|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
4-330 |
0e+00 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 747.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 4 MKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 83
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 84 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYPSIPTVMMDWAPFDGTSDLIQDNSLL 163
Cdd:PRK10423 81 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMQRYPSVPTVMMDWAPFDGDSDLIQDNSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 164 GGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVF 243
Cdd:PRK10423 161 GGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRPQAVF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 244 IGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPV 323
Cdd:PRK10423 241 TGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPE 320
|
....*..
gi 489959095 324 LMERGSV 330
Cdd:PRK10423 321 LMERGSV 327
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
1-330 |
4.76e-158 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 445.32 E-value: 4.76e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 1 MATMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRG 80
Cdd:PRK10703 1 MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 81 VERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYPSIPTVMMDWAPFDGT-SDLIQD 159
Cdd:PRK10703 81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYRHIPMVVMDWGEAKADfTDAIID 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 160 NSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRP 239
Cdd:PRK10703 161 NAFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 240 QAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQ 319
Cdd:PRK10703 241 TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIE 320
|
330
....*....|.
gi 489959095 320 LTPVLMERGSV 330
Cdd:PRK10703 321 VHPRLVERRSV 331
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-330 |
2.02e-150 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 425.77 E-value: 2.02e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 1 MATMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRG 80
Cdd:COG1609 3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 81 VERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYpSIPTVMMDWAPFDGTSDLIQDN 160
Cdd:COG1609 83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEA-GIPVVLIDRPLPDPGVPSVGVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 161 SLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQ 240
Cdd:COG1609 162 NRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 241 AVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQL 320
Cdd:COG1609 242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321
|
330
....*....|
gi 489959095 321 TPVLMERGSV 330
Cdd:COG1609 322 PPELVVREST 331
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
61-329 |
7.06e-145 |
|
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: 409.34 E-value: 7.06e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYPSI 140
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDF 220
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 221 EFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELA 300
Cdd:cd06275 161 EPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGELA 240
|
250 260
....*....|....*....|....*....
gi 489959095 301 IDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06275 241 VELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
61-325 |
1.11e-108 |
|
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: 317.15 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYpSI 140
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAA-GI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDF 220
Cdd:cd06267 80 PVVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 221 EFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELA 300
Cdd:cd06267 160 SEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAA 239
|
250 260
....*....|....*....|....*
gi 489959095 301 IDVLIHRMAQPTLQQQRLQLTPVLM 325
Cdd:cd06267 240 AELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-330 |
1.93e-95 |
|
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: 283.73 E-value: 1.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRyPSI 140
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAA-RGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDF 220
Cdd:cd06285 80 PVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 221 EFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELA 300
Cdd:cd06285 160 TIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRA 239
|
250 260 270
....*....|....*....|....*....|
gi 489959095 301 IDVLIHRMAQPTLQQQRLQLTPVLMERGSV 330
Cdd:cd06285 240 AELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
61-329 |
1.66e-90 |
|
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: 271.33 E-value: 1.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLctETHQPSKEIIQRYPSI 140
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILL--SGRLDAELLSELSKRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMM-DWAPFDGTSDLIQDNsLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGD 219
Cdd:cd06284 79 PIVQCcEYIPDSGVPSVSIDN-EAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 220 FEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGEL 299
Cdd:cd06284 158 FSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGET 237
|
250 260 270
....*....|....*....|....*....|
gi 489959095 300 AIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06284 238 AAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-329 |
9.17e-89 |
|
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: 266.81 E-value: 9.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYPSI 140
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDF 220
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 221 EFNGGFEAMQKLLAQEPrPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELA 300
Cdd:cd19976 161 SLEGGYKAAEELLKSKN-PTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239
|
250 260
....*....|....*....|....*....
gi 489959095 301 IDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd19976 240 AKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
61-329 |
7.00e-86 |
|
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: 259.37 E-value: 7.00e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLcteTHQPSKEIIQRYpSI 140
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILG---SHSLDIEEYKKL-NI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWAPFDG----TSDLIQdnsllGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRI 216
Cdd:cd06291 77 PIVSIDRYLSEGipsvSSDNYQ-----GGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEID 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 217 TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDEL 296
Cdd:cd06291 152 ENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEM 231
|
250 260 270
....*....|....*....|....*....|...
gi 489959095 297 GELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06291 232 AKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
61-329 |
2.54e-84 |
|
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: 255.55 E-value: 2.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLI-TASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQpsKEIIQRYPS 139
Cdd:cd06288 1 TIGLITdDIATTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHRE--VTLPPELTD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMD-WAPFDGTSDLIQDNSLlGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITG 218
Cdd:cd06288 79 IPLVLLNcFDDDPSLPSVVPDDEQ-GGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 219 DFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGE 298
Cdd:cd06288 158 DWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGR 237
|
250 260 270
....*....|....*....|....*....|.
gi 489959095 299 LAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06288 238 RAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
1.16e-80 |
|
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: 246.03 E-value: 1.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPS-KEIIQRypS 139
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHlARLRAR--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMD--WAPFDGTSDLIQDnsLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRIT 217
Cdd:cd06293 79 TAVVLLDrpAPGPAGCSVSVDD--VQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVREL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 218 GDFEFN--GGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDE 295
Cdd:cd06293 157 SAPDANaeLGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYE 236
|
250 260 270
....*....|....*....|....*....|....
gi 489959095 296 LGELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06293 237 LGRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
61-327 |
1.70e-80 |
|
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: 245.51 E-value: 1.70e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTetHQPSKEIIQRYPSI 140
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSR--ALSDEELILIAEKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMdwapFDGTSDLIQDNSL-----LGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYR 215
Cdd:cd06270 79 PPLVV----INRYIPGLADRCVwldneQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 216 ITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDE 295
Cdd:cd06270 155 IEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEE 234
|
250 260 270
....*....|....*....|....*....|..
gi 489959095 296 LGELAIDVLIHRMAQPTLQQQRlQLTPVLMER 327
Cdd:cd06270 235 MAQAAAELALNLAYGEPLPISH-EFTPTLIER 265
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
4.09e-80 |
|
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: 244.83 E-value: 4.09e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTE-THQPSKEIIqryPS 139
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFgDEELLKLLA---EG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGD 219
Cdd:cd06290 78 IPVVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 220 FEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGEL 299
Cdd:cd06290 158 FTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKT 237
|
250 260 270
....*....|....*....|....*....|.
gi 489959095 300 AIDVLIHRMaQPTLQQQRLQLTPV-LMERGS 329
Cdd:cd06290 238 AAEILLELI-EGKGRPPRRIILPTeLVIRES 267
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
61-329 |
7.11e-78 |
|
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: 239.02 E-value: 7.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNT-EGDEQRMNRNLETLMQKRVDGLLLLctETHQPSKEIIQRYP- 138
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVdEDDPASVREALDRLLSQRVDGIIVI--APDEAVLEALRRLPp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 SIPTVMMDWAPFDGTSDLIQDNSLlGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDgyRITG 218
Cdd:cd01574 79 GLPVVIVGSGPSPGVPTVSIDQEE-GARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPP--VVEG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 219 DFEFNGGFEAMQKLLAQePRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGE 298
Cdd:cd01574 156 DWSAASGYRAGRRLLDD-GPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGR 234
|
250 260 270
....*....|....*....|....*....|.
gi 489959095 299 LAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd01574 235 RAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
61-329 |
1.44e-76 |
|
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: 235.53 E-value: 1.44e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLcteTHQPSKEIIQ--RYP 138
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFA---SGTLTEENKQllKNM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 SIPTVM-MDWAPFDGTSDLIQDNSLLGGDmATQHLIDKGHTRIACITGPL-DKTPARLRLEGYLSAMERAGLAIPDGYRI 216
Cdd:cd19975 78 NIPVVLvSTESEDPDIPSVKIDDYQAAYD-ATNYLIKKGHRKIAMISGPLdDPNAGYPRYEGYKKALKDAGLPIKENLIV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 217 TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDEL 296
Cdd:cd19975 157 EGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEM 236
|
250 260 270
....*....|....*....|....*....|...
gi 489959095 297 GELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd19975 237 GKKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
61-325 |
6.13e-74 |
|
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: 228.95 E-value: 6.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPS-KEIIQRypS 139
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLiEKLVKS--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYrITGD 219
Cdd:cd19977 79 IPVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEEL-IKHV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 220 FEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGEL 299
Cdd:cd19977 158 DRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRK 237
|
250 260
....*....|....*....|....*..
gi 489959095 300 AIDVLIHRM-AQPTLQQQRLQLTPVLM 325
Cdd:cd19977 238 AAELLLDRIeNKPKGPPRQIVLPTELI 264
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
2-330 |
1.71e-73 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 230.27 E-value: 1.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 2 ATMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGmLITASTN---PfySELV 78
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIG-LATTSLAlhaP--SQIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 79 RGVERSCFERGYSLVLCNTE-GDEQRMNRNLETLMQKRVDGLLL---LCTETHQPskeIIQRYPSIPTVMMDWAPfdgTS 154
Cdd:PRK09526 83 AAIKSRADQLGYSVVISMVErSGVEACQAAVNELLAQRVSGVIInvpLEDADAEK---IVADCADVPCLFLDVSP---QS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 155 DL--IQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRitGDFEFNGGFEAMQKL 232
Cdd:PRK09526 157 PVnsVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQPIAVRE--GDWSAMSGYQQTLQM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 233 LAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPT 312
Cdd:PRK09526 235 LREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQGQA 314
|
330
....*....|....*...
