|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
3-339 |
1.10e-136 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 391.48 E-value: 1.10e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 3 NTPVTIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSAML 82
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 83 NSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKNIPLVLFDRYAESIDVSKV 162
Cdd:COG1609 81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDD--ARLERLAEAGIPVVLIDRPLPDPGVPSV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 163 IVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALMSLPQ 242
Cdd:COG1609 159 GVDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 243 PPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLRELNATDTniPK 322
Cdd:COG1609 239 RPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDA--PP 316
|
330
....*....|....*..
gi 1702117912 323 ETKVMETQLIVRASSMR 339
Cdd:COG1609 317 ERVLLPPELVVRESTAP 333
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
65-332 |
1.70e-105 |
|
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: 309.83 E-value: 1.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06267 79 IPVVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06267 159 FSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRA 238
|
250 260
....*....|....*....|....*...
gi 1702117912 305 TVRLLLRELNatDTNIPKETKVMETQLI 332
Cdd:cd06267 239 AAELLLERIE--GEEEPPRRIVLPTELV 264
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
65-332 |
1.90e-84 |
|
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: 256.30 E-value: 1.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYehVERLVRKN 144
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDL--IEKLVKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd19977 79 IPVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIKHVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YtQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd19977 159 R-QDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRK 237
|
250 260
....*....|....*....|....*...
gi 1702117912 305 TVRLLLRELNAtDTNIPKETKVMETQLI 332
Cdd:cd19977 238 AAELLLDRIEN-KPKGPPRQIVLPTELI 264
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
65-336 |
5.46e-80 |
|
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: 244.76 E-value: 5.46e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGfIISLsrDTDNYEHVERLVRKN 144
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDG-VILL--SGRLDAELLSELSKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06284 78 YPIVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06284 158 FSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGET 237
|
250 260 270
....*....|....*....|....*....|..
gi 1702117912 305 TVRLLLRELNatDTNIPKETKVMETQLIVRAS 336
Cdd:cd06284 238 AAELLLEKIE--GEGVPPEHIILPHELIVRES 267
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
65-336 |
1.35e-76 |
|
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: 236.26 E-value: 1.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGfIISLSRDTDnyehVERLVRKN 144
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDG-IILGSHSLD----IEEYKKLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRY-AESIDVskVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHC 223
Cdd:cd06291 76 IPIVSIDRYlSEGIPS--VSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06291 154 DFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAK 233
|
250 260 270
....*....|....*....|....*....|...
gi 1702117912 304 ETVRLLLRELNatDTNIPKETKVMETQLIVRAS 336
Cdd:cd06291 234 EAVELLLKLIE--GEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-337 |
4.74e-76 |
|
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: 234.81 E-value: 4.74e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDA--PDLQELAARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06285 79 VPVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06285 159 FTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRR 238
|
250 260 270
....*....|....*....|....*....|...
gi 1702117912 305 TVRLLLRELNATDTniPKETKVMETQLIVRASS 337
Cdd:cd06285 239 AAELLLQLIEGGGR--PPRSITLPPELVVREST 269
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
65-337 |
1.70e-75 |
|
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: 233.70 E-value: 1.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSY----HYFSAMLNSIEEAALQAGYSVLVCqTNESYLRETTNIQNLLRS-QVEGFIISLSRDTDnyEHVER 139
Cdd:cd06292 1 LIGYVVPELPGgfsdPFFDEFLAALGHAAAARGYDVLLF-TASGDEDEIDYYRDLVRSrRVDGFVLASTRHDD--PRVRY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 140 LVRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQY 219
Cdd:cd06292 78 LHEAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 220 VFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQ 299
Cdd:cd06292 158 VVEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPID 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 1702117912 300 EMGTETVRLLLRELNatDTNIPKETKVMETQLIVRASS 337
Cdd:cd06292 238 EIGRAVVDLLLAAIE--GNPSEPREILLQPELVVRESS 273
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
65-336 |
1.07e-72 |
|
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: 226.39 E-value: 1.07e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSrdTDNYEHVERLVRKN 144
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPT--GENSEGLQALIAQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRY-AESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHC 223
Cdd:cd06299 79 LPVVFVDREvEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06299 159 DFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGR 238
|
250 260 270
....*....|....*....|....*....|...
gi 1702117912 304 ETVRLLLRELNATDTniPKETKVmETQLIVRAS 336
Cdd:cd06299 239 RAVELLLALIENGGR--ATSIRV-PTELIPRES 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
65-334 |
2.87e-72 |
|
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: 225.22 E-value: 2.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPS--RELKRLLKHG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06280 79 IPIVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06280 159 STIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRI 238
|
250 260 270
....*....|....*....|....*....|
gi 1702117912 305 TVRLLLRELNATDTNipKETKVMETQLIVR 334
Cdd:cd06280 239 AAQLLLERIEGQGEE--PRRIVLPTELIIR 266
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
65-336 |
4.85e-72 |
|
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: 224.44 E-value: 4.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNyEHVERLVRKN 144
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDE-AIIKLLKEEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd19976 80 IPVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLpQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd19976 160 SSLEGGYKAAEELLKS-KNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
|
250 260 270
....*....|....*....|....*....|..
gi 1702117912 305 TVRLLLRELNatDTNIPKETKVMETQLIVRAS 336
Cdd:cd19976 239 AAKLLLKIIK--NPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
65-336 |
5.57e-71 |
|
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: 222.04 E-value: 5.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSY-HYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISlSRDTDNYEHVERLvrK 143
Cdd:cd06288 1 TIGLITDDIATtPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYA-SMHHREVTLPPEL--T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHC 223
Cdd:cd06288 78 DIPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06288 158 DWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGR 237
|
250 260 270
....*....|....*....|....*....|...
gi 1702117912 304 ETVRLLLRELNatDTNIPKETKVMETQLIVRAS 336
Cdd:cd06288 238 RAAELLLDGIE--GEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
65-335 |
3.14e-69 |
|
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: 217.43 E-value: 3.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNyEHVERLVRKN 144
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTA-ELLRRLKAWG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06289 80 IPVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06289 160 ATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRR 239
|
250 260 270
....*....|....*....|....*....|.
gi 1702117912 305 TVRLLLRELNATDTniPKETKVMETQLIVRA 335
Cdd:cd06289 240 AARLLLRRIEGPDT--PPERIIIEPRLVVRE 268
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
65-336 |
6.36e-67 |
|
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: 211.29 E-value: 6.36e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRE-TTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRK 143
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPASvREALDRLLSQRVDGIIVIAPDEAV--LEALRRLPP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRyAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEqyVFHC 223
Cdd:cd01574 79 GLPVVIVGS-GPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPP--VVEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQEN--TIMQTLALMslpQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEM 301
Cdd:cd01574 156 DWSAASgyRAGRRLLDD---GPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAEL 232
|
250 260 270
....*....|....*....|....*....|....*
gi 1702117912 302 GTETVRLLLRELNATDTniPKETKVMETQLIVRAS 336
Cdd:cd01574 233 GRRAVELLLALIEGPAP--PPESVLLPPELVVRES 265
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
65-335 |
6.54e-66 |
|
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: 208.91 E-value: 6.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSD--EELILIAEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06270 79 PPLVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06270 159 FTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQA 238
|
250 260 270
....*....|....*....|....*....|.
gi 1702117912 305 TVRLLLRELNATDTNIPKEtkvMETQLIVRA 335
Cdd:cd06270 239 AAELALNLAYGEPLPISHE---FTPTLIERD 266
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
65-336 |
1.11e-65 |
|
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: 208.26 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFI-ISLSRDTDNYEHVERLVRk 143
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLlMCSEMTDDDAELLAALRS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 nIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHC 223
Cdd:cd06275 80 -IPVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQEN--TIMQTLalMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEM 301
Cdd:cd06275 159 DFEPEGgyEAMQRL--LSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDEL 236
|
250 260 270
....*....|....*....|....*....|....*
gi 1702117912 302 GTETVRLLLRELnaTDTNIPKETKVMETQLIVRAS 336
Cdd:cd06275 237 GELAVELLLDRI--ENKREEPQSIVLEPELIERES 269
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-336 |
2.46e-65 |
|
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: 207.47 E-value: 2.46e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNyehVERLVRKN 144
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEE---LLKLLAEG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06290 78 IPVVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06290 158 FTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKT 237
|
250 260 270
....*....|....*....|....*....|..
gi 1702117912 305 TVRLLLRELNatDTNIPKETKVMETQLIVRAS 336
Cdd:cd06290 238 AAEILLELIE--GKGRPPRRIILPTELVIRES 267
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
36-337 |
4.67e-65 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 207.93 E-value: 4.67e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 36 TRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNL 115
Cdd:PRK11041 8 TRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 116 LRSQVEGFIISLSR---DTDNYEhverlvRKNIP-LVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGP 191
Cdd:PRK11041 88 ITKQIDGMLLLGSRlpfDASKEE------QRNLPpMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 192 TQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPE 271
Cdd:PRK11041 162 EEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVPQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1702117912 272 DVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLRELNATDtnIPKETKVMETQLIVRASS 337
Cdd:PRK11041 242 DLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHH--VSSGSRLLDCELIIRGST 305
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
65-336 |
7.43e-65 |
|
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: 206.25 E-value: 7.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTE--ENKQLLKNMN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQ-LVLSNQRVAGYRAALAKHGLSVGEQYVFHC 223
Cdd:cd19975 79 IPVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDdPNAGYPRYEGYKKALKDAGLPIKENLIVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd19975 159 DFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGK 238
|
250 260 270
....*....|....*....|....*....|....*
gi 1702117912 304 ETVRLLLRELNatdtNIPKETK--VMETQLIVRAS 336
Cdd:cd19975 239 KAVELLLDLIK----NEKKEEKsiVLPHQIIERES 269
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-336 |
2.52e-64 |
|
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: 204.81 E-value: 2.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTdnYEHVERLVRKN 144
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDD--LSHLARLRARG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06293 79 TAVVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVRELSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLA--LMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMG 302
Cdd:cd06293 159 PDANAELGRAAAaqLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELG 238
|
250 260 270
....*....|....*....|....*....|....
