|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-339 |
2.73e-90 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 273.61 E-value: 2.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 1 MRKATMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLM 80
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 81 SGIQQILQPSQWTVVLGDIAvngiYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAKWDIPVVFVDSPPRGEhNF 159
Cdd:COG1609 81 RGIEEAARERGYQLLLANSD----EDPEREREALRLLLSRRVDGLIlAGSRLDDARLERLAEAGIPVVLIDRPLPDP-GV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 160 PSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSAADKLSQYLD 236
Cdd:COG1609 156 PSVGVDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDpelVVEGDFSAESGYEAARRLLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 237 RQKaLPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLInlEGK 316
Cdd:COG1609 236 RGP-RPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRI--EGP 312
|
330 340
....*....|....*....|...
gi 495597666 317 GEINTQRKVPAELVIRQSCGCKK 339
Cdd:COG1609 313 DAPPERVLLPPELVVRESTAPAP 335
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
64-330 |
1.50e-56 |
|
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: 184.64 E-value: 1.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAKW 142
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLC----NTDEDPEREREYLRLLLSRRVDGIIlAPSSLDDELLEELLAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DIPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVE 219
Cdd:cd06267 78 GIPVVLIDRRLDGL-GVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDpelVVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 220 TENDAQSAADKLSQYLDRQKaLPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEI 299
Cdd:cd06267 157 GDFSEESGYEAARELLALPP-RPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEM 235
|
250 260 270
....*....|....*....|....*....|.
gi 495597666 300 GRQSAEMLIQLInlEGKGEINTQRKVPAELV 330
Cdd:cd06267 236 GRAAAELLLERI--EGEEEPPRRIVLPTELV 264
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
64-332 |
5.94e-54 |
|
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: 178.13 E-value: 5.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAvngiYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAKW 142
Cdd:cd06283 2 IGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSN----NDPEKERDYIESLLSQRVDGLIlQPTGNNNDAYLELAQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DIPVVFVDSPPRGeHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYP-DRWTTRFERERGIREAAERCGATLGVVETE 221
Cdd:cd06283 78 GLPVVLVDRQIEP-LNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPiKGISTRRERLQGFLDALARYNIEGDVYVIE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 222 -NDAQSAADKLSQYLDRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIG 300
Cdd:cd06283 157 iEDTEDLQQALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIG 236
|
250 260 270
....*....|....*....|....*....|..
gi 495597666 301 RQSAEMLIQLInlEGKGEINTQRKVPAELVIR 332
Cdd:cd06283 237 KAAAEILLERI--EGDSGEPKEIELPSELIIR 266
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
64-330 |
3.55e-45 |
|
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: 155.00 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTVTLQPESLTL-LAKW 142
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILC----NTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEkLVKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DIPVVFVDSPPRGeHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATL--GVVET 220
Cdd:cd19977 78 GIPVVFVDRYIPG-LDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVdeELIKH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 221 ENDAQSAADKLSQYLDRQKaLPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIG 300
Cdd:cd19977 157 VDRQDDVRKAISELLKLEK-PPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIG 235
|
250 260 270
....*....|....*....|....*....|
gi 495597666 301 RQSAEMLIQLINLEGKGEiNTQRKVPAELV 330
Cdd:cd19977 236 RKAAELLLDRIENKPKGP-PRQIVLPTELI 264
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-335 |
9.31e-41 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 143.91 E-value: 9.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDiaVNGiyDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAK 141
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLAD--TGD--DPERELAALDSLLSRRVDGLIiTPARDDAPDLQELAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WDIPVVFVDsPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VV 218
Cdd:cd06285 77 RGVPVVLVD-RRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPderIV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 219 ETENDAQSAADKLSQYLDRQkALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEE 298
Cdd:cd06285 156 PGGFTIEAGREAAYRLLSRP-ERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYE 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 495597666 299 IGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQSC 335
Cdd:cd06285 235 MGRRAAELLLQLI--EGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
64-334 |
8.37e-40 |
|
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: 141.12 E-value: 8.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTVTLQPESLtlLAKWD 143
Cdd:cd06291 2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMILC----NSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEE--YKKLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 144 IPVVFVDSPPrgEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLGVVETEND 223
Cdd:cd06291 76 IPIVSIDRYL--SEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 224 AQSAAD--KLSQYLDRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGR 301
Cdd:cd06291 154 DFSEEDayELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAK 233
|
250 260 270
....*....|....*....|....*....|...
gi 495597666 302 QSAEMLIQLINleGKGEINTQRKVPAELVIRQS 334
Cdd:cd06291 234 EAVELLLKLIE--GEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
72-334 |
4.43e-36 |
|
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: 131.63 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 72 SNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTVTLQ-PESLTLLAKWDIPVVFVD 150
Cdd:cd06299 10 RNPFFAELASGIEDEARAHGYSVILG----NSDEDPEREDESLEMLLSQRVDGIIAVPTGEnSEGLQALIAQGLPVVFVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 151 SPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSA 227
Cdd:cd06299 86 REVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDeelVAFGDFRQDSG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 228 ADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEML 307
Cdd:cd06299 166 AAAAHRLLSRGDP-PTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRAVELL 244
|
250 260
....*....|....*....|....*..
gi 495597666 308 IQLINLEGKGEIntqRKVPAELVIRQS 334
Cdd:cd06299 245 LALIENGGRATS---IRVPTELIPRES 268
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
64-333 |
1.29e-35 |
|
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380512 [Multi-domain] Cd Length: 268 Bit Score: 130.38 E-value: 1.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAVNGiydrAQEDRMINRLIESRMAG-IISTVT-LQPESLTLLAK 141
Cdd:cd06289 2 VGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDP----ERQRRFLRRMLEQGVDGlILSPAAgTTAELLRRLKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WDIPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VV 218
Cdd:cd06289 78 WGIPVVLALRDVPGS-DLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDeslIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 219 ETENDAQSAADKLSQYLDRQKaLPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEE 298
Cdd:cd06289 157 PGPATREAGAEAARELLDAAP-PPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPRE 235
|
250 260 270
....*....|....*....|....*....|....*
gi 495597666 299 IGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQ 333
Cdd:cd06289 236 IGRRAARLLLRRI--EGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-334 |
2.87e-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: 126.62 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAG-IISTVTLQPESLTLLAK 141
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLC----NSGRDPERERRYLEMLESQRVRGlIVTPSDDDLSHLARLRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WDIPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLGVVETE 221
Cdd:cd06293 77 RGTAVVLLDRPAPGP-AGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVRE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 222 NDA--------QSAADKLsqyLDRQkALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLN 293
Cdd:cd06293 156 LSApdanaelgRAAAAQL---LAMP-PRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 495597666 294 ENSEEIGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06293 232 QPSYELGRAAADLLLDEI--EGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
64-334 |
1.01e-33 |
|
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: 125.34 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAVngiyDRAQEDRMINRLIESRMAGIISTVTLQPESLTLLAKWD 143
Cdd:cd06284 2 ILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDS----DPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 144 IPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCG---ATLGVVET 220
Cdd:cd06284 78 YPIVQCCEYIPDS-GVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGlpvDEDLIIEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 221 ENDAQSAADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIG 300
Cdd:cd06284 157 DFSFEAGYAAARALLALPER-PTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIG 235
|
250 260 270
....*....|....*....|....*....|....
