52e-10 |
|
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: 59.66 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLlcnISGPKRELDYLTMLQQ------NKVDGII------AITYSPIDD 133
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKII---FVGPESEEDVAGQNSLleelinKKPDAIVvapldsEDLVDPLKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 134 YLSSNIPFVSID-RTYENKAIPCVSSDNQAGAELAADTLIAK--GGRHFAFIGGhNKTINETKKRRLYFEKRIVEAgfPC 210
Cdd:cd06310 78 AKDKGIPVIVIDsGIKGDAYLSYIATDNYAAGRLAAQKLAEAlgGKGKVAVLSL-TAGNSTTDQREEGFKEYLKKH--PG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239654491 211 QVLDLEEPYDDF-----VGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKlgRRVPEDVQVIGYD 271
Cdd:cd06310 155 GIKVLASQYAGSdyakaANETEDLLGKYPDIDGIFATNEITALGAAVAIKS--RKLSGQIKIVGFD 218
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
65-288 |
6.95e-10 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 58.95 E-value: 6.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 65 ETIALIIPTVWHPFFGEFAYHVEVALSKKNYKLL-LCNISGPKREldyLTMLQQNKVDGIIAITYSPID-DYLS------ 136
Cdd:PRK10653 27 DTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVvLDSQNNPAKE---LANVQDLTVRGTKILLINPTDsDAVGnavkma 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 137 --SNIPFVSIDRTYEN-KAIPCVSSDNQAGAELAADTLIAKggrhfafIGGHNKTI--------NETKKRRLYFEKRIVE 205
Cdd:PRK10653 104 nqANIPVITLDRGATKgEVVSHIASDNVAGGKMAGDFIAKK-------LGEGAKVIqlegiagtSAARERGEGFKQAVAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 206 AGFpcQVLdLEEPyDDF-----VGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRrvpEDVQVIGYDGIQ---LAS 277
Cdd:PRK10653 177 HKF--NVL-ASQP-ADFdrtkgLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGK---SDVMVVGFDGTPdgiKAV 249
|
250
....*....|.
gi 1239654491 278 ERSLELSTIRQ 288
Cdd:PRK10653 250 NRGKLAATIAQ 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
66-316 |
8.76e-10 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 58.53 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISGPKREL--DYLTMLQQNkVDGIIAITYSP------IDDYLSS 137
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQvtNANDLIAQG-VDGIIISPTNSsaaptvLDLANEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 138 NIPFVSID-RTYENKAIPCVSSDNQAGAELAADTLIAK------GGRHFAFIGGHNKTINeTKKRRLYFEKRIVEAGFPC 210
Cdd:cd06319 80 KIPVVIADiGTGGGDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVN-GQARTAGFEDALEEAGVEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 211 QV------LDLEEPYDdfvgQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDGIQLASE--RSLE 282
Cdd:cd06319 159 VAlrqtpnSTVEETYS----AAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPEALDliKDGK 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1239654491 283 LSTI--RQPLEaMAQEAVACLV-----DVIEKRERPLQVTL 316
Cdd:cd06319 233 LDGTvaQQPFG-MGARAVELAIqalngDNTVEKEIYLPVLL 272
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
138-303 |
1.52e-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: 58.05 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 138 NIPFVSID-----------RTYENKAIPcvssDNQAGAELAADTLIAKGGRHFAFIggHNKTINETKKRRLYFEKRIVEA 206
Cdd:cd01391 82 DIPQLALDatsqdlsdktlYKYFLSVVF----SDTLGARLGLDIVKRKNWTYVAAI--HGEGLNSGELRMAGFKELAKQE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 207 GFpCQVLdlEEPYDDFVGQ-----VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDGIQLASERSL 281
Cdd:cd01391 156 GI-CIVA--SDKADWNAGEkgfdrALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDEVGY 230
|
170 180
....*....|....*....|....*..