gi 1702117912 303 TETVRLLLRELNATDTniPKETKVMETQLIVRAS 336
Cdd:cd06293 239 RAAADLLLDEIEGPGH--PHEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-336 |
1.89e-63 |
|
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: 202.38 E-value: 1.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTnIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDA-LRQLLQYRVDGVIVTSATLSS--ELAEECARRG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEqyVFHCD 224
Cdd:cd06278 78 IPVVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPPA--VEAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGI-RIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06278 156 YSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGlVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAE 235
|
250 260 270
....*....|....*....|....*....|...
gi 1702117912 304 ETVRLLLRELNATDTniPKETKVMETQLIVRAS 336
Cdd:cd06278 236 AAVDLLLERIENPET--PPERRVLPGELVERGS 266
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
1-340 |
2.90e-62 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 201.76 E-value: 2.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 1 MKNTPVTIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSA 80
Cdd:PRK09526 1 MKSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 81 MLNSIEEAALQAGYSVLVCQTNESYLRE-TTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVrKNIPLVLFDRYAESiDV 159
Cdd:PRK09526 81 IAAAIKSRADQLGYSVVISMVERSGVEAcQAAVNELLAQRVSGVIINVPLEDADAEKIVADC-ADVPCLFLDVSPQS-PV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 160 SKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVgeQYVFHCDYTQENTIMQTLALMS 239
Cdd:PRK09526 159 NSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQP--IAVREGDWSAMSGYQQTLQMLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 240 LPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLlreLNATDTN 319
Cdd:PRK09526 237 EGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRL---LALSQGQ 313
|
330 340
....*....|....*....|.
gi 1702117912 320 IPKETKVMETQLIVRASSMRQ 340
Cdd:PRK09526 314 AVKGSQLLPTSLVVRKSTAPP 334
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
65-337 |
2.12e-61 |
|
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: 197.50 E-value: 2.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTS--RQLRLLRSAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESI-DVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHC 223
Cdd:cd06296 79 IPFVLIDPVGEPDpDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06296 159 DFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGA 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1702117912 304 ETVRLLLRELNatdtNIPKETKVME--TQLIVRASS 337
Cdd:cd06296 239 VAVRLLLRLLE----GGPPDARRIElaTELVVRGST 270
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
65-332 |
2.53e-59 |
|
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: 192.03 E-value: 2.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYH-----YFSAMLNSIEEAALQAGYSVLVcQTNESYLRETTNIQNLLRS-QVEGFIISLSRDTDNYehVE 138
Cdd:cd06294 1 TIGLVLPSSAEElfqnpFFSEVLRGISQVANENGYSLLL-ATGNTEEELLEEVKRMVRGrRVDGFILLYSKEDDPL--IE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 139 RLVRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQ 218
Cdd:cd06294 78 YLKEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 219 YVFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPI 298
Cdd:cd06294 158 YILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINP 237
|
250 260 270
....*....|....*....|....*....|....
gi 1702117912 299 QEMGTETVRLLLRELNatDTNIPKETKVMETQLI 332
Cdd:cd06294 238 YELGREAAKLLINLLE--GPESLPKNVIVPHELI 269
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
65-336 |
4.99e-57 |
|
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: 186.22 E-value: 4.99e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLV--CQTNESYLRETTnIQNLLRSQVEGFIIS--LSrdtDNYEHVERL 140
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSDDEDLADRL-RRFLSRSRPDGVILTppLS---DDPALLDAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 141 VRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYV 220
Cdd:cd01545 77 DELGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 221 FHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQE 300
Cdd:cd01545 157 VQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAE 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1702117912 301 MGTETVRLLLRELNATDTniPKETKVMETQLIVRAS 336
Cdd:cd01545 237 MARRAVELLIAAIRGAPA--GPERETLPHELVIRES 270
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-336 |
1.03e-56 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 185.02 E-value: 1.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDP--ELFELLEQRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQlvlSN----QRVAGYRAALAKHGLSVGEQYV 220
Cdd:cd06273 79 VPYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTA---GNdrarARLAGIRDALAERGLELPEERV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 221 FHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQE 300
Cdd:cd06273 156 VEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPARE 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 1702117912 301 MGTETVRLLLRELNATDtnIPKETkVMETQLIVRAS 336
Cdd:cd06273 236 IGELAARYLLALLEGGP--PPKSV-ELETELIVRES 268
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
61-336 |
1.97e-56 |
|
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: 184.76 E-value: 1.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 61 SRTKTIGVIVPNLSYH-------YFSAMLNSIEEAALQAGYSVLVCQTNESylreTTNIQNLLRSQ-VEGFIISLSrdTD 132
Cdd:cd06295 1 QRSRTIAVVVPMDPHGdqsitdpFFLELLGGISEALTDRGYDMLLSTQDED----ANQLARLLDSGrADGLIVLGQ--GL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 133 NYEHVERLVRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLaGPTQLVLSNQRVAGYRAALAKHG 212
Cdd:cd06295 75 DHDALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFL-GDPPHPEVADRLQGYRDALAEAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 213 LSVGEQYVFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLS 292
Cdd:cd06295 154 LEADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1702117912 293 SISQPIQEMGTETVRLLLRELNatdtNIPKETKVMETQLIVRAS 336
Cdd:cd06295 234 TVRQDLALAGRLLVEKLLALIA----GEPVTSSMLPVELVVRES 273
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
65-334 |
7.76e-56 |
|
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: 182.75 E-value: 7.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFII-SLSRDTDNYehvERLVRK 143
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILqPTGNNNDAY---LELAQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQ-RVAGYRAALAKHGLSvGEQYVFh 222
Cdd:cd06283 78 GLPVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRReRLQGFLDALARYNIE-GDVYVI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 223 cDYTQENTIMQTLA--LMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQE 300
Cdd:cd06283 156 -EIEDTEDLQQALAafLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYE 234
|
250 260 270
....*....|....*....|....*....|....
gi 1702117912 301 MGTETVRLLLRELNAtDTNIPKETKVmETQLIVR 334
Cdd:cd06283 235 IGKAAAEILLERIEG-DSGEPKEIEL-PSELIIR 266
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
65-336 |
2.40e-55 |
|
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: 181.99 E-value: 2.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFII----SlSRDTDNYEHVERL 140
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIeptkS-ALPNPNLDLYEEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 141 VRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIG--FLAGPTQlvlSNQRVAGYRAALAKHGLSVGEQ 218
Cdd:cd01541 80 QKKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAgiFKSDDLQ---GVERYQGFIKALREAGLPIDDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 219 YVFHC---DYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSIS 295
Cdd:cd01541 157 RILWYsteDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1702117912 296 QPIQEMGTETVRLLLRELNAtdtNIPKETKVMETQLIVRAS 336
Cdd:cd01541 237 HPKEELGRKAAELLLRMIEE---GRKPESVIFPPELIERES 274
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
65-336 |
1.25e-54 |
|
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: 180.00 E-value: 1.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIIS---LSRDTdnyehVERLV 141
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTgteHTPAT-----RKLLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 142 RKNIPLV-LFDRYAESIDVSkVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVL-SNQRVAGYRAALAKHGLSVGEQY 219
Cdd:cd01575 76 AAGIPVVeTWDLPDDPIDMA-VGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLPLVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 220 VFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQ 299
Cdd:cd01575 155 LVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRY 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 1702117912 300 EMGTETVRLLLRELNatDTNIPKETKVMETQLIVRAS 336
Cdd:cd01575 235 EIGRKAAELLLARLE--GEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
65-334 |
1.51e-54 |
|
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: 179.28 E-value: 1.51e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTN------ESYLrettniqNLLRS-QVEGFII-SLSRDTDNYEH 136
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNydkekeLRAL-------ELLKTkQIDGLIItSRENDWEVIEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 137 verlVRKNIPLVLFDRYaESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAG--PTQLVLSNQRVAGYRAALAKHGLS 214
Cdd:cd06286 74 ----YAKYGPIVLCEET-DSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGrpESSSASTQARLKAYQDVLGEHGLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 215 VGEQYVFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALfsPTLSSI 294
Cdd:cd06286 149 LREEWIFTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1702117912 295 SQPIQEMGTETVRLLLRELNatdtNIPKETKVMETQLIVR 334
Cdd:cd06286 227 DQPLEEMGKEAFELLLSQLE----SKEPTKKELPSKLIER 262
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-323 |
5.16e-54 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 178.25 E-value: 5.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSrDTDNYEHVERLVRKN 144
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVG-DAQGSEALELLEEEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGP-TQLVLSNQRVAGYRAALAKHGLSVgeQYVFHC 223
Cdd:cd06282 80 VPYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDfSASDRARLRYQGYRDALKEAGLKP--IPIVEV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06282 158 DFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGR 237
|
250 260
....*....|....*....|
gi 1702117912 304 ETVRLLLRELNATDTNIPKE 323
Cdd:cd06282 238 AAADLLLAEIEGESPPTSIR 257
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
8-336 |
9.08e-54 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 179.51 E-value: 9.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 8 IKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSAMLNSIEE 87
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 88 AALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLsrdTDNYEHVERLVRK--NIPLVLFDrYAESIDVSKVIVD 165
Cdd:PRK10423 81 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLC---TETHQPSREIMQRypSVPTVMMD-WAPFDGDSDLIQD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 166 NHAAAFK-ATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALMSLPQPP 244
Cdd:PRK10423 157 NSLLGGDlATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 245 DGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLRELNatDTNIPKET 324
Cdd:PRK10423 237 QAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMA--QPTLQQQR 314
|
330
....*....|..