gi 495597666 301 RQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06284 236 ETAAELLLEKI--EGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
63-332 |
2.94e-33 |
|
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: 123.91 E-value: 2.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTVTLQP-ESLTLLAK 141
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILA----NTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPsRELKRLLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WDIPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGatLGVVE-- 219
Cdd:cd06280 77 HGIPIVLIDREVEGL-ELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAG--IPVDEsl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 220 ------TENDAQSAADKLSQYLDRQKALpdvlIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLN 293
Cdd:cd06280 154 ifegdsTIEGGYEAVKALLDLPPRPTAI----FATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVA 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 495597666 294 ENSEEIGRQSAEMLIQLInlEGKGEINTQRKVPAELVIR 332
Cdd:cd06280 230 QPAYEIGRIAAQLLLERI--EGQGEEPRRIVLPTELIIR 266
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
1-336 |
3.55e-33 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 125.49 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 1 MRKATMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITA----HASNyyy 76
Cdd:PRK09526 3 SKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTslalHAPS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 77 lNLMSGIQQILQPSQWTVVLGDIAVNGIYDrAQedRMINRLIESRMAGIISTVTLQPESLTLLAKW--DIPVVFVDSPPr 154
Cdd:PRK09526 80 -QIAAAIKSRADQLGYSVVISMVERSGVEA-CQ--AAVNELLAQRVSGVIINVPLEDADAEKIVADcaDVPCLFLDVSP- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 155 gEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGAT-LGVVETENDAQSAADKLSQ 233
Cdd:PRK09526 155 -QSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQpIAVREGDWSAMSGYQQTLQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 234 YLdRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLinL 313
Cdd:PRK09526 234 ML-REGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLAL--S 310
|
330 340
....*....|....*....|...
gi 495597666 314 EGKGEINTQRkVPAELVIRQSCG 336
Cdd:PRK09526 311 QGQAVKGSQL-LPTSLVVRKSTA 332
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
81-334 |
3.92e-33 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 123.77 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 81 SGIQQILQPSQWTVVlgdIAVNGiYDRAQEDRMINRLIESRMAGIIST-VTLQPESLTLLAKWDIPVVFVDSPPRGEHnF 159
Cdd:cd06273 19 QALQQTLAEAGYTLL---LATSE-YDPARELEQVRALIERGVDGLILVgSDHDPELFELLEQRQVPYVLTWSYDEDSP-H 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 160 PSVTTDNYHASLLVGNHLAQYDYKNWLLLIYP----DRWTTRFErerGIREAAERCGATLG---VVETENDAQSAADKLS 232
Cdd:cd06273 94 PSIGFDNRAAAARAAQHLLDLGHRRIAVISGPtagnDRARARLA---GIRDALAERGLELPeerVVEAPYSIEEGREALR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 233 QYLDRqKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLIN 312
Cdd:cd06273 171 RLLAR-PPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELAARYLLALLE 249
|
250 260
....*....|....*....|..
gi 495597666 313 legKGEINTQRKVPAELVIRQS 334
Cdd:cd06273 250 ---GGPPPKSVELETELIVRES 268
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
71-334 |
5.84e-32 |
|
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: 120.84 E-value: 5.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 71 ASNYYYLNLMSGIQQILQPSQWTVVLGDIAvngiyDRAQEDRMINRLIES-RMAGIISTVTLQPES-LTLLAKWDIPVVF 148
Cdd:cd06292 13 FSDPFFDEFLAALGHAAAARGYDVLLFTAS-----GDEDEIDYYRDLVRSrRVDGFVLASTRHDDPrVRYLHEAGVPFVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 149 VDsPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQ 225
Cdd:cd06292 88 FG-RANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDpglVVEGENTEE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 226 SAADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAE 305
Cdd:cd06292 167 GGYAAAARLLDLGPP-PTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEIGRAVVD 245
|
250 260
....*....|....*....|....*....
gi 495597666 306 MLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06292 246 LLLAAI--EGNPSEPREILLQPELVVRES 272
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
64-334 |
8.39e-32 |
|
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: 119.91 E-value: 8.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTVTLQ-PESLTLLAKW 142
Cdd:cd01575 2 VAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLG----NTGYSPEREEELIRALLSRRPAGLILTGTEHtPATRKLLRAA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DIPVV-FVDSPPRgehnfP---SVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRF-ERERGIREAAERCGATLGV 217
Cdd:cd01575 78 GIPVVeTWDLPDD-----PidmAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRArQRLEGFRDALAEAGLPLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VETENDAQSAADK---LSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNE 294
Cdd:cd01575 153 VLLVELPSSFALGreaLAELLARHPD-LDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRV 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495597666 295 NSEEIGRQSAEMLIQLINleGKGEINTQRKVPAELVIRQS 334
Cdd:cd01575 232 PRYEIGRKAAELLLARLE--GEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-334 |
4.14e-31 |
|
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: 118.10 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAvngiYDRAQEDRMINRLIESRMAGIISTVTLQPESLTLLAKW 142
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSH----WNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DIPVVFVD-SPPRGehNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VV 218
Cdd:cd06290 77 GIPVVLVDrELEGL--NLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDprlIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 219 ETENDAQSAADKLSQYLDRQKALpDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEE 298
Cdd:cd06290 155 EGDFTEESGYEAMKKLLKRGGPF-TAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYE 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 495597666 299 IGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06290 234 MGKTAAEILLELI--EGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
63-334 |
4.53e-31 |
|
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: 118.01 E-value: 4.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHAS-----NYYYLNLMSGIQQILQPSQWTVVLgdiavngIYDRAQEDRminrLIESRMAGIISTVTLQPESLT 137
Cdd:cd01544 1 TIGIIQWYSEeeeleDPYYLSIRLGIEKEAKKLGYEIKT-------IFRDDEDLE----SLLEKVDGIIAIGKFSKEEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 138 LLAKWDIPVVFVDSPPRgEHNFPSVTTDNYHASLLVGNHLAQ-----------YDYKNWLLLIYPDrwttrfERERGIRE 206
Cdd:cd01544 70 KLKKLNPNIVFVDSNPD-PDGFDSVVPDFEQAVRQALDYLIElghrrigfiggKEYTSDDGEEIED------PRLRAFRE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 207 AAERCG--ATLGVVETENDAQSAADKLSQYLDrQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPL 284
Cdd:cd01544 143 YMKEKGlyNEEYIYIGEFSVESGYEAMKELLK-EGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKY 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495597666 285 LNPPLTVLNENSEEIGRQSAEMLIQLINleGKGEINTQRKVPAELVIRQS 334
Cdd:cd01544 222 VTPPLTTVHIPTEEMGRTAVRLLLERIN--GGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
80-330 |
5.93e-31 |
|
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: 117.60 E-value: 5.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 80 MSGIQQILQPSQWTVVLgdiaVNGIYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAKWDIPVVFVdspprGEH- 157
Cdd:cd01542 18 LEGIDEVLKENGYQPLI----ANTNLDEEREIEYLETLARQKVDGIIlFATEITDEHRKALKKLKIPVVVL-----GQEh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 158 -NFPSVTTDNYHASLLVGNHLAQYDYKNWLLL-IYPDRWTTRFERERGIREAAERCGATLG-VVETENDAQSAADKLSQY 234
Cdd:cd01542 89 eGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIgVDEEDIAVGVARKQGYLDALKEHGIDEVeIVETDFSMESGYEAAKEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 235 LDRQKalPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLINle 314
Cdd:cd01542 169 LKENK--PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAELLLDMIE-- 244
|
250
....*....|....*.
