|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-332 |
5.41e-111 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 326.00 E-value: 5.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 1 MKITIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVY 80
Cdd:COG1609 2 KRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 81 GIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYdnISHKIPLVFINSEYMDSNISYVS 160
Cdd:COG1609 82 GIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERL--AEAGIPVVLIDRPLPDPGVPSVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 161 NDEASGAKIALNYLLDNNHKDILFVRGkDSYSYDIKEKI--YKEIMAKN---FDSSKIInigngNTSDTVDNTMNIFLDI 235
Cdd:COG1609 160 VDNRAGARLATEHLIELGHRRIAFIGG-PADSSSARERLagYREALAEAglpPDPELVV-----EGDFSAESGYEAARRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 236 LNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKIDCDN 314
Cdd:COG1609 234 LARGPRpTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPD 313
|
330
....*....|....*...
gi 959156737 315 KFSKRIILNNSLVERETV 332
Cdd:COG1609 314 APPERVLLPPELVVREST 331
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
62-327 |
8.07e-79 |
|
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: 241.27 E-value: 8.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYdnISHK 141
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEEL--LAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKN---FDSSKIINig 217
Cdd:cd06267 79 IPVVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGpLDLSTSRERLEGYRDALAEAglpVDPELVVE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 218 ngnTSDTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMF 296
Cdd:cd06267 157 ---GDFSEESGYEAARELLALPPRpTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAY 233
|
250 260 270
....*....|....*....|....*....|.
gi 959156737 297 FLGANAAQLLVEKIDCDNKFSKRIILNNSLV 327
Cdd:cd06267 234 EMGRAAAELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
62-331 |
6.18e-69 |
|
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: 216.25 E-value: 6.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPgteNIKAKFYDNISHK 141
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSG---RLDAELLSELSKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIK-EKIYKEIMAKN--FDSSKIINIGN 218
Cdd:cd06284 78 YPIVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARErLEGYRRALAEAglPVDEDLIIEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 219 gNTSDTVDNTMNIFLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFL 298
Cdd:cd06284 158 -FSFEAGYAAARALLA--LPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEI 234
|
250 260 270
....*....|....*....|....*....|...
gi 959156737 299 GANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06284 235 GETAAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
62-331 |
4.17e-67 |
|
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: 211.61 E-value: 4.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVaGPGTENIKakfyDNISHK 141
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIIL-GSHSLDIE----EYKKLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYmDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYS-YDIKEKIYKEIMAK-NFDSSKIINIGNG 219
Cdd:cd06291 76 IPIVSIDRYL-SEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSpANERYRGFEDALKEaGIEYEIIEIDEND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 220 NTSDTVDNTMNIFLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLG 299
Cdd:cd06291 155 FSEEDAYELAKELLE--KYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMA 232
|
250 260 270
....*....|....*....|....*....|..
gi 959156737 300 ANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06291 233 KEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-331 |
4.20e-61 |
|
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: 196.30 E-value: 4.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFydnISHK 141
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKL---LAEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGkDSYSYDIKEKI--YKEIM--AKNFDSSKIINIG 217
Cdd:cd06290 78 IPVVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISG-PEDHPDAQERYagYRRALedAGLEVDPRLIVEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 218 NGNTSDTVDNTMNIfldILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFF 297
Cdd:cd06290 157 DFTEESGYEAMKKL---LKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYE 233
|
250 260 270
....*....|....*....|....*....|....
gi 959156737 298 LGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06290 234 MGKTAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-330 |
1.73e-60 |
|
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: 194.78 E-value: 1.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAgPGTENIKAKFYDNISHK 141
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIA-SSNISDEAIIKLLKEEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYsYDIKEKI--YKEIMAKN---FDSSKIINi 216
Cdd:cd19976 80 IPVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPST-YNEHERIegYKNALQDHnlpIDESWIYS- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 217 gngnTSDTVDNTMNIFLDILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMF 296
Cdd:cd19976 158 ----GESSLEGGYKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIF 233
|
250 260 270
....*....|....*....|....*....|....
gi 959156737 297 FLGANAAQLLVEKIDCDNKFSKRIILNNSLVERE 330
Cdd:cd19976 234 EMGQEAAKLLLKIIKNPAKKKEEIVLPPELIKRD 267
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-331 |
1.33e-55 |
|
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: 181.99 E-value: 1.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGpgtENIKAKFYDNI-SH 140
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFAS---GTLTEENKQLLkNM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGK--DSYSYDIKEKIYKEIMAKN---FDSSKIIn 215
Cdd:cd19975 78 NIPVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPldDPNAGYPRYEGYKKALKDAglpIKENLIV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 216 igngnTSD-TVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQ 293
Cdd:cd19975 157 -----EGDfSFKSGYQAMKRLLKNKKLpTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQ 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 959156737 294 NMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd19975 232 PFYEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-332 |
4.00e-55 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 180.89 E-value: 4.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNisHK 141
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAA--RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSyDIKEKI--YKEIMAK---NFDSSKIINi 216
Cdd:cd06285 79 VPVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNAS-TGRDRLrgYRRALAEaglPVPDERIVP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 217 gNGNTSDTVDNTMNIFLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMF 296
Cdd:cd06285 157 -GGFTIEAGREAAYRLLS--RPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKY 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 959156737 297 FLGANAAQLLVEKIDCDNKFSKRIILNNSLVERETV 332
Cdd:cd06285 234 EMGRRAAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
62-331 |
4.98e-54 |
|
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: 178.14 E-value: 4.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAG--PGTENIKAKFYDNI- 138
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPtkSALPNPNLDLYEELq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 139 SHKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIKEKIYKEIMAKN---FDSSKIIN 215
Cdd:cd01541 81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQGVERYQGFIKALREAglpIDDDRILW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 216 IGNgNTSDTVDNTMNIFLDILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNM 295
Cdd:cd01541 161 YST-EDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVVHPK 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 959156737 296 FFLGANAAQLLVEKIDcDNKFSKRIILNNSLVERET 331
Cdd:cd01541 240 EELGRKAAELLLRMIE-EGRKPESVIFPPELIERES 274
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
62-330 |
4.31e-52 |
|
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: 173.09 E-value: 4.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNisHK 141
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAE--KI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFIN---SEYMDSNISYvsnDEASGAKIALNYLLDNNHKDILFVrgkdSYSYDIKEKI-----YKEIMAKN---FDS 210
Cdd:cd06270 79 PPLVVINryiPGLADRCVWL---DNEQGGRLAAEHLLDLGHRRIACI----TGPLDIPDARerlagYRDALAEAgipLDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 211 SKIINiGNGNTSDTVDNTMNIfLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTT 290
Cdd:cd06270 152 SLIIE-GDFTIEGGYAAAKQL-LA--RGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 959156737 291 MDQNMFFLGANAAQLLVEKIDcDNKFSKRIILNNSLVERE 330
Cdd:cd06270 228 VHYPIEEMAQAAAELALNLAY-GEPLPISHEFTPTLIERD 266
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
62-331 |
4.91e-52 |
|
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: 172.83 E-value: 4.91e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHk 141
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYdIKEKI--YKEIMAK---NFDSSKIINi 216
Cdd:cd06275 80 IPVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSV-SRERLagFRRALAEagiEVPPSWIVE- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 217 GNGNTSDTVDnTMNIFLDIlnNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMF 296
Cdd:cd06275 158 GDFEPEGGYE-AMQRLLSQ--PPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKD 234
|
250 260 270
....*....|....*....|....*....|....*
gi 959156737 297 FLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06275 235 ELGELAVELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
62-321 |
6.77e-52 |
|
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: 172.33 E-value: 6.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAgPgTENIKAKFYDNISHK 141
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIA-P-TGGNEDLIEKLVKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSyDIKEKI--YKEIMAKN--FDSSKIINIG 217
Cdd:cd19977 79 IPVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELS-TRQERLegYKAALADHglPVDEELIKHV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 218 NgnTSDTVDNTMNIFLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFF 297
Cdd:cd19977 158 D--RQDDVRKAISELLK--LEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYE 233
|
250 260
....*....|....*....|....
gi 959156737 298 LGANAAQLLVEKIDCDNKFSKRII 321
Cdd:cd19977 234 IGRKAAELLLDRIENKPKGPPRQI 257
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
4-332 |
1.19e-51 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 174.14 E-value: 1.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 4 TIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVYGIE 83
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 84 NELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-AGPGTENIKAKFYDNIShkIPLVFINSEYMDSNISYVSND 162
Cdd:PRK10703 83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVmCSEYPEPLLAMLEEYRH--IPMVVMDWGEAKADFTDAIID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 163 EA-SGAKIALNYLLDNNHKDILFVRGKDSYS-----YDIKEKIYKE---------IMAKNFDSSkiinigNGNTSdtvdn 227
Cdd:PRK10703 161 NAfEGGYLAGRYLIERGHRDIGVIPGPLERNtgagrLAGFMKAMEEanikvpeewIVQGDFEPE------SGYEA----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 228 tMNiflDILNNSS-STAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLL 306
Cdd:PRK10703 230 -MQ---QILSQKHrPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNML 305
|
330 340
....*....|....*....|....*.
gi 959156737 307 VEKIDCDNKFSKRIILNNSLVERETV 332
Cdd:PRK10703 306 LDRIVNKREEPQTIEVHPRLVERRSV 331
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
70-331 |
1.83e-51 |
|
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.
