|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
1-289 |
0e+00 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 636.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 1 SLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLA 80
Cdd:PRK10703 53 SLKVNHTKSIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 81 MLEEYRHIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVP 160
Cdd:PRK10703 133 MLEEYRHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVP 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQ 240
Cdd:PRK10703 213 EEWIVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQ 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1943035 241 PKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRSVADGPFRDYRR 289
Cdd:PRK10703 293 PKDRLGETAFNMLLDRIVNKREEPQTIEVHPRLVERRSVADGPFRDYRR 341
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
9-278 |
4.09e-164 |
|
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: 456.33 E-value: 4.09e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHI 88
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGEAKaDFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd06275 81 PVVVLDREIAG-DNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGET 248
Cdd:cd06275 160 FEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
|
250 260 270
....*....|....*....|....*....|
gi 1943035 249 AFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06275 240 AVELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
9-273 |
5.54e-161 |
|
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: 448.23 E-value: 5.54e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHI 88
Cdd:cd01537 1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGQNV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd01537 81 PVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGET 248
Cdd:cd01537 161 WDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKT 240
|
250 260
....*....|....*....|....*
gi 1943035 249 AFNMLLDRIVNKREEPQSIEVHPRL 273
Cdd:cd01537 241 TFDLLLNLADNWKIDNKVVRVPYVL 265
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-280 |
8.25e-109 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 318.68 E-value: 8.25e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 1 SLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLA 80
Cdd:COG1609 55 SLRTGRTRTIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 81 MLEEyRHIPMVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVP 160
Cdd:COG1609 135 RLAE-AGIPVVLIDRPLPDPGVPSVGVDN-RAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPD 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQ 240
Cdd:COG1609 213 PELVVEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQ 292
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1943035 241 PKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRSVA 280
Cdd:COG1609 293 PIEEMGRRAAELLLDRIEGPDAPPERVLLPPELVVRESTA 332
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
1-279 |
2.19e-108 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 317.41 E-value: 2.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 1 SLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLA 80
Cdd:PRK10423 50 SLKLNQTRTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSRE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 81 MLEEYRHIPMVVMDWGEAKADfTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVP 160
Cdd:PRK10423 130 IMQRYPSVPTVMMDWAPFDGD-SDLIQDNSLLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQ 240
Cdd:PRK10423 209 DGYEVTGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQ 288
|
250 260 270
....*....|....*....|....*....|....*....
gi 1943035 241 PKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRSV 279
Cdd:PRK10423 289 PKDELGELAIDVLIHRMAQPTLQQQRLQLTPELMERGSV 327
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
10-274 |
1.01e-105 |
|
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.
Pssm-ID: 380491 [Multi-domain] Cd Length: 264 Bit Score: 308.29 E-value: 1.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHIP 89
Cdd:cd06267 2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLA-AGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 90 MVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDF 169
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDN-YAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 170 EPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETA 249
Cdd:cd06267 160 SEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAA 239
|
250 260
....*....|....*....|....*
gi 1943035 250 FNMLLDRIVNKREEPQSIEVHPRLI 274
Cdd:cd06267 240 AELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
9-279 |
2.11e-93 |
|
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: 277.18 E-value: 2.11e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHI 88
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAA-RGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd06285 80 PVVLVDRRIGDTALPSVTVDN-ELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGET 248
Cdd:cd06285 159 FTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRR 238
|
250 260 270
....*....|....*....|....*....|.
gi 1943035 249 AFNMLLDRIVNKREEPQSIEVHPRLIERRSV 279
Cdd:cd06285 239 AAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
21-278 |
7.52e-86 |
|
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: 257.85 E-value: 7.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEeyRHIPMVVM-DWGEAk 99
Cdd:cd06284 13 FYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELS--KRYPIVQCcEYIPD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 100 ADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAMQ 179
Cdd:cd06284 90 SGVPSVSIDN-EAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFSFEAGYAAAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 180 QILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIVN 259
Cdd:cd06284 169 ALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAAELLLEKIEG 248
|
250
....*....|....*....
gi 1943035 260 KREEPQSIEVHPRLIERRS 278
Cdd:cd06284 249 EGVPPEHIILPHELIVRES 267
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
10-278 |
5.11e-83 |
|
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: 250.55 E-value: 5.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYrHIP 89
Cdd:cd19975 2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNM-NIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 90 MVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPL-ERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd19975 81 VVLVSTESEDPDIPSVKIDD-YQAAYDATNYLIKKGHRKIAMISGPLdDPNAGYPRYEGYKKALKDAGLPIKENLIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGET 248
Cdd:cd19975 160 FSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKK 239
|
250 260 270
....*....|....*....|....*....|
gi 1943035 249 AFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd19975 240 AVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
9-278 |
2.44e-80 |
|
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: 243.70 E-value: 2.44e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHI 88
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGeAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd19976 81 PVVVLDRY-IEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQpHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGET 248
Cdd:cd19976 160 SSLEGGYKAAEELLKS-KNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
|
250 260 270
....*....|....*....|....*....|
gi 1943035 249 AFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd19976 239 AAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
9-276 |
3.02e-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: 243.58 E-value: 3.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHI 88
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAE-KIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDwgeakaDFTDAV------IDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPES 162
Cdd:cd06270 80 PLVVIN------RYIPGLadrcvwLDN-EQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 163 WIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPK 242
Cdd:cd06270 153 LIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPI 232
|
250 260 270
....*....|....*....|....*....|....
gi 1943035 243 DSLGETAFNMLLDRiVNKREEPQSIEVHPRLIER 276
Cdd:cd06270 233 EEMAQAAAELALNL-AYGEPLPISHEFTPTLIER 265
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
9-278 |
2.18e-79 |
|
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: 241.37 E-value: 2.18e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILG-NAWNNLEKQRAYLSMMAQKrVDGLLVMCSEYPEPLLAMLEEyrH 87
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVStSHWNADRELEILRLLLARK-VDGIIVVGGFGDEELLKLLAE--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQG 167
Cdd:cd06290 78 IPVVLVDRELEGLNLPVVNVDN-EQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 168 DFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGE 247
Cdd:cd06290 157 DFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGK 236
|
250 260 270
....*....|....*....|....*....|.