gi 495597666 315 gKGEINTQRKVPAELV 330
Cdd:cd01542 245 -GEKVPKKQKLPYELI 259
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-335 |
2.32e-30 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 116.18 E-value: 2.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTV--TLQPESLTLLA 140
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLA----STGNDEERELELLSLFQRRRVDGLILTPgdEDDPELAAALA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 141 KWDIPVVFVDSPPRGEHnfPSVTTDNYHASLLVGNHLAQYDYKNWLLLI-YPDRWTTRfERERGIREAAERCGATLG--V 217
Cdd:cd06281 77 RLDIPVVLIDRDLPGDI--DSVLVDHRSGVRQATEYLLSLGHRRIALLTgGPDIRPGR-ERIAGFKAAFAAAGLPPDpdL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VETEN-DAQSAADKLSQYLdRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENS 296
Cdd:cd06281 154 VRLGSfSADSGFREAMALL-RQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDL 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 495597666 297 EEIGRQSAEMLIQLINLEGKGEINtQRKVPAELVIRQSC 335
Cdd:cd06281 233 DAVGRAAAELLLDRIEGPPAGPPR-RIVVPTELILRDSC 270
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
63-334 |
3.15e-30 |
|
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: 115.82 E-value: 3.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAK 141
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILC----NSDNDPEKQRAYLDMLAEKRVDGLLlMCSEMTDDDAELLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WD-IPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---V 217
Cdd:cd06275 77 LRsIPVVVLDREIAGD-NADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPpswI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VETENDAQSAADKLsQYLDRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSE 297
Cdd:cd06275 156 VEGDFEPEGGYEAM-QRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKD 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 495597666 298 EIGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06275 235 ELGELAVELLLDRI--ENKREEPQSIVLEPELIERES 269
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
64-334 |
1.34e-29 |
|
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: 114.19 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdIAVNgiyDRAQEDRMINRLIESRMAGIIS--TVTLQPES----LT 137
Cdd:cd01541 2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLA-LTNN---DVEKEREILESLLDQNVDGLIIepTKSALPNPnldlYE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 138 LLAKWDIPVVFVDS-PPRGehNFPSVTTDNYHASLLVGNHLAQYDYKNwLLLIYP-DRWTTRfERERGIREAAERCGatL 215
Cdd:cd01541 78 ELQKKGIPVVFINSyYPEL--DAPSVSLDDEKGGYLATKHLIDLGHRR-IAGIFKsDDLQGV-ERYQGFIKALREAG--L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 216 GVVE-------TENDAQS-AADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNP 287
Cdd:cd01541 152 PIDDdrilwysTEDLEDRfFAEELREFLRRLSR-CTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEP 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495597666 288 PLTVLNENSEEIGRQSAEMLIQLINLEGKGEintQRKVPAELVIRQS 334
Cdd:cd01541 231 PLTSVVHPKEELGRKAAELLLRMIEEGRKPE---SVIFPPELIERES 274
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
63-334 |
1.90e-29 |
|
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: 113.83 E-value: 1.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAVngiYDRAQEDRMINRLIESRMAGIISTV--TLQPESLTLLA 140
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDE---DDPASVREALDRLLSQRVDGIIVIApdEAVLEALRRLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 141 KwDIPVVFVDSPPRgeHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLGVVET 220
Cdd:cd01574 78 P-GLPVVIVGSGPS--PGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPPVVE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 221 EN-DAQSAAdKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEI 299
Cdd:cd01574 155 GDwSAASGY-RAGRRLLDDGP-VTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAEL 232
|
250 260 270
....*....|....*....|....*....|....*
gi 495597666 300 GRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd01574 233 GRRAVELLLALI--EGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
79-334 |
2.55e-29 |
|
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: 113.41 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 79 LMSGIQQILQPSQWTVVLGDIAVngiyDRAQEDRMINRLIESRMAGII------STVTLQPEsltllaKWDIPVVFVDSP 152
Cdd:cd06288 18 IIRGAQDAAEEHGYLLLLANTGG----DPELEAEAIRELLSRRVDGIIyasmhhREVTLPPE------LTDIPLVLLNCF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 153 PRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSAAD 229
Cdd:cd06288 88 DDDP-SLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDpslVVHGDWGRESGYE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 230 KLSQYLDrQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQ 309
Cdd:cd06288 167 AAKRLLS-APDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRRAAELLLD 245
|
250 260
....*....|....*....|....*
gi 495597666 310 LInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06288 246 GI--EGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
63-333 |
3.02e-28 |
|
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: 110.69 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVvlgdIAVNGIYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAK 141
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQL----LITSGHHDAEEEREAIEFLLDRRCDAIIlHSRALSDEELILIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WDIPVVFVDspprgeHNFP-----SVTTDNYHASLLVGNHLAQYDYKNwLLLIYPDRWT-TRFERERGIREAAERCGATL 215
Cdd:cd06270 77 KIPPLVVIN------RYIPgladrCVWLDNEQGGRLAAEHLLDLGHRR-IACITGPLDIpDARERLAGYRDALAEAGIPL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 216 G---VVETENDAQSAADKLSQYLDRqKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVL 292
Cdd:cd06270 150 DpslIIEGDFTIEGGYAAAKQLLAR-GLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTV 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 495597666 293 NENSEEIGRQSAEMLIQLINlegKGEINTQRKVPAELVIRQ 333
Cdd:cd06270 229 HYPIEEMAQAAAELALNLAY---GEPLPISHEFTPTLIERD 266
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
64-334 |
8.86e-27 |
|
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: 106.49 E-value: 8.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAvngiYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAKW 142
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTG----SDEEREKKYLQLLKEKRVDGIIfASGTLTEENKQLLKNM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DIPVVFVdSPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNwLLLIYPDRW--TTRFERERGIREAAERCGATLG---V 217
Cdd:cd19975 78 NIPVVLV-STESEDPDIPSVKIDDYQAAYDATNYLIKKGHRK-IAMISGPLDdpNAGYPRYEGYKKALKDAGLPIKenlI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VETENDAQS---AADKLSQyldrQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNE 294
Cdd:cd19975 156 VEGDFSFKSgyqAMKRLLK----NKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 495597666 295 NSEEIGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd19975 232 PFYEMGKKAVELLLDLI--KNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
63-334 |
1.79e-25 |
|
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: 103.10 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLgdiaVNGIYDRAQEDRMINRLIESRMAG-IISTVTLQPESL-TLLA 140
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIIL----CNTYNDFEREKKYIQELKERNVDGiIIASSNISDEAIiKLLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 141 KWDIPVVFVDSPPRgEHNFPSVTTDNYHASLLVGNHLAQYDYKNwLLLIYPDRWTTRF-ERERGIREAAERCGATL--GV 217
Cdd:cd19976 77 EEKIPVVVLDRYIE-DNDSDSVGVDDYRGGYEATKYLIELGHTR-IGCIVGPPSTYNEhERIEGYKNALQDHNLPIdeSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VETENDAQSAADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSE 297
Cdd:cd19976 155 IYSGESSLEGGYKAAEELLKSKN-PTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIF 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 495597666 298 EIGRQSAEMLIQLINLEgkgEINTQRKV-PAELVIRQS 334
Cdd:cd19976 234 EMGQEAAKLLLKIIKNP---AKKKEEIVlPPELIKRDS 268
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
80-326 |
3.03e-25 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 102.36 E-value: 3.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 80 MSGIQQILQPSQWTVVLGDIAvngiYDRAQEDRMINRLIESRMAGIISTVT--LQPESLTLLAKWDIPVVFVDSPPRGEh 157
Cdd:cd06282 18 AQGIQRAARAAGYSLLIATTD----YDPARELDAVETLLEQRVDGLILTVGdaQGSEALELLEEEGVPYVLLFNQTENS- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 158 NFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYP----DRWTTRFErerGIREAAERCG-ATLGVVETENDAQSAADKLS 232
Cdd:cd06282 93 SHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDfsasDRARLRYQ---GYRDALKEAGlKPIPIVEVDFPTNGLEEALT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 233 QYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLIN 312
Cdd:cd06282 170 SLLSGPNP-PTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGRAAADLLLAEIE 248
|
250
....*....|....