Pssm-ID: 380486 [Multi-domain] Cd Length: 269 Bit Score: 171.55 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 70 INNMFFTELVYGIENELKTNSLSIILACTNGDSDEEqkcvnnlISRNVSGIIVAGPGTENIKAKFYDNISHkipLVFINS 149
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAIGKFSKEEIEKLKKLNPN---IVFVDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 150 EYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYS------YDIKEKIYKEIM-AKNFDSSKIINIGNGNTS 222
Cdd:cd01544 84 NPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSddgeeiEDPRLRAFREYMkEKGLYNEEYIYIGEFSVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 223 DTVDNTMNIfldILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANA 302
Cdd:cd01544 164 SGYEAMKEL---LKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTA 240
|
250 260
....*....|....*....|....*....
gi 959156737 303 AQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd01544 241 VRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
1-332 |
1.04e-50 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 171.72 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 1 MK---ITIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTE 77
Cdd:PRK09526 1 MKskpVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 78 LVYGIENELKTNSLSIILACTN-GDSDEEQKCVNNLISRNVSGIIVAGP-GTENIKAKFYDNIShkIPLVFINSEyMDSN 155
Cdd:PRK09526 81 IAAAIKSRADQLGYSVVISMVErSGVEACQAAVNELLAQRVSGVIINVPlEDADAEKIVADCAD--VPCLFLDVS-PQSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 156 ISYVSNDEASGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKNfdSSKIINIGNGNTSdtvdnTMNIF-- 232
Cdd:PRK09526 158 VNSVSFDPEDGTRLGVEHLVELGHQRIALLAGpESSVSARLRLAGWLEYLTDY--QLQPIAVREGDWS-----AMSGYqq 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 233 -LDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKI 310
Cdd:PRK09526 231 tLQMLREGPVpSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALS 310
|
330 340
....*....|....*....|..
gi 959156737 311 DCDNKFSkRIILNNSLVERETV 332
Cdd:PRK09526 311 QGQAVKG-SQLLPTSLVVRKST 331
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
62-331 |
3.63e-47 |
|
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: 160.02 E-value: 3.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFT-ELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKA--KFYDni 138
Cdd:cd06288 1 TIGLITDDIATTPFAgDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLppELTD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 139 shkIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSySYDIKEKI--YKEIMAKN---FDSSKI 213
Cdd:cd06288 79 ---IPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPED-SLATRLRLagYRAALAEAgipYDPSLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 214 InIGNGNTSDTVDNTMNIFldilnnSSS---TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTT 290
Cdd:cd06288 155 V-HGDWGRESGYEAAKRLL------SAPdrpTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 959156737 291 MDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06288 228 VALPYYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
62-329 |
1.37e-46 |
|
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: 158.58 E-value: 1.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVA--GPGTENIKAKFydniS 139
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILApsAGPSRELKRLL----K 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 HKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIkEKI--YKEIMAKN---FDSSkII 214
Cdd:cd06280 77 HGIPIVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTR-ERLagYREALAEAgipVDES-LI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 215 NIGNGNTSDTVDNTMNIfLDIlnNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQN 294
Cdd:cd06280 155 FEGDSTIEGGYEAVKAL-LDL--PPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQP 231
|
250 260 270
....*....|....*....|....*....|....*
gi 959156737 295 MFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVER 329
Cdd:cd06280 232 AYEIGRIAAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-331 |
1.21e-44 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380629 [Multi-domain] Cd Length: 270 Bit Score: 153.86 E-value: 1.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSI---NNMFFTELVYGIENELKTNSLSIILACTNgDSDEEQKCVNNLIS-RNVSGIIVAGPgtenIKAKFYDN 137
Cdd:cd19974 1 NIAVLIPERffgDNSFYGKIYQGIEKELSELGYNLVLEIIS-DEDEEELNLPSIISeEKVDGIIILGE----ISKEYLEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 138 I-SHKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVrGKDSYSYDIKEKI--YKEIMAKN----FDS 210
Cdd:cd19974 76 LkELGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFV-GDINYTSSFMDRYlgYRKALLEAglppEKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 211 SKIINigngnTSDTVDNTMNIFLDILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTT 290
Cdd:cd19974 155 EWLLE-----DRDDGYGLTEEIELPLKLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTT 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 959156737 291 MDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd19974 230 VEVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
5-332 |
1.18e-43 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 152.93 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 5 IQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVYGIEN 84
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 85 ELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNIShKIPLVFINSEYMDSNISYVSNDEA 164
Cdd:PRK10423 81 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRYP-SVPTVMMDWAPFDGDSDLIQDNSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 165 SGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKnfdSSKIINIGNGNTSD----TVDNTMNIFLDIlnNS 239
Cdd:PRK10423 160 LGGDLATQYLIDKGYTRIACITGpLDKTPARLRLEGYRAAMKR---AGLNIPDGYEVTGDfefnGGFDAMQQLLAL--PL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 240 SSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKIDCDNKFSKR 319
Cdd:PRK10423 235 RPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQR 314
|
330
....*....|...
gi 959156737 320 IILNNSLVERETV 332
Cdd:PRK10423 315 LQLTPELMERGSV 327
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
3-291 |
3.44e-43 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 152.24 E-value: 3.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 3 ITIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVYGI 82
Cdd:PRK10401 2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 83 ENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-AGPGTENIKAKFYDNishkIP-LVFINSEYMDSNISYVS 160
Cdd:PRK10401 82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVhSKALSDDELAQFMDQ----IPgMVLINRVVPGYAHRCVC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 161 NDEASGAKIALNYLLDNNHKDILFVRGkdsySYDIKEKIYKEIMAKNFDSSKIIN-----IGNGnTSDTVDNTMNIFLDI 235
Cdd:PRK10401 158 LDNVSGARMATRMLLNNGHQRIGYLSS----SHGIEDDAMRRAGWMSALKEQGIIppeswIGTG-TPDMQGGEAAMVELL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 959156737 236 LNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTM 291
Cdd:PRK10401 233 GRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTV 288
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
62-327 |
2.30e-42 |
|
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380484 [Multi-domain] Cd Length: 259 Bit Score: 147.26 E-value: 2.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-AGPGTENIKaKFYDNIsh 140
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILfATEITDEHR-KALKKL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFINSEYmdSNISYVSNDEASGAKIALNYLLDNNHKDILFVrGKDSYSYDIKEKIYKEIMAKnFDSSKIINIGNGN 220
Cdd:cd01542 78 KIPVVVLGQEH--EGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYI-GVDEEDIAVGVARKQGYLDA-LKEHGIDEVEIVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 221 TSDTVDNTMNIFLDILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGA 300
Cdd:cd01542 154 TDFSMESGYEAAKELLKENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGE 233
|
250 260
....*....|....*....|....*..
gi 959156737 301 NAAQLLVEKIDcDNKFSKRIILNNSLV 327
Cdd:cd01542 234 KAAELLLDMIE-GEKVPKKQKLPYELI 259
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-330 |
2.96e-42 |
|
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: 147.33 E-value: 2.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAG-PGTeniKAKFYDNI-S 139
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaAGT---TAELLRRLkA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 HKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYS-YDIKEKIYKEIMAKN---FDSSKIIn 215
Cdd:cd06289 78 WGIPVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSStRRERLAGFRAALAEAglpLDESLIV- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 216 iGNGNTSDTVDNTMNIFLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNM 295
Cdd:cd06289 157 -PGPATREAGAEAARELLD--AAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHP 233
|
250 260 270
....*....|....*....|....*....|....*
gi 959156737 296 FFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERE 330
Cdd:cd06289 234 REIGRRAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
62-331 |
3.85e-42 |
|
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: 147.05 E-value: 3.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGII-VAGPGTENIKAKFYDNish 140
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIfMGDELTEEIREEFKRS--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG--KDSYSYDIKEKIYKEIMAKN---FDSSKIIN 215
Cdd:cd06298 78 PVPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGplKEYINNDKKLQGYKRALEEAgleFNEPLIFE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 216 igngnTSDTVDNTMNIFLDILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNM 295
Cdd:cd06298 158 -----GDYDYDSGYELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPL 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 959156737 296 FFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06298 233 YDIGAVAMRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
74-330 |
5.91e-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: 380500 [Multi-domain] Cd Length: 275 Bit Score: 141.61 E-value: 5.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 74 FFTELVYGIENELKTNSLS-IILACTNGDSDEEQkcVNNLISRNVSGIIVAGPGTENIKAKFYDNIShkIPLVFINSEYM 152
Cdd:cd06277 20 FFSELIDGIEREARKYGYNlLISSVDIGDDFDEI--LKELTDDQSSGIILLGTELEEKQIKLFQDVS--IPVVVVDNYFE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 153 DSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGkdsySYDIK-----EKIYKEIMAK-NFDSSKIINIGNGNTSDTVD 226
Cdd:cd06277 96 DLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLAS----SYRIKnfeerRRGFRKAMRElGLSEDPEPEFVVSVGPEGAY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 227 NTMNIFLDIlNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLL 306
Cdd:cd06277 172 KDMKALLDT-GPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRL 250
|
250 260
....*....|....*....|....