gi 489959095 313 lQQQRLQLTPVLMERGSV 330
Cdd:PRK09526 315 -VKGSQLLPTSLVVRKST 331
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
61-327 |
2.32e-72 |
|
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: 224.75 E-value: 2.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLL-CTEThqpSKEIIQRY-- 137
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSpAAGT---TAELLRRLka 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 PSIPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRIT 217
Cdd:cd06289 78 WGIPVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 218 GDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELG 297
Cdd:cd06289 158 GPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIG 237
|
250 260 270
....*....|....*....|....*....|
gi 489959095 298 ELAIDVLIHRMAQPTLQQQRLQLTPVLMER 327
Cdd:cd06289 238 RRAARLLLRRIEGPDTPPERIIIEPRLVVR 267
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
61-329 |
3.76e-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: 224.46 E-value: 3.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRyPSI 140
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIA-QGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWA-PFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGD 219
Cdd:cd06299 80 PVVFVDREvEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 220 FEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGEL 299
Cdd:cd06299 160 FRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRR 239
|
250 260 270
....*....|....*....|....*....|
gi 489959095 300 AIDVLIHRMAQPTlQQQRLQLTPVLMERGS 329
Cdd:cd06299 240 AVELLLALIENGG-RATSIRVPTELIPRES 268
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
61-329 |
5.44e-72 |
|
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: 224.36 E-value: 5.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPS------KEII 134
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPNpnldlyEELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 135 QRypSIPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITgPLDKTPARLRLEGYLSAMERAGLAIPDGY 214
Cdd:cd01541 81 KK--GIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIF-KSDDLQGVERYQGFIKALREAGLPIDDDR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 215 RI---TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQ 291
Cdd:cd01541 158 ILwysTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVVH 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 489959095 292 PKDELGELAIDVLIHRMAQPTLQQQRLqLTPVLMERGS 329
Cdd:cd01541 238 PKEELGRKAAELLLRMIEEGRKPESVI-FPPELIERES 274
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
61-327 |
1.14e-71 |
|
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: 222.90 E-value: 1.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLlcTETHQPSKEIIQRYPS- 139
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIIL--APSAGPSRELKRLLKHg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPfDGTS-DLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITG 218
Cdd:cd06280 79 IPIVLIDREV-EGLElDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 219 DFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGE 298
Cdd:cd06280 158 DSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGR 237
|
250 260
....*....|....*....|....*....
gi 489959095 299 LAIDVLIHRMAQPTLQQQRLQLTPVLMER 327
Cdd:cd06280 238 IAAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
61-329 |
7.61e-71 |
|
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: 221.28 E-value: 7.61e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVL--CNTeGDEQRMNRNLETLMQKRVDGLLL---LCTetHQPSKEIIQ 135
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDS-DDEDLADRLRRFLSRSRPDGVILtppLSD--DPALLDALD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 136 RYpSIPTVMMdwAPF--DGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDG 213
Cdd:cd01545 78 EL-GIPYVRI--APGtdDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 214 YRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPK 293
Cdd:cd01545 155 LVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 489959095 294 DELGELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd01545 235 AEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
62-324 |
4.80e-70 |
|
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: 219.04 E-value: 4.80e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYPSIP 141
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQNVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 142 TVMMDWAPFDGT-SDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDF 220
Cdd:cd01537 82 VVFFDKEPSRYDkAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 221 EFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELA 300
Cdd:cd01537 162 DTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKTT 241
|
250 260
....*....|....*....|....
gi 489959095 301 IDVLIHRMAQPTLQQQRLQLTPVL 324
Cdd:cd01537 242 FDLLLNLADNWKIDNKVVRVPYVL 265
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
28-330 |
1.85e-69 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 218.71 E-value: 1.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 28 VSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSCFERGYsLVLCnteGDEQRMNRN 107
Cdd:PRK11041 4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGY-LVLI---GDCAHQNQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 108 LET----LMQKRVDGLLLLctETHQP---SKEIIQRYPsiPTVMM-DWAPFDGTSDLIQDNsLLGGDMATQHLIDKGHTR 179
Cdd:PRK11041 80 EKTfvnlIITKQIDGMLLL--GSRLPfdaSKEEQRNLP--PMVMAnEFAPELELPTVHIDN-LTAAFEAVNYLHELGHKR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 180 IACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQ 259
Cdd:PRK11041 155 IACIAGPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKR 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489959095 260 AGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPVLMERGSV 330
Cdd:PRK11041 235 MGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
61-329 |
2.81e-69 |
|
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: 217.14 E-value: 2.81e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITAS----TNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPskeiiqR 136
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDP------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 137 YPS-----IPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIP 211
Cdd:cd06292 75 VRYlheagVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 212 DGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQ 291
Cdd:cd06292 155 PGLVVEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQ 234
|
250 260 270
....*....|....*....|....*....|....*....
gi 489959095 292 PKDELGELAIDVLIHRM-AQPTLQQQRLqLTPVLMERGS 329
Cdd:cd06292 235 PIDEIGRAVVDLLLAAIeGNPSEPREIL-LQPELVVRES 272
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
7.85e-68 |
|
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: 213.14 E-value: 7.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYpSI 140
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQR-QV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMdWApFDGTSDLIQ---DNSLlGGDMATQHLIDKGHTRIACITGPLDKTP-ARLRLEGYLSAMERAGLAIPDGYRI 216
Cdd:cd06273 80 PYVLT-WS-YDEDSPHPSigfDNRA-AAARAAQHLLDLGHRRIAVISGPTAGNDrARARLAGIRDALAERGLELPEERVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 217 TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDEL 296
Cdd:cd06273 157 EAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREI 236
|
250 260 270
....*....|....*....|....*....|....
gi 489959095 297 GELAIDVLIHRMA-QPTLQQQRLQLTpvLMERGS 329
Cdd:cd06273 237 GELAARYLLALLEgGPPPKSVELETE--LIVRES 268
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
61-329 |
3.81e-67 |
|
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: 211.61 E-value: 3.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITAS-----TNPFYSELVRGVERSCFERGYSLVLCNTEGDEQrmnrnleTLMQKRVDGLLLLCTETHQPSKEIIQ 135
Cdd:cd01544 1 TIGIIQWYSeeeelEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDL-------ESLLEKVDGIIAIGKFSKEEIEKLKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 136 RYPSIptVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITG----PLDKTPAR-LRLEGYLSAMERAGLAI 210
Cdd:cd01544 74 LNPNI--VFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGkeytSDDGEEIEdPRLRAFREYMKEKGLYN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 211 PDgYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIH 290
Cdd:cd01544 152 EE-YIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVH 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 489959095 291 QPKDELGELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd01544 231 IPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
2.21e-66 |
|
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: 209.70 E-value: 2.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQrMNRNLETLMQKRVDGLLLLcteTHQPSKEIIQRYPS- 139
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDGVIVT---SATLSSELAEECARr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 -IPTVMMDWAPFDGTSDLIQ-DNSLlGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDgyRIT 217
Cdd:cd06278 77 gIPVVLFNRVVEDPGVDSVScDNRA-GGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPPA--VEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 218 GDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQAL-YQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDEL 296
Cdd:cd06278 154 GDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEM 233
|
250 260 270
....*....|....*....|....*....|...
gi 489959095 297 GELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06278 234 AEAAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-330 |
3.21e-66 |
|
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: 209.40 E-value: 3.21e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLL-LCTETHQPSKEIIQRYPs 139
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILtPGDEDDPELAAALARLD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPfDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGD 219
Cdd:cd06281 80 IPVVLIDRDL-PGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 220 FEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGEL 299
Cdd:cd06281 159 FSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRA 238
|
250 260 270
....*....|....*....|....*....|..
gi 489959095 300 AIDVLIHRMAQPTLQQ-QRLQLTPVLMERGSV 330
Cdd:cd06281 239 AAELLLDRIEGPPAGPpRRIVVPTELILRDSC 270
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
61-330 |
3.84e-65 |
|
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: 206.36 E-value: 3.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLcNTEGDEQRMNRN-LETLMQKRVDGLLLLCTETHQPSKEIIQRyPS 139
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVV-TATRAGRAPVDDwVRRAVARGSAGVVLVTSDPTSRQLRLLRS-AG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPFDGTSDL-IQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITG 218
Cdd:cd06296 79 IPFVLIDPVGEPDPDLPsVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 219 DFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGE 298
Cdd:cd06296 159 DFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGA 238
|
250 260 270
....*....|....*....|....*....|..
gi 489959095 299 LAIDVLIHRMAQPTLQQQRLQLTPVLMERGSV 330
Cdd:cd06296 239 VAVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
61-329 |
4.99e-63 |
|
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: 201.18 E-value: 4.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRyPSI 140
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRA-AGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTV-MMDWA--PFD---GTSdliqdNSLLGGDMAtQHLIDKGHTRIACITGPLDKTP-ARLRLEGYLSAMERAGLAIPDG 213
Cdd:cd01575 80 PVVeTWDLPddPIDmavGFS-----NFAAGRAMA-RHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLPLV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 214 YRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPK 293
Cdd:cd01575 154 LLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPR 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 489959095 294 DELGELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd01575 234 YEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
61-305 |
2.40e-57 |
|
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: 186.25 E-value: 2.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITAST-----NPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNrNLETLMQ-KRVDGLLLLCTETHQPSKEII 134
Cdd:cd06294 1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLE-EVKRMVRgRRVDGFILLYSKEDDPLIEYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 135 QRYpSIPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGY 214
Cdd:cd06294 80 KEE-GFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 215 RITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKD 294
Cdd:cd06294 159 ILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPY 238
|
250
....*....|.