gi 1943035 248 TAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06290 237 TAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
9-278 |
1.99e-78 |
|
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: 238.99 E-value: 1.99e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLA-TSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMcSEYPEPLLAMLEEYrH 87
Cdd:cd06288 1 TIGLITdDIATTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYA-SMHHREVTLPPELT-D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDwGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQG 167
Cdd:cd06288 79 IPLVLLN-CFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 168 DFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGE 247
Cdd:cd06288 158 DWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGR 237
|
250 260 270
....*....|....*....|....*....|.
gi 1943035 248 TAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06288 238 RAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
9-278 |
1.15e-76 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380497 [Multi-domain] Cd Length: 268 Bit Score: 234.33 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHI 88
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQ-RQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERN-TGAGRLAGFMKAMEEAMIKVPESWIVQG 167
Cdd:cd06273 80 PYVLTWSYDEDSPHPSIGFDN-RAAAARAAQHLLDLGHRRIAVISGPTAGNdRARARLAGIRDALAERGLELPEERVVEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 168 DFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGE 247
Cdd:cd06273 159 PYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGE 238
|
250 260 270
....*....|....*....|....*....|.
gi 1943035 248 TAFNMLLDRIvNKREEPQSIEVHPRLIERRS 278
Cdd:cd06273 239 LAARYLLALL-EGGPPPKSVELETELIVRES 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
9-276 |
2.30e-76 |
|
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: 233.69 E-value: 2.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHI 88
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLK-HGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGEAKADfTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd06280 80 PIVLIDREVEGLE-LDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGET 248
Cdd:cd06280 159 STIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRI 238
|
250 260
....*....|....*....|....*...
gi 1943035 249 AFNMLLDRIVNKREEPQSIEVHPRLIER 276
Cdd:cd06280 239 AAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
10-278 |
5.15e-76 |
|
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380514 [Multi-domain] Cd Length: 264 Bit Score: 232.41 E-value: 5.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLvMCSEYPEpllamLEEY--RH 87
Cdd:cd06291 2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGII-LGSHSLD-----IEEYkkLN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDwgeakADFTDAVI----DNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESW 163
Cdd:cd06291 76 IPIVSID-----RYLSEGIPsvssDN-YQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 164 IVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKD 243
Cdd:cd06291 150 IDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIE 229
|
250 260 270
....*....|....*....|....*....|....*
gi 1943035 244 SLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06291 230 EMAKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
9-278 |
2.86e-75 |
|
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: 230.55 E-value: 2.86e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEK--QRAYLSMMAQkRVDGLLVMcsEYPEPLLAMLEEYR 86
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPAsvREALDRLLSQ-RVDGIIVI--APDEAVLEALRRLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 H-IPMVVMDwGEAKADFTDAVIDNAfEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPesWIV 165
Cdd:cd01574 78 PgLPVVIVG-SGPSPGVPTVSIDQE-EGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPP--PVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 166 QGDFEPESGYRAMQQILSQPhRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSL 245
Cdd:cd01574 154 EGDWSAASGYRAGRRLLDDG-PVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAEL 232
|
250 260 270
....*....|....*....|....*....|...
gi 1943035 246 GETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd01574 233 GRRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
9-278 |
1.25e-72 |
|
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: 224.07 E-value: 1.25e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHI 88
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRA-RGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESwIVQGD 168
Cdd:cd06293 80 AVVLLDRPAPGPAGCSVSVDD-VQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEV-VRELS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEP---ESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSL 245
Cdd:cd06293 158 APDanaELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYEL 237
|
250 260 270
....*....|....*....|....*....|...
gi 1943035 246 GETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06293 238 GRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
10-274 |
1.32e-72 |
|
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: 223.95 E-value: 1.32e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVM-CSEYPEPLLAMLEeyRHI 88
Cdd:cd19977 2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIApTGGNEDLIEKLVK--SGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMD--WGEAKADFTdaVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIvQ 166
Cdd:cd19977 80 PVVFVDryIPGLDVDTV--VVDN-FKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELI-K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 167 GDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLG 246
Cdd:cd19977 156 HVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIG 235
|
250 260
....*....|....*....|....*....
gi 1943035 247 ETAFNMLLDRIVNKRE-EPQSIEVHPRLI 274
Cdd:cd19977 236 RKAAELLLDRIENKPKgPPRQIVLPTELI 264
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
10-278 |
4.62e-72 |
|
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: 222.82 E-value: 4.62e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEK-QRAYLSMMAQKRVDGLLV---MCSEypEPLLAMLEEy 85
Cdd:cd01545 2 IGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCDSDDEDlADRLRRFLSRSRPDGVILtppLSDD--PALLDALDE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 RHIPMVVMDWGEAKADFTDAVIDNAfEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIV 165
Cdd:cd01545 79 LGIPYVRIAPGTDDDRSPSVRIDDR-AAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 166 QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSL 245
Cdd:cd01545 158 QGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEM 237
|
250 260 270
....*....|....*....|....*....|...
gi 1943035 246 GETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd01545 238 ARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
10-276 |
1.13e-69 |
|
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380512 [Multi-domain] Cd Length: 268 Bit Score: 216.66 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVM-CSEYPEPLLAMLEEYRhI 88
Cdd:cd06289 2 VGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSpAAGTTAELLRRLKAWG-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVM--DWGEAKADFtdAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQ 166
Cdd:cd06289 81 PVVLAlrDVPGSDLDY--VGIDN-RLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 167 GDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLG 246
Cdd:cd06289 158 GPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIG 237
|
250 260 270
....*....|....*....|....*....|
gi 1943035 247 ETAFNMLLDRIVNKREEPQSIEVHPRLIER 276
Cdd:cd06289 238 RRAARLLLRRIEGPDTPPERIIIEPRLVVR 267
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
9-278 |
9.85e-69 |
|
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: 214.06 E-value: 9.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVM----CSEYPEPLLAMlee 84
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVptgeNSEGLQALIAQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 85 yrHIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWI 164
Cdd:cd06299 78 --GLPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 165 VQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDS 244
Cdd:cd06299 156 AFGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVER 235
|
250 260 270
....*....|....*....|....*....|....