gi 1239654491 282 E-----LSTIRQPLEAMAQEAVACLVD 303
Cdd:cd01391 231 EveangLTTIKQQKMGFGITAIKAMAD 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
66-321 |
6.76e-09 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 55.83 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVA---LSKKNYKLLLCniSGPKRELDYLTMLQQNKVDGIIAITY------SPIDDYLS 136
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQakeLADLEYKLVTS--SNANEQVSQLEDLIAQKVDAIVILPQdseeltVAAQKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 137 SNIPFVSIDRTY-ENKAIPCVSSDN----QAGAELAADTLiaKGGRHFAFIGGHN-KTINEtkKRRLYFEKrIVEAGFPC 210
Cdd:cd06311 79 AGIPVVNFDRGLnVLIYDLYVAGDNpgmgVVSAEYIGKKL--GGKGNVVVLEVPSsGSVNE--ERVAGFKE-VIKGNPGI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 211 QVLDLEepYDDFVGQ-----VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDGIQ-----LASERS 280
Cdd:cd06311 154 KILAMQ--AGDWTREdglkvAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRT--DIKVMTGGGGSQeyfkrIMDGDP 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1239654491 281 LELSTIRQPlEAMAQEAVACLVDVIEKRERPL-QVTLPISYV 321
Cdd:cd06311 230 IWPASATYS-PAMIADAIKLAVLILKGGKTVEkEVIIPSTLV 270
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
86-271 |
1.04e-08 |
|
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: 380661 [Multi-domain] Cd Length: 274 Bit Score: 55.30 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 86 VEVALSKKNYKLllcNISGPKRELDYLT---MLQQ---NKVDGII--AITYS----PIDDYLSSNIPFVSIDRTYENKAI 153
Cdd:cd20006 23 AEAAAKEYGVDL---EFLGPESEEDIDGqieLIEEaiaQKPDAIVlaASDYDrlveAVERAKKAGIPVITIDSPVNSKKA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 154 PC-VSSDN-QAGAELA--ADTLIAKGGRhfAFIGGHNKTINETKKR--------RLYFEKRIVEAGFpCQVlDLEEPYDd 221
Cdd:cd20006 100 DSfVATDNyEAGKKAGekLASLLGEKGK--VAIVSFVKGSSTAIEReegfkqalAEYPNIKIVETEY-CDS-DEEKAYE- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1239654491 222 fvgQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYD 271
Cdd:cd20006 175 ---ITKELLSKYPDINGIVALNEQSTLGAARALKELGLG--GKVKVVGFD 219
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
113-322 |
3.01e-07 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 51.11 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 113 TMLQQNkVDGIIAITYS------PIDDYLSSNIPFVSIDRTYENKA--------IPCVSSDNQAGAELAADTLIAK--GG 176
Cdd:cd06320 52 TMLNKG-YDAILVSPISdtnlipPIEKANKKGIPVINLDDAVDADAlkkaggkvTSFIGTDNVAAGALAAEYIAEKlpGG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 177 RHFAFIGGHNKTINETKKRRLYFEKriVEAGFPCQVL-------DLEEPYDdfvgQVEEFLINNPQVDAIFTINDFTALD 249
Cdd:cd06320 131 GKVAIIEGLPGNAAAEARTKGFKET--FKKAPGLKLVasqpadwDRTKALD----AATAILQAHPDLKGIYAANDTMALG 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1239654491 250 TLAVLEKLGRRvpEDVQVIGYDGIQLASE--RSLELS-TIRQPLEAMAQEAVACLVDVIEKRERPLQVTLPISYVD 322
Cdd:cd06320 205 AVEAVKAAGKT--GKVLVVGTDGIPEAKKsiKAGELTaTVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALIT 278
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
66-298 |
3.60e-07 |
|
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380622 [Multi-domain] Cd Length: 272 Bit Score: 50.78 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGII------AITYSPIDDYLSSN 138
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNdTAKEAELFDTAIASGAKAIIldpadaDASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 139 IPFVSIDR--TYENKAIPCVSSDNQAGAELAAD---TLIAKGGRHFAFIGghNKTINETKKRRLYFEkriveagfpcQVL 213
Cdd:cd19967 81 IPVFLIDReiNAEGVAVAQIVSDNYQGAVLLAQyfvKLMGEKGLYVELLG--KESDTNAQLRSQGFH----------SVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 214 DlEEPYDDFVGQ-------------VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRrvPEDVQVIGYDGIQLASERS 280
Cdd:cd19967 149 D-QYPELKMVAQqsadwdrteafekMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDGSNDVRDAI 225
|
250 260
....*....|....*....|.