gi 959156737 307 VEKIDCDNKFSKRIILNNSLVERE 330
Cdd:cd06277 251 IEKIKDPDGGTLKILVSTKLVERG 274
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
62-322 |
3.57e-39 |
|
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: 139.26 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSIN-----NMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTEN--IKAKf 134
Cdd:cd06294 1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDplIEYL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 135 ydnISHKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIKEKI-YKEIMAKN---FDS 210
Cdd:cd06294 80 ---KEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQgYKQALKEAglpLDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 211 SKIINigngnTSDTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLT 289
Cdd:cd06294 157 DYILL-----LDFSEEDGYDALQELLSKPPPpTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLT 231
|
250 260 270
....*....|....*....|....*....|...
gi 959156737 290 TMDQNMFFLGANAAQLLVEKIDCDNKFSKRIIL 322
Cdd:cd06294 232 SVDINPYELGREAAKLLINLLEGPESLPKNVIV 264
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
62-330 |
4.29e-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: 139.34 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENikAKFYDNISHK 141
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENS--EGLQALIAQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFIN---SEYMDSNIsyVSNDEASGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKNFDSSKIINIG 217
Cdd:cd06299 79 LPVVFVDrevEGLGGVPV--VTSDNRPGAREAVEYLVSLGHRRIGYISGpLSTSTGRERLAAFRAALTAAGIPIDEELVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 218 NGNTsdTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMF 296
Cdd:cd06299 157 FGDF--RQDSGAAAAHRLLSRGDPpTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVE 234
|
250 260 270
....*....|....*....|....*....|....
gi 959156737 297 FLGANAAQLLVEKIDcDNKFSKRIILNNSLVERE 330
Cdd:cd06299 235 RIGRRAVELLLALIE-NGGRATSIRVPTELIPRE 267
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-331 |
1.73e-38 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 137.64 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGpgtENIKAKFYDNI-SH 140
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVG---SDHDPELFELLeQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIKEKI--YKEIMAKN---FDSSKIIN 215
Cdd:cd06273 78 QVPYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLagIRDALAERgleLPEERVVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 216 igngnTSDTVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQN 294
Cdd:cd06273 158 -----APYSIEEGREALRRLLArPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVP 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 959156737 295 MFFLGANAAQLLVEKIDcDNKFSKRIILNNSLVERET 331
Cdd:cd06273 233 AREIGELAARYLLALLE-GGPPPKSVELETELIVRES 268
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
62-331 |
1.79e-38 |
|
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: 137.63 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAG----PGTEN-IKAkfyd 136
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGtehtPATRKlLRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 137 nisHKIPLVfinsEYMDS-------NISYvSNDEAsGAKIAlNYLLDNNHKDILFVRGKDSYSYDIKEKI--YKEIMAKN 207
Cdd:cd01575 77 ---AGIPVV----ETWDLpddpidmAVGF-SNFAA-GRAMA-RHLIERGYRRIAFVGARLDGDSRARQRLegFRDALAEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 208 FDSskIINIGNGNTSDTVDNTMNIFLDILNNSSST-AVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEP 286
Cdd:cd01575 147 GLP--LPLVLLVELPSSFALGREALAELLARHPDLdAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPP 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 959156737 287 KLTTMDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd01575 225 ALTTVRVPRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
62-329 |
1.14e-37 |
|
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: 135.37 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVagpGTENIKAKFYDNISHK 141
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLIL---QPTGNNNDAYLELAQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 -IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVrgkdsySYDIKE--------KIYKEIMAKNFDSSK 212
Cdd:cd06283 78 gLPVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFV------TEPIKGistrrerlQGFLDALARYNIEGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 213 IINIgngnTSDTVDNTMNIFLDILNNSSS--TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTT 290
Cdd:cd06283 152 VYVI----EIEDTEDLQQALAAFLSQHDGgkTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITT 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 959156737 291 MDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVER 329
Cdd:cd06283 228 IRQPTYEIGKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
62-329 |
8.24e-37 |
|
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: 133.05 E-value: 8.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAgpgTENIKAKFYDNISHK 141
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIIT---SRENDWEVIEPYAKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINsEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG---KDSYSYDIKEKIYKEIMAKNFDSSKIINIGN 218
Cdd:cd06286 78 GPIVLCE-ETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGrpeSSSASTQARLKAYQDVLGEHGLSLREEWIFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 219 GntSDTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFvePKLTTMDQNMFF 297
Cdd:cd06286 157 N--CHTIEDGYKLAKKLLALKERpDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTIDQPLEE 232
|
250 260 270
....*....|....*....|....*....|..
gi 959156737 298 LGANAAQLLVEKIDCDNKfsKRIILNNSLVER 329
Cdd:cd06286 233 MGKEAFELLLSQLESKEP--TKKELPSKLIER 262
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
62-331 |
3.30e-36 |
|
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: 131.55 E-value: 3.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACT-NGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKfyDNISH 140
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVdEDDPASVREALDRLLSQRVDGIIVIAPDEAVLEAL--RRLPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFINSeYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKN-FDSSKIInign 218
Cdd:cd01574 79 GLPVVIVGS-GPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGpLDWVDARARLRGWREALEEAgLPPPPVV---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 219 gnTSD-TVDNTMNIFLDILNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFF 297
Cdd:cd01574 154 --EGDwSAASGYRAGRRLLDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAE 231
|
250 260 270
....*....|....*....|....*....|....
gi 959156737 298 LGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd01574 232 LGRRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
62-331 |
1.12e-35 |
|
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: 130.47 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSIN----NMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGpgTENIKAKFYDN 137
Cdd:cd06292 1 LIGYVVPELPggfsDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLAS--TRHDDPRVRYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 138 ISHKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKN---FDSSKI 213
Cdd:cd06292 79 HEAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGpEGSVPSDDRLAGYRAALEEAglpFDPGLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 214 InIGNGNTSDTVDNTMNifldiLNNSSS--TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTM 291
Cdd:cd06292 159 V-EGENTEEGGYAAAAR-----LLDLGPppTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 959156737 292 DQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06292 233 RQPIDEIGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-331 |
3.18e-34 |
|
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: 126.23 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAgPGTENIkAKFYDNISHK 141
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVT-PSDDDL-SHLARLRARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSY--DIKEKIYKEIMAKNFDSSKIInIGNG 219
Cdd:cd06293 79 TAVVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQvaERLAGARAAVAEAGLDPDEVV-RELS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 220 NTSDTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFL 298
Cdd:cd06293 158 APDANAELGRAAAAQLLAMPPRpTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYEL 237
|
250 260 270
....*....|....*....|....*....|...
gi 959156737 299 GANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06293 238 GRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-310 |
1.04e-33 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 125.09 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGII--VAGPGTENIKAKFYDNis 139
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLIltVGDAQGSEALELLEEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 hKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG--KDSYSYDIKEKIYKEIM-AKNFDSSKIINI 216
Cdd:cd06282 79 -GVPYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGdfSASDRARLRYQGYRDALkEAGLKPIPIVEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 217 GNgNTSDTVDNTMNIFLdilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMF 296
Cdd:cd06282 158 DF-PTNGLEEALTSLLS---GPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSR 233
|
250
....*....|....
gi 959156737 297 FLGANAAQLLVEKI 310
Cdd:cd06282 234 DMGRAAADLLLAEI 247
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-329 |
5.37e-33 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 124.82 E-value: 5.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 2 KITIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVYG 81
Cdd:PRK10014 6 KITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 82 IENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAG---PGTENI-KAKfydniSHKIPLVFINSEYMDSNIS 157
Cdd:PRK10014 86 LTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGaagSSDDLReMAE-----EKGIPVVFASRASYLDDVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 158 YVSNDEASGAKIALNYLLDNNHKDILFVRGKdSYSYDIKEKI--YKEIMAK---NFDSSKIINIGNGNTS--DTVDNTMN 230
Cdd:PRK10014 161 TVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQ-SSSLTRAERVggYCATLLKfglPFHSEWVLECTSSQKQaaEAITALLR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 231 ifldilNNSSSTAVFACNDLMAV----GVLNACKKLG-IKVPN----EISIIGYDNIPLSKFVEPKLTTMDQNMFFLGAN 301
Cdd:PRK10014 240 ------HNPTISAVVCYNETIAMgawfGLLRAGRQSGeSGVDRyfeqQVALAAFTDVPEAELDDPPLTWASTPAREIGRT 313
|
330 340
....*....|....*....|....*...