gi 495597666 313 LEgkgEINTQRKVP 326
Cdd:cd06282 249 GE---SPPTSIRLP 259
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
64-334 |
1.09e-24 |
|
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: 100.81 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAvngiYDRAQEDRMINRLIESRMAGIIStVTLQP--ESLTLLAK 141
Cdd:cd06296 2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATR----AGRAPVDDWVRRAVARGSAGVVL-VTSDPtsRQLRLLRS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WDIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VV 218
Cdd:cd06296 77 AGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDpdlVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 219 ETENDAQSAADKLSQYLDRQKaLPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEE 298
Cdd:cd06296 157 EGDFTYEAGYRAARELLELPD-PPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLRE 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 495597666 299 IGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06296 236 MGAVAVRLLLRLL--EGGPPDARRIELATELVVRGS 269
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-334 |
1.95e-24 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 100.30 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLgdIAVNgiyDRAQEDRMINRLIESRMAGIIST-VTLQPESLTLLAKW 142
Cdd:cd06278 2 VGVVVGDLSNPFYAELLEELSRALQARGLRPLL--FNVD---DEDDVDDALRQLLQYRVDGVIVTsATLSSELAEECARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DIPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYP-DRWTTRfERERGIREAAERCGATLGVVE-T 220
Cdd:cd06278 77 GIPVVLFNRVVEDP-GVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPeGTSTSR-ERERGFRAALAELGLPPPAVEaG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 221 ENDAQSAADKLSQYLDrQKALPDVLIAGNNPILLGSLKQLQQR-QIAIPEDMALIAYD---EFDWAPLlnpPLTVLNENS 296
Cdd:cd06278 155 DYSYEGGYEAARRLLA-APDRPDAIFCANDLMALGALDAARQEgGLVVPEDISVVGFDdipMAAWPSY---DLTTVRQPI 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 495597666 297 EEIGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd06278 231 EEMAEAAVDLLLERI--ENPETPPERRVLPGELVERGS 266
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
4-334 |
3.68e-24 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 100.95 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 4 ATMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMSGI 83
Cdd:PRK10703 2 ATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 84 QQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTVTLQPE-SLTLLAKW-DIPVVFVDSPPRGEhNFPS 161
Cdd:PRK10703 82 EKNCYQKGYTLILC----NAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEpLLAMLEEYrHIPMVVMDWGEAKA-DFTD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 162 VTTDN-YHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSAADKLSQYLdR 237
Cdd:PRK10703 157 AIIDNaFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPeewIVQGDFEPESGYEAMQQIL-S 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 238 QKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLINLegKG 317
Cdd:PRK10703 236 QKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVN--KR 313
|
330
....*....|....*..
gi 495597666 318 EINTQRKVPAELVIRQS 334
Cdd:PRK10703 314 EEPQTIEVHPRLVERRS 330
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
6-334 |
9.44e-24 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 99.77 E-value: 9.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 6 MRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMSGIQQ 85
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 86 ILQPSQWTVVLgdiaVNGIYDRAQEDRMINRLIESRMAG--IISTVTLQPESLTLLAKWDIPVVFVD-SPPRGEHNfpsV 162
Cdd:PRK10423 81 SCFERGYSLVL----CNTEGDEQRMNRNLETLMQKRVDGllLLCTETHQPSREIMQRYPSVPTVMMDwAPFDGDSD---L 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 163 TTDNyhaSLLVG----NHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATL--GVVETENDAQSAADKLSQYLD 236
Cdd:PRK10423 154 IQDN---SLLGGdlatQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIpdGYEVTGDFEFNGGFDAMQQLL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 237 RQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGrqsaEMLI-QLINLEG 315
Cdd:PRK10423 231 ALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELG----ELAIdVLIHRMA 306
|
330 340
....*....|....*....|
gi 495597666 316 KGEINTQRKV-PAELVIRQS 334
Cdd:PRK10423 307 QPTLQQQRLQlTPELMERGS 326
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
199-335 |
1.30e-23 |
|
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: 95.10 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 199 ERERGIREAAERCGATLGVVETENDAQSAADKLSQYLDRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDE 278
Cdd:pfam13377 26 LRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEVALGVLQALREAGLRVPEDLSVIGFDD 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 495597666 279 FDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLINleGKGEINTQRKVPAELVIRQSC 335
Cdd:pfam13377 106 SPLAALVSPPLTTVRVDAEELGRAAAELLLDLLN--GEPAPPERVLLPPELVEREST 160
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
105-330 |
2.08e-23 |
|
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: 97.28 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 105 YDRAQEDRMINRLIESRMAGIISTVTLQPESLTLLA-KWDIPVVFVDSPPRGEHnFPSVTTDNYHASLLVGNHLAQYDYK 183
Cdd:cd06274 39 DDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCqAAGLPVVFLDRPFSGSD-APSVVSDNRAGARALTEKLLAAGPG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 184 NWLLLIYPDRWTTRFERERGIREAAERCGATLGVVETE---NDAQSAADKLSQYLDRQKALPDVLIAGNNPILLGSLKQL 260
Cdd:cd06274 118 EIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILaegYDRESGYQLMAELLARLGGLPQALFTSSLTLLEGVLRFL 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495597666 261 QQRQIAIPEDMALIAydeFDWAPLLN--P-PLTVLNENSEEIGRQSAEMLIQLINLEGKGEintQRKVPAELV 330
Cdd:cd06274 198 RERLGAIPSDLVLGT---FDDHPLLDflPnPVDSVRQDHDEIAEHAFELLDALIEGQPEPG---VIIIPPELI 264
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
72-334 |
3.85e-23 |
|
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: 96.86 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 72 SNYYYLNLMSGIQQILQPSQWTVVLGDIavnGIYDRAQEDRMINRLIESRMAGIIST--VTLQPESLTLLAKWDIPVVFV 149
Cdd:cd01545 10 SASYVSALQVGALRACREAGYHLVVEPC---DSDDEDLADRLRRFLSRSRPDGVILTppLSDDPALLDALDELGIPYVRI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 150 dSPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQS 226
Cdd:cd01545 87 -APGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDpdlVVQGDFTFES 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 227 ---AADKLsqyLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQS 303
Cdd:cd01545 166 gleAAEAL---LDLPDR-PTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMARRA 241
|
250 260 270
....*....|....*....|....*....|.
gi 495597666 304 AEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd01545 242 VELLIAAI--RGAPAGPERETLPHELVIRES 270
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-332 |
1.89e-22 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 96.32 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 2 RKATMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMS 81
Cdd:PRK10014 5 KKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 82 GIQQILQPSQWTVVLgdiaVNGIYDRAQEDRMINRLIESRMAGII--STVTLQPESLTLLAKWDIPVVFVdSPPRGEHNF 159
Cdd:PRK10014 85 GLTEALEAQGRMVFL----LQGGKDGEQLAQRFSTLLNQGVDGVViaGAAGSSDDLREMAEEKGIPVVFA-SRASYLDDV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 160 PSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRferergireaAERCG---ATL----------GVVETENDAQS 226
Cdd:PRK10014 160 DTVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTR----------AERVGgycATLlkfglpfhseWVLECTSSQKQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 227 AADKLSQYLDRQKALPDVLiAGNNPILLGSLKQLQQ--RQIA-------IPEDMALIAYDEFDWAPLLNPPLTVLNENSE 297
Cdd:PRK10014 230 AAEAITALLRHNPTISAVV-CYNETIAMGAWFGLLRagRQSGesgvdryFEQQVALAAFTDVPEAELDDPPLTWASTPAR 308
|
330 340 350
....*....|....*....|....*....|....*.