gi 1702117912 325 KVMETQLIVRAS 336
Cdd:PRK10423 315 LQLTPELMERGS 326
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
65-332 |
9.71e-53 |
|
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: 175.05 E-value: 9.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVP----NLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYlRETTNIQNLLRS-QVEGFIISLSRDTDnyEHVER 139
Cdd:cd20010 1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGE-DELATYRRLVERgRVDGFILARTRVND--PRIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 140 LVRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQY 219
Cdd:cd20010 78 LLERGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 220 VFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSAL-FSPTLSSISQPI 298
Cdd:cd20010 158 VREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEyFSPPLTTTRSSL 237
|
250 260 270
....*....|....*....|....*....|....
gi 1702117912 299 QEMGTETVRLLLRELNatDTNIPKETKVMETQLI 332
Cdd:cd20010 238 RDAGRRLAEMLLALID--GEPAAELQELWPPELI 269
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-336 |
5.98e-52 |
|
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: 173.12 E-value: 5.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSY---HYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIIsLSRDTDNYehVERLV 141
Cdd:cd19974 1 NIAVLIPERFFgdnSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIII-LGEISKEY--LEKLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 142 RKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLaGPTQLVLS-NQRVAGYRAALAKHGLSVGEQYV 220
Cdd:cd19974 78 ELGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFV-GDINYTSSfMDRYLGYRKALLEAGLPPEKEEW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 221 FHCDYTQENTIMQTLAL---MSLPqppDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQP 297
Cdd:cd19974 157 LLEDRDDGYGLTEEIELplkLMLP---TAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVD 233
|
250 260 270
....*....|....*....|....*....|....*....
gi 1702117912 298 IQEMGTETVRLLLRELNATDTniPKETKVMETQLIVRAS 336
Cdd:cd19974 234 KEAMGRRAVEQLLWRIENPDR--PFEKILVSGKLIERDS 270
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
7-336 |
4.53e-51 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 172.99 E-value: 4.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 7 TIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSAMLNSIE 86
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 87 EAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRkNIPLVLFDRYAESIDVSKVIVDN 166
Cdd:PRK10703 83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYR-HIPMVVMDWGEAKADFTDAIIDN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 167 -HAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALMSLPQPPD 245
Cdd:PRK10703 162 aFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 246 GVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLRELNATDtnipKETK 325
Cdd:PRK10703 242 AVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKR----EEPQ 317
|
330
....*....|...
gi 1702117912 326 VMET--QLIVRAS 336
Cdd:PRK10703 318 TIEVhpRLVERRS 330
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
77-336 |
1.02e-50 |
|
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: 169.63 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 77 YFSAMLNSIEEAALQAGYSVlvcqtneSYLRETTNIQNLLRSQVEGFII--SLSRDTdnyehVERLVRKNIPLVLFDRYA 154
Cdd:cd01544 18 YYLSIRLGIEKEAKKLGYEI-------KTIFRDDEDLESLLEKVDGIIAigKFSKEE-----IEKLKKLNPNIVFVDSNP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 155 ESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAG-----PTQLVLSNQRVAGYRAALAKHGLSVgEQYVFHCDYTQEN 229
Cdd:cd01544 86 DPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGkeytsDDGEEIEDPRLRAFREYMKEKGLYN-EEYIYIGEFSVES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 230 TIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLL 309
Cdd:cd01544 165 GYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLL 244
|
250 260
....*....|....*....|....*..
gi 1702117912 310 LRELNaTDTNIPKETkVMETQLIVRAS 336
Cdd:cd01544 245 LERIN-GGRTIPKKV-LLPTKLIERES 269
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
65-336 |
6.87e-49 |
|
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: 165.10 E-value: 6.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNyEHVERLVRKN 144
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDP-ELAAALARLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESiDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06281 80 IPVVLIDRDLPG-DIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd06281 159 FSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRA 238
|
250 260 270
....*....|....*....|....*....|..
gi 1702117912 305 TVRLLLRELnATDTNIPKETKVMETQLIVRAS 336
Cdd:cd06281 239 AAELLLDRI-EGPPAGPPRRIVVPTELILRDS 269
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
65-333 |
2.12e-48 |
|
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: 163.62 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGfIISLSrDTDNYEHVERLVRKN 144
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDG-IIFMG-DELTEEIREEFKRSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQL-VLSNQRVAGYRAALAKHGLSVGEQYVFHC 223
Cdd:cd06298 79 VPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEyINNDKKLQGYKRALEEAGLEFNEPLIFEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSLpQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06298 159 DYDYDSGYELYEELLES-GEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGA 237
|
250 260 270
....*....|....*....|....*....|
gi 1702117912 304 ETVRLLlrelnatdTNIPKETKVMETQLIV 333
Cdd:cd06298 238 VAMRLL--------TKLMNKEEVEETIVKL 259
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
77-336 |
5.88e-46 |
|
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: 157.40 E-value: 5.88e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 77 YFSAMLNSIEEAALQAGYSVL--VCQTNESYLRETTNIQNllrSQVEGfIISLSRDTDNyEHVERLVRKNIPLVLFDRYA 154
Cdd:cd06277 20 FFSELIDGIEREARKYGYNLLisSVDIGDDFDEILKELTD---DQSSG-IILLGTELEE-KQIKLFQDVSIPVVVVDNYF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 155 ESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQT 234
Cdd:cd06277 95 EDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 235 LALMS-LPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLREL 313
Cdd:cd06277 175 KALLDtGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKI 254
|
250 260
....*....|....*....|...
gi 1702117912 314 NatDTNIPKETKVMETQLIVRAS 336
Cdd:cd06277 255 K--DPDGGTLKILVSTKLVERGS 275
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
65-336 |
7.16e-46 |
|
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: 157.76 E-value: 7.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVP-NLSY----HYFSAMLNSIEEAALQAGYSVLVCqtneSYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVER 139
Cdd:cd06279 1 AIGVLLPdDLSYafsdPVAAQFLRGVAEVCEEEGLGLLLL----PATDEGSAAAAVRNAAVDGFIVYGLSDDD--PAVAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 140 LVRKNIPLVLFDRYAESiDVSKVIVDNHAAAFKATEHLIENGCRRIGFL-----AGPTQLVLS------------NQRVA 202
Cdd:cd06279 75 LRRRGLPLVVVDGPAPP-GIPSVGIDDRAAARAAARHLLDLGHRRIAILslrldRGRERGPVSaerlaaatnsvaRERLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 203 GYRAALAKHGLSVGEQYVFHCDY-TQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNE 281
Cdd:cd06279 154 GYRDALEEAGLDLDDVPVVEAPGnTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDI 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1702117912 282 PVSALFSPTLSSISQPIQEMGTETVRLLLRELNATdtniPKETKVMETQLIVRAS 336
Cdd:cd06279 234 PEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGA----PPRPVILPTELVVRAS 284
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
65-332 |
1.16e-45 |
|
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: 156.12 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVRKN 144
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITD--EHRKALKKLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAEsiDVSKVIVDNHAAAFKATEHLIENGCRRIGFLA-GPTQLVLSNQRVAGYRAALAKHGLSvgEQYVFHC 223
Cdd:cd01542 79 IPVVVLGQEHE--GFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGvDEEDIAVGVARKQGYLDALKEHGID--EVEIVET 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 224 DYTQENTIMQTLALMSlPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd01542 155 DFSMESGYEAAKELLK-ENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGE 233
|
250 260
....*....|....*....|....*....
gi 1702117912 304 ETVRLLLRELNatDTNIPKETKvMETQLI 332
Cdd:cd01542 234 KAAELLLDMIE--GEKVPKKQK-LPYELI 259
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
7-336 |
7.86e-41 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 146.06 E-value: 7.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 7 TIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSAMLNSIE 86
Cdd:PRK10727 3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 87 EAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyEHVERLVrKNIP-LVLFDRYAESIDVSKVIVD 165
Cdd:PRK10727 83 QVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPD--AELASLM-KQIPgMVLINRILPGFENRCIALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 166 NHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALMSLPQPPD 245
Cdd:PRK10727 160 DRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 246 GVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLRElnATDTNIPKETK 325
Cdd:PRK10727 240 AVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALAL--ADNRPLPEITN 317
|
330
....*....|.