gi 489959095 295 ELGELAIDVLI 305
Cdd:cd06294 239 ELGREAAKLLI 249
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
1-330 |
9.58e-57 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 187.27 E-value: 9.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 1 MATMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRG 80
Cdd:PRK10727 1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 81 VERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLlctetHQ---PSKEIIQRYPSIP-TVMMDWAPFDGTSDL 156
Cdd:PRK10727 81 VEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVV-----HAkmiPDAELASLMKQIPgMVLINRILPGFENRC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 157 IQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQE 236
Cdd:PRK10727 156 IALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 237 PRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQ 316
Cdd:PRK10727 236 RNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLPEI 315
|
330
....*....|....
gi 489959095 317 RLQLTPVLMERGSV 330
Cdd:PRK10727 316 TNVFSPTLVRRHSV 329
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
57-305 |
5.06e-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: 183.22 E-value: 5.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 57 NQTRTIGMLI-------TASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRmnrNLETLMQKRVDGLLLL-CTETHQ 128
Cdd:cd06295 1 QRSRTIAVVVpmdphgdQSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQ---LARLLDSGRADGLIVLgQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 129 PSKEIIQRypSIPTVMmdWAPFDGTSDLI---QDNsLLGGDMATQHLIDKGHTRIACITGPLDKTPArLRLEGYLSAMER 205
Cdd:cd06295 78 ALRELAQQ--GLPMVV--WGAPEDGQSYCsvgSDN-VKGGALATEHLIEIGRRRIAFLGDPPHPEVA-DRLQGYRDALAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 206 AGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPP 285
Cdd:cd06295 152 AGLEADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPP 231
|
250 260
....*....|....*....|
gi 489959095 286 LTTIHQPKDELGELAIDVLI 305
Cdd:cd06295 232 LTTVRQDLALAGRLLVEKLL 251
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
5.79e-55 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 180.17 E-value: 5.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLL-LCTETHQPSKEIIQRYpS 139
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILtVGDAQGSEALELLEEE-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMM-DWAPFDGTSDLIQDNSLLGGDmATQHLIDKGHTRIACITGPLDKTP-ARLRLEGYLSAMERAGLAIPDGYRIt 217
Cdd:cd06282 80 VPYVLLfNQTENSSHPFVSVDNRLASYD-VAEYLIALGHRRIAMVAGDFSASDrARLRYQGYRDALKEAGLKPIPIVEV- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 218 gDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELG 297
Cdd:cd06282 158 -DFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMG 236
|
250 260 270
....*....|....*....|....*....|..
gi 489959095 298 ELAIDVLIHRMAQPTLQQQRlQLTPVLMERGS 329
Cdd:cd06282 237 RAAADLLLAEIEGESPPTSI-RLPHHLREGGS 267
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
9.56e-55 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380629 [Multi-domain] Cd Length: 270 Bit Score: 179.67 E-value: 9.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLIT---ASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCtETHQPSKEIIQRY 137
Cdd:cd19974 1 NIAVLIPerfFGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILG-EISKEYLEKLKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 PsIPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACItGPLDKTPA-RLRLEGYLSAMERAGLAIPDGYRI 216
Cdd:cd19974 80 G-IPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFV-GDINYTSSfMDRYLGYRKALLEAGLPPEKEEWL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 217 TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDEL 296
Cdd:cd19974 158 LEDRDDGYGLTEEIELPLKLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDKEAM 237
|
250 260 270
....*....|....*....|....*....|...
gi 489959095 297 GELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd19974 238 GRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
61-327 |
4.24e-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: 177.74 E-value: 4.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLcteTHQPSKEIIQRY--- 137
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIIT---SRENDWEVIEPYaky 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 -----------PSIPTVMMDwaPFDGTSDliqdnsllggdmATQHLIDKGHTRIACITG--PLDKTPARLRLEGYLSAME 204
Cdd:cd06286 78 gpivlceetdsPDIPSVYID--RYEAYLE------------ALEYLKEKGHRKIGYCLGrpESSSASTQARLKAYQDVLG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 205 RAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARymTP 284
Cdd:cd06286 144 EHGLSLREEWIFTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISE--LL 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 489959095 285 PLTTIHQPKDELGELAIDVLIHRMaqPTLQQQRLQLTPVLMER 327
Cdd:cd06286 222 NLTTIDQPLEEMGKEAFELLLSQL--ESKEPTKKELPSKLIER 262
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
61-318 |
1.20e-53 |
|
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: 176.53 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYPsI 140
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLK-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMM--DwapFDGTSDLIQDNSLLGGDMaTQHLIDKGHTRIACITGPL-DKTPARLRLEGYLSAMERAGlaIPDGYRIT 217
Cdd:cd01542 80 PVVVLgqE---HEGFSCVYHDDYGAGKLL-GEYLLKKGHKNIAYIGVDEeDIAVGVARKQGYLDALKEHG--IDEVEIVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 218 GDFEFNGGFEAMQKLLAQEPrPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELG 297
Cdd:cd01542 154 TDFSMESGYEAAKELLKENK-PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAG 232
|
250 260
....*....|....*....|.
gi 489959095 298 ELAIDVLIHRMAQPTLQQQRL 318
Cdd:cd01542 233 EKAAELLLDMIEGEKVPKKQK 253
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
60-329 |
4.02e-53 |
|
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: 175.89 E-value: 4.02e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 60 RTIGMLITASTnPFYSELVRGVERSCFERGYSLVLCNTEGDEQRmNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYpS 139
Cdd:cd06277 8 SDNGDGVVNET-PFFSELIDGIEREARKYGYNLLISSVDIGDDF-DEILKELTDDQSSGIILLGTELEEKQIKLFQDV-S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGD 219
Cdd:cd06277 85 IPVVVVDNYFEDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 220 FEFNGGFEAMQKLLAQEPR-PQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGE 298
Cdd:cd06277 165 VGPEGAYKDMKALLDTGPKlPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGK 244
|
250 260 270
....*....|....*....|....*....|.
gi 489959095 299 LAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06277 245 LAVRRLIEKIKDPDGGTLKILVSTKLVERGS 275
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
61-319 |
5.25e-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: 5.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLI----TASTNPFYSELVRGVERSCFERGYSLVL--CNTEGDEqrmnrnLETLMQ----KRVDGLLLLCTETHQPS 130
Cdd:cd20010 1 AIGLVLpldpGDLGDPFFLEFLAGLSEALAERGLDLLLapAPSGEDE------LATYRRlverGRVDGFILARTRVNDPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 131 KEIIQRYpSIPTVMM---------DWAPFDGTSdliqdnsllGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLS 201
Cdd:cd20010 75 IAYLLER-GIPFVVHgrsesgapyAWVDIDNEG---------AFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 202 AMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDI-ELAR 280
Cdd:cd20010 145 ALAEAGLPVDPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALE 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489959095 281 YMTPPLTTIHQPKDELGELAIDVLIHRMA-QPTLQQQRLQ 319
Cdd:cd20010 225 YFSPPLTTTRSSLRDAGRRLAEMLLALIDgEPAAELQELW 264
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
61-329 |
1.05e-50 |
|
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: 169.70 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLIT-----ASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLmqkrVDGLLLLCTETHQPSKEIIQ 135
Cdd:cd06279 1 AIGVLLPddlsyAFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAA----VDGFIVYGLSDDDPAVAALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 136 RYpSIPTVMMDWAPFDGTSD-LIQDNSllGGDMATQHLIDKGHTRIACITGPLDKTP-----------------ARLRLE 197
Cdd:cd06279 77 RR-GLPLVVVDGPAPPGIPSvGIDDRA--AARAAARHLLDLGHRRIAILSLRLDRGRergpvsaerlaaatnsvARERLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 198 GYLSAMERAGLAIPDGYRI-TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDI 276
Cdd:cd06279 154 GYRDALEEAGLDLDDVPVVeAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDI 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489959095 277 ELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTpvLMERGS 329
Cdd:cd06279 234 PEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPRPVILPTE--LVVRAS 284
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
61-327 |
2.26e-49 |
|
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: 165.80 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLL-LCTETHQPSKEIIQRYps 139
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILqPTGNNNDAYLELAQKG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPAR-LRLEGYLSAMERAGLAIpDGYRITG 218
Cdd:cd06283 79 LPVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRrERLQGFLDALARYNIEG-DVYVIEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 219 DFEfnggfEAMQKLLAQ-----EPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPK 293
Cdd:cd06283 158 EDT-----EDLQQALAAflsqhDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPT 232
|
250 260 270
....*....|....*....|....*....|....