gi 1943035 245 LGETAFNMLLDRIVNKrEEPQSIEVHPRLIERRS 278
Cdd:cd06299 236 IGRRAVELLLALIENG-GRATSIRVPTELIPRES 268
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
10-278 |
6.27e-68 |
|
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: 212.13 E-value: 6.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSE----AAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEy 85
Cdd:cd06292 2 IGYVVPELPggfsDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPRVRYLHE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 RHIPMVVMDWGEAKADFTDAVIDNAfEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIV 165
Cdd:cd06292 81 AGVPFVAFGRANPDLDFPWVDVDGA-AGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 166 QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSL 245
Cdd:cd06292 160 EGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEI 239
|
250 260 270
....*....|....*....|....*....|...
gi 1943035 246 GETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06292 240 GRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
10-278 |
2.95e-67 |
|
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: 210.49 E-value: 2.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMC--SEYPEPLLAMLEEY-- 85
Cdd:cd01541 2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPtkSALPNPNLDLYEELqk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 RHIPMVVMDWGEAKADFtDAVIDNAFEGGYMAGRYLIERGHREIGVI------PGPLerntgagRLAGFMKAMEEAMIKV 159
Cdd:cd01541 82 KGIPVVFINSYYPELDA-PSVSLDDEKGGYLATKHLIDLGHRRIAGIfksddlQGVE-------RYQGFIKALREAGLPI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 160 PES---WIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALT 236
Cdd:cd01541 154 DDDrilWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLT 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1943035 237 TIHQPKDSLGETAFNMLLDRIvNKREEPQSIEVHPRLIERRS 278
Cdd:cd01541 234 SVVHPKEELGRKAAELLLRMI-EEGRKPESVIFPPELIERES 274
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
9-278 |
4.09e-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: 210.07 E-value: 4.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEA-----AYFAEIIEAVEKNCFQKGYTLIL----GNAWNNLEKQraylsmmaqkrVDGLLVMCSEYPEPLL 79
Cdd:cd01544 1 TIGIIQWYSEEeeledPYYLSIRLGIEKEAKKLGYEIKTifrdDEDLESLLEK-----------VDGIIAIGKFSKEEIE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 80 AMLEEYRHIpmVVMDWGEAKADFtDAVIDNAFEGGYMAGRYLIERGHREIGVIpGPLERNTGAG------RLAGFMKAME 153
Cdd:cd01544 70 KLKKLNPNI--VFVDSNPDPDGF-DSVVPDFEQAVRQALDYLIELGHRRIGFI-GGKEYTSDDGeeiedpRLRAFREYMK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 154 EAMIKVPEsWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTP 233
Cdd:cd01544 146 EKGLYNEE-YIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTP 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1943035 234 ALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd01544 225 PLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
10-279 |
2.44e-64 |
|
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: 202.89 E-value: 2.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHIP 89
Cdd:cd06296 2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRS-AGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 90 MVVMD-WGEAKADFTDAVIDNAfEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd06296 81 FVLIDpVGEPDPDLPSVGATNW-AGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGET 248
Cdd:cd06296 160 FTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAV 239
|
250 260 270
....*....|....*....|....*....|.
gi 1943035 249 AFNMLLDRIVNKREEPQSIEVHPRLIERRSV 279
Cdd:cd06296 240 AVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
10-278 |
3.93e-64 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 202.38 E-value: 3.93e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAyLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHIP 89
Cdd:cd06278 2 VGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDA-LRQLLQYRVDGVIVTSATLSSELAEECAR-RGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 90 MVVMDWGEAKADfTDAV-IDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAmiKVPESWIVQGD 168
Cdd:cd06278 80 VVLFNRVVEDPG-VDSVsCDN-RAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAEL--GLPPPAVEAGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGAL-CAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGE 247
Cdd:cd06278 156 YSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALdAARQEGGLVVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAE 235
|
250 260 270
....*....|....*....|....*....|.
gi 1943035 248 TAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06278 236 AAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
10-278 |
1.09e-60 |
|
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: 193.48 E-value: 1.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHIP 89
Cdd:cd01575 2 VAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRA-AGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 90 MV-VMDWGEakaDFTDAVI--DNaFEGGYMAGRYLIERGHREIGVIPGPLERNT-GAGRLAGFMKAMEEAMIKVPESWIV 165
Cdd:cd01575 81 VVeTWDLPD---DPIDMAVgfSN-FAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLPLVLLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 166 QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSL 245
Cdd:cd01575 157 ELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEI 236
|
250 260 270
....*....|....*....|....*....|...
gi 1943035 246 GETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd01575 237 GRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
1-280 |
1.99e-60 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 194.06 E-value: 1.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 1 SLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPepLLA 80
Cdd:PRK11041 29 NLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLIITKQIDGMLLLGSRLP--FDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 81 MLEEYRHIPMVVMdwgeaKADFTDAV------IDN---AFEggymAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKA 151
Cdd:PRK11041 107 SKEEQRNLPPMVM-----ANEFAPELelptvhIDNltaAFE----AVNYLHELGHKRIACIAGPEEMPLCHYRLQGYVQA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 152 MEEAMIKVPESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYF 231
Cdd:PRK11041 178 LRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQYC 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1943035 232 TPALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRSVA 280
Cdd:PRK11041 258 DPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGSTA 306
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
9-274 |
1.89e-58 |
|
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: 187.76 E-value: 1.89e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLL----ATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEE 84
Cdd:cd20010 1 AIGLVlpldPGDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 85 yRHIPMVVMDWGEAKADFT--DavIDNAfEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPES 162
Cdd:cd20010 81 -RGIPFVVHGRSESGAPYAwvD--IDNE-GAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 163 WIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNV-RNARYFTPALTTIHQP 241
Cdd:cd20010 157 LVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLTTTRSS 236
|
250 260 270
....*....|....*....|....*....|...
gi 1943035 242 KDSLGETAFNMLLDRIVNKREEPQSIEVHPRLI 274
Cdd:cd20010 237 LRDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
22-279 |
4.06e-57 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 184.36 E-value: 4.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 22 FAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLV-MCSEYPEPLLAMLEEYRhIPMVVMDwGEAKA 100
Cdd:cd06281 14 YARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILtPGDEDDPELAAALARLD-IPVVLID-RDLPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 101 DfTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAMQQ 180
Cdd:cd06281 92 D-IDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGSFSADSGFREAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 181 ILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRI-VN 259
Cdd:cd06281 171 LLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRAAAELLLDRIeGP 250
|
250 260
....*....|....*....|
gi 1943035 260 KREEPQSIEVHPRLIERRSV 279
Cdd:cd06281 251 PAGPPRRIVVPTELILRDSC 270
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
10-276 |
2.31e-55 |
|
ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.