gi 495597666 298 EIGRQSAEMLIQLINlegKGEINTQRK-VPAELVIR 332
Cdd:PRK10014 309 EIGRTLADRMMQRIT---HEETHSRNLiIPPRLIAR 341
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
57-334 |
3.60e-22 |
|
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: 94.24 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 57 RRSSRDSVAVITAHA-----SNYYYLNLMSGIQQILQPSQWTVVLGDIAvngiydraQEDRMINRLIESRMA-GII-STV 129
Cdd:cd06295 1 QRSRTIAVVVPMDPHgdqsiTDPFFLELLGGISEALTDRGYDMLLSTQD--------EDANQLARLLDSGRAdGLIvLGQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 130 TLQPESLTLLAKWDIPVVfVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNwLLLIYPDRWTTRFERERGIREA-A 208
Cdd:cd06295 73 GLDHDALRELAQQGLPMV-VWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRR-IAFLGDPPHPEVADRLQGYRDAlA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 209 ERCGA--TLGVVETENDAQSAADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLN 286
Cdd:cd06295 151 EAGLEadPSLLLSCDFTEESGYAAMRALLDSGTA-FDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFR 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 495597666 287 PPLTVLNENSEEIGRQSAEMLIQLINlegkGEINTQRKVPAELVIRQS 334
Cdd:cd06295 230 PPLTTVRQDLALAGRLLVEKLLALIA----GEPVTSSMLPVELVVRES 273
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
63-334 |
1.46e-21 |
|
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: 92.23 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAH---ASNYYYLNLMSGIQQILQPSQWTVVLgdiavNGIYDRAQEDRMINRLI-ESRMAGIISTVTLQPESLTL 138
Cdd:cd19974 1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVL-----EIISDEDEEELNLPSIIsEEKVDGIIILGEISKEYLEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 139 LAKWDIPVVFVDSPPRgEHNFPSVTTDNYHASLLVGNHLAQYDYKNwLLLIYPDRWTTRF-ERERGIREAAERCGATL-- 215
Cdd:cd19974 76 LKELGIPVVLVDHYDE-ELNADSVLSDNYYGAYKLTSYLIEKGHKK-IGFVGDINYTSSFmDRYLGYRKALLEAGLPPek 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 216 --GVVETENDAQSAADKLSQYLDRQkaLPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLN 293
Cdd:cd19974 154 eeWLLEDRDDGYGLTEEIELPLKLM--LPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVE 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 495597666 294 ENSEEIGRQSAEMLIQLInlEGKGEINTQRKVPAELVIRQS 334
Cdd:cd19974 232 VDKEAMGRRAVEQLLWRI--ENPDRPFEKILVSGKLIERDS 270
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
64-330 |
2.18e-21 |
|
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: 91.88 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHAS-----NYYYLNLMSGIQQILQPSQWTVVLgdiaVNGIYDRAQEDRmINRLIESRMA-GIISTVTLQPESLT 137
Cdd:cd06294 2 IGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLL----ATGNTEEELLEE-VKRMVRGRRVdGFILLYSKEDDPLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 138 -LLAKWDIPVVFVDSPPrGEHNFPSVTTDNYHASLLVGNHLAQYDYKNwLLLIYPD-RWTTRFERERGIREAAERCGATL 215
Cdd:cd06294 77 eYLKEEGFPFVVIGKPL-DDNDVLYVDNDNVQAGYEATEYLIDKGHKR-IAFIGGDkNLVVSIDRLQGYKQALKEAGLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 216 ---GVVETENDAQSAADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVL 292
Cdd:cd06294 155 dddYILLLDFSEEDGYDALQELLSKPPP-PTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSV 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 495597666 293 NENSEEIGRQSAEMLIQLInlEGKGEINTQRKVPAELV 330
Cdd:cd06294 234 DINPYELGREAAKLLINLL--EGPESLPKNVIVPHELI 269
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
76-330 |
5.61e-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: 90.69 E-value: 5.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 76 YLNLMSGIQQILQPSQWtvvlgDIAVNGIYDRAQEDRMINRLIESRMAG--IISTVTLQPESLTLLAKWDIP-VVFVDSP 152
Cdd:cd20010 18 FLEFLAGLSEALAERGL-----DLLLAPAPSGEDELATYRRLVERGRVDgfILARTRVNDPRIAYLLERGIPfVVHGRSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 153 PRGEHNFpsVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSAAD 229
Cdd:cd20010 93 SGAPYAW--VDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDpalVREGPLTEEGGYQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 230 KLSQYLdRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYD-EFDWAPLLNPPLTVLNENSEEIGRQSAEMLI 308
Cdd:cd20010 171 AARRLL-ALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDdLLPALEYFSPPLTTTRSSLRDAGRRLAEMLL 249
|
250 260
....*....|....*....|..
gi 495597666 309 QLInlEGKGEINTQRKVPAELV 330
Cdd:cd20010 250 ALI--DGEPAAELQELWPPELI 269
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
104-334 |
1.39e-20 |
|
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: 89.61 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 104 IYDRAQEDRMINRLIESRMAGIISTVT-LQPESLTLLAKWDIPVVFVDSPPRgEHNFPSVTTDNYHASLLVGNHLAQYDY 182
Cdd:cd06277 44 VDIGDDFDEILKELTDDQSSGIILLGTeLEEKQIKLFQDVSIPVVVVDNYFE-DLNFDCVVIDNEDGAYEAVKYLVELGH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 183 KNwLLLIYPDRWTTRF-ERERGIREAAERcgatLGVVETENDA-------QSAADKLSQYLDRQKALPDVLIAGNNPILL 254
Cdd:cd06277 123 TR-IGYLASSYRIKNFeERRRGFRKAMRE----LGLSEDPEPEfvvsvgpEGAYKDMKALLDTGPKLPTAFFAENDIIAL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 255 GSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLINLEGKGeiNTQRKVPAELVIRQS 334
Cdd:cd06277 198 GCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPDGG--TLKILVSTKLVERGS 275
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
4-73 |
1.14e-19 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 81.48 E-value: 1.14e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 4 ATMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASN 73
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
28-334 |
1.20e-19 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 87.75 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 28 DGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAvngiYDR 107
Cdd:PRK11041 2 EKVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCA----HQN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 108 AQEDRMINRLIESRMAGIISTVTLQPESLTLLAKWDIP--VVFVDSPPrgEHNFPSVTTDNYHASLLVGNHLAQYDYKNW 185
Cdd:PRK11041 78 QQEKTFVNLIITKQIDGMLLLGSRLPFDASKEEQRNLPpmVMANEFAP--ELELPTVHIDNLTAAFEAVNYLHELGHKRI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 186 LLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSAADKLSQYLDRQKAlPDVLIAGNNPILLGSLKQLQQ 262
Cdd:PRK11041 156 ACIAGPEEMPLCHYRLQGYVQALRRCGITVDpqyIARGDFTFEAGAKALKQLLDLPQP-PTAVFCHSDVMALGALSQAKR 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495597666 263 RQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSaeMLIQLINLEGKGEINTQRKVPAELVIRQS 334
Cdd:PRK11041 235 MGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREA--MLLLLEQLQGHHVSSGSRLLDCELIIRGS 304
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
63-334 |
3.02e-19 |
|
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: 86.11 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHA-----SNYYYLNLMSGIQQILQPSQWTVVLgdiaVNGIYDRAQEDRMINRLIEsrmAGIISTVTLQPESLT 137
Cdd:cd06279 1 AIGVLLPDDlsyafSDPVAAQFLRGVAEVCEEEGLGLLL----LPATDEGSAAAAVRNAAVD---GFIVYGLSDDDPAVA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 138 LLAKWDIPVVFVDSPPRGehNFPSVTTDNYHASLLVGNHLAQY------------DYKNWLLLIYPDR-WTTRF----ER 200
Cdd:cd06279 74 ALRRRGLPLVVVDGPAPP--GIPSVGIDDRAAARAAARHLLDLghrriailslrlDRGRERGPVSAERlAAATNsvarER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 201 ERGIREAAERCGATLG---VVE----TENDAQSAADKLsqyLDRQkALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMAL 273
Cdd:cd06279 152 LAGYRDALEEAGLDLDdvpVVEapgnTEEAGRAAARAL---LALD-PRPTAILCMSDVLALGALRAARERGLRVPEDLSV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495597666 274 IAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLINlegkGEINTQRKVPAELVIRQS 334
Cdd:cd06279 228 TGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLP----GAPPRPVILPTELVVRAS 284
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
78-333 |
2.77e-18 |
|
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: 83.19 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 78 NLMSGIQQILQPSQWTVVLgDIAVNGIYDRAQEDRMINRLiesRMAGIISTVTLQPESLTL-LAKWDIPVVFVDSPPRGe 156
Cdd:cd06272 17 RLLSGINEAISKQGYNINL-SICPYKVGHLCTAKGLFSEN---RFDGVIVFGISDSDIEYLnKNKPKIPIVLYNRESPK- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 157 hnFPSVTTDNYHASLLVGNHLAQYDYKN--WLLLIYPDRWTTrfERERGIREAAERCGATLG---VVETENDAQSAADKL 231
Cdd:cd06272 92 --YSTVNVDNEKAGRLAVLLLIQKGHKSiaYIGNPNSNRNQT--LRGKGFIETCEKHGIHLSdsiIDSRGLSIEGGDNAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 232 SQYLDRqKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLI 311
Cdd:cd06272 168 KKLLKK-KTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLI 246
|
250 260
....*....|....*....|..