gi 1702117912 326 VMETQLIVRAS 336
Cdd:PRK10727 318 VFSPTLVRRHS 328
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
1-335 |
5.69e-40 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 143.70 E-value: 5.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 1 MKNTPVTIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSA 80
Cdd:PRK10014 2 ATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 81 MLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNyEHVERLVRKNIPLVLFDR--YAESID 158
Cdd:PRK10014 82 LTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSD-DLREMAEEKGIPVVFASRasYLDDVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 159 VskVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALM 238
Cdd:PRK10014 161 T--VRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 239 SLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPED---------VAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLL 309
Cdd:PRK10014 239 RHNPTISAVVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRM 318
|
330 340
....*....|....*....|....*.
gi 1702117912 310 LRELNATDTniPKETKVMETQLIVRA 335
Cdd:PRK10014 319 MQRITHEET--HSRNLIIPPRLIARK 342
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
65-336 |
9.72e-39 |
|
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: 138.37 E-value: 9.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGY-----SVLVCQTNESYLRETTNIQnllrsQVEGFIISLSRDTDNYEhvER 139
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYdlaifPLLSEYRLEKYLRNSTLAY-----QCDGLVMASLDLTELFE--EV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 140 LVRKNIPLVLFDRYAESIDVskVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSN----QRVAGYRAALAKHGLSV 215
Cdd:cd06297 74 IVPTEKPVVLIDANSMGYDC--VYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTEtvfrEREQGFLEALNKAGRPI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 216 GEQYVFHCDYTQ---ENTIMQTLALMSlpqPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSAlfSPTLS 292
Cdd:cd06297 152 SSSRMFRIDNSSkkaECLARELLKKAD---NPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLT 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1702117912 293 SISQPIQEMGTETVRLLLRELNAtDTNIPKETKVmETQLIVRAS 336
Cdd:cd06297 227 TVRQPVEEMGEAAAKLLLKRLNE-YGGPPRSLKF-EPELIVRES 268
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
176-337 |
1.00e-38 |
|
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: 135.16 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 176 HLIENGCRRIGFLA--GPTQLVLSNQRVAGYRAALAKHGLSVgEQYVFHCDYTQENTIMQtLALMSLPQPPDGVVIISDR 253
Cdd:pfam13377 1 HLAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGLDV-EPTLYAGDDEAEAAAAR-ERLRWLGALPTAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 254 MAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLRELNatDTNIPKETKVMETQLIV 333
Cdd:pfam13377 79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLN--GEPAPPERVLLPPELVE 156
|
....
gi 1702117912 334 RASS 337
Cdd:pfam13377 157 REST 160
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
76-329 |
5.91e-37 |
|
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: 133.70 E-value: 5.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 76 HYFSAMLNSIEEAALQAGYSVLVcqTNESYLRETTNIQNLLRS-QVEGFIISLSRDTDnyEHVERLVRKNIPLVLFDRYA 154
Cdd:cd06271 15 GTVSE*VSGITEEAGTTGYHLLV--WPFEEAES*VPIRDLVETgSADGVILSEIEPND--PRVQFLTKQNFPFVAHGRSD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 155 ESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLsvgEQYVFHCDYTQENTIMQT 234
Cdd:cd06271 91 *PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGL---TGYPLDADTTLEAGRAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 235 LALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEP-VSALFSPTLSSISQPIQEMGTETVRLLLREL 313
Cdd:cd06271 168 QRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVHAPIAEAGRELAKALLARI 247
|
250
....*....|....*.
gi 1702117912 314 NATDtniPKETKVMET 329
Cdd:cd06271 248 DGED---PETLQVLVQ 260
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
5-311 |
6.22e-37 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 135.67 E-value: 6.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 5 PVTIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSAMLNS 84
Cdd:PRK10401 1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 85 IEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDnyehvERLVR--KNIP-LVLFDRYAESIDVSK 161
Cdd:PRK10401 81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSD-----DELAQfmDQIPgMVLINRVVPGYAHRC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 162 VIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALMSLP 241
Cdd:PRK10401 156 VCLDNVSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRN 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 242 QPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLR 311
Cdd:PRK10401 236 LQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQ 305
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
65-313 |
1.53e-34 |
|
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: 127.32 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHveRLVRKN 144
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYY--LCQAAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd06274 79 LPVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALM-SLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT 303
Cdd:cd06274 159 YDRESGYQLMAELLaRLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIAE 238
|
250
....*....|
gi 1702117912 304 ETVRLLLREL 313
Cdd:cd06274 239 HAFELLDALI 248
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
66-310 |
3.67e-33 |
|
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: 123.90 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 66 IGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRkNI 145
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQ-NV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 146 PLVLFDRYAESIDVSKVIVDNH-AAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCD 224
Cdd:cd01537 81 PVVFFDKEPSRYDKAYYVITDSkEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 225 YTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTE 304
Cdd:cd01537 161 WDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKT 240
|
....*.
gi 1702117912 305 TVRLLL 310
Cdd:cd01537 241 TFDLLL 246
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
77-332 |
1.79e-32 |
|
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: 121.88 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 77 YFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTnIQNLLRSQ-VEGFIISLSRDTDnyEHVERLVRKNIPLVLFDRYAE 155
Cdd:cd20009 15 FTSQLISGISEALRGTPYHLVVTPEFPGDDPLEP-VRYIVENRlADGIIISHTEPQD--PRVRYLLERGFPFVTHGRTEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 156 SIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTL 235
Cdd:cd20009 92 STPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAAR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 236 ALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGTETVRLLLRELNA 315
Cdd:cd20009 172 RLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEG 251
|
250
....*....|....*..
gi 1702117912 316 TDtnIPKETKVMETQLI 332
Cdd:cd20009 252 EP--AEPLQTLERPELI 266
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
124-337 |
2.65e-29 |
|
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: 113.45 E-value: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 124 IISLSRDTdnyEHVERLVRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLaGPTQLVLSNQRVAG 203
Cdd:cd01543 54 IIARLDDP---ELAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFC-GFRNAAWSRERGEG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 204 YRAALAKHGLSVgeqYVFHCDYTQE----NTIMQTLA--LMSLPQPpdgVVIIS--DRMAYSAMYAMKQKGIRIPEDVAV 275
Cdd:cd01543 130 FREALREAGYEC---HVYESPPSGSsrswEEEREELAdwLKSLPKP---VGIFAcnDDRARQVLEACREAGIRVPEEVAV 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1702117912 276 VSFNNEPVSALFS-PTLSSISQPIQEMGTETVRLLLRELNatDTNIPKETKVME-TQLIVRASS 337
Cdd:cd01543 204 LGVDNDELICELSsPPLSSIALDAEQIGYEAAELLDRLMR--GERVPPEPILIPpLGVVTRQST 265
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
7-278 |
3.12e-29 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 114.59 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 7 TIKDIARSLNISISTVSRALRG---MQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVP---NLSYhyfsA 80
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINGkakQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPdleNTSY----A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 81 ML-NSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIIS--LSRDTDNYEhveRLVRKNIPLVLFDRYAESI 157
Cdd:PRK11303 78 RIaKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVStsLPPEHPFYQ---RLQNDGLPIIALDRALDRE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 158 DVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSV----GEQYVFHCDYTQENTIMQ 233
Cdd:PRK11303 155 HFTSVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREVhylyANSFEREAGAQLFEKWLE 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1702117912 234 TLALmslpqpPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSF 278
Cdd:PRK11303 235 THPM------PDALFTTSYTLLQGVLDVLLERPGELPSDLAIATF 273
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
55-326 |
6.09e-28 |
|
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: 110.78 E-value: 6.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 55 AKNLAKSRTKTIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNY 134
Cdd:COG1879 25 EAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 135 EHVERLVRKNIPLVLFDRYAESID-VSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKH 211
Cdd:COG1879 105 PALKKAKAAGIPVVTVDSDVDGSDrVAYVGSDNYAAGRLAAEYLAKalGGKGKVAILTGSPGAPAANERTDGFKEALKEY 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 212 -GLS-VGEQYvfhCDYTQEN--TIMQTLaLMSLPQpPDGVVIISDRMAYSAMYAMKQKGirIPEDVAVVSFNNEP--VSA 285
Cdd:COG1879 185 pGIKvVAEQY---ADWDREKalEVMEDL-LQAHPD-IDGIFAANDGMALGAAQALKAAG--RKGDVKVVGFDGSPeaLQA 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1702117912 286 LFSPTLS-SISQPIQEMGTETVRLLLRELNATDtnIPKETKV 326
Cdd:COG1879 258 IKDGTIDaTVAQDPYLQGYLAVDAALKLLKGKE--VPKEILT 297
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
63-315 |
1.25e-26 |
|
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: 106.44 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 63 TKTIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISlSRDTDnYEHVERLVR 142
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIIT-TPAPS-GDDITAKAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 143 -KNIPLVLFDRYAES-IDVSKVIVDNHAAAFKATEHLIENGCRR-IGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQY 219
Cdd:pfam00532 79 gYGIPVIAADDAFDNpDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGREVKIYH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 220 VFHCDYTQENtimQTLALMS-LPQPPDGVVII--SDRMAYSAMYAMKQKG-IRIPEDV-----AVVSFNN---EPVSALF 287
Cdd:pfam00532 159 VATGDNDIPD---AALAANAmLVSHPTIDAIVamNDEAAMGAVRALLKQGrVKIPDIVgiginSVVGFDGlskAQDTGLY 235
|
250 260
....*....|....*....|....*...