gi 1239654491 281 LE---LSTIRQPLEAMAQEAV 298
Cdd:cd19967 226 KEgkiSATVLQPAKLIARLAV 246
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
223-318 |
1.24e-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 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: 49.21 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 223 VGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpeDVQVIGYDGIQ-----LASERSLELSTIRQPLEAMAQEA 297
Cdd:cd06321 168 LSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---DIVITSVDGSPeavaaLKREGSPFIATAAQDPYDMARKA 244
|
90 100
....*....|....*....|.
gi 1239654491 298 VACLVDVIeKRERPLQVTLPI 318
Cdd:cd06321 245 VELALKIL-NGQEPAPELVLI 264
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
66-309 |
1.56e-06 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 48.76 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEfayhVEVALSKKNYKLLLCNI-SGPKRELDY---LTMLQQ---NKVDGII------AITYSPID 132
Cdd:cd20008 1 KIAVIVKDTDSEYWQT----VLKGAEKAAKELGVEVTfLGPATEADIagqVNLVENaisRKPDAIVlapndtAALVPAVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 133 DYlSSNIPFVSIDR-TYENKAIPCVSSDNQAGAELAADTLIA------KGGRHFAFIGGHN--KTINEtkkRRLYFEKRI 203
Cdd:cd20008 77 AA-DAGIPVVLVDSgANTDDYDAFLATDNVAAGALAADELAEllkasgGGKGKVAIISFQAgsQTLVD---REEGFRDYI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 204 VEAGFPCQVLDLEepYDD-----FVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDG---IQL 275
Cdd:cd20008 153 KEKYPDIEIVDVQ--YSDgdiakALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKA--GKIVLVGFDSspdEVA 228
|
250 260 270
....*....|....*....|....*....|....
gi 1239654491 276 ASERSLELSTIRQPLEAMAQEAVACLVDVIEKRE 309
Cdd:cd20008 229 LLKSGVIKALVVQDPYQMGYEGVKTAVKALKGEE 262
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
114-320 |
3.55e-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: 380626 [Multi-domain] Cd Length: 267 Bit Score: 47.58 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 114 MLQQnKVDGIIaitYSPIDDYL---------SSNIPFVSID-RTYENKAIPC-VSSDN-QAGaELAADTLIAK---GGRh 178
Cdd:cd19971 51 MINQ-GVDAIF---LNPVDSEGirpaleaakEAGIPVINVDtPVKDTDLVDStIASDNyNAG-KLCGEDMVKKlpeGAK- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 179 FAFIggHNKTINETKKRRLYFEKRIveAGFP----CQVLDLEEPYDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVL 254
Cdd:cd19971 125 IAVL--DHPTAESCVDRIDGFLDAI--KKNPkfevVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAAL 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 255 EKLGRrvPEDVQVIGYDG----IQLASERSLELSTIRQPLEaMAQEAVACLVDVIEKRERPLQVTLPISY 320
Cdd:cd19971 201 KAAGK--LGDILVYGVDGspdaKAAIKDGKMTATAAQSPIE-IGKKAVETAYKILNGEKVEKEIVVPTFL 267
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
119-317 |
1.28e-05 |
|
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: 46.00 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 119 KVDGIIAITYSP------IDDYLSSNIPFVSIDR-TYENKAIPCVSSDN----QAGAELAADTLIAKG------------ 175
Cdd:cd06308 56 GVDLLIVSPNEAdaltpvVKKAYDAGIPVIVLDRkVSGDDYTAFIGADNveigRQAGEYIAELLNGKGnvveiqglpgss 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 176 ---GRHFAFIgghnktiNETKKrrlYFEKRIVeAGFPCQVLDleepyDDFVGQVEEFLINNPQVDAIFTINDFTALDTLA 252
Cdd:cd06308 136 paiDRHKGFL-------EAIAK---YPGIKIV-ASQDGDWLR-----DKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQ 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1239654491 253 VLEKLGRRvpEDVQVIGYDGIQLASERSLE----LSTIRQPLeaMAQEAVACLVDVIEKRERPLQVTLP 317