gi 489959095 294 DELGELAIDVLIHRMAQPTLQQQRLQLTPVLMER 327
Cdd:cd06283 233 YEIGKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
1-330 |
9.80e-49 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 166.49 E-value: 9.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 1 MATMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRG 80
Cdd:PRK10401 1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 81 VERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLL----LCTE------THQPSKEIIQRypSIPTVMMDWAPF 150
Cdd:PRK10401 81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVhskaLSDDelaqfmDQIPGMVLINR--VVPGYAHRCVCL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 151 DGTSdliqdnsllGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQ 230
Cdd:PRK10401 159 DNVS---------GARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 231 KLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQ 310
Cdd:PRK10401 230 ELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAG 309
|
330 340
....*....|....*....|
gi 489959095 311 PTLQQQRLQLTPVLMERGSV 330
Cdd:PRK10401 310 NLDPRASHCFMPTLVRRHSV 329
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-328 |
2.75e-47 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 162.57 E-value: 2.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 2 ATMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGV 81
Cdd:PRK10014 7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 82 ERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGlLLLCTETHQPSKEIIQ-RYPSIPTVMMDWAPFDGTSDLIQDN 160
Cdd:PRK10014 87 TEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDG-VVIAGAAGSSDDLREMaEEKGIPVVFASRASYLDDVDTVRPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 161 SLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQ 240
Cdd:PRK10014 166 NMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHNPTIS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 241 AVFIGNDAMAFGAYQALYQAGLRVPDD---------MAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQP 311
Cdd:PRK10014 246 AVVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQRITHE 325
|
330
....*....|....*..
gi 489959095 312 TLQQQRLQLTPVLMERG 328
Cdd:PRK10014 326 ETHSRNLIIPPRLIARK 342
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
171-330 |
3.55e-45 |
|
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: 151.34 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 171 HLIDKGHTRIACIT--GPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMqkLLAQEPRPQAVFIGNDA 248
Cdd:pfam13377 1 HLAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARER--LRWLGALPTAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 249 MAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPVLMERG 328
Cdd:pfam13377 79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158
|
..
gi 489959095 329 SV 330
Cdd:pfam13377 159 ST 160
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
61-329 |
1.88e-43 |
|
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: 150.52 E-value: 1.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYPsI 140
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSP-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVmmdwapFDGTSDLIQ-------DNSLLGGDmATQHLIDKGHTRIACITGPLDKTPAR-LRLEGYLSAMERAGLAIPD 212
Cdd:cd06298 80 PVV------LAGTVDSDHeipsvniDYEQAAYD-ATKSLIDKGHKKIAFVSGPLKEYINNdKKLQGYKRALEEAGLEFNE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 213 GYRITGDFEFNGGFEAMQKLLAQEpRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQP 292
Cdd:cd06298 153 PLIFEGDYDYDSGYELYEELLESG-EPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQP 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 489959095 293 KDELGELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06298 232 LYDIGAVAMRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
61-329 |
1.33e-38 |
|
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: 137.60 E-value: 1.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEgDEQRMNRNLE-TLMQKRVDGLLLLCTETHQPSKEIIQRYpS 139
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLL-SEYRLEKYLRnSTLAYQCDGLVMASLDLTELFEEVIVPT-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDwaPFDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLD----KTPARLRLEGYLSAMERAGLAIPDGYR 215
Cdd:cd06297 79 KPVVLID--ANSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDtvftETVFREREQGFLEALNKAGRPISSSRM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 216 ITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARymTPPLTTIHQPKDE 295
Cdd:cd06297 157 FRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQPVEE 234
|
250 260 270
....*....|....*....|....*....|....
gi 489959095 296 LGELAIDVLIHRMAQPTLQQQRLQLTPVLMERGS 329
Cdd:cd06297 235 MGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
4-330 |
6.59e-38 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 137.85 E-value: 6.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 4 MKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 83
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 84 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGlLLLCTETHQPSKEIIQRYPSIPTVMMdwapFDGTSDLIQ----- 158
Cdd:PRK14987 88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDG-LILTERTHTPRTLKMIEVAGIPVVEL----MDSQSPCLDiavgf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 159 DNSLLGGDMaTQHLIDKGHTRIACITGPLDKTPArLRLEGYLSAMERAGLaIPDGYRITGDFEFNGGFEAMQKLLAQEPR 238
Cdd:PRK14987 163 DNFEAARQM-TTAIIARGHRHIAYLGARLDERTI-IKQKGYEQAMLDAGL-VPYSVMVEQSSSYSSGIELIRQARREYPQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 239 PQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRL 318
Cdd:PRK14987 240 LDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKML 319
|
330
....*....|..
gi 489959095 319 QLTPVLMERGSV 330
Cdd:PRK14987 320 DLGFTLSPGGSI 331
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
71-324 |
3.86e-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: 3.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 71 NPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMN-RNLetLMQKRVDGLLLLCTETHQPSKEIIQRyPSIPTVMMD--- 146
Cdd:cd06271 14 NGTVSE*VSGITEEAGTTGYHLLVWPFEEAES*VPiRDL--VETGSADGVILSEIEPNDPRVQFLTK-QNFPFVAHGrsd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 147 ------WAPFDGTSdliqdnsllGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAipdGYRITGDF 220
Cdd:cd06271 91 *pighaWVDIDNEA---------GAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGLT---GYPLDADT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 221 EFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIE-LARYMTPPLTTIHQPKDELGEL 299
Cdd:cd06271 159 TLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVHAPIAEAGRE 238
|
250 260
....*....|....*....|....*
gi 489959095 300 AIDVLIHRMAQPTLQQQRLQLTPVL 324
Cdd:cd06271 239 LAKALLARIDGEDPETLQVLVQPSL 263
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
2-71 |
4.04e-35 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 122.31 E-value: 4.04e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 2 ATMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTN 71
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
46-305 |
1.81e-32 |
|
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: 122.34 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 46 APSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTE 125
Cdd:COG1879 20 GSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 126 tHQPSKEIIQRY--PSIPTVMMDwAPFDG---TSDLIQDNSLLG---GDMATQHLIDKGhtRIACITGPLDKTPARLRLE 197
Cdd:COG1879 100 -PDALAPALKKAkaAGIPVVTVD-SDVDGsdrVAYVGSDNYAAGrlaAEYLAKALGGKG--KVAILTGSPGAPAANERTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 198 GYLSAM-ERAGLAIPDgyRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvPDDMAIVGYDDI 276
Cdd:COG1879 176 GFKEALkEYPGIKVVA--EQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDGS 251
|
250 260 270
....*....|....*....|....*....|....*
gi 489959095 277 ELAR------YMTpplTTIHQPKDELGELAIDVLI 305
Cdd:COG1879 252 PEALqaikdgTID---ATVAQDPYLQGYLAVDAAL 283
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
1-307 |
1.23e-31 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 120.63 E-value: 1.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 1 MATMKDVARMAGVSTSTVSHVINNDRFVS--EAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLI------TASTNP 72
Cdd:PRK10339 1 MATLKDIAIEAGVSLATVSRVLNDDPTLNvkEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIysyqqeLEINDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 73 FYSELVRGVERSCFERGYSLVLC-NTEGDEQrmnrnletlmQKRVDGLLLLctetHQPSKEIIQRYPSI--PTVMMDWAP 149
Cdd:PRK10339 81 YYLAIRHGIETQCEKLGIELTNCyEHSGLPD----------IKNVTGILIV----GKPTPALRAAASALtdNICFIDFHE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 150 FDGTSDLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIP-DGYRitGDFEFNGGFEA 228
Cdd:PRK10339 147 PGSGYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQVVREeDIWR--GGFSSSSGYEL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489959095 229 MQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHR 307
Cdd:PRK10339 225 AKQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEK 303
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
61-306 |
2.46e-31 |
|
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: 118.44 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTEThQPSKEIIQRYPS- 139
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDS-EALVPAVKKANAa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 -IPTVMMDwAPFDGTSDLI----QDNSLLG---GDMATQHLIDKGhtRIACITGPLDKTPARLRLEGYLSAMERAG---- 207
Cdd:cd01536 80 gIPVVAVD-TDIDGGGDVVafvgTDNYEAGklaGEYLAEALGGKG--KVAILEGPPGSSTAIDRTKGFKEALKKYPdiei 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 208 LAipdgyRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvPDDMAIVGYDDIELAR------Y 281
Cdd:cd01536 157 VA-----EQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTPEALkaikdgE 229
|
250 260
....*....|....*....|....*
gi 489959095 282 MTPpltTIHQPKDELGELAIDVLIH 306
Cdd:cd01536 230 LDA---TVAQDPYLQGYLAVEAAVK 251
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
59-321 |
1.18e-29 |
|
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: 114.53 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 59 TRTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYP 138
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 SIPTVMM-DWAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTR-IACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRI 216
Cdd:pfam00532 81 GIPVIAAdDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 217 TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAG-LRVPDDM-----AIVGYDDIELARYMT---PPLT 287
Cdd:pfam00532 161 TGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVgiginSVVGFDGLSKAQDTGlylSPLT 240
|
250 260 270
....*....|....*....|....*....|....
gi 489959095 288 TIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLT 321
Cdd:pfam00532 241 VIQLPRQLLGIKASDMVYQWIPKFREHPRVLLIP 274
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
4-315 |
3.74e-28 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 111.51 E-value: 3.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 4 MK--DVARMAGVSTSTVSHVIN---NDRFVSEAIREKVDAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELV 78
Cdd:PRK11303 1 MKldEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 79 RGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLlcTETHQPSKEIIQRYP--SIPTVMMDWA-PFDGTSD 155
Cdd:PRK11303 81 KYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIV--STSLPPEHPFYQRLQndGLPIIALDRAlDREHFTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 156 LIQDNsLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYriTGDFEFNGGFEAMQKLLAQ 235
Cdd:PRK11303 159 VVSDD-QDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREVHYLY--ANSFEREAGAQLFEKWLET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 236 EPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQ 315
Cdd:PRK11303 236 HPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGDNELLDFLPCPVNAVAQQHRLIAERALELALAALDEPRKPK 315
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
61-325 |
5.82e-28 |
|
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: 109.22 E-value: 5.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLL-CTETHQPSKEIIQRypS 139
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVApSTPPDDIYYLCQAA--G 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDwAPFDGT------SDLIQDNSLLggdmaTQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDG 213
Cdd:cd06274 79 LPVVFLD-RPFSGSdapsvvSDNRAGARAL-----TEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 214 YRITGDFEFNGGFEAMQKLLAQEPR-PQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQP 292
Cdd:cd06274 153 WILAEGYDRESGYQLMAELLARLGGlPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQD 232
|
250 260 270
....*....|....*....|....*....|...