gi 959156737 302 AAQLLVEKIDCDNKFSKRIILNNSLVER 329
Cdd:PRK10014 314 LADRMMQRITHEETHSRNLIIPPRLIAR 341
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-331 |
7.04e-33 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 122.64 E-value: 7.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKcVNNLISRNVSGIIVAG--PGTENIKAKfydnIS 139
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDA-LRQLLQYRVDGVIVTSatLSSELAEEC----AR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 HKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKnfdsSKIINIGN 218
Cdd:cd06278 76 RGIPVVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGpEGTSTSRERERGFRAALAE----LGLPPPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 219 GNTSDTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACK-KLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMF 296
Cdd:cd06278 152 EAGDYSYEGGYEAARRLLAAPDRpDAIFCANDLMALGALDAARqEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIE 231
|
250 260 270
....*....|....*....|....*....|....*
gi 959156737 297 FLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06278 232 EMAEAAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
62-332 |
3.02e-32 |
|
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: 121.23 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVA-GPGTENIKAKFYDNish 140
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVtSDPTSRQLRLLRSA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFIN--SEYMDSNISyVSNDEASGAKIALNYLLDNNHKDILFVRGkDSYSYDIKEKI--YKEIMAKN---FDSSKI 213
Cdd:cd06296 78 GIPFVLIDpvGEPDPDLPS-VGATNWAGGRLATEHLLDLGHRRIAVITG-PPRSVSGRARLagYRAALAEAgiaVDPDLV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 214 INIGNgntsdTVDNTMNIFLDILNNSS-STAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMD 292
Cdd:cd06296 156 REGDF-----TYEAGYRAARELLELPDpPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVH 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 959156737 293 QNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERETV 332
Cdd:cd06296 231 QPLREMGAVAVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
4-305 |
2.30e-30 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 117.94 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 4 TIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVYGIE 83
Cdd:PRK10727 3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 84 NE-LKTNSLSIIlacTNG--DSDEEQKCVNNLISRNVSGIIVAG---PGTENIkakfydNISHKIP-LVFINSEYMDSNI 156
Cdd:PRK10727 83 QVaYHTGNFLLI---GNGyhNEQKERQAIEQLIRHRCAALVVHAkmiPDAELA------SLMKQIPgMVLINRILPGFEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 157 SYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSyDIKEKI--YKEIMAKNF--DSSKIINIGNGNTSDTvDNTMNIF 232
Cdd:PRK10727 154 RCIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSIS-DAEDRLqgYYDALAESGipANDRLVTFGEPDESGG-EQAMTEL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 959156737 233 LDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQL 305
Cdd:PRK10727 232 LG--RGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAEL 302
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
3-72 |
2.36e-30 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 109.98 E-value: 2.36e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 3 ITIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINN 72
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
29-332 |
5.30e-29 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 113.55 E-value: 5.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 29 VKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVYGIENELKTNSLSIILactnGDSDEEQK- 107
Cdd:PRK11041 4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLI----GDCAHQNQq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 108 ---CVNNLISRNVSGIIVAGP------GTENIKakfydNIShkiPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNN 178
Cdd:PRK11041 80 ektFVNLIITKQIDGMLLLGSrlpfdaSKEEQR-----NLP---PMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 179 HKDILFVRGKDSYSY-DIKEKIYKEIMAKN---FDSSKIINignGN-TSDTVDNTMNIFLDIlnNSSSTAVFACNDLMAV 253
Cdd:PRK11041 152 HKRIACIAGPEEMPLcHYRLQGYVQALRRCgitVDPQYIAR---GDfTFEAGAKALKQLLDL--PQPPTAVFCHSDVMAL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 959156737 254 GVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERETV 332
Cdd:PRK11041 227 GALSQAKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
173-332 |
8.31e-29 |
|
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: 108.96 E-value: 8.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 173 YLLDNNHKDILFVRG---KDSYSYDIKEKIYKEIMAK-NFDSSKIINIGNGNTSDTVDNTMNIFLDILnnssSTAVFACN 248
Cdd:pfam13377 1 HLAELGHRRIALIGPegdRDDPYSDLRERGFREAARElGLDVEPTLYAGDDEAEAAAARERLRWLGAL----PTAVFVAN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 249 DLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVE 328
Cdd:pfam13377 77 DEVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVE 156
|
....
gi 959156737 329 RETV 332
Cdd:pfam13377 157 REST 160
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
5.86e-28 |
|
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: 109.63 E-value: 5.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAgPGTENiKAKFYDNISH- 140
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILT-PGDED-DPELAAALARl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFINSEyMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGkDSYSYDIKEKI--YKEIMAK---NFDSsKIIN 215
Cdd:cd06281 79 DIPVVLIDRD-LPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTG-GPDIRPGRERIagFKAAFAAaglPPDP-DLVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 216 IGNGNTSDTVDNTMNIFLDIlnnSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNM 295
Cdd:cd06281 156 LGSFSADSGFREAMALLRQP---RPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDL 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 959156737 296 FFLGANAAQLLVEKIDCDNKF-SKRIILNNSLVERE 330
Cdd:cd06281 233 DAVGRAAAELLLDRIEGPPAGpPRRIVVPTELILRD 268
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
62-331 |
6.61e-28 |
|
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: 109.57 E-value: 6.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIIL-ACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENikAKFYDNIS- 139
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVePCDSDDEDLADRLRRFLSRSRPDGVILTPPLSDD--PALLDALDe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 HKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRG-KDSYSYDIKEKIYKEIMAKN---FDSSkIIN 215
Cdd:cd01545 79 LGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGpPDHGASAERLEGFRDALAEAglpLDPD-LVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 216 IGNgNTSDTVDNTMNIFLDIlnNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNM 295
Cdd:cd01545 158 QGD-FTFESGLEAAEALLDL--PDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 959156737 296 FFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd01545 235 AEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
58-309 |
3.71e-27 |
|
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: 107.72 E-value: 3.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 58 QKSTTIGVVVP-------SINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNnliSRNVSGIIVAGPGtENI 130
Cdd:cd06295 1 QRSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLD---SGRADGLIVLGQG-LDH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 131 KAkFYDNISHKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIKEKIYKEIMAK---N 207
Cdd:cd06295 77 DA-LRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVADRLQGYRDALAEaglE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 208 FDSSKIINigngnTSDTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEP 286
Cdd:cd06295 156 ADPSLLLS-----CDFTEESGYAAMRALLDSGTAfDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRP 230
|
250 260
....*....|....*....|...
gi 959156737 287 KLTTMDQNMfflgANAAQLLVEK 309
Cdd:cd06295 231 PLTTVRQDL----ALAGRLLVEK 249
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
62-331 |
1.30e-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: 106.52 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVP-----SINNMFFTELVYGIENELKTNSLSIIL-ACTNGDSDEEQkcvnnLISRNVSGIIVAGPGTEN--IKAK 133
Cdd:cd06279 1 AIGVLLPddlsyAFSDPVAAQFLRGVAEVCEEEGLGLLLlPATDEGSAAAA-----VRNAAVDGFIVYGLSDDDpaVAAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 134 fydnISHKIPLVFINSEyMDSNISYVSNDEASGAKIALNYLLDNNHKDILFV----------------RGKDSYSYDIKE 197
Cdd:cd06279 76 ----RRRGLPLVVVDGP-APPGIPSVGIDDRAAARAAARHLLDLGHRRIAILslrldrgrergpvsaeRLAAATNSVARE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 198 KI--YKEIM-AKNFDSSK--IINIGNGntsdTVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKVPNEIS 271
Cdd:cd06279 151 RLagYRDALeEAGLDLDDvpVVEAPGN----TEEAGRAAARALLAlDPRPTAILCMSDVLALGALRAARERGLRVPEDLS 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 272 IIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKIDCDNkfSKRIILNNSLVERET 331
Cdd:cd06279 227 VTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAP--PRPVILPTELVVRAS 284
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
56-332 |
2.26e-26 |
|
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: 106.16 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 56 TKQKSTTIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKA--- 132
Cdd:COG1879 29 AAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPalk 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 133 KFYDNishKIPLVFINSEYMDSN-ISYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDIK-EKIYKEIMAKNF 208
Cdd:COG1879 109 KAKAA---GIPVVTVDSDVDGSDrVAYVGSDNYAAGRLAAEYLAKalGGKGKVAILTGSPGAPAANErTDGFKEALKEYP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 209 DsSKIINIGNGNtsDTVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIP--LSKFVE 285
Cdd:COG1879 186 G-IKVVAEQYAD--WDREKALEVMEDLLQaHPDIDGIFAANDGMALGAAQALKAAGRK--GDVKVVGFDGSPeaLQAIKD 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 959156737 286 PKLT-TMDQNMFFLGANAAQLLVEKIDcDNKFSKRIILNNSLVERETV 332
Cdd:COG1879 261 GTIDaTVAQDPYLQGYLAVDAALKLLK-GKEVPKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
62-311 |
2.52e-25 |
|
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: 102.64 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSE--YMDSNISYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDIK-EKIYKEIMAKNFDsSKIINI 216
Cdd:cd01536 81 IPVVAVDTDidGGGDVVAFVGTDNYEAGKLAGEYLAEalGGKGKVAILEGPPGSSTAIDrTKGFKEALKKYPD-IEIVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 217 GNGNTSdtVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIP--LSKFVEPKLT-TMD 292
Cdd:cd01536 160 QPANWD--RAKALTVTENLLQaNPDIDAVFAANDDMALGAAEALKAAGRT--GDIKIVGVDGTPeaLKAIKDGELDaTVA 235
|
250
....*....|....*....