Cdd:cd06308 200 ALKKAGRE--KEIKIIGVDGLPEAGEKAVKdgilAATFLYPT--GGKEAIEAALKILNGEKVPKEIVLP 264
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
66-306 |
2.48e-05 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 45.27 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKlllCNISGPKR-----ELDYLTMLQQNKVDGIIAitySPIDDY------ 134
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVN---VEFVGPQKsdaaeQVQLIEDLIARGVDGIAI---SPNDPEavtpvi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 135 ---LSSNIPFVSID-------R-TYenkaipcVSSDNQAGAELAADTLIA---KGGRHFAFIGG-HNKTINEtkkRRLYF 199
Cdd:cd06314 75 nkaADKGIPVITFDsdapdskRlAY-------IGTDNYEAGREAGELMKKalpGGGKVAIITGGlGADNLNE---RIQGF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 200 EKRIVE-AGFpcQVLDLEEPYDDF---VGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDG--- 272
Cdd:cd06314 145 KDALKGsPGI--EIVDPLSDNDDIakaVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKV--GKVKIVGFDTlpe 220
|
250 260 270
....*....|....*....|....*....|....*
gi 1239654491 273 -IQLASERSLELSTIRQPLEaMAQEAVACLVDVIE 306
Cdd:cd06314 221 tLQGIKDGVIAATVGQRPYE-MGYLSVKLLYKLLK 254
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
67-318 |
5.49e-05 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 44.09 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 67 IALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNIS-----GPKRELDYLTMLQQnKVDGIIAITY-SP-----IDDYL 135
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIHfvdslDPEALAAALRRLAA-GCDGVALVAPdHPlvraaIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 136 SSNIPFVSI--DRTyENKAIPCVSSDN-QAG---AELAADTLIAKGGRHFAFIGGHNKTINETkkRRLYFEKRIVEAGFP 209
Cdd:cd06307 81 ARGIPVVTLvsDLP-GSRRLAYVGIDNrAAGrtaAWLMGRFLGRRPGKVLVILGSHRFRGHEE--REAGFRSVLRERFPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 210 CQVLDLEEPYDDFVG---QVEEFLINNPQVDAIFTIN-DFTALdtLAVLEKLGRrvPEDVQVIGYD----GIQLASERSL 281
Cdd:cd06307 158 LTVLEVLEGLDDDELayeLLRELLARHPDLVGIYNAGgGNEGI--ARALREAGR--ARRVVFIGHEltpeTRRLLRDGTI 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 1239654491 282 ELsTIRQPLEAMAQEAVACLVDVIEKRERPL-QVTLPI 318
Cdd:cd06307 234 DA-VIDQDPELQARRAIEVLLAHLGGKGPAPpQPPIPI 270
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
66-321 |
7.09e-05 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 43.90 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISG-PKRELDYLTMLQQNKVDGIIAitySPIDDYLSS------- 137
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDdPSKQNTAVDNYIARGVDAIIL---DAIDVNGSIpaikras 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 138 --NIPFVSIDRTYENKAIPC-VSSDN-QAGAEL---AADTLIAK--GGRHFAFIGGHNKTINETkkRRLYFEKRIvEAGF 208
Cdd:cd06317 78 eaGIPVIAYDAVIPSDFQAAqVGVDNlEGGKEIgkyAADYIKAElgGQAKIGVVGALSSLIQNQ--RQKGFEEAL-KANP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 209 PCQVLDLEEPY---DDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDG----IQLASERSL 281
Cdd:cd06317 155 GVEIVATVDGQnvqEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQ--GKIKVFGWDLtkqaIFLGIDEGV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1239654491 282 ELSTIRQPLEAMAQEAVACLVDVIEKRERPLQVTLPISYV 321
Cdd:cd06317 233 LQAVVQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIV 272
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
73-309 |
7.28e-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: 43.55 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 73 TVWHPFFGEFAYHVEVALSKKNYKLLLCNISG--PKRELDYLTMLQQNkVDGIIAITYSP------IDDYLSSNIPFVSI 144