gi 489959095 293 KDELGELAIDVLIHRMAQPTLQQQRLqLTPVLM 325
Cdd:cd06274 233 HDEIAEHAFELLDALIEGQPEPGVII-IPPELI 264
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
167-319 |
3.12e-27 |
|
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: 107.62 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 167 MATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGN 246
Cdd:cd20009 108 EAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPPRPDGIICAS 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489959095 247 DAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQ-QRLQ 319
Cdd:cd20009 188 EIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPlQTLE 261
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
61-305 |
1.89e-25 |
|
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: 102.82 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLL-CTETHQPSKEIIQRYPS 139
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISpTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPFDGTSD--LIQDNsLLGGDMATQHLIDK------GHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIP 211
Cdd:cd06319 81 IPVVIADIGTGGGDYVsyIISDN-YDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 212 dGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYDDIELARYMTPPLT---T 288
Cdd:cd06319 160 -ALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPEALDLIKDGKldgT 236
|
250
....*....|....*..
gi 489959095 289 IHQPKDELGELAIDVLI 305
Cdd:cd06319 237 VAQQPFGMGARAVELAI 253
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
115-327 |
3.25e-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: 99.37 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 115 RVDGLLLlcTETHQPSKEIIQR-YPSIPTVMMDwAPFDGTSDLIQDNSLLGgDMATQHLIDKGHTRIACITGPLDKTPAR 193
Cdd:cd06272 56 RFDGVIV--FGISDSDIEYLNKnKPKIPIVLYN-RESPKYSTVNVDNEKAG-RLAVLLLIQKGHKSIAYIGNPNSNRNQT 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 194 LRLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGY 273
Cdd:cd06272 132 LRGKGFIETCEKHGIHLSDSIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSY 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489959095 274 DDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPVLMER 327
Cdd:cd06272 212 DNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFR 265
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
61-316 |
7.49e-24 |
|
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: 98.52 E-value: 7.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCT--ETHQPSKEIIQRyP 138
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTdsDAVSPAVEEANE-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 SIPTVMMDWAPFDG-TSDLIQDNSLLGGDMATQHLIDKGHTR--IACITGPLDKTPARLRLEGYLSAMERAG----LAip 211
Cdd:cd06323 80 GIPVITVDRSVTGGkVVSHIASDNVAGGEMAAEYIAKKLGGKgkVVELQGIPGTSAARERGKGFHNAIAKYPkinvVA-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 212 dgyRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGlrvPDDMAIVGYDDIELA------RYMtpp 285
Cdd:cd06323 158 ---SQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTPDAvkavkdGKL--- 228
|
250 260 270
....*....|....*....|....*....|.
gi 489959095 286 LTTIHQPKDELGELAIDVLIHRMAQPTLQQQ 316
Cdd:cd06323 229 AATVAQQPEEMGAKAVETADKYLKGEKVPKK 259
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
61-276 |
2.18e-21 |
|
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: 91.90 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPS---KEIIQRy 137
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDpvlKEAKDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 pSIPTVMMD----------WAPFDGtSDLIQDNSLLGGDMATQHLIDKGHtrIACITGPLDKTPARLRLEGYLSAMERAG 207
Cdd:cd06309 80 -GIPVILVDrtidgedgslYVTFIG-SDFVEEGRRAAEWLVKNYKGGKGN--VVELQGTAGSSVAIDRSKGFREVIKKHP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489959095 208 laipdGYRI----TGDFEFNGGFEAMQKLLAQEPRP-QAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDI 276
Cdd:cd06309 156 -----NIKIvasqSGNFTREKGQKVMENLLQAGPGDiDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQ 224
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
5-55 |
2.63e-21 |
|
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.
Pssm-ID: 143331 [Multi-domain] Cd Length: 52 Bit Score: 85.15 E-value: 2.63e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489959095 5 KDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPSALARSLK 55
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLR 51
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
3-48 |
2.87e-21 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 85.00 E-value: 2.87e-21
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489959095 3 TMKDVARMAGVSTSTVSHVINNDRFVSEAIREKVDAAIKELNYAPS 48
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
62-330 |
4.70e-21 |
|
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: 90.72 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITASTNPFYsELVRGVERSCFERGY-SLVLcntegDEQRMNRNLETLMQKRVDGLLllCTETHQPSKEIIQRYpSI 140
Cdd:cd01543 2 VALLLETSRGYGR-RLLRGIARYAREHGPwSLYL-----EPPGYEELLDLLKGWKGDGII--ARLDDPELAEALRRL-GI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWA-PFDGTSDLIQDNSLLGgDMATQHLIDKGHTRIACItGPLDKTPARLRLEGYLSAMERAGLAIpDGYRITGD 219
Cdd:cd01543 73 PVVNVSGSrPEPGFPRVTTDNEAIG-RMAAEHLLERGFRHFAFC-GFRNAAWSRERGEGFREALREAGYEC-HVYESPPS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 220 FEFNGGFEAMQKL---LAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYDDIELARYMT-PPLTTIHQPKDE 295
Cdd:cd01543 150 GSSRSWEEEREELadwLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSsPPLSSIALDAEQ 229
|
250 260 270
....*....|....*....|....*....|....*
gi 489959095 296 LGELAIDVLiHRMaqptLQQQRLQLTPVLMERGSV 330
Cdd:cd01543 230 IGYEAAELL-DRL----MRGERVPPEPILIPPLGV 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-302 |
3.99e-20 |
|
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: 88.46 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFER-GYSLVL--CNTEGDEQRMNRNLETLMQKRVDGLLLLCTEthqpSKEIIqry 137
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKEAnGYELLVkgIKQETDIEQQIAIVENLIAQKVDAIVIAPAD----SKALV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 PS--------IPTVMMDWA-------------PFDGTsdliqDNSlLGGDMATQHLIDK--GHTRIACITGPLDKTPARL 194
Cdd:cd19970 74 PVlkkavdagIAVINIDNRldadalkegginvPFVGP-----DNR-QGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 195 RLEGYLSAMERAGLAIPDgyRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYD 274
Cdd:cd19970 148 RKAGFLKAFEEAGMKIVA--SQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFD 223
|
250 260 270
....*....|....*....|....*....|.
gi 489959095 275 DIELAR-YMTPP--LTTIHQPKDELGELAID 302
Cdd:cd19970 224 NIPAVRpLLKDGkmLATIDQHPAKQAVYGIE 254
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
73-329 |
1.14e-19 |
|
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: 87.09 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 73 FYSELVRGVERSCFERGYSLVLCNTEGDeqrmNRNLETLmqkRVDGLLLLCTETHQP-SKEIIQRypSIPTVMMDWAPFD 151
Cdd:cd06287 21 FMMEVAAAAAEEALEHDLALVLVPPLHH----VSMLDAL---DVDGAIVVEPTVEDPiLARLRQR--GVPVVSIGRAPGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 152 GTS-DLIQDNSLLGGDMATQHLIDKGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAiPDGYRITGDFEFNGGFEAMQ 230
Cdd:cd06287 92 DEPvPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRFAQEYGTT-PVVYKVPESEGERAGYEAAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 231 KLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVG-YDDIElARYMTPPLTTIHQPKDELGELAIDVLIHRMA 309
Cdd:cd06287 171 ALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTrYDGIR-ARTADPPLTAVDLHLDRVARTAIDLLFASLS 249
|
250 260
....*....|....*....|
gi 489959095 310 QPTlQQQRLQLTPVLMERGS 329
Cdd:cd06287 250 GEE-RSVEVGPAPELVVRAS 268
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
40-302 |
1.40e-19 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 87.07 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 40 IKELNYAPSALARSLKLNQT----RTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKR 115
Cdd:PRK10653 3 MKKLATLVSAVALSATVSANamakDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 116 VDGLLLLCTETHQPSKEI-IQRYPSIPTVMMDWAPFDGT--SDLIQDNsLLGGDMATQHLIDK--GHTRIACITGPLDKT 190
Cdd:PRK10653 83 TKILLINPTDSDAVGNAVkMANQANIPVITLDRGATKGEvvSHIASDN-VAGGKMAGDFIAKKlgEGAKVIQLEGIAGTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 191 PARLRLEGYLSAMERAGLAI----PdgyritGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGlrvPD 266
Cdd:PRK10653 162 AARERGEGFKQAVAAHKFNVlasqP------ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KS 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489959095 267 DMAIVGYDDIE----------LArymtpplTTIHQPKDELGELAID 302
Cdd:PRK10653 233 DVMVVGFDGTPdgikavnrgkLA-------ATIAQQPDQIGAIGVE 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-325 |
2.07e-19 |
|
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: 86.19 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYS--LVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQ-RY 137
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGakVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRaKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 PSIPTVMMDwAPFDGTSDLIQDNSLLGGDMATQHLIDK--GHTRIACITGPlDKTPARLRLEGYLSAMERA-GLAIPDGY 214
Cdd:cd06321 81 AGIIVVAVD-VAAEGADATVTTDNVQAGYLACEYLVEQlgGKGKVAIIDGP-PVSAVIDRVNGCKEALAEYpGIKLVDDQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 215 RitGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvpDDMAIVGYD---DI--ELARYMTPPLTTI 289
Cdd:cd06321 159 N--GKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGR---DDIVITSVDgspEAvaALKREGSPFIATA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 489959095 290 HQPKDELGELAIDvlihrMAQPTLQQQRLQLTPVLM 325
Cdd:cd06321 234 AQDPYDMARKAVE-----LALKILNGQEPAPELVLI 264
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
61-274 |
2.64e-19 |
|
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: 85.68 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVER-SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETH---QPSKEIIQR 136
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAeAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADaltPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 137 ypSIPTVMMDwapfdgtSDLIQDN--SLLGGD------MATQHLID--KGHTRIACITGPLDKTPARLRLEGYLSAMERA 206
Cdd:cd06308 81 --GIPVIVLD-------RKVSGDDytAFIGADnveigrQAGEYIAEllNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKY 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489959095 207 glaiPDGYRI---TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYD 274
Cdd:cd06308 152 ----PGIKIVasqDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVD 216
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
62-306 |
3.30e-19 |
|
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.