gi 959156737 293 QNMFFLGANAAQLLVEKID 311
Cdd:cd01536 236 QDPYLQGYLAVEAAVKLLN 254
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
62-331 |
6.50e-25 |
|
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: 101.39 E-value: 6.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGpgtENIKAKFYDNI-SH 140
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMAS---LDLTELFEEVIvPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 141 KIPLVFINSEYMdsNISYVSNDEASGAKIALNYLLDNNHKDILF--VRGKDSYSYDI---KEKIYKEIMAKNF---DSSK 212
Cdd:cd06297 78 EKPVVLIDANSM--GYDCVYVDNVKGGFMATEYLAGLGEREYVFfgIEEDTVFTETVfreREQGFLEALNKAGrpiSSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 213 IINIGNGntsdtVDNTMNIFLDILNNSS-STAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKfvEPKLTTM 291
Cdd:cd06297 156 MFRIDNS-----SKKAECLARELLKKADnPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTV 228
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 959156737 292 DQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERET 331
Cdd:cd06297 229 RQPVEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
4-310 |
1.83e-23 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 98.68 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 4 TIQDVAEKANVSVATVSRVMNGN--YPVKAETRETVLKVIKELNY--IPNMQARELTKQKSTTIGVVV----PSINNMFF 75
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNDDptLNVKEETKHRILEIAEKLEYktSSARKLQTGAVNQHHILAIYSyqqeLEINDPYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 76 TELVYGIENElkTNSLSIIL-ACTNGDSDEEQKcvnnlisrNVSGIIVAGPGTENIKAKFYdniSHKIPLVFINSEYMDS 154
Cdd:PRK10339 83 LAIRHGIETQ--CEKLGIELtNCYEHSGLPDIK--------NVTGILIVGKPTPALRAAAS---ALTDNICFIDFHEPGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 155 NISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSY-DIKEKIYKEI-MAKNFDSSKIINIGNGNTSDTVDNTMNIF 232
Cdd:PRK10339 150 GYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKaDIREVAFAEYgRLKQVVREEDIWRGGFSSSSGYELAKQML 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 959156737 233 LDilnNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKI 310
Cdd:PRK10339 230 AR---EDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKA 304
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
1-185 |
3.61e-23 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 97.64 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 1 MKITiqDVAEKANVSVATVSRVMNG---NYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTE 77
Cdd:PRK11303 1 MKLD--EIARLAGVSRTTASYVINGkakQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 78 LVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAG---PGTEnikakFYDNISHK-IPLVFINsEYMD 153
Cdd:PRK11303 79 IAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTslpPEHP-----FYQRLQNDgLPIIALD-RALD 152
|
170 180 190
....*....|....*....|....*....|....
gi 959156737 154 SN--ISYVSNDEASGAKIAlNYLLDNNHKDILFV 185
Cdd:PRK11303 153 REhfTSVVSDDQDDAEMLA-ESLLKFPAESILLL 185
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
5-310 |
1.93e-22 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 95.86 E-value: 1.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 5 IQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQARELTKQKSTTIGVVVPSINNMFFTELVYGIEN 84
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 85 ELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNIShkIPLVfinsEYMDS-----NISyV 159
Cdd:PRK14987 88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAG--IPVV----ELMDSqspclDIA-V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 160 SNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIKEKIYKEIMaknfdsskiINIGNGNTSDTVDNTMNIF--LDILN 237
Cdd:PRK14987 161 GFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQKGYEQAM---------LDAGLVPYSVMVEQSSSYSsgIELIR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 959156737 238 NSSST-----AVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKI 310
Cdd:PRK14987 232 QARREypqldGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARI 309
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
6-55 |
4.75e-21 |
|
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: 84.77 E-value: 4.75e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 959156737 6 QDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPNMQAREL 55
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSL 50
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
62-311 |
7.37e-21 |
|
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: 90.30 E-value: 7.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPS----INNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYdn 137
Cdd:cd20010 1 AIGLVLPLdpgdLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 138 ISHKIP-LVFINSEyMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSY-DIKEKIYKEIMAKN---FDSSK 212
Cdd:cd20010 79 LERGIPfVVHGRSE-SGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFaHQRRDGYRAALAEAglpVDPAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 213 IINIGNgntsdTVDNTMNIFLDILNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIP-LSKFVEPKLTT 290
Cdd:cd20010 158 VREGPL-----TEEGGYQAARRLLALPPPpTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLpALEYFSPPLTT 232
|
250 260
....*....|....*....|.
gi 959156737 291 MDQNMFFLGANAAQLLVEKID 311
Cdd:cd20010 233 TRSSLRDAGRRLAEMLLALID 253
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
62-330 |
2.14e-20 |
|
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380496 [Multi-domain] Cd Length: 266 Bit Score: 88.97 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINN-MFFTELVYGIENELKTNSLSIILA-----CTNGDSDEEqkcvnnLISRN-VSGIIVAGPGTENIKakF 134
Cdd:cd06272 1 TIGLYWPSVGErVALTRLLSGINEAISKQGYNINLSicpykVGHLCTAKG------LFSENrFDGVIVFGISDSDIE--Y 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 135 YDNISHKIPLVFINSEYMDSNISYVSNDEAsgAKIALNYLLDNNHKDILFVRGKDSYS-YDIKEKIYKEIMAKN--FDSS 211
Cdd:cd06272 73 LNKNKPKIPIVLYNRESPKYSTVNVDNEKA--GRLAVLLLIQKGHKSIAYIGNPNSNRnQTLRGKGFIETCEKHgiHLSD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 212 KIINIGNGNTSDTvDNTMNIFLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTM 291
Cdd:cd06272 151 SIIDSRGLSIEGG-DNAAKKLLK--KKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVV 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 959156737 292 DQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERE 330
Cdd:cd06272 228 GVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFRE 266
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
63-311 |
1.70e-19 |
|
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: 86.21 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 63 IGVVVPSINNMFFTELVYGIENELKTNSL-SIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGeVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSN-ISYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDI-KEKIYKEIMAKNFDSSKIINIG 217
Cdd:pfam13407 81 IPVVTFDSDAPSSPrLAYVGFDNEAAGEAAGELLAEalGGKGKVAILSGSPGDPNANeRIDGFKKVLKEKYPGIKVVAEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 218 NGnTSDTVDNTMNIFLDIL--NNSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIPLSK--FVEPKLT-TMD 292
Cdd:pfam13407 161 EG-TNWDPEKAQQQMEALLtaYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEALeaIKDGTIDaTVL 237
|
250
....*....|....*....
gi 959156737 293 QNMFFLGANAAQLLVEKID 311
Cdd:pfam13407 238 QDPYGQGYAAVELAAALLK 256
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
63-311 |
3.24e-19 |
|
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: 85.76 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 63 IGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-----AGPGTENIKAkfYDN 137
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAInlvdpAAAGVAEKAR--GQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 138 IshkiPLVFIN-SEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSY-------SYDIKEKIYKEIMAKNFD 209
Cdd:cd01537 80 V----PVVFFDkEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHpdaearlAGVIKELNDKGIKTEQLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 210 sskiINIGNGNTSDTVDNTMNIfldiLNNSSS-TAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKL 288
Cdd:cd01537 156 ----LDTGDWDTASGKDKMDQW----LSGPNKpTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLL 227
|
250 260
....*....|....*....|...
gi 959156737 289 TTMDQNMFFLGANAAQLLVEKID 311
Cdd:cd01537 228 TTILQDANNLGKTTFDLLLNLAD 250
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
63-308 |
8.61e-19 |
|
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: 84.63 E-value: 8.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 63 IGVVVPS---INNMFFTELVYGIENELKTNSLS--IILACTNGDSDEEQkcVNNLISRNVSGIIVAGPGTENI----KAK 133
Cdd:cd01391 2 IGVVTSSlhqIREQFGIQRVEAIFHTADKLGASveIRDSCWHGSVALEQ--SIEFIRDNIAGVIGPGSSSVAIviqnLAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 134 FYDnishkIPLVFINSEYMDSNISYVSNDEAS-------GAKIALNYLLDNNHKDILFVRGKDSYSYDIKEKIYKEIMAK 206
Cdd:cd01391 80 LFD-----IPQLALDATSQDLSDKTLYKYFLSvvfsdtlGARLGLDIVKRKNWTYVAAIHGEGLNSGELRMAGFKELAKQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 207 NfdSSKIINIGNGNTsDTVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIPLSKFVE 285
Cdd:cd01391 155 E--GICIVASDKADW-NAGEKGFDRALRKLReGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDEVG 229
|
250 260
....*....|....*....|....*...
gi 959156737 286 -----PKLTTMDQNMFFLGANAAQLLVE 308
Cdd:cd01391 230 yeveaNGLTTIKQQKMGFGITAIKAMAD 257
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
4-49 |
1.17e-17 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 75.37 E-value: 1.17e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 959156737 4 TIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVIKELNYIPN 49
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
112-306 |
1.38e-17 |
|
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: 81.09 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 112 LISRNVSGIIVAGPGTENIKAKfydnISHKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSY 191
Cdd:cd01543 46 LKGWKGDGIIARLDDPELAEAL----RRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 192 SYDIKEKIYKEIMAKNFDSSKIINIGNGNTSDTVDNTMNIFLDILnnsSS----TAVFACNDLMAVGVLNACKKLGIKVP 267
Cdd:cd01543 122 WSRERGEGFREALREAGYECHVYESPPSGSSRSWEEEREELADWL---KSlpkpVGIFACNDDRARQVLEACREAGIRVP 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 959156737 268 NEISIIGYDNIPL-SKFVEPKLTTMDQNMFFLGANAAQLL 306
Cdd:cd01543 199 EEVAVLGVDNDELiCELSSPPLSSIALDAEQIGYEAAELL 238
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-276 |
1.51e-17 |
|
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: 81.17 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEY-MDSNISYVSNDEASGAKIALNYLLDNNHK---DILFVRGKDSYSYDIKEKIYKEIMAKNfDSSKIINIG 217
Cdd:cd06322 81 IPVFTVDVKAdGAKVVTHVGTDNYAGGKLAGEYALKALLGgggKIAIIDYPEVESVVLRVNGFKEAIKKY-PNIEIVAEQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 218 NGNTSDTVdnTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGikVPNEISIIGYD 276
Cdd:cd06322 160 PGDGRREE--ALAATEDMLQaNPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFD 215
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
62-279 |
6.07e-17 |
|
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.