gi 1702117912 288 SPTLSSISQPIQEMGTETVRLLLRELNA 315
Cdd:pfam00532 236 LSPLTVIQLPRQLLGIKASDMVYQWIPK 263
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
1-311 |
4.59e-25 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 103.57 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 1 MKNTPVTIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLSYHYFSA 80
Cdd:PRK14987 1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 81 MLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIisLSRDTDNYEHVERLVRKNIPLV-LFDRYAESIDV 159
Cdd:PRK14987 81 VLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLI--LTERTHTPRTLKMIEVAGIPVVeLMDSQSPCLDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 160 SkVIVDNHAAAFKATEHLIENGCRRIGFL-AGPTQLVLSNQRvaGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLALM 238
Cdd:PRK14987 159 A-VGFDNFEAARQMTTAIIARGHRHIAYLgARLDERTIIKQK--GYEQAMLDAGLVPYSVMVEQSSSYSSGIELIRQARR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1702117912 239 SLPQpPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQEMGT-ETVRLLLR 311
Cdd:PRK14987 236 EYPQ-LDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSiGAERLLAR 308
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
65-326 |
2.66e-24 |
|
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: 99.95 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSrDTDNYEH-VERLVRK 143
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPV-DSEALVPaVKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRYAESID--VSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLS--VGE 217
Cdd:cd01536 80 GIPVVAVDTDIDGGGdvVAFVGTDNYEAGKLAGEYLAEalGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYPDIeiVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 218 QYvfhCDYTQEN--TIMQTLaLMSLPQpPDGVVIISDRMAYSAMYAMKQKGirIPEDVAVVSFNNEP--VSALFSPTLS- 292
Cdd:cd01536 160 QP---ANWDRAKalTVTENL-LQANPD-IDAVFAANDDMALGAAEALKAAG--RTGDIKIVGVDGTPeaLKAIKDGELDa 232
|
250 260 270
....*....|....*....|....*....|....
gi 1702117912 293 SISQPIQEMGTETVRLLLRELNatDTNIPKETKV 326
Cdd:cd01536 233 TVAQDPYLQGYLAVEAAVKLLN--GEKVPKEILT 264
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
65-335 |
3.43e-24 |
|
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: 99.76 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPN-LSYHYFSAMLNSIEEAALQAGYSVLV--CQTNESYLRETTNIQNllRSQVEGFIISLSRDTDnyehVERLV 141
Cdd:cd06272 1 TIGLYWPSvGERVALTRLLSGINEAISKQGYNINLsiCPYKVGHLCTAKGLFS--ENRFDGVIVFGISDSD----IEYLN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 142 RKN--IPLVLFDRyaESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLSVGEQY 219
Cdd:cd06272 75 KNKpkIPIVLYNR--ESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 220 VFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQ 299
Cdd:cd06272 153 IDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIE 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 1702117912 300 EMGTETVRLLLRELNAtdtnIPKETKVM--ETQLIVRA 335
Cdd:cd06272 233 KIAEESLRLILKLIEG----RENEIQQLilYPELIFRE 266
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
66-314 |
3.68e-23 |
|
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: 96.61 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 66 IGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNE-SYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRKN 144
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEaDAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESID-VSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLS---VGEQ 218
Cdd:pfam13407 81 IPVVTFDSDAPSSPrLAYVGFDNEAAGEAAGELLAEalGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGikvVAEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 219 YVFHCDYTQENTIMQTLaLMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRipEDVAVVSFNNEPVS--ALFSPTLS-SIS 295
Cdd:pfam13407 161 EGTNWDPEKAQQQMEAL-LTAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEAleAIKDGTIDaTVL 237
|
250
....*....|....*....
gi 1702117912 296 QPIQEMGTETVRLLLRELN 314
Cdd:pfam13407 238 QDPYGQGYAAVELAAALLK 256
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
6-74 |
2.48e-22 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 88.80 E-value: 2.48e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1702117912 6 VTIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKTIGVIVPNLS 74
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDIT 69
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
65-332 |
2.07e-21 |
|
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: 92.04 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRKN 144
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESID-VSKVIVDNHAAAFKATEHLIEN------GCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGL-SVG 216
Cdd:cd06319 81 IPVVIADIGTGGGDyVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVeEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 217 EQYVfhCDYTQENT--IMQTLalmsLPQPPD--GVVIISDRMAYSAMYAMKQKGIRipEDVAVVSFNNEP--VSALFSPT 290
Cdd:cd06319 161 LRQT--PNSTVEETysAAQDL----LAANPDikGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPeaLDLIKDGK 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1702117912 291 LSSI--SQPIqEMGTETVRLLLRELNAtdTNIPKETKVMETQLI 332
Cdd:cd06319 233 LDGTvaQQPF-GMGARAVELAIQALNG--DNTVEKEIYLPVLLV 273
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
65-282 |
2.44e-18 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 83.59 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISlSRDTDNYE-HVERLVRK 143
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVS-PIDVKALVpAIEAAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRYAESID-VSKVIVDNHAAAFKATEHLIEN--GCRRIGFLAGPTQLVLSNQRVAGYRAALAKhglsvGEQYV 220
Cdd:cd19968 80 GIPVVTVDRRAEGAApVPHVGADNVAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGFHEELAA-----GPKIK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1702117912 221 FHCDYT------QENTIMQTlALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIpEDVAVVSFNNEP 282
Cdd:cd19968 155 VVFEQTgnferdEGLTVMEN-ILTSLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFDAVP 220
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
65-327 |
8.24e-17 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380545 [Multi-domain] Cd Length: 270 Bit Score: 79.24 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISlsrDTDN---YEHVERLV 141
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILA---PVDSggiVPAIEAAN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 142 RKNIPLVLFDRYAESIDV-SKVIVDNHAAAFKATEHLIE---NGCRRIGFLAGPTQlVLSNQRVAGYRAALAKHGlsvGE 217
Cdd:cd06322 78 EAGIPVFTVDVKADGAKVvTHVGTDNYAGGKLAGEYALKallGGGGKIAIIDYPEV-ESVVLRVNGFKEAIKKYP---NI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 218 QYVFHCDY-TQENTIMQTLALMSLPQPP-DGVVIISDRMAYSAMYAMKQKGIRipEDVAVVSF--NNEPVSALF--SPTL 291
Cdd:cd06322 154 EIVAEQPGdGRREEALAATEDMLQANPDlDGIFAIGDPAALGALTAIESAGKE--DKIKVIGFdgNPEAIKAIAkgGKIK 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1702117912 292 SSISQPIQEMGTETVRLLLRELN--ATDTNIPKETKVM 327
Cdd:cd06322 232 ADIAQQPDKIGQETVEAIVKYLAgeTVEKEILIPPKLY 269
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
7-310 |
1.59e-16 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 79.03 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 7 TIKDIARSLNISISTVSRALRG--MQEIHPDTRKAVMRLAEELDYQPNQLAKNLAKSRTKtigvivpnlsyHYFSAMLNS 84
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNDdpTLNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQ-----------HHILAIYSY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 85 IEEAALQAGYsvlvcqtnesYLrettNIQNLLRSQVEGFIISLsrdTDNYEHVERLVRKNI------------------- 145
Cdd:PRK10339 72 QQELEINDPY----------YL----AIRHGIETQCEKLGIEL---TNCYEHSGLPDIKNVtgilivgkptpalraaasa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 146 ---PLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRvagyRAALAKHGL---SVGEQY 219
Cdd:PRK10339 135 ltdNICFIDFHEPGSGYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIR----EVAFAEYGRlkqVVREED 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 220 VFHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLSSISQPIQ 299
Cdd:PRK10339 211 IWRGGFSSSSGYELAKQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSE 290
|
330
....*....|.
gi 1702117912 300 EMGTETVRLLL 310
Cdd:PRK10339 291 MMGSQGVNLLY 301
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
9-60 |
5.45e-16 |
|
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: 70.90 E-value: 5.45e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1702117912 9 KDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPNQLAKNLAK 60
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
65-279 |
6.67e-16 |
|
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.