gi 495597666 312 nlEGKGEINTQRKVPAELVIRQ 333
Cdd:cd06272 247 --EGRENEIQQLILYPELIFRE 266
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
62-332 |
9.25e-18 |
|
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: 82.17 E-value: 9.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 62 DSVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLgdIAVNgiYDRAQEDRMINRLIESRMAG-IISTVTLQPESLTLLA 140
Cdd:pfam00532 2 LKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFL--LAVG--DGEDTLTNAIDLLLASGADGiIITTPAPSGDDITAKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 141 K-WDIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIY-PDRWTTRFERERGIREAAERCGATLG-- 216
Cdd:pfam00532 78 EgYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRPIAVMAgPASALTARERVQGFMAALAAAGREVKiy 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 217 -VVETENDAQSAADKLSQYLdRQKALPDVLIAGNNPILLGSLKQLQQR-QIAIPEDM-----ALIAYDEFDWAP---LLN 286
Cdd:pfam00532 158 hVATGDNDIPDAALAANAML-VSHPTIDAIVAMNDEAAMGAVRALLKQgRVKIPDIVgiginSVVGFDGLSKAQdtgLYL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495597666 287 PPLTVLNENSEEIGRQSAEMLIQLINLEGKGEINTQrkVPAELVIR 332
Cdd:pfam00532 237 SPLTVIQLPRQLLGIKASDMVYQWIPKFREHPRVLL--IPRDFFKE 280
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
63-334 |
2.24e-17 |
|
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: 80.80 E-value: 2.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGII-STVTLQPESLTLLAK 141
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILS----NSDNNVDKELDLLNTMLSKQVDGIIfMGDELTEEIREEFKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 WDIPVVFVDSPpRGEHNFPSVTTDNYHASLLVGNHLAQYDYKN-WLLLIYPDRWTTRFERERGIREAAERCGATLG---V 217
Cdd:cd06298 77 SPVPVVLAGTV-DSDHEIPSVNIDYEQAAYDATKSLIDKGHKKiAFVSGPLKEYINNDKKLQGYKRALEEAGLEFNeplI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VETENDAQSAADKLSQYLDRQKalPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSE 297
Cdd:cd06298 156 FEGDYDYDSGYELYEELLESGE--PDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLY 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 495597666 298 EIGRQSAEMLIQLINLEGKgeINTQRKVPAELVIRQS 334
Cdd:cd06298 234 DIGAVAMRLLTKLMNKEEV--EETIVKLPHSIIWRQS 268
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
7-58 |
2.41e-17 |
|
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: 74.75 E-value: 2.41e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 495597666 7 RDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRR 58
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
75-334 |
8.96e-17 |
|
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: 79.05 E-value: 8.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 75 YYLNLMSGIQQILQPSQWtvvlgDIAVNGIYDRAQEDR-MINRLIESRMAGIISTVTLQPESLT-LLAKWDIPVVFVDSp 152
Cdd:cd06297 13 FYMRLLTGVERALDENRY-----DLAIFPLLSEYRLEKyLRNSTLAYQCDGLVMASLDLTELFEeVIVPTEKPVVLIDA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 153 prGEHNFPSVTTDNYHASLLVGNHLAQYdYKNWLLLIYPD---RWTTRFERER--GIREA---AERCGATLGVVETENDA 224
Cdd:cd06297 87 --NSMGYDCVYVDNVKGGFMATEYLAGL-GEREYVFFGIEedtVFTETVFREReqGFLEAlnkAGRPISSSRMFRIDNSS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 225 QSAADKLSQYLDRQKaLPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPllNPPLTVLNENSEEIGRQSA 304
Cdd:cd06297 164 KKAECLARELLKKAD-NPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQPVEEMGEAAA 240
|
250 260 270
....*....|....*....|....*....|
gi 495597666 305 EMLIQLINleGKGEINTQRKVPAELVIRQS 334
Cdd:cd06297 241 KLLLKRLN--EYGGPPRSLKFEPELIVRES 268
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
5-290 |
6.83e-16 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 77.51 E-value: 6.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 5 TMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMSGIQ 84
Cdd:PRK10401 3 TIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 85 QILQPSQWTVVLGDiavngIYDRAQEDR-MINRLIESRM-AGIISTVTLQPESLTLLAKwDIP--VVFVDSPPRGEHNfp 160
Cdd:PRK10401 83 LVAQQHQKYVLIGN-----SYHEAEKERhAIEVLIRQRCnALIVHSKALSDDELAQFMD-QIPgmVLINRVVPGYAHR-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 161 SVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSAADKLSQYLDR 237
Cdd:PRK10401 155 CVCLDNVSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPeswIGTGTPDMQGGEAAMVELLGR 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 495597666 238 QKALPDVLiAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLT 290
Cdd:PRK10401 235 NLQLTAVF-AYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLT 286
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
4-312 |
1.07e-15 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 77.10 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 4 ATMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMSGI 83
Cdd:PRK10727 2 ATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 84 QQILQPSQWTVVLGdiavNGIYDRAQEDRMINRLIESRMAGIISTVTLQP-ESLTLLAKwDIP--VVFVDSPPRGEHNfp 160
Cdd:PRK10727 82 EQVAYHTGNFLLIG----NGYHNEQKERQAIEQLIRHRCAALVVHAKMIPdAELASLMK-QIPgmVLINRILPGFENR-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 161 SVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLG---VVETENDAQSAADKLSQYLDR 237
Cdd:PRK10727 155 CIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANdrlVTFGEPDESGGEQAMTELLGR 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495597666 238 QKALPDVlIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLIN 312
Cdd:PRK10727 235 GRNFTAV-ACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALAD 308
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
52-330 |
4.56e-15 |
|
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: 74.58 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 52 AAQALRRSSRDSVAVITAHASNYYYLNLMSGIQQILQPSQWTVvlgdIAVNGIYDRAQEDRMINRLIESRMAGIIST--- 128
Cdd:COG1879 24 AEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVEL----IVVDAEGDAAKQISQIEDLIAQGVDAIIVSpvd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 129 VTLQPESLTLLAKWDIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQY--DYKNWLLLIYPDRWTTRFERERGIRE 206
Cdd:COG1879 100 PDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 207 AAERCGAT--LGVVETENDAQSAADKLSQYLDRQKALpDVLIAGNNPILLGSLKQLQQ----RQIAI------PEDMALI 274
Cdd:COG1879 180 ALKEYPGIkvVAEQYADWDREKALEVMEDLLQAHPDI-DGIFAANDGMALGAAQALKAagrkGDVKVvgfdgsPEALQAI 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 495597666 275 AYDEFDWAPLLNPpltvlnensEEIGRQSAEMLIQLINleGKgEINTQRKVPAELV 330
Cdd:COG1879 259 KDGTIDATVAQDP---------YLQGYLAVDAALKLLK--GK-EVPKEILTPPVLV 302
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
64-332 |
9.83e-15 |
|
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: 72.96 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLgdIAVNgiYDRAQEDRMINRLIESRMAGIIST-VTLQPESLTLLAKW 142
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLL--LQTN--YDKEKELRALELLKTKQIDGLIITsRENDWEVIEPYAKY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 DiPVVFVDSPprGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLI---YPDRWTTRfERERGIREAAERCGATL---- 215
Cdd:cd06286 78 G-PIVLCEET--DSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLgrpESSSASTQ-ARLKAYQDVLGEHGLSLreew 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 216 --GVVETENDAQSAADKLSQyldrQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNppLTVLN 293
Cdd:cd06286 154 ifTNCHTIEDGYKLAKKLLA----LKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELLN--LTTID 227
|
250 260 270
....*....|....*....|....*....|....*....