Pssm-ID: 380524 [Multi-domain] Cd Length: 272 Bit Score: 79.58 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKT-NSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-------AGPGTENIKAK 133
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVnpvdtdaSAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 134 fydnishKIPLVFINSEY--MDSNISYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDIK-EKIYKEIMAKNf 208
Cdd:cd06301 82 -------GIPLVYVNREPdsKPKGVAFVGSDDIESGELQMEYLAKllGGKGNIAILDGVLGHEAQILrTEGNKDVLAKY- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 959156737 209 DSSKIINIGNGNTS-----DTVDNTMNIFLDIlnnsssTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIP 279
Cdd:cd06301 154 PGMKIVAEQTANWSrekamDIVENWLQSGDKI------DAIVANNDEMAIGAILALEAAGKK--DDILVAGIDATP 221
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
62-321 |
1.22e-16 |
|
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: 78.40 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAgPGTENIkAKFYDNISHK 141
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVA-PSTPPD-DIYYLCQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVrGKDSYSYDIKEKI--YKEIMAKNFDSSKIINI-GN 218
Cdd:cd06274 79 LPVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFL-GGRPELPSTAERIrgFRAALAEAGITEGDDWIlAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 219 GNTSDTVDNTMNIFLDILNN------SSSTAVFAcndlmavGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMD 292
Cdd:cd06274 158 GYDRESGYQLMAELLARLGGlpqalfTSSLTLLE-------GVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVR 230
|
250 260
....*....|....*....|....*....
gi 959156737 293 QNMFFLGANAAQLLVEKIDCDNKFSKRII 321
Cdd:cd06274 231 QDHDEIAEHAFELLDALIEGQPEPGVIII 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-332 |
4.27e-15 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380542 [Multi-domain] Cd Length: 278 Bit Score: 74.32 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-------AGPGTENIKAKf 134
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIIsptnssaAPTVLDLANEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 135 ydnishKIPLVFIN-----SEYmdsnISYVSNDEASGAKIALNYLLDNnhkdiLFVRGKDSYSYDI------------KE 197
Cdd:cd06319 80 ------KIPVVIADigtggGDY----VSYIISDNYDGGYQAGEYLAEA-----LKENGWGGGSVGIiaipqsrvngqaRT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 198 KIYKEIMAK-NFDSSKIINIGNgntsDTVDNTMNIFLDIL-NNSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGY 275
Cdd:cd06319 145 AGFEDALEEaGVEEVALRQTPN----STVEETYSAAQDLLaANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGF 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 959156737 276 DNIPLS-KFVEPKltTMD----QNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLVERETV 332
Cdd:cd06319 219 DGDPEAlDLIKDG--KLDgtvaQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV 278
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
62-276 |
5.12e-14 |
|
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: 71.17 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEYMDSNISYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDIKEKIYKEIMAKNFDSSKIINIGNG 219
Cdd:cd06305 81 IPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKdlNGEGNIAVFNVFGVPPLDKRYDIYKAVLKANPGIKKIVAELGD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 220 NTSDTVDNTMNIFLDILN---NSSSTAVFACNDLMAVGVLNACKKLGikvPNEISIIGYD 276
Cdd:cd06305 161 VTPNTAADAQTQVEALLKkypEGGIDAIWAAWDEPAKGAVQALEEAG---RTDIKVYGVD 217
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
62-276 |
4.54e-13 |
|
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: 68.14 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIE---NELKTNsLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNI 138
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEaaaKDLGVK-IIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 139 SHKIPLVFINSE-YMDSNISYVSNDEASGAKIALNYL---LDNNHK-DILFVRGKDSySYDIKEKIYKEIMAKNFDSSKI 213
Cdd:cd06310 80 DKGIPVIVIDSGiKGDAYLSYIATDNYAAGRLAAQKLaeaLGGKGKvAVLSLTAGNS-TTDQREEGFKEYLKKHPGGIKV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 959156737 214 INIGNGNtsDTVDNTMNIFLDIL-NNSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYD 276
Cdd:cd06310 159 LASQYAG--SDYAKAANETEDLLgKYPDIDGIFATNEITALGAAVAIKSRKLS--GQIKIVGFD 218
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
62-279 |
9.05e-13 |
|
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: 67.30 E-value: 9.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVA-------GPGTENIKAKf 134
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVpvdadalAPAVEKAKEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 135 ydnishKIPLV----FINSEYMDsniSYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDI-KEKIYKEIMAKN 207
Cdd:cd06313 80 ------GIPLVgvnaLIENEDLT---AYVGSDDVVAGELEGQAVADrlGGKGNVVILEGPIGQSAQIdRGKGIENVLKKY 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 959156737 208 FDsSKIINIGNGNTSDtvDNTMNIFLDILNNSSS--TAVFACNDLMAVGVLNACKKLGIkvpNEISIIGYDNIP 279
Cdd:cd06313 151 PD-IKVLAEQTANWSR--DEAMSLMENWLQAYGDeiDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDGIE 218
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
62-327 |
6.28e-12 |
|
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380495 [Multi-domain] Cd Length: 264 Bit Score: 64.75 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPS---INNMFFTELVYGIENELKTNSLSIILacTNGDSDEEQKCVNNLI-SRNVSGIIVAGPGTENIKAKFYdn 137
Cdd:cd06271 1 VIALVFPVtetELNGTVSE*VSGITEEAGTTGYHLLV--WPFEEAES*VPIRDLVeTGSADGVILSEIEPNDPRVQFL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 138 ISHKIPLVFINSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSY-DIKEKIYKE------IMAKNFDS 210
Cdd:cd06271 77 TKQNFPFVAHGRSD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPhDRRLQGYVRa*rdagLTGYPLDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 211 SKIINIGNGNTSDTVDntmnifLDILnnssSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIP-LSKFVEPKLT 289
Cdd:cd06271 157 DTTLEAGRAAAQRLLA------LSPR----PTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLT 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 959156737 290 TMDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLV 327
Cdd:cd06271 227 TVHAPIAEAGRELAKALLARIDGEDPETLQVLVQPSLS 264
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
62-321 |
9.09e-12 |
|
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: 64.45 E-value: 9.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTEnikakfYDNISHK 141
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPS------GDDITAK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 -----IPLVFI-NSEYMDSNISYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSYDIKEKI--YKEIMAKNFDSSKI 213
Cdd:pfam00532 77 aegygIPVIAAdDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRPIAVMAGPASALTARERVqgFMAALAAAGREVKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 214 INIGngntsdTVDNTMNIFLDILN-----NSSSTAVFACNDLMAVGVLNACKKLG-IKVPNEI-----SIIGYDNIPL-- 280
Cdd:pfam00532 157 YHVA------TGDNDIPDAALAANamlvsHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVgiginSVVGFDGLSKaq 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 959156737 281 -SKFVEPKLTTMDQNMFFLGANAAQLLVEKIDCDNKFSKRII 321
Cdd:pfam00532 231 dTGLYLSPLTVIQLPRQLLGIKASDMVYQWIPKFREHPRVLL 272
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
62-279 |
2.97e-11 |
|
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.
Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 62.95 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNS-LSIILACTNGDSDEEQKCVNNLISRNVSGIIV----AGPGTENIKaKFYD 136
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPnVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVspneADALTPVVK-KAYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 137 nisHKIPLVFINSEyMDSN--ISYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDI-KEKIYKEIMAKNfDSS 211
Cdd:cd06308 80 ---AGIPVIVLDRK-VSGDdyTAFIGADNVEIGRQAGEYIAEllNGKGNVVEIQGLPGSSPAIdRHKGFLEAIAKY-PGI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 959156737 212 KIINIGNGNTSDtvDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIP 279
Cdd:cd06308 155 KIVASQDGDWLR--DKAIKVMEDLLQaHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVDGLP 219
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
62-279 |
4.50e-11 |
|
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: 62.31 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-------AGPGTENIKAKf 134
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLInptdsdaVSPAVEEANEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 135 ydnishKIPLVFINSEYMDSNI-SYVSNDEASGAKIALNYLLDNNHK--DILFVRGKDSYSYDI-KEKIYKEIMAKNfDS 210
Cdd:cd06323 80 ------GIPVITVDRSVTGGKVvSHIASDNVAGGEMAAEYIAKKLGGkgKVVELQGIPGTSAAReRGKGFHNAIAKY-PK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 211 SKIINIGNGNTSDTvdNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGikvPNEISIIGYDNIP 279
Cdd:cd06323 153 INVVASQTADFDRT--KGLNVMENLLQaHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTP 217
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-304 |
2.55e-10 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGII-------VAGPGTENIKAKf 134
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIyipagatAAAVPVKAARAA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 135 ydnishKIPLVFINSEYMDSNI-SYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDI-KEKIYKEIMAKNFDs 210
Cdd:cd19972 80 ------GIPVIAVDRNPEDAPGdTFIATDSVAAAKELGEWVIKqtGGKGEIAILHGQLGTTPEVdRTKGFQEALAEAPG- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 211 skiINIGNGNTSD-TVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIkvPNEISIIGYDNIPLS-KFVEPK 287
Cdd:cd19972 153 ---IKVVAEQTADwDQDEGFKVAQDMLQaNPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFDGDVAGlKAVKDG 227
|
250
....*....|....*....
gi 959156737 288 LT--TMDQNMFFLGANAAQ 304
Cdd:cd19972 228 VLdaTMTQQTQKMGRLAVD 246
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
62-310 |
2.79e-10 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 60.09 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEY-MDSNISYVSNDEASGAKIALNYLLDN--NHKDILFVRGKDSYSYDI-KEKIYKEIMAKNfDSSKIINIG 217
Cdd:cd19968 81 IPVVTVDRRAeGAAPVPHVGADNVAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIdRTKGFHEELAAG-PKIKVVFEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 218 NGNTSDtvDNTMNIFLDILNNSSS--TAVFACNDLMAVGVLNACKKLGIKVPNeISIIGYDNIP--LSKFVEPKL-TTMD 292
Cdd:cd19968 160 TGNFER--DEGLTVMENILTSLPGppDAIICANDDMALGAIEAMRAAGLDLKK-VKVIGFDAVPdaLQAIKDGELyATVE 236
|
250
....*....|....*...
gi 959156737 293 QNMFFLGANAAQLLVEKI 310
Cdd:cd19968 237 QPPGGQARTALRILVDYL 254
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
63-312 |
4.23e-10 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 59.58 E-value: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 63 IGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEE---QKCvNNLISRNVSGIIVAGPGTENIKAKFYDNIS 139
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPSETDTQgqlNLL-ETMLNKGYDAILVSPISDTNLIPPIEKANK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 HKIPLVFINSEYMDSN--------ISYVSNDEASGAKIALNYLLDNNHK--DILFVRGKD-SYSYDIKEKIYKEIMAKNf 208
Cdd:cd06320 81 KGIPVINLDDAVDADAlkkaggkvTSFIGTDNVAAGALAAEYIAEKLPGggKVAIIEGLPgNAAAEARTKGFKETFKKA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 209 DSSKIINIGNGN--TSDTVDNTMNIfldILNNSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIPLSK--FV 284
Cdd:cd06320 160 PGLKLVASQPADwdRTKALDAATAI---LQAHPDLKGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDGIPEAKksIK 234
|
250 260
....*....|....*....|....*....
gi 959156737 285 EPKLT-TMDQNMFFLGANAAQLLVEKIDC 312
Cdd:cd06320 235 AGELTaTVAQYPYLEGAMAVEAALRLLQG 263
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
63-335 |
2.97e-09 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 57.19 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 63 IGVVVPSINNMFFTELVYGIENELKTNSLS--IILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENI---------K 131
Cdd:PRK09701 27 YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSvdIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLvmpvarawkK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 132 AKFYDNISHKIPLVfiNSEYMDSNI-SYVSNDE-ASGAKIAlNYLLDN---NHKDILFVRGKdsySYDIKEKIYKEIMAK 206
Cdd:PRK09701 107 GIYLVNLDEKIDMD--NLKKAGGNVeAFVTTDNvAVGAKGA-SFIIDKlgaEGGEVAIIEGK---AGNASGEARRNGATE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 207 NFDSSKIINIGNGNTSD-----TVDNTMNIfldILNNSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIPLS 281
Cdd:PRK09701 181 AFKKASQIKLVASQPADwdrikALDVATNV---LQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEA 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 959156737 282 KFV--EPKLT-TMDQNMFFLGANAAQLLVEKIDcdnkfSKRIILNNSLVERETVISI 335
Cdd:PRK09701 256 RKMveAGQMTaTVAQNPADIGATGLKLMVDAEK-----SGKVIPLDKAPEFKLVDSI 307
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
62-276 |
4.22e-09 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 56.47 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIIL--ACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNIS 139
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWrgPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 HKIPLVFINSEYMDSN-ISYVSNDEASGAKIALNYLLD--NNHKDILFVR-GKDSYSYDIKEKIYKEIMAKNFDSSKIIN 215
Cdd:cd20004 81 QGIPVVIIDSDLGGDAvISFVATDNYAAGRLAAKRMAKllNGKGKVALLRlAKGSASTTDRERGFLEALKKLAPGLKVVD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 959156737 216 IGNGNTsdTVDNTMNIFLDILNNSSST-AVFACNDLMAVGVLNACKKLGikVPNEISIIGYD 276
Cdd:cd20004 161 DQYAGG--TVGEARSSAENLLNQYPDVdGIFTPNESTTIGALRALRRLG--LAGKVKFIGFD 218
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
62-279 |
4.29e-08 |
|
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.
Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 53.76 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVF----INSEYMDSNISYVSND-EASGAKIAlNYLLDNNHKD---ILFVRGKDSYSYDIK-EKIYKEIMAKNfDSSK 212
Cdd:cd06309 81 IPVILvdrtIDGEDGSLYVTFIGSDfVEEGRRAA-EWLVKNYKGGkgnVVELQGTAGSSVAIDrSKGFREVIKKH-PNIK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 959156737 213 II--NIGNGNTSDTVDNTMNIFLDilNNSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIP 279
Cdd:cd06309 159 IVasQSGNFTREKGQKVMENLLQA--GPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQK 225
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
157-311 |
4.45e-07 |
|
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: 50.23 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 157 SYVSNDEASGAKIALNYLLDNNHKDILFVRGKDSYSY--DIKEKIYKEIMAKNFDSSKIINIGNGNTSDTVDntmNIFLD 234
Cdd:cd20009 96 AYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYaqHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIR---AAARR 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 959156737 235 ILN-NSSSTAVFACNDLMAVGVLNACKKLGIKVPNEISIIGYDNIPLSKFVEPKLTTMDQNMFFLGANAAQLLVEKID 311
Cdd:cd20009 173 LLRqPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIE 250
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-263 |
2.43e-06 |
|
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: 48.13 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV----AGPGTENIKAkfydN 137
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVIlpqdSEELTVAAQK----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 138 ISHKIPLVFINSEYMDSN-ISYVSNDEASGAKIALNYLLD--NNHKDILFVRGKDSYSYDI-KEKIYKEIMAKNFDsskI 213
Cdd:cd06311 77 KDAGIPVVNFDRGLNVLIyDLYVAGDNPGMGVVSAEYIGKklGGKGNVVVLEVPSSGSVNEeRVAGFKEVIKGNPG---I 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 959156737 214 INIGNGNTSDTVDNTMNIFLDIL-NNSSSTAVFACNDLMAVGVLNACKKLG 263
Cdd:cd06311 154 KILAMQAGDWTREDGLKVAQDILtKNKKIDAVWAADDDMAIGVLQAIKEAG 204
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-279 |
4.03e-06 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 47.63 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIEN-ELKTNSLSIILACTNGDSDEEQK--CVNNLISRNVSGIIVAGPGTENIKAKFYDNI 138
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKhAKEANGYELLVKGIKQETDIEQQiaIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 139 SHKIPLVFINSEYMDS-------NISYVSNDEASGAKIALNYLLDNNHKD-----ILFVRGKDSySYDIKEKIYKEIMAK 206
Cdd:cd19970 81 DAGIAVINIDNRLDADalkeggiNVPFVGPDNRQGAYLAGDYLAKKLGKGgkvaiIEGIPGADN-AQQRKAGFLKAFEEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 959156737 207 NFdssKIINIGNGNTSdtVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIP 279
Cdd:cd19970 160 GM---KIVASQSANWE--IDEANTVAANLLTaHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNIP 226
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
62-279 |
5.54e-06 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 47.19 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKT-NSLSIILACTNGDSDEEQKCVNNLISRNVSGIIV-----AGPGTENIKAKfy 135
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAgGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVnlvdrTAAQTIIDKAK-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 136 dniSHKIPLVFINSEYMDSNIS------YV-SNDEASG---AKIALNYLLDNNHKD--------ILFVRG-KDSYSYDIK 196
Cdd:cd01539 80 ---AANIPVIFFNREPSREDLKsydkayYVgTDAEESGimqGEIIADYWKANPEIDkngdgkiqYVMLKGePGHQDAIAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 197 EKIYKEIMAKNFDSSKIINIGNGN-TSDTVDNTMNIFLDILNNSSStAVFACNDLMAVGVLNACKKLGIK---VPNEISI 272
Cdd:cd01539 157 TKYSVKTLNDAGIKTEQLAEDTANwDRAQAKDKMDAWLSKYGDKIE-LVIANNDDMALGAIEALKAAGYNtgdGDKYIPV 235
|
....*..