Pssm-ID: 380477 [Multi-domain] Cd Length: 280 Bit Score: 85.78 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITA---STNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQRYP 138
Cdd:cd01391 2 IGVVTSSlhqIREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 SIPTVMMDWAPFDGTSDLIQDNSL-------LGGDMATQHLIDKGHTRIACITGPLDKTpARLRLEGYLSAMERAGLaIP 211
Cdd:cd01391 82 DIPQLALDATSQDLSDKTLYKYFLsvvfsdtLGARLGLDIVKRKNWTYVAAIHGEGLNS-GELRMAGFKELAKQEGI-CI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 212 DGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYDDIELAR--YM---TPPL 286
Cdd:cd01391 160 VASDKADWNAGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDevGYeveANGL 237
|
250 260
....*....|....*....|
gi 489959095 287 TTIHQPKDELGELAIDVLIH 306
Cdd:cd01391 238 TTIKQQKMGFGITAIKAMAD 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
61-305 |
4.38e-18 |
|
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: 82.32 E-value: 4.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETH--QPSKEIIQRyP 138
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGgiVPAIEAANE-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 SIPTVMMDWAPFDGTSD-LIQDNSLLGGDMATQHL---IDKGHTRIACITGPlDKTPARLRLEGYLSAMER-AGLAIPDg 213
Cdd:cd06322 80 GIPVFTVDVKADGAKVVtHVGTDNYAGGKLAGEYAlkaLLGGGGKIAIIDYP-EVESVVLRVNGFKEAIKKyPNIEIVA- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 214 yRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGlrVPDDMAIVGYDDIELARYMTPP----LTTI 289
Cdd:cd06322 158 -EQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDGNPEAIKAIAKggkiKADI 234
|
250
....*....|....*.
gi 489959095 290 HQPKDELGELAIDVLI 305
Cdd:cd06322 235 AQQPDKIGQETVEAIV 250
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
62-304 |
6.29e-18 |
|
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: 81.97 E-value: 6.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITASTNPFYSELVRGVERSCFERGY-SLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTEtHQPSKEIIQRYPS- 139
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGeVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVD-PTALAPVLKKAKDa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 -IPTVMMDwAPFDGTSDLI---QDNSLLG---GDMATQHLIDKGhtRIACITGPLDKTPARLRLEGYLSAMER--AGLAI 210
Cdd:pfam13407 80 gIPVVTFD-SDAPSSPRLAyvgFDNEAAGeaaGELLAEALGGKG--KVAILSGSPGDPNANERIDGFKKVLKEkyPGIKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 211 PDGYrITGDFEFNGGFEAMQKLLAQEPRP-QAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYD-DIELARYMTPPL-- 286
Cdd:pfam13407 157 VAEV-EGTNWDPEKAQQQMEALLTAYPNPlDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDaTPEALEAIKDGTid 233
|
250
....*....|....*...
gi 489959095 287 TTIHQPKDELGELAIDVL 304
Cdd:pfam13407 234 ATVLQDPYGQGYAAVELA 251
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
64-302 |
1.53e-17 |
|
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: 81.21 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 64 MLITAS-TNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTEThQPSKEIIQRYPS--I 140
Cdd:cd19967 3 AVIVSTpNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADA-DASIAAVKKAKDagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 141 PTVMMDWA-PFDG--TSDLIQDNSLlGGDMATQHLIDK--GHTRIACITGPLDKTPARLRLEGYLSA------MERAGLA 209
Cdd:cd19967 82 PVFLIDREiNAEGvaVAQIVSDNYQ-GAVLLAQYFVKLmgEKGLYVELLGKESDTNAQLRSQGFHSVidqypeLKMVAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 210 IPDGYRITGdfefnggFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvPDDMAIVGYD--DIELARYMTPPLT 287
Cdd:cd19967 161 SADWDRTEA-------FEKMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDgsNDVRDAIKEGKIS 231
|
250
....*....|....*.
gi 489959095 288 -TIHQPKDELGELAID 302
Cdd:cd19967 232 aTVLQPAKLIARLAVE 247
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
72-306 |
2.71e-15 |
|
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: 74.75 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 72 PFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLlctETHQPS--KEIIQRYPS--IPTVMMDW 147
Cdd:cd06318 12 PYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLIL---NPVDPEglTPAVKAAKAagIPVITVDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 148 A--PFDGTSDLIQDNSLLGGDMATQHLID---KGHTRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRIT----- 217
Cdd:cd06318 89 AldPSANVATQVGRDNKQNGVLVGKEAAKalgGDPGKIIELSGDKGNEVSRDRRDGFLAGVNEYQLRKYGKSNIKvvaqp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 218 -GDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYDD-------IELARYMTpplTTI 289
Cdd:cd06318 169 yGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADGqkealklIKDGKYVA---TGL 243
|
250
....*....|....*..
gi 489959095 290 HQPkDELGELAIDVLIH 306
Cdd:cd06318 244 NDP-DLLGKTAVDTAAK 259
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-321 |
7.72e-15 |
|
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: 73.24 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLL---CTETHQPSKeiIQRY 137
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIpagATAAAVPVK--AARA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 PSIPTVMMDWAPFDGTSD-LIQDNSLLG-GDMATQhLIDK--GHTRIACITGPLDKTPARLRLEGYLSAMERA-GLAIPD 212
Cdd:cd19972 79 AGIPVIAVDRNPEDAPGDtFIATDSVAAaKELGEW-VIKQtgGKGEIAILHGQLGTTPEVDRTKGFQEALAEApGIKVVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 213 gyRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvPDDMAIVGYD-DIELARYMTPPLT--TI 289
Cdd:cd19972 158 --EQTADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFDgDVAGLKAVKDGVLdaTM 233
|
250 260 270
....*....|....*....|....*....|....*
gi 489959095 290 HQPKDELGELAIDV---LIHRMAQPTLQQQRLQLT 321
Cdd:cd19972 234 TQQTQKMGRLAVDSaidLLNGKAVPKEQLQDAVLT 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-274 |
4.96e-14 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 71.08 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLL--LCTETHQPSKEIIQRYp 138
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLnpVDSEGIRPALEAAKEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 SIPTVMMDWAPFDgtSDLIQ-----DN----SLLGGDMAtQHLIDKGhtRIACITGPLDKTpARLRLEGYLSAMER-AGL 208
Cdd:cd19971 80 GIPVINVDTPVKD--TDLVDstiasDNynagKLCGEDMV-KKLPEGA--KIAVLDHPTAES-CVDRIDGFLDAIKKnPKF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489959095 209 AIPDGYRITGDFEfnGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvPDDMAIVGYD 274
Cdd:cd19971 154 EVVAQQDGKGQLE--VAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGK--LGDILVYGVD 215
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
61-274 |
1.06e-12 |
|
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380623 [Multi-domain] Cd Length: 271 Bit Score: 67.03 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPS---KEIIQRy 137
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVpaiEAAIKA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 pSIPTVMMDWApFDGTSDL--IQDNSLLGGDMATQHLIDK--GHTRIACITGPLDKTPARLRLEGYlsameRAGLAIPDG 213
Cdd:cd19968 80 -GIPVVTVDRR-AEGAAPVphVGADNVAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGF-----HEELAAGPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489959095 214 YRI----TGDFEFNGGFEAMQKLLAQEP-RPQAVFIGNDAMAFGAYQALYQAGLRVpDDMAIVGYD 274
Cdd:cd19968 153 IKVvfeqTGNFERDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFD 217
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
98-274 |
1.28e-11 |
|
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: 64.55 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 98 EGDEQRMNRNLETLMQ--KRVDGLLLLcTETHQPSK--EIIQRYpSIPTVMMDWAPFDGTSDLIQ--------------- 158
Cdd:cd06324 39 NRNRFKMLELAEELLArpPKPDYLILV-NEKGVAPEllELAEQA-KIPVFLINNDLTDEERALLGkprekfkywlgsivp 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 159 DNSLLGGDMAtQHLIDKGHT-------RIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGyRITGDFEFNGGFEAMQK 231
Cdd:cd06324 117 DNEQAGYLLA-KALIKAARKksddgkiRVLAISGDKSTPASILREQGLRDALAEHPDVTLLQ-IVYANWSEDEAYQKTEK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489959095 232 LLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRVPDDMAIVGYD 274
Cdd:cd06324 195 LLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGID 237
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
61-305 |
8.87e-11 |
|
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: 61.52 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTEThQPSKEIIQR---- 136
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDA-DALAPAVEKakea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 137 -YPSIPTVMM----DWAPFDGTSDLiqdnslLGGDMATQHLIDK--GHTRIACITGPLDKTPARLRLEGYLSAMERAgla 209
Cdd:cd06313 80 gIPLVGVNALieneDLTAYVGSDDV------VAGELEGQAVADRlgGKGNVVILEGPIGQSAQIDRGKGIENVLKKY--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 210 iPDGYRI---TGDFEfngGFEAMQK----LLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvpDDMAIVGYDDIELARYM 282
Cdd:cd06313 151 -PDIKVLaeqTANWS---RDEAMSLmenwLQAYGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDGIEDALQA 223
|
250 260
....*....|....*....|....*.