Pssm-ID: 380532 [Multi-domain] Cd Length: 285 Bit Score: 76.87 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISlSRDTDNYEHVERLVRK- 143
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILIS-PIDATGWDPVLKEAKDa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRYAESID----VSKVIVDNHA----AAFKATEHLIENGCRrIGFLAGPTQLVLSNQRVAGYRAALAKHGlsv 215
Cdd:cd06309 80 GIPVILVDRTIDGEDgslyVTFIGSDFVEegrrAAEWLVKNYKGGKGN-VVELQGTAGSSVAIDRSKGFREVIKKHP--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 216 GEQYVFHC--DYTQEN--TIMQTLALMslpQPPDGVVII--SDRMAYSAMYAMKQKGIRIPEDVAVVSFN 279
Cdd:cd06309 156 NIKIVASQsgNFTREKgqKVMENLLQA---GPGDIDVIYahNDDMALGAIQALKEAGLKPGKDVLVVGID 222
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
65-323 |
8.24e-16 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 76.33 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRKN 144
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDVSKVIV-DNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGL--SVGEQY 219
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTFIAtDSVAAAKELGEWVIKqtGGKGEIAILHGQLGTTPEVDRTKGFQEALAEAPGikVVAEQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 220 VfhcDYTQEN--TIMQTLalmsLPQPPDGVVII--SDRMAYSAMYAMKQKGirIPEDVAVVSFNNEP--VSALFSPTLS- 292
Cdd:cd19972 161 A---DWDQDEgfKVAQDM----LQANPNITVFFgqSDAMALGAAQAVKVAG--LDHKIWVVGFDGDVagLKAVKDGVLDa 231
|
250 260 270
....*....|....*....|....*....|.
gi 1702117912 293 SISQPIQEMGTETVRLLLRELNATDtnIPKE 323
Cdd:cd19972 232 TMTQQTQKMGRLAVDSAIDLLNGKA--VPKE 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
65-314 |
2.98e-13 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 68.91 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSV--LVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVR 142
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIifVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 143 KNIPLVLFD-RYAESIDVSKVIVDNHAAAFKATEHLIE--NGCRRIGFLagptQLVLSN----QRVAGYRAALAKHGLSV 215
Cdd:cd06310 81 KGIPVIVIDsGIKGDAYLSYIATDNYAAGRLAAQKLAEalGGKGKVAVL----SLTAGNsttdQREEGFKEYLKKHPGGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 216 GEQYVFHCDyTQENTIM-QTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRipEDVAVVSF--NNEPVSALFSPTLS 292
Cdd:cd06310 157 KVLASQYAG-SDYAKAAnETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLS--GQIKIVGFdsQEELLDALKNGKID 233
|
250 260
....*....|....*....|...
gi 1702117912 293 -SISQPIQEMGTETVRLLLRELN 314
Cdd:cd06310 234 aLVVQNPYEIGYEGIKLALKLLK 256
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
65-326 |
4.15e-13 |
|
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380546 [Multi-domain] Cd Length: 268 Bit Score: 68.48 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRKN 144
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESIDV-SKVIVDNHAAAFKATEHLIEngcrrigFLAGPTQLVL---------SNQRVAGYRAALAKH-GL 213
Cdd:cd06323 81 IPVITVDRSVTGGKVvSHIASDNVAGGEMAAEYIAK-------KLGGKGKVVElqgipgtsaARERGKGFHNAIAKYpKI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 214 SVGEQYVFHCDYTQENTIMQTLalmsLPQPP--DGVVIISDRMAYSAMYAMKQKGiriPEDVAVVSFN--NEPVSALFSP 289
Cdd:cd06323 154 NVVASQTADFDRTKGLNVMENL----LQAHPdiDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDgtPDAVKAVKDG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1702117912 290 TLS-SISQPIQEMG---TETVRLLLRElNATDTNIPKETKV 326
Cdd:cd06323 227 KLAaTVAQQPEEMGakaVETADKYLKG-EKVPKKIPVPLKL 266
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
65-314 |
6.00e-13 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 68.08 E-value: 6.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESY--LRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVR 142
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGAKVTVVDARYdlAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 143 KNIPLVLFDRYAESIDvSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPtQLVLSNQRVAGYRAALAKHG--LSVGEQ 218
Cdd:cd06321 81 AGIIVVAVDVAAEGAD-ATVTTDNVQAGYLACEYLVEqlGGKGKVAIIDGP-PVSAVIDRVNGCKEALAEYPgiKLVDDQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 219 yvfHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRipeDVAVVSFNNEP--VSALF---SPTLSS 293
Cdd:cd06321 159 ---NGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---DIVITSVDGSPeaVAALKregSPFIAT 232
|
250 260
....*....|....*....|.
gi 1702117912 294 ISQPIQEMGTETVRLLLRELN 314
Cdd:cd06321 233 AAQDPYDMARKAVELALKILN 253
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
65-332 |
7.68e-13 |
|
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.
Pssm-ID: 380531 [Multi-domain] Cd Length: 268 Bit Score: 67.57 E-value: 7.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSI-EEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISlSRDTDN-YEHVERLVR 142
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIkAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVS-PNEADAlTPVVKKAYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 143 KNIPLVLFDRYAESIDV-SKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKH-GLSVGEQ 218
Cdd:cd06308 80 AGIPVIVLDRKVSGDDYtAFIGADNVEIGRQAGEYIAEllNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYpGIKIVAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 219 YvfHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRipEDVAVVSfnnepVSALFSPTLSSISQPI 298
Cdd:cd06308 160 Q--DGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIG-----VDGLPEAGEKAVKDGI 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1702117912 299 QE-------MGTETVRLLLRELNatDTNIPKETkVMETQLI 332
Cdd:cd06308 231 LAatflyptGGKEAIEAALKILN--GEKVPKEI-VLPTPLI 268
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
7-52 |
3.54e-11 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 57.65 E-value: 3.54e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1702117912 7 TIKDIARSLNISISTVSRALRGMQEIHPDTRKAVMRLAEELDYQPN 52
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
136-336 |
1.45e-09 |
|
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: 57.82 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 136 HVERLVRKNIPLVLFDRY-AESIDVSKVIVDNHAAAFKATEHLIENGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLS 214
Cdd:cd06287 71 ILARLRQRGVPVVSIGRApGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRFAQEYGTT 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 215 vgeQYVFHCDYTQ-ENTIMQTLALMSLPQPP-DGVVIISDRMAYSAMYAMKQKGIRIPEDVAVVSFNNEPVSALFSPTLS 292
Cdd:cd06287 151 ---PVVYKVPESEgERAGYEAAAALLAAHPDiDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLT 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1702117912 293 SISQPIQEMGTETVRLLLRELNATDtnipKETKVMET-QLIVRAS 336
Cdd:cd06287 228 AVDLHLDRVARTAIDLLFASLSGEE----RSVEVGPApELVVRAS 268
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
65-318 |
2.30e-09 |
|
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: 57.31 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVpNLSYHYFSAM-LNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRK 143
Cdd:cd06305 1 TIAVVR-NGTSGDWDQQaLQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAG----PTQlvlsnQRVAGYRAALAKH--GLSV 215
Cdd:cd06305 80 GIPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKdlNGEGNIAVFNVfgvpPLD-----KRYDIYKAVLKANpgIKKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 216 GEQYVFHCDYTQENTIMQTLALmsLPQPPDGVV--IIS--DRMAYSAMYAMKQKG---IRI------PEDVAVVSFNNEP 282
Cdd:cd06305 155 VAELGDVTPNTAADAQTQVEAL--LKKYPEGGIdaIWAawDEPAKGAVQALEEAGrtdIKVygvdisNQDLELMADEGSP 232
|
250 260 270
....*....|....*....|....*....|....*.
gi 1702117912 283 VSAlfsptlsSISQPIQEMGTETVRLLLRELNATDT 318
Cdd:cd06305 233 WVA-------TAAQDPALIGTVAVRNVARKLAGEDL 261
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
65-266 |
1.26e-08 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 55.06 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNlSYHYFSAMLN-SIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIIsLSRDTDNYEHVERLVR- 142
Cdd:cd06311 1 TIGISIPS-ADHGWTAGVAyYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVI-LPQDSEELTVAAQKAKd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 143 KNIPLVLFDR-YAESIDVSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKH-GLSVGEQ 218
Cdd:cd06311 79 AGIPVVNFDRgLNVLIYDLYVAGDNPGMGVVSAEYIGKklGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpGIKILAM 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1702117912 219 YvfHCDYTQE--NTIMQTLaLMSLPQpPDGVVIISDRMAYSAMYAMKQKG 266
Cdd:cd06311 159 Q--AGDWTREdgLKVAQDI-LTKNKK-IDAVWAADDDMAIGVLQAIKEAG 204
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
111-270 |
2.91e-08 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 54.17 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 111 NIQNLLRSQVEGFIIS-LSRDTDNyEHVERLVRKNIPLVLFDRYAESID-VSKVIVDNHAAAFKATEHLIE--NGCRRIG 186
Cdd:cd19996 50 DIQDLIAQGVDAIIVSpNSPTALL-PAIEKAAAAGIPVVLFDSGVGSDKyTAFVGVDDAAFGRVGAEWLVKqlGGKGNII 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 187 FLAGPTQLVLSNQRVAGYRAALAKHGLS--VGEQYvfhCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQ 264
Cdd:cd19996 129 ALRGIAGVSVSEDRWAGAKEVFKEYPGIkiVGEVY---ADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEE 205
|
....*.
gi 1702117912 265 KGIRIP 270
Cdd:cd19996 206 AGRPLV 211
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
65-302 |
3.22e-08 |
|
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.