Pssm-ID: 380509 [Multi-domain] Cd Length: 262 Bit Score: 179.66 E-value: 2.31e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLlVMCS-EYPEPLLAMLEEY--- 85
Cdd:cd06286 2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGL-IITSrENDWEVIEPYAKYgpi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 --------RHIPMVVMDwgeakadftdavidnAFEGGYMAGRYLIERGHREIGVIPG--PLERNTGAGRLAGFMKAMEEA 155
Cdd:cd06286 81 vlceetdsPDIPSVYID---------------RYEAYLEALEYLKEKGHRKIGYCLGrpESSSASTQARLKAYQDVLGEH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 156 MIKVPESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARyfTPAL 235
Cdd:cd06286 146 GLSLREEWIFTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISE--LLNL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1943035 236 TTIHQPKDSLGETAFNMLLDRIVNKreEPQSIEVHPRLIER 276
Cdd:cd06286 224 TTIDQPLEEMGKEAFELLLSQLESK--EPTKKELPSKLIER 262
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
9-278 |
3.37e-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: 3.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATS---SEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCsEYPEPLLAMLEEY 85
Cdd:cd19974 1 NIAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILG-EISKEYLEKLKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 rHIPMVVMDwGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIpGplerNTGAG-----RLAGFMKAMEEAMI-KV 159
Cdd:cd19974 80 -GIPVVLVD-HYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFV-G----DINYTssfmdRYLGYRKALLEAGLpPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 160 PESWIVQGDfepESGYRAMQQILSQPH--RPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTT 237
Cdd:cd19974 153 KEEWLLEDR---DDGYGLTEEIELPLKlmLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTT 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1943035 238 IHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd19974 230 VEVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
64-278 |
6.87e-55 |
|
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: 179.33 E-value: 6.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 64 VDGLLVMCSEYPEPLLAMLEEyRHIPMVVMDwGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAG 143
Cdd:cd06279 57 VDGFIVYGLSDDDPAVAALRR-RGLPLVVVD-GPAPPGIPSVGIDD-RAAARAAARHLLDLGHRRIAILSLRLDRGRERG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 144 -----------------RLAGFMKAMEEAMIKVPESWIVQ-GDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCA 205
Cdd:cd06279 134 pvsaerlaaatnsvareRLAGYRDALEEAGLDLDDVPVVEaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRA 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943035 206 ADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIVnkREEPQSIEVHPRLIERRS 278
Cdd:cd06279 214 ARERGLRVPEDLSVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLP--GAPPRPVILPTELVVRAS 284
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
16-274 |
2.82e-54 |
|
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: 176.92 E-value: 2.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 16 SSEAAyfAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRhIPMVVMdw 95
Cdd:cd01542 10 DSYST--SRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLK-IPVVVL-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 96 GEAKADFTdAVIDNAFEGGYMAGRYLIERGHREIGVIpGPLERN--TGAGRLAGFMKAMEEAmiKVPESWIVQGDFEPES 173
Cdd:cd01542 85 GQEHEGFS-CVYHDDYGAGKLLGEYLLKKGHKNIAYI-GVDEEDiaVGVARKQGYLDALKEH--GIDEVEIVETDFSMES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 174 GYRAMQQILSQpHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNML 253
Cdd:cd01542 161 GYEAAKELLKE-NKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAELL 239
|
250 260
....*....|....*....|.
gi 1943035 254 LDRIvNKREEPQSIEVHPRLI 274
Cdd:cd01542 240 LDMI-EGEKVPKKQKLPYELI 259
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
10-274 |
2.59e-53 |
|
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: 174.69 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGL-LATSSEAAY----FAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEE 84
Cdd:cd06294 2 IGLvLPSSAEELFqnpfFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDPLIEYLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 85 yRHIPMVVMdwGEAkADFTDAV-IDN-AFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPES 162
Cdd:cd06294 82 -EGFPFVVI--GKP-LDDNDVLyVDNdNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 163 WIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPK 242
Cdd:cd06294 158 YILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINP 237
|
250 260 270
....*....|....*....|....*....|..
gi 1943035 243 DSLGETAFNMLLDRIVNKREEPQSIEVHPRLI 274
Cdd:cd06294 238 YELGREAAKLLINLLEGPESLPKNVIVPHELI 269
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
21-278 |
5.99e-51 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380500 [Multi-domain] Cd Length: 275 Bit Score: 168.57 E-value: 5.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRaYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHIPMVVMD-WGE-A 98
Cdd:cd06277 20 FFSELIDGIEREARKYGYNLLISSVDIGDDFDE-ILKELTDDQSSGIILLGTELEEKQIKLFQD-VSIPVVVVDnYFEdL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 99 KADFTdaVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAM 178
Cdd:cd06277 98 NFDCV--VIDN-EDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 179 QQILSQ-PHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRI 257
Cdd:cd06277 175 KALLDTgPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKI 254
|
250 260
....*....|....*....|.
gi 1943035 258 VNKREEPQSIEVHPRLIERRS 278
Cdd:cd06277 255 KDPDGGTLKILVSTKLVERGS 275
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
120-279 |
4.07e-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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 149.80 E-value: 4.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 120 YLIERGHREIGVIPGPLERNTGAG--RLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAMQQILSqpHRPTAVFCGGDI 197
Cdd:pfam13377 1 HLAELGHRRIALIGPEGDRDDPYSdlRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLG--ALPTAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 198 MAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERR 277
Cdd:pfam13377 79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158
|
..
gi 1943035 278 SV 279
Cdd:pfam13377 159 ST 160
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
10-269 |
5.95e-45 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 152.82 E-value: 5.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLV-MCSEYPEPLLAMLEEyRHI 88
Cdd:cd06282 2 IGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILtVGDAQGSEALELLEE-EGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMdWGEAKADFTDAV-IDNaFEGGYMAGRYLIERGHREIGVIPGPLER-NTGAGRLAGFMKAMEEAMIKVPEswIVQ 166
Cdd:cd06282 81 PYVLL-FNQTENSSHPFVsVDN-RLASYDVAEYLIALGHRRIAMVAGDFSAsDRARLRYQGYRDALKEAGLKPIP--IVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 167 GDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLG 246
Cdd:cd06282 157 VDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMG 236
|
250 260
....*....|....*....|...