gi 495597666 294 ENSEEIGRQSAEMLIQLINLEGkgeiNTQRKVPAELVIR 332
Cdd:cd06286 228 QPLEEMGKEAFELLLSQLESKE----PTKKELPSKLIER 262
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
2-314 |
1.34e-14 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 73.52 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 2 RKATMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMS 81
Cdd:PRK14987 4 KRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 82 GIQQILQPSQWTVVLGDIAvngiYDRAQEDRMINRLIESRMAGIISTV-TLQPESLTLLAKWDIPVV-FVDSppRGEHNF 159
Cdd:PRK14987 84 GIESVTDAHGYQTMLAHYG----YKPEMEQERLESMLSWNIDGLILTErTHTPRTLKMIEVAGIPVVeLMDS--QSPCLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 160 PSVTTDNYHASLLVGNHLAQYDYKNWLLLiyPDRWTTR-FERERGIREAAERCGAT-LGVVETENDAQSAADKLSQYLDR 237
Cdd:PRK14987 158 IAVGFDNFEAARQMTTAIIARGHRHIAYL--GARLDERtIIKQKGYEQAMLDAGLVpYSVMVEQSSSYSSGIELIRQARR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495597666 238 QKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQLINLE 314
Cdd:PRK14987 236 EYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGE 312
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
63-329 |
2.27e-14 |
|
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: 71.89 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQPSQWTVVLGDIAVNGIYDRAQedrmINRLIESRMAGIISTVTLQPES-LTLLAK 141
Cdd:cd01537 1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQ----IDVLLAKRVKGLAINLVDPAAAgVAEKAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 142 W-DIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGAT---LGV 217
Cdd:cd01537 77 GqNVPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKteqLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VETENDAQSAADKLSQYLDrQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSE 297
Cdd:cd01537 157 DTGDWDTASGKDKMDQWLS-GPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDAN 235
|
250 260 270
....*....|....*....|....*....|..
gi 495597666 298 EIGRQSAEMLIQLInlEGKGEINTQRKVPAEL 329
Cdd:cd01537 236 NLGKTTFDLLLNLA--DNWKIDNKVVRVPYVL 265
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
63-330 |
4.04e-14 |
|
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380664 [Multi-domain] Cd Length: 266 Bit Score: 71.42 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVI--TAHASNYYYLNLMSGIQQILQPSQWTVVLgdiavngIYDRAQEDRM--INRLIESRMA-GIISTVTlQPEslt 137
Cdd:cd20009 1 VIALVlpTEDEIDGFTSQLISGISEALRGTPYHLVV-------TPEFPGDDPLepVRYIVENRLAdGIIISHT-EPQ--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 138 llakwDIPVVFVDspprgEHNFPSVT--------------TDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERG 203
Cdd:cd20009 70 -----DPRVRYLL-----ERGFPFVThgrtelstphayfdFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 204 IREAAERCGAT---LGVVETENDAQSAADKLSQYLdRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFD 280
Cdd:cd20009 140 FRRALAEAGLEvepLLIVTLDSSAEAIRAAARRLL-RQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSP 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 495597666 281 WAPLLNPPLTVLNENSEEIGRQSAEMLIQLInlEGKGEINTQRKVPAELV 330
Cdd:cd20009 219 ILDYFRPPIDTLYEDIEEAGRFLAEALLRRI--EGEPAEPLQTLERPELI 266
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
4-332 |
2.89e-13 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 69.40 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 4 ATMRDVSEATGFSMFTVSRALNGGD--GVADDSRELILKVARELGY--VPNRAAQALRRSSRDSVAVIT----AHASNYY 75
Cdd:PRK10339 2 ATLKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYktSSARKLQTGAVNQHHILAIYSyqqeLEINDPY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 76 YLNLMSGIQQilQPSQWtvvlgDIAVNGIYDRAQEDRMinrlieSRMAGIISTVTLQPESLTLLAKWDIPVVFVDSPPRG 155
Cdd:PRK10339 82 YLAIRHGIET--QCEKL-----GIELTNCYEHSGLPDI------KNVTGILIVGKPTPALRAAASALTDNICFIDFHEPG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 156 EhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERErgirEAAERCGATLGVVEtEND------AQSAAD 229
Cdd:PRK10339 149 S-GYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIRE----VAFAEYGRLKQVVR-EEDiwrggfSSSSGY 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 230 KLSQYLDRQKALPDVLIAGNNPILLGSLKQLQQRQIAIPEDMALIAYDEFDWAPLLNPPLTVLNENSEEIGRQSAEMLIQ 309
Cdd:PRK10339 223 ELAKQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYE 302
|
330 340
....*....|....*....|...
gi 495597666 310 LINlEGKgEINTQRKVPAELVIR 332
Cdd:PRK10339 303 KAR-DGR-ALPLLVFVPSKLKLR 323
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
124-334 |
4.10e-12 |
|
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: 65.30 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 124 GIISTVTLqPESLTLLAKWDIPVVFVDSPPRgEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRfERERG 203
Cdd:cd01543 53 GIIARLDD-PELAEALRRLGIPVVNVSGSRP-EPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAWSR-ERGEG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 204 IREAAERCGATLGVVE-----TENDAQSAADKLSQYLdrqKALP--------------DVLIAgnnpillgslkqLQQRQ 264
Cdd:cd01543 130 FREALREAGYECHVYEsppsgSSRSWEEEREELADWL---KSLPkpvgifacnddrarQVLEA------------CREAG 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495597666 265 IAIPEDMALIA--YDEFdWAPLLNPPLTVLNENSEEIGRQSAEMLIQLINlegkGEINTQRKV---PAELVIRQS 334
Cdd:cd01543 195 IRVPEEVAVLGvdNDEL-ICELSSPPLSSIALDAEQIGYEAAELLDRLMR----GERVPPEPIlipPLGVVTRQS 264
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
5-50 |
5.18e-12 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 59.96 E-value: 5.18e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 495597666 5 TMRDVSEATGFSMFTVSRALNGGDGVADDSRELILKVARELGYVPN 50
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
64-329 |
8.17e-10 |
|
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: 58.73 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVLgdiaVNGIYDRAQEDRMINRLIESRMAGIIsTVTLQPESLT-LLAKW 142
Cdd:cd01536 2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVV----LDAQGDVAKQISQIEDLIAQGVDAII-IAPVDSEALVpAVKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 ---DIPVVFVDSPPRGEHNFPS-VTTDNYHASLLVGNHLAQY--DYKNWLLLIYPDRWTTRFERERGIREAAERCGAT-- 214
Cdd:cd01536 77 naaGIPVVAVDTDIDGGGDVVAfVGTDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKEALKKYPDIei 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 215 LGVVETENDAQSAADKLSQYLDRQKALpDVLIAGNNPILLGSLKQLQQR----QIAI------PEDMALIAYDEFDwapl 284
Cdd:cd01536 157 VAEQPANWDRAKALTVTENLLQANPDI-DAVFAANDDMALGAAEALKAAgrtgDIKIvgvdgtPEALKAIKDGELD---- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 495597666 285 lnppLTVLNeNSEEIGRQSAEMLIQLINlegKGEINTQRKVPAEL 329
Cdd:cd01536 232 ----ATVAQ-DPYLQGYLAVEAAVKLLN---GEKVPKEILTPVTL 268
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
117-315 |
1.38e-09 |
|
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: 57.82 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 117 LIESRMAG--IISTVTLQPESLTLLAKWDIPVVFVDSPPRGEhNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRW 194
Cdd:cd06271 52 LVETGSADgvILSEIEPNDPRVQFLTKQNFPFVAHGRSD*PI-GHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 195 TTRFERERGIREAAERCGAT---LGVVETENDAQSAADKLSQYLDRqkalPDVLIAGNNPILLGSLKQLQQRQIAIPEDM 271
Cdd:cd06271 131 SPHDRRLQGYVRA*RDAGLTgypLDADTTLEAGRAAAQRLLALSPR----PTAIVTMNDSATIGLVAGLQAAGLKIGEDV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 495597666 272 ALIAYDEfdwAPLLN----PPLTVLNENSEEIGRQSAEMLIQLINLEG 315
Cdd:cd06271 207 SIIGKDS---APFLGamitPPLTTVHAPIAEAGRELAKALLARIDGED 251
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
106-285 |
1.45e-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: 58.01 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 106 DRAQEDRMINRLIESRMAGII----STVTLQPESLTLLAKwDIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQ-- 179
Cdd:cd20004 42 DVEAQIQIIEYFIDQGVDGIVlaplDRKALVAPVERARAQ-GIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKll 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 180 YDYKNWLLLIY-PDRWTTRfERERGIREAAERCGATLGVVE------TENDAQSAADK-LSQYLDrqkalPDVLIAGNNP 251
Cdd:cd20004 121 NGKGKVALLRLaKGSASTT-DRERGFLEALKKLAPGLKVVDdqyaggTVGEARSSAENlLNQYPD-----VDGIFTPNES 194
|
170 180 190
....*....|....*....|....*....|....