Pssm-ID: 380622 [Multi-domain] Cd Length: 272 Bit Score: 53.87 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGfIISLSRDTDN-YEHVERLVRK 143
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKA-IILDPADADAsIAAVKKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRY--AESIDVSKVIVDNHAAAFKATEHLIE-------------------NGCRRIGF---LAGPTQLVLSNQ 199
Cdd:cd19967 80 GIPVFLIDREinAEGVAVAQIVSDNYQGAVLLAQYFVKlmgekglyvellgkesdtnAQLRSQGFhsvIDQYPELKMVAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 200 RVAGYraalakhglsvgeqyvfhcDYTQENTIMQTLaLMSLPQpPDGVVIISDRMAYSAMYAMKQKGirIPEDVAVVSFN 279
Cdd:cd19967 160 QSADW-------------------DRTEAFEKMESI-LQANPD-IKGVICGNDEMALGAIAALKAAG--RAGDVIIVGFD 216
|
250 260
....*....|....*....|....*.
gi 1702117912 280 --NEPVSALFSPTLS-SISQPIQEMG 302
Cdd:cd19967 217 gsNDVRDAIKEGKISaTVLQPAKLIA 242
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
66-332 |
5.97e-08 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 53.42 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 66 IGVIVPNLSYHYFSAMLNSIEEAALQAG--YSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRK 143
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGvkVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFD-------RYAESIDV-SKVIVDNHAAAFKATEHLIEN--GCRRIGFLAGPTQLVLSNQRVAGYRAALAK-HG 212
Cdd:cd06320 82 GIPVINLDdavdadaLKKAGGKVtSFIGTDNVAAGALAAEYIAEKlpGGGKVAIIEGLPGNAAAEARTKGFKETFKKaPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 213 LSVGEqyVFHCDYTQENTIMQTLALMSlpQPPDGVVII--SDRMAYSAMYAMKQKGIRipEDVAVVS--FNNEPVSALFS 288
Cdd:cd06320 162 LKLVA--SQPADWDRTKALDAATAILQ--AHPDLKGIYaaNDTMALGAVEAVKAAGKT--GKVLVVGtdGIPEAKKSIKA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1702117912 289 PTLS-SISQPIQEMGTETVRLLLRELNATDT--NIPKETKVMETQLI 332
Cdd:cd06320 236 GELTaTVAQYPYLEGAMAVEAALRLLQGQKVpaVVATPQALITKDNV 282
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
112-284 |
7.02e-08 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 52.99 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 112 IQNLLRSQVEGFIISLSRDTDNYEHVERLVRKNIPLVLFDRYAESIDV-SKVIVDNHAAAFKATEHLIENGCRR-----I 185
Cdd:cd20006 52 IEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPVNSKKAdSFVATDNYEAGKKAGEKLASLLGEKgkvaiV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 186 GFLAGPTQlvlSNQRVAGYRAALAKHG--LSVGEQYvfhCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMK 263
Cdd:cd20006 132 SFVKGSST---AIEREEGFKQALAEYPniKIVETEY---CDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALK 205
|
170 180
....*....|....*....|.
gi 1702117912 264 QKGIRipEDVAVVSFNNEPVS 284
Cdd:cd20006 206 ELGLG--GKVKVVGFDSSVEE 224
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
52-326 |
7.05e-08 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 53.17 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 52 NQLAKNlaksrtkTIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLrsqVEGFIISLSRDT 131
Cdd:PRK10653 22 NAMAKD-------TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLT---VRGTKILLINPT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 132 DNyEHVERLV----RKNIPLVLFDRYAESIDV-SKVIVDNHAAAFKATEHLIE---NGCRRIGF--LAGPTQlvlSNQRV 201
Cdd:PRK10653 92 DS-DAVGNAVkmanQANIPVITLDRGATKGEVvSHIASDNVAGGKMAGDFIAKklgEGAKVIQLegIAGTSA---ARERG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 202 AGYRAALAKHGLSVGEQYVFHCDYTQENTIMQTLalmsLPQPPD--GVVIISDRMAYSAMYAMKQKGiriPEDVAVVSFN 279
Cdd:PRK10653 168 EGFKQAVAAHKFNVLASQPADFDRTKGLNVMQNL----LTAHPDvqAVFAQNDEMALGALRALQTAG---KSDVMVVGFD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1702117912 280 --NEPVSALFSPTLSSI--SQP--IQEMGTETVRLLLRElNATDTNIPKETKV 326
Cdd:PRK10653 241 gtPDGIKAVNRGKLAATiaQQPdqIGAIGVETADKVLKG-EKVEAKIPVDLKL 292
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
65-314 |
9.84e-08 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 52.64 E-value: 9.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQA-GYSVLVCQTNE--SYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLV 141
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEAnGYELLVKGIKQetDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 142 RKNIPLVLFDRY-------AESIDVSKVIVDNHAAAFKATEHLIEN--GCRRIGFLAGPTQLVLSNQRVAGYRAALAKHG 212
Cdd:cd19970 81 DAGIAVINIDNRldadalkEGGINVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 213 LSVGEQYVFHCDYTQENTIMQTLalmsLPQPPD--GVVIISDRMAYSAMYAMKQKGIRipEDVAVVSFNNEP--VSALFS 288
Cdd:cd19970 161 MKIVASQSANWEIDEANTVAANL----LTAHPDirGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNIPavRPLLKD 234
|
250 260
....*....|....*....|....*..
gi 1702117912 289 PT-LSSISQPIQEMGTETVRLLLRELN 314
Cdd:cd19970 235 GKmLATIDQHPAKQAVYGIEYALKMLN 261
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
65-314 |
2.85e-07 |
|
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.
Pssm-ID: 380529 [Multi-domain] Cd Length: 269 Bit Score: 51.04 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQ----TNESylRETTNIQNLLRSQVEGFIISlSRDTDNYEH-VER 139
Cdd:cd06306 1 KICVLFPHLKDSYWVGVNYGIVDEAKRLGVKLTVYEaggyTNLS--KQISQLEDCVASGADAILLG-AISFDGLDPkVAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 140 LVRKNIPLVLF--DRYAESIDvSKVIVDNHAAAFKATEHLIENGCRR---IGFLAGPTQLVLSNQRVAGYRAALAKHGLS 214
Cdd:cd06306 78 AAAAGIPVIDLvnGIDSPKVA-ARVLVDFYDMGYLAGEYLVEHHPGKpvkVAWFPGPAGAGWAEDREKGFKEALAGSNVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 215 VGEqyVFHCDyTQENTIMQTL--ALMSlpQPPDGVVIISDRMAYSAMYAMKQKGIRipEDVAVVSFN-NEPV-------S 284
Cdd:cd06306 157 IVA--TKYGD-TGKAVQLNLVedALQA--HPDIDYIVGNAVAAEAAVGALREAGLT--GKVKVVSTYlTPGVyrgikrgK 229
|
250 260 270
....*....|....*....|....*....|
gi 1702117912 285 ALFSPTLSSISQpiqemGTETVRLLLRELN 314
Cdd:cd06306 230 ILAAPSDQPVLQ-----GRIAVDQAVRALE 254
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
66-310 |
3.13e-07 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 51.12 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 66 IGVIVPNL---SYHYFSAMLNSIEEAALQAGYSV---LVCQTNESYLretTNIQNLLRSQVEGFIISLSRDtDNYEHVER 139
Cdd:cd01391 2 IGVVTSSLhqiREQFGIQRVEAIFHTADKLGASVeirDSCWHGSVAL---EQSIEFIRDNIAGVIGPGSSS-VAIVIQNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 140 LVRKNIPLVLFDryAESIDVS---------KVIVDNHAAAFKATEHLIENGCRRIGFLAGPtQLVLSNQRVAGYRAALAK 210
Cdd:cd01391 78 AQLFDIPQLALD--ATSQDLSdktlykyflSVVFSDTLGARLGLDIVKRKNWTYVAAIHGE-GLNSGELRMAGFKELAKQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 211 HGLSVGEQYVFHCDyTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRipEDVAVVSFNNEPVS-----A 285
Cdd:cd01391 155 EGICIVASDKADWN-AGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRdevgyE 231
|
250 260
....*....|....*....|....*
gi 1702117912 286 LFSPTLSSISQPIQEMGTETVRLLL 310
Cdd:cd01391 232 VEANGLTTIKQQKMGFGITAIKAMA 256
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
68-311 |
3.19e-07 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 51.04 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 68 VIVPNLSYH-YFSAMLNSIEEAALQAGYSVLVCQTNESYLRE-TTNIQNLLRSQVEGFIISLSrDTDNYEHV-ERLVRKN 144
Cdd:cd06314 3 ALVPKGLNNpFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEqVQLIEDLIARGVDGIAISPN-DPEAVTPViNKAADKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 145 IPLVLFDRYAESidvSKVI----VDNHAAAFKATEHLIE---NGCRRIGFLAGPTQLVLsNQRVAGYRAALAKHGlsvGE 217
Cdd:cd06314 82 IPVITFDSDAPD---SKRLayigTDNYEAGREAGELMKKalpGGGKVAIITGGLGADNL-NERIQGFKDALKGSP---GI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 218 QYVfhCDYTQENTIMQTLALMS--LPQPPD--GVVIISDRMAYSAMYAMKQKGIRipEDVAVVSFNNEPvsalfsPTLSS 293
Cdd:cd06314 155 EIV--DPLSDNDDIAKAVQNVEdiLKANPDldAIFGVGAYNGPAIAAALKDAGKV--GKVKIVGFDTLP------ETLQG 224
|
250 260
....*....|....*....|....*...