Cdd:cd06318 8 TLASPYYAALVAAAKAEAKKLGVELVVTDAQNdlTKQISDVEDLITRG-VDVLILNPVDPegltpaVKAAKAAGIPVITV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 145 DRTYENKAIPC--VSSDNQAGAEL----AADTLIAKGGRhFAFIGGhNKTINETKKRRLYFEKRIVEA----GFPCQVLD 214
Cdd:cd06318 87 DSALDPSANVAtqVGRDNKQNGVLvgkeAAKALGGDPGK-IIELSG-DKGNEVSRDRRDGFLAGVNEYqlrkYGKSNIKV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 215 LEEPYDDF-----VGQVEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRvpEDVQVIGYDG----IQLASERSLELST 285
Cdd:cd06318 165 VAQPYGNWirsgaVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADGqkeaLKLIKDGKYVATG 242
|
250 260
....*....|....*....|....
gi 1239654491 286 IRQPlEAMAQEAVACLVDVIEKRE 309
Cdd:cd06318 243 LNDP-DLLGKTAVDTAAKVVKGEE 265
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
113-274 |
1.10e-04 |
|
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: 43.36 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 113 TMLQQnKVDGII--AITYSPIDDYL----SSNIPFVSIDRTYENKA----IPCVSSDN----QAGAELAADTLIAKGGR- 177
Cdd:cd06309 50 DLIAQ-GVDAILisPIDATGWDPVLkeakDAGIPVILVDRTIDGEDgslyVTFIGSDFveegRRAAEWLVKNYKGGKGNv 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 178 -HFAFIGGHNKTINETKKRRLYFEK----RIVEAgfpcQVLDLEEPYddfvGQ--VEEFLINNPQ-VDAIFTINDFTALD 249
Cdd:cd06309 129 vELQGTAGSSVAIDRSKGFREVIKKhpniKIVAS----QSGNFTREK----GQkvMENLLQAGPGdIDVIYAHNDDMALG 200
|
170 180
....*....|....*....|....*
gi 1239654491 250 TLAVLEKLGRRVPEDVQVIGYDGIQ 274
Cdd:cd06309 201 AIQALKEAGLKPGKDVLVVGIDGQK 225
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
110-271 |
2.52e-04 |
|
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: 42.21 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 110 DYLTMLQQ--------NKVDGIIAITY-SPIDDYLS----SNIPFVSIDR--TYENKA------------IPCVSSDN-Q 161
Cdd:cd06324 41 NRFKMLELaeellarpPKPDYLILVNEkGVAPELLElaeqAKIPVFLINNdlTDEERAllgkprekfkywLGSIVPDNeQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 162 AGAELA------ADTLIAKGGRHFAFIGGHNKT---INETKKRRLYFEK-------RIVEAGFpcqvlDLEEPYDdfvgQ 225
Cdd:cd06324 121 AGYLLAkalikaARKKSDDGKIRVLAISGDKSTpasILREQGLRDALAEhpdvtllQIVYANW-----SEDEAYQ----K 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1239654491 226 VEEFLINNPQVDAIFTINDFTALDTLAVLEKLGRRVPEDVQVIGYD 271
Cdd:cd06324 192 TEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGID 237
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
66-296 |
2.70e-04 |
|
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380528 [Multi-domain] Cd Length: 273 Bit Score: 41.90 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 66 TIALIIPTVWHPFFGEFAYHVEVALSKKNYKLLLCNISGPKRELdyLTMLQQ---NKVDGIIAI------TYSPIDDYLS 136
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARM--ADQIQQaitQKVDAIIIShgdadaLDPKLKKALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 137 SNIPFVSIDRTYENKAIPCVSSDNQAGAELAADTLIA--KGGRHFAFIGGHNKTIneTKKRRLYFEKriVEAGFPcQVLD 214
Cdd:cd06305 79 AGIPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKdlNGEGNIAVFNVFGVPP--LDKRYDIYKA--VLKANP-GIKK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 215 LEEPYDDFVG--------QVEEFLINNPQ--VDAIFTINDFTALDTLAVLEKLGRrvpEDVQVIGYDGiqlaserslelS 284
Cdd:cd06305 154 IVAELGDVTPntaadaqtQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAGR---TDIKVYGVDI-----------S 219
|
250
....*....|..