gi 495597666 252 ILLGSLKQLqqRQIAIPEDMALIAydeFDWAPLL 285
Cdd:cd20004 195 TTIGALRAL--RRLGLAGKVKFIG---FDASDLL 223
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
64-316 |
2.09e-08 |
|
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: 54.24 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 64 VAVITAHASNYYYLNLMSGIQQILQPSQWTVVlgdIAVNGIYDRAQEDRMINRLIESRMAGIIsTVTLQPESLT-LLAKW 142
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVI---VVGPAEADAAEQVAQIEDAIAQGVDAII-VAPVDPTALApVLKKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 143 ---DIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQY--DYKNWLLLIYPDRWTTRFERERGIREAAERCGATLGV 217
Cdd:pfam13407 77 kdaGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 218 VE----TENDAQSAADKLSQYLDRQKALPDVLIAGNNPILLGSLKQLQQRQIAipEDMALIAYDEFDWA-PLLNPPL--- 289
Cdd:pfam13407 157 VAevegTNWDPEKAQQQMEALLTAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEAlEAIKDGTida 234
|
250 260
....*....|....*....|....*..
gi 495597666 290 TVLNeNSEEIGRQSAEMLIQLinLEGK 316
Cdd:pfam13407 235 TVLQ-DPYGQGYAAVELAAAL--LKGK 258
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
72-333 |
1.09e-07 |
|
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: 52.36 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 72 SNYYYLNLMSGIQQILQPSQWTVVLGDiAVNgiyDRAQEDRMINRLIESRMAGIISTVTlQPES----LTLLAKWDIPVV 147
Cdd:cd06319 10 DNPFWQIMERGVQAAAEELGYEFVTYD-QKN---SANEQVTNANDLIAQGVDGIIISPT-NSSAaptvLDLANEAKIPVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 148 FVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQY-DYKNW------LLLIYPDRwTTRFERERGIREAAERCGATLGVVE- 219
Cdd:cd06319 85 IADIGTGGGDYVSYIISDNYDGGYQAGEYLAEAlKENGWgggsvgIIAIPQSR-VNGQARTAGFEDALEEAGVEEVALRq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 220 TENDAQSAADKLSQylDRQKALPDV--LIAGNNPILLGSLKQLQQ----RQI------AIPEDMALIAYDEFDWAPLLNP 287
Cdd:cd06319 164 TPNSTVEETYSAAQ--DLLAANPDIkgIFAQNDQMAQGALQAIEEagrtGDIlvvgfdGDPEALDLIKDGKLDGTVAQQP 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 495597666 288 PLtvlnenseeIGRQSAEMLIQLINleGKGEINTQRKVPAELVIRQ 333
Cdd:cd06319 242 FG---------MGARAVELAIQALN--GDNTVEKEIYLPVLLVTSE 276
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
139-334 |
1.41e-07 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 52.04 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 139 LAKWDIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQYDYKNWLLLIYPDRWTTRFERERGIREAAERCGATLGVV 218
Cdd:cd06287 75 LRQRGVPVVSIGRAPGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRFAQEYGTTPVVY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 219 ET-----ENDAQSAADKLsqyldrQKALPDV--LIAGNNPILLGSLKQLQQRQIAIPEDMALIA-YDEFDwAPLLNPPLT 290
Cdd:cd06287 155 KVpesegERAGYEAAAAL------LAAHPDIdaVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTrYDGIR-ARTADPPLT 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495597666 291 VLNENSEEIGRQSAEMLIQLINlegkGEINTQRKVPA-ELVIRQS 334
Cdd:cd06287 228 AVDLHLDRVARTAIDLLFASLS----GEERSVEVGPApELVVRAS 268
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
14-273 |
2.81e-07 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 51.42 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 14 GFSMFTVSRALNGGDG---VADDSRELILKVARELGYVPNRAAQALRRSSRDSVAVITAHASNYYYLNLMSGIQQILQPS 90
Cdd:PRK11303 11 GVSRTTASYVINGKAKqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAKYLERQARQR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 91 QWTVVLG---DiavngiyDRAQEDRMINRLIESRMAGIISTVTLQPES---LTLLAKwDIPVVFVDSPPRGEHnFPSVTT 164
Cdd:PRK11303 91 GYQLLIAcsdD-------QPDNEMRCAEHLLQRQVDALIVSTSLPPEHpfyQRLQND-GLPIIALDRALDREH-FTSVVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 165 DNYHASLLVGNHLAQYDYKNWLLL-IYPDrWTTRFERERGIREAAERCGATLGVVETENDAQSAADKL-SQYLDRQkALP 242
Cdd:PRK11303 162 DDQDDAEMLAESLLKFPAESILLLgALPE-LSVSFEREQGFRQALKDDPREVHYLYANSFEREAGAQLfEKWLETH-PMP 239
|
250 260 270
....*....|....*....|....*....|.
gi 495597666 243 DVLIAGNNPILLGSLKQLQQRQIAIPEDMAL 273
Cdd:PRK11303 240 DALFTTSYTLLQGVLDVLLERPGELPSDLAI 270
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
63-278 |
1.17e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 46.18 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 63 SVAVITAHASNYYYLNLMSGIQQILQpsqwtvvlgDIAVNGI--YDRAQEDR-----MINRLIESRMAGII-----STVT 130
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAK---------DLGVKIIfvGPESEEDVagqnsLLEELINKKPDAIVvapldSEDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 131 LQPesLTLLAKWDIPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQY---DYKNWLLLIYPDRWTTRfERERGIREA 207
Cdd:cd06310 72 VDP--LKDAKDKGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEAlggKGKVAVLSLTAGNSTTD-QREEGFKEY 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495597666 208 AERCGATLGVVETE---NDAQSAADKLSQYLDRQKALpDVLIAGNNPILLGSLKQLQQRQIAipEDMALIAYDE 278
Cdd:cd06310 149 LKKHPGGIKVLASQyagSDYAKAANETEDLLGKYPDI-DGIFATNEITALGAAVAIKSRKLS--GQIKIVGFDS 219
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
144-277 |
2.41e-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: 380661 [Multi-domain] Cd Length: 274 Bit Score: 45.28 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 144 IPVVFVDSPPRGEHNFPSVTTDNYHASLLVGNHLAQY-DYKNWLLLIYPDRWT-TRFERERGIREAAERCGATLgVVETE 221
Cdd:cd20006 85 IPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLlGEKGKVAIVSFVKGSsTAIEREEGFKQALAEYPNIK-IVETE 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495597666 222 ---NDAQSAADK----LSQYLDrqkalPDVLIAGNNPILLGSLKQLQQRqiAIPEDMALIAYD 277
Cdd:cd20006 164 ycdSDEEKAYEItkelLSKYPD-----INGIVALNEQSTLGAARALKEL--GLGGKVKVVGFD 219
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
194-319 |
5.30e-03 |
|
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: 38.05 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495597666 194 WTTRFERerGIREAAERCGATLGVVETENDAQSAADKLSQYLDRQkalPDVLIagnnpILLGSLKQLQQR-QIAIPEDMA 272
Cdd:cd06305 13 WDQQALQ--GAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQK---VDAII-----ISHGDADALDPKlKKALDAGIP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 495597666 273 LIAYDefdwAPLLNPPLTVLNENSEEIGRQSAEMLIQliNLEGKGEI 319
Cdd:cd06305 83 VVTFD----TDSQVPGVNNITQDDYALGTLSLGQLVK--DLNGEGNI 123
|
|
| |