gi 1943035 247 ETAFNMLLDRIvNKREEPQSIEV 269
Cdd:cd06282 237 RAAADLLLAEI-EGESPPTSIRL 258
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
6-280 |
1.02e-44 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 154.38 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 6 HTKSIGLlATSSEAAYFA-EIIEAVEKNCFQKGYTLILG--NAWNNLEKQRAYLSMMAQkRVDGLLVMCSEYPEPLLAML 82
Cdd:PRK09526 62 QSLTIGL-ATTSLALHAPsQIAAAIKSRADQLGYSVVISmvERSGVEACQAAVNELLAQ-RVSGVIINVPLEDADAEKIV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 83 EEYRHIPMVVMDwgeaKADFTDA--VIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKvP 160
Cdd:PRK09526 140 ADCADVPCLFLD----VSPQSPVnsVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQ-P 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESwIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQ 240
Cdd:PRK09526 215 IA-VREGDWSAMSGYQQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQ 293
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1943035 241 PKDSLGETAFNMLLDRIVNKrEEPQSIEVHPRLIERRSVA 280
Cdd:PRK09526 294 DFRLLGKEAVDRLLALSQGQ-AVKGSQLLPTSLVVRKSTA 332
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
21-278 |
8.17e-44 |
|
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: 150.09 E-value: 8.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQKGYTLIL--GNAWNNlekqrAYLSMMAQKRVDGLLVM-CSEYPEPLLAMLEeyRHIPMVVmdWGE 97
Cdd:cd06295 24 FFLELLGGISEALTDRGYDMLLstQDEDAN-----QLARLLDSGRADGLIVLgQGLDHDALRELAQ--QGLPMVV--WGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 98 AkADFTDAVI---DNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAgRLAGFMKAMEEAMIKVPESWIVQGDFEPESG 174
Cdd:cd06295 95 P-EDGQSYCSvgsDN-VKGGALATEHLIEIGRRRIAFLGDPPHPEVAD-RLQGYRDALAEAGLEADPSLLLSCDFTEESG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 175 YRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPkdslGETAFNMLL 254
Cdd:cd06295 172 YAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTVRQD----LALAGRLLV 247
|
250 260
....*....|....*....|....*.
gi 1943035 255 DRIVN--KREEPQSIEVHPRLIERRS 278
Cdd:cd06295 248 EKLLAliAGEPVTSSMLPVELVVRES 273
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
20-276 |
2.07e-41 |
|
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: 143.85 E-value: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 20 AYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVM-CSEYPEPLLAMLEeyRHIPMVVMDwGEA 98
Cdd:cd06283 12 PFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQpTGNNNDAYLELAQ--KGLPVVLVD-RQI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 99 KADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERN-TGAGRLAGFMKAMEEAMIKVPESWIVQGDfePESGYRA 177
Cdd:cd06283 89 EPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGIsTRRERLQGFLDALARYNIEGDVYVIEIED--TEDLQQA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 178 MQQILSQPH-RPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDR 256
Cdd:cd06283 167 LAAFLSQHDgGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKAAAEILLER 246
|
250 260
....*....|....*....|
gi 1943035 257 IVNKREEPQSIEVHPRLIER 276
Cdd:cd06283 247 IEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
9-278 |
1.47e-39 |
|
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.
Pssm-ID: 380520 [Multi-domain] Cd Length: 268 Bit Score: 139.14 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVmcSEYPepLLAMLEEYR-- 86
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVM--ASLD--LTELFEEVIvp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 -HIPMVVMDWGEAKADFTDavIDNAfEGGYMAGRYLIERGHREI---GVIPGPLERNT-GAGRLAGFMKAMEEAMIKVPE 161
Cdd:cd06297 77 tEKPVVLIDANSMGYDCVY--VDNV-KGGFMATEYLAGLGEREYvffGIEEDTVFTETvFREREQGFLEALNKAGRPISS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 162 SWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARyfTPALTTIHQP 241
Cdd:cd06297 154 SRMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQP 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1943035 242 KDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06297 232 VEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
7-280 |
4.13e-38 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 137.20 E-value: 4.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 7 TKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLeeYR 86
Cdd:PRK10727 59 TETVGLVVGDVSDPFFGAMVKAVEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASL--MK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIP-MVVMDwgEAKADFTDAVI--DNAFeGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESW 163
Cdd:PRK10727 137 QIPgMVLIN--RILPGFENRCIalDDRY-GAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 164 IVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKD 243
Cdd:PRK10727 214 VTFGEPDESGGEQAMTELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIV 293
|
250 260 270
....*....|....*....|....*....|....*...
gi 1943035 244 SLGETAFNMLLdRIVNKREEPQSIEV-HPRLIERRSVA 280
Cdd:PRK10727 294 TMATQAAELAL-ALADNRPLPEITNVfSPTLVRRHSVS 330
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
20-278 |
7.91e-38 |
|
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: 134.34 E-value: 7.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 20 AYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRhIPMVVMDWGEAK 99
Cdd:cd06298 12 LYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSP-VPVVLAGTVDSD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 100 ADFTDAVIDNAfEGGYMAGRYLIERGHREIGVIPGPLERNT-GAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAM 178
Cdd:cd06298 91 HEIPSVNIDYE-QAAYDATKSLIDKGHKKIAFVSGPLKEYInNDKKLQGYKRALEEAGLEFNEPLIFEGDYDYDSGYELY 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 179 QQILSQpHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDrIV 258
Cdd:cd06298 170 EELLES-GEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVAMRLLTK-LM 247
|
250 260
....*....|....*....|.