gi 1239654491 285 TirQPLEAMAQE 296
Cdd:cd06305 220 N--QDLELMADE 229
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
3-41 |
4.40e-04 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 37.88 E-value: 4.40e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1239654491 3 EQKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKV 41
Cdd:smart00530 7 EEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKL 45
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
113-278 |
8.33e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380539 [Multi-domain] Cd Length: 294 Bit Score: 40.68 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 113 TMLQQnKVDGIIAItysPIDDY---------LSSNIPFVSIDR-----TYENKAIPCVSSDN----QAGAELAADTLIAK 174
Cdd:cd06316 51 TLIAL-KPDIIISI---PVDPVataaaykkvADAGIKLVFMDNvpdglEAGKDYVSVVSSDNrgngQIAAELLAEAIGGK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 175 GGRHFAFIGGHNKTINEtkkRRLYFEKRIvEAGFPCQVLDLEEPYDDFvGQVEE----FLINNPQVDAIFTINDFTALDT 250
Cdd:cd06316 127 GKVGIIYHDADFYATNQ---RDKAFKDTL-KEKYPDIKIVAEQGFADP-NDAEEvasaMLTANPDIDGIYVSWDTPALGV 201
|
170 180
....*....|....*....|....*....
gi 1239654491 251 LAVLEKLGRrvpEDVQVIGYD-GIQLASE 278
Cdd:cd06316 202 ISALRAAGR---SDIKITTVDlGTEIALD 227
|
|
| HTH_26 |
pfam13443 |
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ... |
4-53 |
1.01e-03 |
|
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to DNA.
Pssm-ID: 433211 [Multi-domain] Cd Length: 63 Bit Score: 36.75 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1239654491 4 QKSITMKDVARLAGVSVGTVSRVINKEP-GIKESTLEKVQTAIQE-----LNYIPD 53
Cdd:pfam13443 8 DRGISKSDLARATGISRATLSRLRKGKPkRVSLDTLDKICDALGCqpgdlLEYVPD 63
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
3-41 |
1.42e-03 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 36.38 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1239654491 3 EQKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKV 41
Cdd:cd00093 9 KEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKL 47
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
1-52 |
1.83e-03 |
|
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];
Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 36.92 E-value: 1.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1239654491 1 MEEQKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKVQTAI-QELNYIP 52
Cdd:COG3620 25 MRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALgKELSAVL 77
|
|
| PBP1_ABC_sugar_binding-like |
cd06312 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
110-259 |
3.06e-03 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380535 [Multi-domain] Cd Length: 272 Bit Score: 38.75 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 110 DYLTMLQQ---NKVDGIIAITYSP------IDDYLSSNIPFVSI-----DRTYENKAIPCVSSDNQAGAELAADTLIAKG 175
Cdd:cd06312 45 DQARLIEQaiaAKPDGIIVTIPDPdalepaLKRAVAAGIPVIAInsgddRSKERLGALTYVGQDEYLAGQAAGERALEAG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 176 GRHfAFIGGHNKTINETKKRRLYFEKRIVEAGFPCQVLDLEEPYDDFVGQVEEFLINNPQVDAIFTINDFTALDTLAVLE 255
Cdd:cd06312 125 PKN-ALCVNHEPGNPGLEARCKGFADAFKGAGILVELLDVGGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVK 203
|
....