gi 959156737 273 IGYDNIP 279
Cdd:cd01539 236 FGVDATP 242
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-279 |
1.03e-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: 46.22 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEY-MDSNISYVSNDEASGAKI----ALNYLLDNNHKD--ILFVRGKDSYSYDIKEKIYKEIMAKNfDSSKII 214
Cdd:cd06317 81 IPVIAYDAVIpSDFQAAQVGVDNLEGGKEigkyAADYIKAELGGQakIGVVGALSSLIQNQRQKGFEEALKAN-PGVEIV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 959156737 215 NIGNGntSDTVDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDNIP 279
Cdd:cd06317 160 ATVDG--QNVQEKALSAAENLLTaNPDLDAIYATGEPALLGAVAAVRSQGRQ--GKIKVFGWDLTK 221
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
98-276 |
1.79e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 45.70 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 98 TNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHKIPLV-F---INSEYMDSNISyvSNDEASGAKIA--L 171
Cdd:cd20005 39 TESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEKGIPVVtFdsgVPSDLPLATVA--TDNYAAGALAAdhL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 172 NYLLDNNHKDILFVRGKDSYSYDIKEKIYKEIMAKNFDSSKIINI--GNGNTSDTVDNTMNIfldILNNSSSTAVFACND 249
Cdd:cd20005 117 AELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDIKVVNVqyGVGDHAKAADIAKAI---LQANPDLKGIYATNE 193
|
170 180
....*....|....*....|....*..
gi 959156737 250 LMAVGVLNACKKLGikVPNEISIIGYD 276
Cdd:cd20005 194 GAAIGVANALKEMG--KLGKIKVVGFD 218
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-327 |
5.74e-05 |
|
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: 44.20 E-value: 5.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSD--EEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNIS 139
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGAKVTVVDARYDlaKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 140 HKIPLVFIN--SEYMDSNIsyVSNDEASGAkIALNYLLD--NNHKDILFVRGKDSYSydIKEKI--YKEIMAKNFDSsKI 213
Cdd:cd06321 81 AGIIVVAVDvaAEGADATV--TTDNVQAGY-LACEYLVEqlGGKGKVAIIDGPPVSA--VIDRVngCKEALAEYPGI-KL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 214 INIGNGNTSDtvDNTMNIFLDILN-NSSSTAVFACNDLMAVGVLNACKKLGikvPNEISIIGYDNIP-----LSKFVEPK 287
Cdd:cd06321 155 VDDQNGKGSR--AGGLSVMTRMLTaHPDVDGVFAINDPGAIGALLAAQQAG---RDDIVITSVDGSPeavaaLKREGSPF 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 959156737 288 LTTMDQNMFFLGANAAQLLVEKIDCDNKFSKRIILNNSLV 327
Cdd:cd06321 230 IATAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLV 269
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
62-276 |
1.32e-04 |
|
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: 43.08 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 62 TIGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHK 141
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 142 IPLVFINSEyMDSNISYVSN---DEASGAKIALNYLLDNNHKDILFVR--GKDS----------YSYDIKEKIYKEIMAK 206
Cdd:cd19967 81 IPVFLIDRE-INAEGVAVAQivsDNYQGAVLLAQYFVKLMGEKGLYVEllGKESdtnaqlrsqgFHSVIDQYPELKMVAQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 959156737 207 ---NFDSSKIINIgngntsdtVDNTMNIFLDILnnssstAVFACNDLMAVGVLNACKKLGIkvPNEISIIGYD 276
Cdd:cd19967 160 qsaDWDRTEAFEK--------MESILQANPDIK------GVICGNDEMALGAIAALKAAGR--AGDVIIVGFD 216
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
2-45 |
2.39e-04 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 38.65 E-value: 2.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 959156737 2 KITIQDVAEKANVSVATVSRVMNGNYPVkaeTRETVLKVIKELN 45
Cdd:smart00530 10 GLTQEELAEKLGVSRSTLSRIENGKRKP---SLETLKKLAKALG 50
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
63-267 |
2.79e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 41.80 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 63 IGVVVPSINNMFFTELVYGIENELKTNSLSIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENI-----KAKfydn 137
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAanivdKAK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 138 iSHKIPLVFINSEYMDSNIS-YVSNDEASGAKIALNYLLDNNHK-DILFVRGK--DSYSYDIKEKiYKEIMAKNFDSSKI 213
Cdd:cd19992 78 -AAGVPVISYDRLILNADVDlYVGRDNYKVGQLQAEYALEAVPKgNYVILSGDpgDNNAQLITAG-AMDVLQPAIDSGDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 959156737 214 INIGNGNTSD-TVDNTMNIFLDIL--NNSSSTAVFACNDLMAVGVLNACKKLGI--KVP 267
Cdd:cd19992 156 KIVLDQYVKGwSPDEAMKLVENALtaNNNNIDAVLAPNDGMAGGAIQALKAQGLagKVF 214
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
96-277 |
5.78e-04 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 41.06 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 96 ACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTEN---IKAKFYDNIshkiPLVFI----NSEYMDSniSYVSNDEASGAK 168
Cdd:cd20008 37 PATEADIAGQVNLVENAISRKPDAIVLAPNDTAAlvpAVEAADAGI----PVVLVdsgaNTDDYDA--FLATDNVAAGAL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 169 IA------LNYLLDNNHKDILFVRGKDSYSYDIKEKIYKEIMAKNFDSSKIINI--GNGNTSdtvdNTMNIFLDIL-NNS 239
Cdd:cd20008 111 AAdelaelLKASGGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKYPDIEIVDVqySDGDIA----KALNQTTDLLtANP 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 959156737 240 SSTAVFACNDLMAVGVLNACKKLGIKvpNEISIIGYDN 277
Cdd:cd20008 187 DLVGIFGANNPSAVGVAQALAEAGKA--GKIVLVGFDS 222
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
1-41 |
8.22e-04 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 37.15 E-value: 8.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 959156737 1 MKITIQDVAEKANVSVATVSRVMNGNYPVKAETRETVLKVI 41
Cdd:cd00093 11 KGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKAL 51
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
101-277 |
1.14e-03 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 39.89 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 101 DSDEEQKCVNNLISRNVSGIIVAG-------PGTENIKAKfydnishKIPLVFINSEyMDSNI--SYVSNDEASGAKIAL 171
Cdd:cd20006 44 DIDGQIELIEEAIAQKPDAIVLAAsdydrlvEAVERAKKA-------GIPVITIDSP-VNSKKadSFVATDNYEAGKKAG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 172 NYLLDNNHKD-----ILFVrgKDSYSYDIKEKIYKEIMAKN-FDSSKIINIGNGNTSDTVDNTMNIfldILNNSSSTAVF 245
Cdd:cd20006 116 EKLASLLGEKgkvaiVSFV--KGSSTAIEREEGFKQALAEYpNIKIVETEYCDSDEEKAYEITKEL---LSKYPDINGIV 190
|
170 180 190
....*....|....*....|....*....|..
gi 959156737 246 ACNDLMAVGVLNACKKLGIKvpNEISIIGYDN 277
Cdd:cd20006 191 ALNEQSTLGAARALKELGLG--GKVKVVGFDS 220
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
92-267 |
2.67e-03 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 39.00 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 92 SIILACTNGDSDEEQKCVNNLISRNVSGIIVAGPGTENIKAKFYDNISHKIPLVFINSEYMDSNISYVSND-------EA 164
Cdd:cd19993 31 KYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLIENPIAFYISFDnvevgrmQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 959156737 165 SG---AKIALNYLL------DNNHkdILFVRGKDsysydikekiykEIMAKNFDSSKIINIGNGNTSD-TVDNTMNIFLD 234
Cdd:cd19993 111 RGvlkAKPEGNYVFikgsptDPNA--DFLRAGQM------------EVLQPAIDSGKIKIVGEQYTDGwKPANAQKNMEQ 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 959156737 235 IL--NNSSSTAVFACNDLMAVGVLNACKKLGI--KVP 267
Cdd:cd19993 177 ILtaNNNKVDAVVASNDGTAGGAVAALAAQGLagKVP 213
|
|
| HipB |
COG1396 |
Transcriptional regulator, contains XRE-family HTH domain [Transcription]; |
2-45 |
3.52e-03 |
|
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
Pssm-ID: 441006 [Multi-domain] Cd Length: 83 Bit Score: 36.13 E-value: 3.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 959156737 2 KITIQDVAEKANVSVATVSRVMNGNYPVkaeTRETVLKVIKELN 45
Cdd:COG1396 20 GLTQEELAERLGVSRSTISRIERGRRNP---SLETLLKLAKALG 60
|
|
| VapI |
COG3093 |
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ... |
1-33 |
3.67e-03 |
|
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];
Pssm-ID: 442327 [Multi-domain] Cd Length: 87 Bit Score: 35.94 E-value: 3.67e-03
10 20 30
....*....|....*....|....*....|...
gi 959156737 1 MKITIQDVAEKANVSVATVSRVMNGNYPVKAET 33
Cdd:COG3093 21 LGLSQTELAKALGVSRQRISEILNGKRAITADT 53
|
|
| |