gi 1943035 259 NKRE-EPQSIEVHPRLIERRS 278
Cdd:cd06298 248 NKEEvEETIVKLPHSIIWRQS 268
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
9-280 |
7.32e-34 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 126.04 E-value: 7.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyrHI 88
Cdd:PRK10401 61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMD--QI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 P-MVVMDWGEAKADFTDAVIDNAfEGGYMAGRYLIERGHREIGVIPG--PLERNtgAGRLAGFMKAMEEAMIKVPESWIV 165
Cdd:PRK10401 139 PgMVLINRVVPGYAHRCVCLDNV-SGARMATRMLLNNGHQRIGYLSSshGIEDD--AMRRAGWMSALKEQGIIPPESWIG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 166 QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSL 245
Cdd:PRK10401 216 TGTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASM 295
|
250 260 270
....*....|....*....|....*....|....*
gi 1943035 246 GETAFNMLLDRIVNKREEPQSIEVHPRLIERRSVA 280
Cdd:PRK10401 296 AKLATELALQGAAGNLDPRASHCFMPTLVRRHSVA 330
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
7-276 |
4.43e-32 |
|
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: 119.92 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 7 TKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYR 86
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGH-REIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIV 165
Cdd:pfam00532 81 GIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHkRPIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 166 QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMG-LRVPQDV-----SLIGYDNVRNAR---YFTPALT 236
Cdd:pfam00532 161 TGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVgiginSVVGFDGLSKAQdtgLYLSPLT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1943035 237 TIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIER 276
Cdd:pfam00532 241 VIQLPRQLLGIKASDMVYQWIPKFREHPRVLLIPRDFFKE 280
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
10-276 |
1.35e-31 |
|
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: 118.25 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLL-ATSSEAAYFAEIIEAVEKNCFQKGYTLIL-------GNAWNNLEKQRAYlsmmaqkRVDGLLVMcSEYPEPLLAM 81
Cdd:cd06272 2 IGLYwPSVGERVALTRLLSGINEAISKQGYNINLsicpykvGHLCTAKGLFSEN-------RFDGVIVF-GISDSDIEYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 82 LEEYRHIPMVVmdWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIpGPLERNTG-AGRLAGFMKAMEEAMIKVP 160
Cdd:cd06272 74 NKNKPKIPIVL--YNRESPKYSTVNVDN-EKAGRLAVLLLIQKGHKSIAYI-GNPNSNRNqTLRGKGFIETCEKHGIHLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQ 240
Cdd:cd06272 150 DSIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGV 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1943035 241 PKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIER 276
Cdd:cd06272 230 PIEKIAEESLRLILKLIEGRENEIQQLILYPELIFR 265
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
50-274 |
2.25e-29 |
|
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: 112.13 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 50 EKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHIPMVVM-----DWGEAKADFtdaviDNAfEGGYMAGRYLIER 124
Cdd:cd06271 44 ES*VPIRDLVETGSADGVILSEIEPNDPRVQFLTK-QNFPFVAHgrsd*PIGHAWVDI-----DNE-AGAYEAVERLAGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 125 GHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIkvpESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALC 204
Cdd:cd06271 117 GHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGL---TGYPLDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1943035 205 AADEMGLRVPQDVSLIGYDNVRN-ARYFTPALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLI 274
Cdd:cd06271 194 GLQAAGLKIGEDVSIIGKDSAPFlGAMITPPLTTVHAPIAEAGRELAKALLARIDGEDPETLQVLVQPSLS 264
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
107-274 |
6.83e-29 |
|
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: 111.09 E-value: 6.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 107 IDN-AFegGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGDFEPESGYRAMQQILSQP 185
Cdd:cd20009 100 FDNeAF--AYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQP 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 186 HRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIVNKREEP- 264
Cdd:cd20009 178 PRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPl 257
|
170
....*....|
gi 1943035 265 QSIEVhPRLI 274
Cdd:cd20009 258 QTLER-PELI 266
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
7-274 |
7.82e-29 |
|
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: 111.56 E-value: 7.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 7 TKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEY- 85
Cdd:COG1879 33 GKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVD-PDALAPALKKAk 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 -RHIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEAM-IKVPE 161
Cdd:COG1879 112 aAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKEALKEYPgIKVVA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 162 SwiVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLrvPQDVSLIGYDNVRNARyftPAL------ 235
Cdd:COG1879 192 E--QYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDGSPEAL---QAIkdgtid 264
|
250 260 270
....*....|....*....|....*....|....*....
gi 1943035 236 TTIHQPKDSLGETAFNMLLdRIVNKREEPQSIEVHPRLI 274
Cdd:COG1879 265 ATVAQDPYLQGYLAVDAAL-KLLKGKEVPKEILTPPVLV 302
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
10-273 |
1.28e-25 |
|
periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.
Pssm-ID: 380478 [Multi-domain] Cd Length: 268 Bit Score: 102.26 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEYR--H 87
Cdd:cd01536 2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVD-SEALVPAVKKANaaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDWGEAKADFTDAVI--DNaFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEAmikvPESW 163
Cdd:cd01536 81 IPVVAVDTDIDGGGDVVAFVgtDN-YEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKEALKKY----PDIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 164 IV---QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLrvPQDVSLIGYDNVrnaryfTPALT---- 236
Cdd:cd01536 156 IVaeqPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGT------PEALKaikd 227
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1943035 237 -----TIHQPKDSLGETAFNMLLDrIVNKREEPQSIEVHPRL 273
Cdd:cd01536 228 geldaTVAQDPYLQGYLAVEAAVK-LLNGEKVPKEILTPVTL 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
10-223 |
1.49e-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: 102.44 E-value: 1.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVmCSEYPEPLLAMLE--EYRH 87
Cdd:cd06319 2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIII-SPTNSSAAPTVLDlaNEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER------GHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPE 161
Cdd:cd06319 81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1943035 162 SwIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRvpQDVSLIGYD 223
Cdd:cd06319 161 L-RQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFD 219
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
21-273 |
1.21e-23 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 98.29 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQKGYTLIlgNAWNNLEKQraylsmmAQKRVDGLLVMCSEYPEPLLAMleEYRHIPMVVMDWGEAKA 100
Cdd:PRK10339 81 YYLAIRHGIETQCEKLGIELT--NCYEHSGLP-------DIKNVTGILIVGKPTPALRAAA--SALTDNICFIDFHEPGS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 101 DFTDAVIDNAFEGGYMAGrYLIERGHREIGVIPGPLERNTGAGRLAGFMkamEEAMIK--VPESWIVQGDFEPESGYRAM 178
Cdd:PRK10339 150 GYDAVDIDLARISKEIID-FYINQGVNRIGFIGGEDEPGKADIREVAFA---EYGRLKqvVREEDIWRGGFSSSSGYELA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 179 QQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLGETAFNMLLDRIV 258
Cdd:PRK10339 226 KQMLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKAR 305
|
250
....*....|....*
gi 1943035 259 NKREEPQSIEVHPRL 273
Cdd:PRK10339 306 DGRALPLLVFVPSKL 320
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
10-277 |
9.15e-23 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 95.93 E-value: 9.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEII----EAVEkncfQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVM-CSEYPEPLLAMLEE 84
Cdd:PRK10014 67 IGLIVRDLSAPFYAELTagltEALE----AQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAgAAGSSDDLREMAEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 85 yRHIPMVVMdwgeAKADFTDAV----IDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVP 160
Cdd:PRK10014 143 -KGIPVVFA----SRASYLDDVdtvrPDN-MQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFH 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESWIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRV---------PQDVSLIGYDNVRNARYF 231
Cdd:PRK10014 217 SEWVLECTSSQKQAAEAITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQSgesgvdryfEQQVALAAFTDVPEAELD 296
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1943035 232 TPALTTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERR 277
Cdd:PRK10014 297 DPPLTWASTPAREIGRTLADRMMQRITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
9-274 |
1.82e-22 |
|
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: 93.81 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEyRHI 88
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQA-AGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 89 PMVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESWIVQGD 168
Cdd:cd06274 80 PVVFLDRPFSGSDAPSVVSDN-RAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 169 FEPESGYRAMQQILsQPHR--PTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSLG 246
Cdd:cd06274 159 YDRESGYQLMAELL-ARLGglPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIA 237
|
250 260
....*....|....*....|....*...