gi 1239654491 256 KLGR 259
Cdd:cd06312 204 EAGL 207
|
|
| YozG |
COG3655 |
DNA-binding transcriptional regulator, XRE family [Transcription]; |
3-41 |
4.10e-03 |
|
DNA-binding transcriptional regulator, XRE family [Transcription];
Pssm-ID: 442872 [Multi-domain] Cd Length: 69 Bit Score: 35.50 E-value: 4.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1239654491 3 EQKSITMKDVARLAGVSVGTVSRVIN-KEPGIKESTLEKV 41
Cdd:COG3655 11 AERGMTKKELAEATGISRATLSRLKNgKAKAVRLDTLEKI 50
|
|
| HipB |
COG1396 |
Transcriptional regulator, contains XRE-family HTH domain [Transcription]; |
3-41 |
4.27e-03 |
|
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
Pssm-ID: 441006 [Multi-domain] Cd Length: 83 Bit Score: 35.74 E-value: 4.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1239654491 3 EQKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKV 41
Cdd:COG1396 17 KARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKL 55
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
113-306 |
4.58e-03 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 38.02 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 113 TMLQQnKVDGIIAITYS------PIDDYLSSNIPFVSIDRTYENK-AIPCVSSDNQAGAELAADTLIAKGGRH---FAFI 182
Cdd:cd06313 50 TLIAQ-GVDAIIVVPVDadalapAVEKAKEAGIPLVGVNALIENEdLTAYVGSDDVVAGELEGQAVADRLGGKgnvVILE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 183 G--GHNKTINETKKrrlyfEKRIVEAGFPCQVLDlEEPYD---DFVGQVEEFLINN--PQVDAIFTINDFTALDTLAVLE 255
Cdd:cd06313 129 GpiGQSAQIDRGKG-----IENVLKKYPDIKVLA-EQTANwsrDEAMSLMENWLQAygDEIDGIIAQNDDMALGALQAVK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1239654491 256 KLGRrvpEDVQVIGYDGIQ---LASERSLELSTIRQPLEAMAQEAVACLVDVIE 306
Cdd:cd06313 203 AAGR---DDIPVVGIDGIEdalQAVKSGELIATVLQDAEAQGKGAVEVAVDAVK 253
|
|
| HTH_3 |
pfam01381 |
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ... |
3-41 |
5.26e-03 |
|
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.
Pssm-ID: 460181 [Multi-domain] Cd Length: 55 Bit Score: 34.82 E-value: 5.26e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1239654491 3 EQKSITMKDVARLAGVSVGTVSRVINKEPGIKESTLEKV 41
Cdd:pfam01381 6 EELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKL 44
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
114-297 |
6.55e-03 |
|
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380646 [Multi-domain] Cd Length: 284 Bit Score: 37.60 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 114 MLQQNkVDGIIAI-----TYSPI-DDYLSSNIPFVSIDRTYENKAIPC-VSSDNQAGAELAADTLIAKGGR-HFAFIGGH 185
Cdd:cd19991 51 LIEQG-VDVLVVVpnngeALAPIvKEAKKAGVPVLAYDRLILNADVDLyVSFDNEKVGELQAEALVKAKPKgNYVLLGGS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1239654491 186 NKTINETKKRRLYFE--KRIVEAGfpcqvlDLEEPYDDFVG---------QVEEFL-INNPQVDAIFTINDFTALDTLAV 253
Cdd:cd19991 130 PTDNNAKLFREGQMKvlQPLIDSG------DIKVVGDQWVDdwdpeealkIMENALtANNNKIDAVIASNDGTAGGAIQA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1239654491 254 LEklGRRVPEDVQVIGYDGiQLAS----ERSLELSTIRQPLEAMAQEA 297
Cdd:cd19991 204 LA--EQGLAGKVAVSGQDA-DLAAcqriVEGTQTMTIYKPIKELAEKA 248
|
|
| |