gi 1702117912 294 I----------SQPIqEMGTETVRLLLR 311
Cdd:cd06314 225 IkdgviaatvgQRPY-EMGYLSVKLLYK 251
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
65-279 |
8.51e-07 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 49.72 E-value: 8.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIIslsrDTDNYEHVERLVRK- 143
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLIL----NPVDPEGLTPAVKAa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 ---NIPLVLFDRYAESID--VSKVIVDNHAAAFKATEHLIE---NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKHGLS- 214
Cdd:cd06318 77 kaaGIPVITVDSALDPSAnvATQVGRDNKQNGVLVGKEAAKalgGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYQLRk 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1702117912 215 --------VGEQYvfhCDYTQENTI--MQTLalmsLPQPPD--GVVIISDRMAYSAMYAMKQKGIRipEDVAVVSFN 279
Cdd:cd06318 157 ygksnikvVAQPY---GNWIRSGAVaaMEDL----LQAHPDinVVYAENDDMALGAMKALKAAGML--DKVKVAGAD 224
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
112-266 |
6.43e-06 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 46.84 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 112 IQNLLRSQVEGFIISLSRDTDNYEHVERLVRKNIPLVLFDR-YAESIDVSKVIVDNHAAAFKATEHLIE--NGCRRIGFL 188
Cdd:cd20004 50 IEYFIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSdLGGDAVISFVATDNYAAGRLAAKRMAKllNGKGKVALL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 189 -----AGPTqlvlsNQRVAGYRAALAKH--GLSV-GEQYVfhcDYTQENTIMQTL-ALMSLPQpPDGVVIISDRMAYSAM 259
Cdd:cd20004 130 rlakgSAST-----TDRERGFLEALKKLapGLKVvDDQYA---GGTVGEARSSAEnLLNQYPD-VDGIFTPNESTTIGAL 200
|
....*..
gi 1702117912 260 YAMKQKG 266
Cdd:cd20004 201 RALRRLG 207
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
65-210 |
6.84e-06 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 46.95 E-value: 6.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTN-IQNLLRSQVEGFIISLSRDTDNYEHVERLVRK 143
Cdd:cd19969 1 YYVMVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITaIEQAIAKNPDGIAVSAIDPEALTPTINKAVDA 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 144 NIPLVLFDRYA-ESIDVSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSnQRVAGYRAALAK 210
Cdd:cd19969 81 GIPVVTFDSDApESKRISYVGTDNYEAGYAAAEKLAEllGGKGKVAVLTGPGQPNHE-ERVEGFKEAFAE 149
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
65-282 |
8.52e-06 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380547 [Multi-domain] Cd Length: 317 Bit Score: 46.83 E-value: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAA---LQAGYSVLVCQTNESYLREttNIQNLLRSQ--VEGFIISlsrdtdNYEHV-E 138
Cdd:cd06324 1 RVVFINPGKEDEPFWQNVTRFMQAAakdLGIELEVLYANRNRFKMLE--LAEELLARPpkPDYLILV------NEKGVaP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 139 RLVR----KNIPLVLFDRYAESIDVSK--------------VIVDNHAAAFKATEHLIENGcrRIGFLAGPTQLVL---- 196
Cdd:cd06324 73 ELLElaeqAKIPVFLINNDLTDEERALlgkprekfkywlgsIVPDNEQAGYLLAKALIKAA--RKKSDDGKIRVLAisgd 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 197 -----SNQRVAGYRAALAKHGLSVGEQYVfHCDYTQENTIMQTLALMSLPQPPDGVVIISDRMAYSAMYAMKQKGIRIPE 271
Cdd:cd06324 151 kstpaSILREQGLRDALAEHPDVTLLQIV-YANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGK 229
|
250
....*....|.
gi 1702117912 272 DVAVVSFNNEP 282
Cdd:cd06324 230 DVLVGGIDWSP 240
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
65-297 |
1.14e-05 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380654 [Multi-domain] Cd Length: 313 Bit Score: 46.53 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAA---LQAGY--SVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVER 139
Cdd:cd19999 1 VIGVSNGYVGNEWRAQMIADFEEVAaeyKEEGVisDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 140 LVRKNIPLVLFDRYAESIDVSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKH-GLSVg 216
Cdd:cd19999 81 AQAAGILVVSFDQPVSSPDAINVVIDQYKWAAIQAQWLAEqlGGKGNIVAINGVAGNPANEARVKAADDVFAKYpGIKV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 217 EQYVFH-CDYTQENTIMQTLaLMSLPQpPDGvVIISDRMAYSAMYAMKQKGIRIPEDV--AVVSFNNEpVSALFSPTLSS 293
Cdd:cd19999 160 LASVPGgWDQATAQQVMATL-LATYPD-IDG-VLTQDGMAEGVLRAFQAAGKDPPVMTgdYRKGFLRK-WKELDLPDFES 235
|
....
gi 1702117912 294 ISQP 297
Cdd:cd19999 236 IGVV 239
|
|
| PBP1_ABC_xylose_binding-like |
cd19993 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
65-268 |
1.12e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380648 [Multi-domain] Cd Length: 287 Bit Score: 43.23 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVivpnlSYHYFSAMLNSIEEAAL-----QAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIIsLSRDTDNY-EHVE 138
Cdd:cd19993 1 VVGV-----SWSNFQEERWKTDEAAMkkaleKAGAKYISADAQSSAEKQLDDIESLISQGAKALIV-LAQDGDAIlPAVE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 139 RLVRKNIPLVLFDRYAESIDVSKVIVDNHAAA-FKATEHLIENGCRRIGFLAG-PTQlvlSNQRV--AGYRAALAKHGLS 214
Cdd:cd19993 75 KAAAEGIPVIAYDRLIENPIAFYISFDNVEVGrMQARGVLKAKPEGNYVFIKGsPTD---PNADFlrAGQMEVLQPAIDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1702117912 215 -----VGEQYVFHCDYTQENTIMQTLaLMSLPQPPDGVVIISDRMAYSAMYAMKQKGIR 268
Cdd:cd19993 152 gkikiVGEQYTDGWKPANAQKNMEQI-LTANNNKVDAVVASNDGTAGGAVAALAAQGLA 209
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
65-314 |
1.94e-04 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 42.60 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLV-CQTNESYLRETTNI-QNLLRSQVEGFIISLSrDTDNYEHVERLVR 142
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFlGPATEADIAGQVNLvENAISRKPDAIVLAPN-DTAALVPAVEAAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 143 KNIPLVLFDRYAESID-VSKVIVDNHAAAFKATEHLIE------NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKH--GL 213
Cdd:cd20008 80 AGIPVVLVDSGANTDDyDAFLATDNVAAGALAADELAEllkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKypDI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 214 S-VGEQYvfhCDYTQENTIMQTLALMSlpQPPDGVVIISD--RMAYSAMYAMKQKGIRipEDVAVVSFNNEP--VSALFS 288
Cdd:cd20008 160 EiVDVQY---SDGDIAKALNQTTDLLT--ANPDLVGIFGAnnPSAVGVAQALAEAGKA--GKIVLVGFDSSPdeVALLKS 232
|
250 260
....*....|....*....|....*...
gi 1702117912 289 PTLSSI--SQPIQeMGTETVRLLLRELN 314
Cdd:cd20008 233 GVIKALvvQDPYQ-MGYEGVKTAVKALK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
65-210 |
2.07e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 42.36 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRKN 144
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1702117912 145 IPLVLFDRYAESIDV-SKVIVDNHAAAFK----ATEHLIEN--GCRRIGFLAGPTQLVlSNQRVAGYRAALAK 210
Cdd:cd06317 81 IPVIAYDAVIPSDFQaAQVGVDNLEGGKEigkyAADYIKAElgGQAKIGVVGALSSLI-QNQRQKGFEEALKA 152
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
65-277 |
2.78e-03 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 38.79 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAALQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIIslsrDTDNYE----HVERL 140
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIV----VPVDADalapAVEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 141 VRKNIPLVLFDRYAESID-VSKVIVDNHAAAFKATEHLIE--NGCRRIGFLAGPTQLVLSNQRVAGYRAALAKH-GLSVG 216
Cdd:cd06313 77 KEAGIPLVGVNALIENEDlTAYVGSDDVVAGELEGQAVADrlGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1702117912 217 EQYVfhCDYTQEN--TIMQTLaLMSLPQPPDGVVIISDRMAYSAMYAMKQKGIripEDVAVVS 277
Cdd:cd06313 157 AEQT--ANWSRDEamSLMENW-LQAYGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVG 213
|
|
| MntR |
COG1321 |
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription]; |
2-31 |
3.62e-03 |
|
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
Pssm-ID: 440932 [Multi-domain] Cd Length: 135 Bit Score: 37.11 E-value: 3.62e-03
10 20 30
....*....|....*....|....*....|
gi 1702117912 2 KNTPVTIKDIARSLNISISTVSRALRGMQE 31
Cdd:COG1321 21 EGGPVRTSDIAERLGVSPPSVTEMLKKLEE 50
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
65-152 |
7.45e-03 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 37.56 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1702117912 65 TIGVIVPNLSYHYFSAMLNSIEEAA-LQAGYSVLVCQTNESYLRETTNIQNLLRSQVEGFIISLSRDTDNYEHVERLVRK 143
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAkAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAA 81
|
....*....
gi 1702117912 144 NIPLVLFDR 152
Cdd:cd01539 82 NIPVIFFNR 90
|
|
| |