gi 1943035 247 ETAFNMLLDRIVnKREEPQSIEVHPRLI 274
Cdd:cd06274 238 EHAFELLDALIE-GQPEPGVIIIPPELI 264
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
10-281 |
7.86e-22 |
|
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: 92.28 E-value: 7.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAA-YFAE---IIEAVEKNcfqkGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYpEPLLAMLEEY 85
Cdd:cd06309 2 VGFSQAGSESPwRVANtksIKEAAKKR----GYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDA-TGWDPVLKEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 RH--IPMVVMDW---GEAKADFTDAVIDNAFEGGYMAGRYLIE---RGHREIGVIPGPLERNTGAGRLAGFMKAMEEA-M 156
Cdd:cd06309 77 KDagIPVILVDRtidGEDGSLYVTFIGSDFVEEGRRAAEWLVKnykGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHpN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 157 IKVPESwiVQGDFEPESGYRAMQQIL-SQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYD-------NVRNA 228
Cdd:cd06309 157 IKIVAS--QSGNFTREKGQKVMENLLqAGPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDgqkdaleAIKAG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1943035 229 RYftpALTTIHQPKdsLGETAFNmLLDRIVNKREEPQSIEVHPRLIERRSVAD 281
Cdd:cd06309 235 EL---NATVECNPL--FGPTAFD-TIAKLLAGEKVPKLIIVEERLFDKDNAAE 281
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
10-260 |
8.46e-20 |
|
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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 86.21 E-value: 8.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLIL-GNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEYR-- 86
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVvGPAEADAAEQVAQIEDAIAQGVDAIIVAPVD-PTALAPVLKKAKda 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEE--AMIKVPES 162
Cdd:pfam13407 80 GIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKEkyPGIKVVAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 163 WIVQGDfEPESGYRAMQQILSQ-PHRPTAVFCGGDIMAMGALCAADEMGLRvpQDVSLIGYDNVRNARYFTPA---LTTI 238
Cdd:pfam13407 160 VEGTNW-DPEKAQQQMEALLTAyPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEALEAIKDgtiDATV 236
|
250 260
....*....|....*....|..
gi 1943035 239 HQPKDSLGETAFNMLLDRIVNK 260
Cdd:pfam13407 237 LQDPYGQGYAAVELAAALLKGK 258
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
10-274 |
1.11e-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: 380545 [Multi-domain] Cd Length: 270 Bit Score: 86.18 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEYR--H 87
Cdd:cd06322 2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVD-SGGIVPAIEAANeaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER---GHREIGVIPGPLERNTGAgRLAGFmkamEEAMIKVPESWI 164
Cdd:cd06322 81 IPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKAllgGGGKIAIIDYPEVESVVL-RVNGF----KEAIKKYPNIEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 165 VQ---GDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGlrVPQDVSLIGYDNVRNARYFTPA----LTT 237
Cdd:cd06322 156 VAeqpGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDGNPEAIKAIAKggkiKAD 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 1943035 238 IHQPKDSLGETAFNMLLDRIVNKREEPQsIEVHPRLI 274
Cdd:cd06322 234 IAQQPDKIGQETVEAIVKYLAGETVEKE-ILIPPKLY 269
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
7-269 |
2.13e-18 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 83.54 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 7 TKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEeYR 86
Cdd:PRK14987 63 SRAIGVLLPSLTNQVFAEVLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIE-VA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIPMV-VMDWGEAKADFtdAVIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTgAGRLAGFMKAMEEAMIkVPESWIV 165
Cdd:PRK14987 142 GIPVVeLMDSQSPCLDI--AVGFDNFEAARQMTTAIIARGHRHIAYLGARLDERT-IIKQKGYEQAMLDAGL-VPYSVMV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 166 QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTTIHQPKDSL 245
Cdd:PRK14987 218 EQSSSYSSGIELIRQARREYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERM 297
|
250 260
....*....|....*....|....
gi 1943035 246 GETAFNMLLDRIVNKREEPQSIEV 269
Cdd:PRK14987 298 GSIGAERLLARIRGESVTPKMLDL 321
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
21-264 |
5.05e-18 |
|
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: 81.93 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLEEYRHIPMVV------MD 94
Cdd:cd01391 16 FGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQLFDIPQLAldatsqDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 95 WGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGVIPGPlERNTGAGRLAGFMKAMEEAMIKV----PESWivqgdFE 170
Cdd:cd01391 96 SDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGE-GLNSGELRMAGFKELAKQEGICIvasdKADW-----NA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 171 PESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRvpQDVSLIGYDNVRNARYF-----TPALTTIHQPKDSL 245
Cdd:cd01391 170 GEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDEVgyeveANGLTTIKQQKMGF 247
|
250
....*....|....*....