gi 489959095 283 TPP---LTTIHQPKDELGELAIDVLI 305
Cdd:cd06313 224 VKSgelIATVLQDAEAQGKGAVEVAV 249
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
61-303 |
1.03e-09 |
|
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: 58.75 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERG-YSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSkEIIQRYPS 139
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQ-TIIDKAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 --IPTV----------MMDW--APFDGTsdliqDNSLLG---GDMATQHL-----IDK---GHTRIACITGPLDKTPARL 194
Cdd:cd01539 81 anIPVIffnrepsredLKSYdkAYYVGT-----DAEESGimqGEIIADYWkanpeIDKngdGKIQYVMLKGEPGHQDAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 195 RLEGYLSAMERAGLAIPDGYRITGDFEFNGGFEAMQKLLAQ-EPRPQAVFIGNDAMAFGAYQALYQAGL---RVPDDMAI 270
Cdd:cd01539 156 RTKYSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKyGDKIELVIANNDDMALGAIEALKAAGYntgDGDKYIPV 235
|
250 260 270
....*....|....*....|....*....|....*....
gi 489959095 271 VGYDDIELAR------YMtppLTTIHQPKDELGELAIDV 303
Cdd:cd01539 236 FGVDATPEALeaikegKM---LGTVLNDAKAQAKAIYEL 271
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
61-326 |
1.35e-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: 58.08 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLC--TETHQPS-KEIIQRy 137
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHgdADALDPKlKKALDA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 pSIPTVMMDWA-PFDGTSDLIQDNSLLGGDMATQhLID--KGHTRIACITG----PLDKtpaRLRlegylsAMERAGLAI 210
Cdd:cd06305 80 -GIPVVTFDTDsQVPGVNNITQDDYALGTLSLGQ-LVKdlNGEGNIAVFNVfgvpPLDK---RYD------IYKAVLKAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 211 PDGYRI---TGDFEFNGGFEAMQK---LLAQEPRP--QAVFIGNDAMAFGAYQALYQAGLrvpDDMAIVGYD----DIEL 278
Cdd:cd06305 149 PGIKKIvaeLGDVTPNTAADAQTQveaLLKKYPEGgiDAIWAAWDEPAKGAVQALEEAGR---TDIKVYGVDisnqDLEL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489959095 279 ARYMTPPLT-TIHQPKDELGELAIDVLIHRMA-QPTLqqQRLQLTPVLME 326
Cdd:cd06305 226 MADEGSPWVaTAAQDPALIGTVAVRNVARKLAgEDLP--DKYSLVPVLIT 273
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-274 |
1.59e-09 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 57.74 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVL--CNTEGDEQRMNRNLETLMQKRVDGLLLLCTETH---QPSKEIIQ 135
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFvgPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEdlvDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 136 RypSIPTVMMD--WAPFDGTSDLIQDNsLLGGDMATQHLIDK--GHTRIACITGPLDKTPARLRLEGYLSAMER--AGL- 208
Cdd:cd06310 81 K--GIPVIVIDsgIKGDAYLSYIATDN-YAAGRLAAQKLAEAlgGKGKVAVLSLTAGNSTTDQREEGFKEYLKKhpGGIk 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489959095 209 AIPDGYritGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYD 274
Cdd:cd06310 158 VLASQY---AGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLS--GQIKIVGFD 218
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
62-280 |
1.59e-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: 54.96 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITASTNPFYSELVRGVERSCFERGYSLVL--CNTEGDEQRMNRNLETLMQKRVDGLLLL---CTETHQPSKEIIQR 136
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVqaAPSETDTQGQLNLLETMLNKGYDAILVSpisDTNLIPPIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 137 ypSIPTVMMD---------WAPFDGTSDLIQDNSLLGGdMATQHLIDK--GHTRIACITGPLDKTPARLRLEGYLSAMER 205
Cdd:cd06320 82 --GIPVINLDdavdadalkKAGGKVTSFIGTDNVAAGA-LAAEYIAEKlpGGGKVAIIEGLPGNAAAEARTKGFKETFKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489959095 206 AGlaipdGYRI----TGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYDDIELAR 280
Cdd:cd06320 159 AP-----GLKLvasqPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDGIPEAK 230
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
87-276 |
2.09e-08 |
|
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.
Pssm-ID: 380524 [Multi-domain] Cd Length: 272 Bit Score: 54.54 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 87 ERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEI-IQRYPSIPTVMMDWAPFDGTSDL--IQDNSLL 163
Cdd:cd06301 29 YPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVdAAADAGIPLVYVNREPDSKPKGVafVGSDDIE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 164 GGDMATQHLIDK--GHTRIACITGPLDKTPARLRLEGYLSAMER-AGLAIPDgyRITGDFEFNGGFEAMQKLLAQEPRPQ 240
Cdd:cd06301 109 SGELQMEYLAKLlgGKGNIAILDGVLGHEAQILRTEGNKDVLAKyPGMKIVA--EQTANWSREKAMDIVENWLQSGDKID 186
|
170 180 190
....*....|....*....|....*....|....*.
gi 489959095 241 AVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYDDI 276
Cdd:cd06301 187 AIVANNDEMAIGAILALEAAGKK--DDILVAGIDAT 220
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
61-272 |
3.89e-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: 53.52 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERG---YSLVlcnTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQ---PSKEII 134
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELAdleYKLV---TSSNANEQVSQLEDLIAQKVDAIVILPQDSEEltvAAQKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 135 QRypSIPTVMMDwapfDGTSDLIQDNSLLG-----GDMATQHLIDK--GHTRIACITGPLDKTPARLRLEGYLSAME-RA 206
Cdd:cd06311 78 DA--GIPVVNFD----RGLNVLIYDLYVAGdnpgmGVVSAEYIGKKlgGKGNVVVLEVPSSGSVNEERVAGFKEVIKgNP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489959095 207 GLAIPDGYriTGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVG 272
Cdd:cd06311 152 GIKILAMQ--AGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGRT--DIKVMTG 213
|
|
| PBP1_ABC_sugar_binding-like |
cd19973 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
61-274 |
6.46e-08 |
|
monosaccharide ABC transporter substrate-binding protein; 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: 380628 [Multi-domain] Cd Length: 285 Bit Score: 53.24 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLC--NTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSKEIIQ-RY 137
Cdd:cd19973 1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAagKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKaRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 PSIPTVMMD--WAPFDGTSDLIQDNSLLGGDMATQHLIDKGHTR---IACITGPLDKTPARLRLEGYLSAMeraGLAIPD 212
Cdd:cd19973 81 AGVLVIALDtpTDPIDAADATFATDNFKAGVLIGEWAKAALGAKdakIATLDLTPGHTVGVLRHQGFLKGF---GIDEKD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489959095 213 GYRIT--------------GDFEfnGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYD 274
Cdd:cd19973 158 PESNEdeddsqvvgsadtnGDQA--KGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKE--KGVLIVSVD 229
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
62-303 |
1.39e-07 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 52.20 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQpSKEIIQRYPS-- 139
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGA-AANIVDKAKAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPTVMMDWAPFDGTSDLI--QDNSLLGGDMAtQHLID---KGHtrIACITGPLDKTPARLRLEGYLSAMEraglAIPDGY 214
Cdd:cd19992 81 VPVISYDRLILNADVDLYvgRDNYKVGQLQA-EYALEavpKGN--YVILSGDPGDNNAQLITAGAMDVLQ----PAIDSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 215 RIT--GDfEFNGGF---EAMQK----LLAQEPRPQAVFIGNDAMAFGAYQALYQAGLrvPDDMAIVGYD-DIELARY--- 281
Cdd:cd19992 154 DIKivLD-QYVKGWspdEAMKLvenaLTANNNNIDAVLAPNDGMAGGAIQALKAQGL--AGKVFVTGQDaELAALKRive 230
|
250 260
....*....|....*....|....
gi 489959095 282 --MTpplTTIHQPKDELGELAIDV 303
Cdd:cd19992 231 gtQT---MTVWKDLKELARAAADA 251
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-274 |
3.35e-07 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380662 [Multi-domain] Cd Length: 271 Bit Score: 50.70 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVlcnTEG----DEQRMNRNLETLMQKRVDGLLLLCTETHQ---PSKEI 133
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELD---VQGpptfDPTLQTPIVNAVIAKKPDALLIAPTDPQAliaPLKRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 134 IQRypSIPTVMMDwAPFDGTSDL---IQDNSLLGGDMATQHLID----KGhtRIACITGPLDKTPARLRLEGYLSAMERA 206
Cdd:cd20007 78 ADA--GIKVVTVD-TTLGDPSFVlsqIASDNVAGGALAAEALAEliggKG--KVLVINSTPGVSTTDARVKGFAEEMKKY 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489959095 207 GLAIPDGYRITGDfEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYD 274
Cdd:cd20007 153 PGIKVLGVQYSEN-DPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKT--GKVKVVGFD 217
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
61-277 |
3.91e-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: 50.66 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLC-NTEGDEQRMNRNLETLMQKRVDGLLLLC--TETHQPS-KEIIQR 136
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVgPQKSDAAEQVQLIEDLIARGVDGIAISPndPEAVTPViNKAADK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 137 ypSIPTVMMDwapfdgtSDLIQ---------DNSLLG---GDMATQHLIDKGhtRIACITGPLDKTPARLRLEGYLSAM- 203
Cdd:cd06314 81 --GIPVITFD-------SDAPDskrlayigtDNYEAGreaGELMKKALPGGG--KVAIITGGLGADNLNERIQGFKDALk 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489959095 204 ERAGLAIPDgyRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYDDIE 277
Cdd:cd06314 150 GSPGIEIVD--PLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKV--GKVKIVGFDTLP 219
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-262 |
7.20e-07 |
|
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: 49.92 E-value: 7.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVL--CNTEGDEQRMNRNLETLMQKRVDGLLLLCTETH---QPSKEIIQ 135
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWrgPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKalvAPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 136 RypSIPTVMMDwAPFDGTSDL--IQDNSLLGGDMATQHLIDKGHTRIACITGPLDK--TPARLRLEGYLSAMERA--GLA 209
Cdd:cd20004 81 Q--GIPVVIID-SDLGGDAVIsfVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKgsASTTDRERGFLEALKKLapGLK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489959095 210 IPDGYRITGDFEfnGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGL 262
Cdd:cd20004 158 VVDDQYAGGTVG--EARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGL 208
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
62-308 |
1.13e-06 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 49.10 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITASTNPFYSELVRGVERSCFERGY----SLVLCNTEGDEQRMNRNLETLMqKRVDGLLLLCTEtHQPSKEIIQRY 137
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDrrvrLRIHFVDSLDPEALAAALRRLA-AGCDGVALVAPD-HPLVRAAIDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 138 PS--IPTVMMdwapfdgTSDLIQ---------DNSLLG---GDMATQHLIDKGHtRIACITGPLDKTPARLRLEGYLSAM 203
Cdd:cd06307 80 AArgIPVVTL-------VSDLPGsrrlayvgiDNRAAGrtaAWLMGRFLGRRPG-KVLVILGSHRFRGHEEREAGFRSVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 204 ERAG-----LAIPDGYritGDFEFNggFEAMQKLLAQEPRPQAVFI---GNDAMAfgayQALYQAGLrvPDDMAIVGYDD 275
Cdd:cd06307 152 RERFpdltvLEVLEGL---DDDELA--YELLRELLARHPDLVGIYNaggGNEGIA----RALREAGR--ARRVVFIGHEL 220
|
250 260 270
....*....|....*....|....*....|....*....
gi 489959095 276 IELAR------YMTpplTTIHQPKDELGELAIDVLIHRM 308
Cdd:cd06307 221 TPETRrllrdgTID---AVIDQDPELQARRAIEVLLAHL 256
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
62-272 |
2.30e-05 |
|
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380482 [Multi-domain] Cd Length: 294 Bit Score: 45.36 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 62 IGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLlCTETHQPSKEIIQRYPS-- 139
Cdd:cd01540 2 IGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVI-CTPDQKLGPAIAAKAKAag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 IPtVM-----------MDWAPFDG--TSDLIQDN-SLLGGDMATQHLIDKGHTRIACITgpLDKTP-ARLRLEGYLSAME 204
Cdd:cd01540 81 IP-VIavddqlvdadpMKIVPFVGidAYKIGEAVgEWLAKEMKKRGWDDVKEVGVLAIT--MDTLSvCVDRTDGAKDALK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489959095 205 RAGLA----IPDGYRITgDFEfnGGFEAMQKLLAQEP--RPQAVFIGNDAMAFGAYQALYQAGLRvPDDMAIVG 272
Cdd:cd01540 158 AAGFPedqiFQAPYKGT-DTE--GAFNAANAVITAHPevKHWLVVGCNDEGVLGAVRALEQAGFD-AEDIIGVG 227
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
52-305 |
2.61e-05 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 45.25 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 52 RSLKLNQTRTIGMLITAST--------------NPFYSELVRGVERSCFERGYS--LVLCNTEGDEQRMNRNLETLMQKR 115
Cdd:PRK09701 3 KYLKYFSGTLVGLMLSTSAfaaaeyavvlktlsNPFWVDMKKGIEDEAKTLGVSvdIFASPSEGDFQSQLQLFEDLSNKN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 116 VDG----------LLLLCTETHQPSKEIIQRYPSIPTVMMDWAPFDGTSDLIQDNSLLGGDMAtQHLIDK-GHT--RIAC 182
Cdd:PRK09701 83 YKGiafaplssvnLVMPVARAWKKGIYLVNLDEKIDMDNLKKAGGNVEAFVTTDNVAVGAKGA-SFIIDKlGAEggEVAI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 183 ITGPLDKTPARLRLEGYLSAMERAGlAIPDGYRITGDFEFNGGFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGL 262
Cdd:PRK09701 162 IEGKAGNASGEARRNGATEAFKKAS-QIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489959095 263 RvpDDMAIVGYDDIELARYMTPP--LT-TIHQPKDELGELAIDVLI 305
Cdd:PRK09701 241 T--GKVLVVGTDGIPEARKMVEAgqMTaTVAQNPADIGATGLKLMV 284
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
61-279 |
3.37e-04 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380663 [Multi-domain] Cd Length: 277 Bit Score: 41.83 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLC--NTEGDEQRMNRNLETLMQKRVDGLLLLCTEThQPSKEIIQRYP 138
Cdd:cd20008 1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDT-AALVPAVEAAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 139 S-IPTVMMDWAP-FDGTSDLIQDNSLLGGDMATQHLID------KGHTRIACITGPLDKTPARLRLEGYLSAMEraglAI 210
Cdd:cd20008 80 AgIPVVLVDSGAnTDDYDAFLATDNVAAGALAADELAEllkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIK----EK 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489959095 211 PDGYRITGDFEFNG----GFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYD--DIELA 279
Cdd:cd20008 156 YPDIEIVDVQYSDGdiakALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKA--GKIVLVGFDssPDEVA 228
|
|
| PBP1_ABC_xylose_binding-like |
cd01538 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ... |
61-308 |
7.22e-04 |
|
periplasmic xylose-like sugar-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; Periplasmic xylose-like sugar-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: 380480 [Multi-domain] Cd Length: 283 Bit Score: 40.87 E-value: 7.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 61 TIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTEThQPSKEIIQRYPS- 139
Cdd:cd01538 1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDG-QALSPVVAEAKAe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 140 -IPTVMMDWAPFDGTSDLIQ--DNSLLGgDMATQHLID-KGHTRIACITGPLDKTPARLRLEGYLSAMERA----GLAIP 211
Cdd:cd01538 80 gIKVIAYDRLILNADVDYYIsfDNEKVG-ELQAQALLDaKPEGNYVLIGGSPTDNNAKLFRDGQMKVLQPAidsgKIKVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 212 DGYRITgDFEFNGGFEAMQKLL-AQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpDDMAIVGyDDIELA---RYMTPPLT 287
Cdd:cd01538 159 GDQWVD-DWLPANAQQIMENALtANGNNVDAVVASNDGTAGGAIAALKAQGLS--GGVPVSG-QDADLAaikRILAGTQT 234
|
250 260
....*....|....*....|..
gi 489959095 288 -TIHQPKDELGELAIDVLIHRM 308
Cdd:cd01538 235 mTVYKDIRLLADAAAEVAVALM 256
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| PBP1_LuxPQ_Quorum_Sensing |
cd06303 |
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ... |
196-273 |
1.05e-03 |
|
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.
Pssm-ID: 380526 [Multi-domain] Cd Length: 320 Bit Score: 40.43 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 196 LEGYLSAMeRAG-----LAIPDGYRITGDFEFNG----GFEAMQKLLAQEPRPQAVFIGNDAMAFGAYQALYQAGLRvpD 266
Cdd:cd06303 168 TEGYVSDQ-RGDtfideVARHSNLELVSAYYTDFdresAREAARALLARHPDLDFIYACSTDIALGAIDALQELGRE--T 244
|
....*..
gi 489959095 267 DMAIVGY 273
Cdd:cd06303 245 DIMINGW 251
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
165-287 |
2.79e-03 |
|
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: 38.72 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489959095 165 GDMATQHLIDKGH---TRIACITGPLDKTPARLRLEGYLSAMERAGLAIPDGYRitGDFEFNGGFEAMQKLLAQEPRPqA 241
Cdd:cd06306 109 GYLAGEYLVEHHPgkpVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVATKY--GDTGKAVQLNLVEDALQAHPDI-D 185
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489959095 242 VFIGNDAMAFGAYQALYQAGLRvpDDMAIVGYddielarYMTPPLT 287
Cdd:cd06306 186 YIVGNAVAAEAAVGALREAGLT--GKVKVVST-------YLTPGVY 222
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