gi 1943035 246 GETAFNMLLDRIVNKREEP 264
Cdd:cd01391 248 GITAIKAMADGSQNMHEEV 266
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
56-278 |
1.53e-17 |
|
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380485 [Multi-domain] Cd Length: 265 Bit Score: 80.32 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 56 LSMMAQKRVDGLLvmCSEYPEPLLAMLEEyRHIPMVVMDWGEAKADFTDAVIDNAfEGGYMAGRYLIERGHREIGVIpGP 135
Cdd:cd01543 43 LDLLKGWKGDGII--ARLDDPELAEALRR-LGIPVVNVSGSRPEPGFPRVTTDNE-AIGRMAAEHLLERGFRHFAFC-GF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 136 LERNTGAGRLAGFMKAMEEAMIKV------PESWIVQGDFEPEsgyRAMQQILSQPhRPTAVFCGGDIMAMGALCAADEM 209
Cdd:cd01543 118 RNAAWSRERGEGFREALREAGYEChvyespPSGSSRSWEEERE---ELADWLKSLP-KPVGIFACNDDRARQVLEACREA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1943035 210 GLRVPQDVSLIGYDN---VRNARYftPALTTIHQPKDSLG-ETAfnMLLDRIVNKRE-EPQSIEVHP-RLIERRS 278
Cdd:cd01543 194 GIRVPEEVAVLGVDNdelICELSS--PPLSSIALDAEQIGyEAA--ELLDRLMRGERvPPEPILIPPlGVVTRQS 264
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
9-275 |
3.64e-17 |
|
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: 79.26 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLV--MCSEYPEPLLAMLEEyR 86
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLInpTDSDAVSPAVEEANE-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHREIGV-----IPGplernTGAG--RLAGFmkamEEAMIKV 159
Cdd:cd06323 80 GIPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVvelqgIPG-----TSAAreRGKGF----HNAIAKY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 160 PESWIV---QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGlrvPQDVSLIGYDN-------VRNAR 229
Cdd:cd06323 151 PKINVVasqTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGtpdavkaVKDGK 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1943035 230 YftpALTTIHQPKDsLG----ETAfnmllDRIVNKREEPQSIEVHPRLIE 275
Cdd:cd06323 228 L---AATVAQQPEE-MGakavETA-----DKYLKGEKVPKKIPVPLKLVT 268
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
23-274 |
5.17e-17 |
|
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: 78.74 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 23 AEIIEAVEKNcfqKGYTLILGNAWNNLEKQRAYLSMMAQKRVDgLLVMCSEYPEPLLAMLEE-YRH-IPMVVMDWGEAKA 100
Cdd:cd06308 19 EEIKAEAAKY---PNVELIVTDAQGDAAKQIADIEDLIAQGVD-LLIVSPNEADALTPVVKKaYDAgIPVIVLDRKVSGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 101 DFTdAVI--DNaFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEAM-IKVPESwiVQGDFEPESGY 175
Cdd:cd06308 95 DYT-AFIgaDN-VEIGRQAGEYIAELlnGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYPgIKIVAS--QDGDWLRDKAI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 176 RAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRvpQDVSLIGYD--------NVRNARYFtpalTTIHQPkdSLGE 247
Cdd:cd06308 171 KVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVDglpeagekAVKDGILA----ATFLYP--TGGK 242
|
250 260
....*....|....*....|....*..
gi 1943035 248 TAFNMLLDrIVNKREEPQSIEVHPRLI 274
Cdd:cd06308 243 EAIEAALK-ILNGEKVPKEIVLPTPLI 268
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
13-278 |
8.65e-17 |
|
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: 78.23 E-value: 8.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 13 LATSSEAA---YFAEIIEAVEKNCFQKGYTLIL------GNAWNNLEkqraylsmmaqkrVDGLLVMCSEYPEPLLAMLE 83
Cdd:cd06287 10 FAIAGGASrlgFMMEVAAAAAEEALEHDLALVLvpplhhVSMLDALD-------------VDGAIVVEPTVEDPILARLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 84 EyRHIPMVVMdwGEAKADFTDA--VIDNAFEGGYMAGRYLIERGHREIGVIPGPLERNTGAGRLAGFMK-----AMEEAM 156
Cdd:cd06287 77 Q-RGVPVVSI--GRAPGTDEPVpyVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRfaqeyGTTPVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 157 IKVPESwivQGDFEpesGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIG-YDNVRnARYFTPAL 235
Cdd:cd06287 154 YKVPES---EGERA---GYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTrYDGIR-ARTADPPL 226
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1943035 236 TTIHQPKDSLGETAFNMLLdRIVNKREEPQSIEVHPRLIERRS 278
Cdd:cd06287 227 TAVDLHLDRVARTAIDLLF-ASLSGEERSVEVGPAPELVVRAS 268
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
107-273 |
1.81e-16 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380625 [Multi-domain] Cd Length: 275 Bit Score: 77.29 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 107 IDNaFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEAMIKVPESwiVQGDFEPESGYRAMQQILSQ 184
Cdd:cd19970 110 PDN-RQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAGMKIVAS--QSANWEIDEANTVAANLLTA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 185 PHRPTAVFCGGDIMAMGALCAADEMGLRvpQDVSLIGYDNVRNARyftPALT------TIHQPKDSLGETAFNMLLdRIV 258
Cdd:cd19970 187 HPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNIPAVR---PLLKdgkmlaTIDQHPAKQAVYGIEYAL-KML 260
|
170
....*....|....*
gi 1943035 259 NKREEPQSIEVHPRL 273
Cdd:cd19970 261 NGEEVPGWVKTPVEL 275
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
21-223 |
1.57e-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: 380626 [Multi-domain] Cd Length: 267 Bit Score: 74.54 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLV--MCSEYPEPLLAMLEEYrHIPMVVMDWGEA 98
Cdd:cd19971 13 FFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLnpVDSEGIRPALEAAKEA-GIPVINVDTPVK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 99 KADFTDAVI--DNaFEGGYMAGRYLIERgHRE---IGVIPGPlERNTGAGRLAGFMKAMEEAmikvPESWIVQ---GDFE 170
Cdd:cd19971 92 DTDLVDSTIasDN-YNAGKLCGEDMVKK-LPEgakIAVLDHP-TAESCVDRIDGFLDAIKKN----PKFEVVAqqdGKGQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1943035 171 PESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLrvPQDVSLIGYD 223
Cdd:cd19971 165 LEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGK--LGDILVYGVD 215
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
10-274 |
2.62e-15 |
|
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: 73.96 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLV--MCSEYPEPLL-AMLEEyr 86
Cdd:cd19968 2 IGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVspIDVKALVPAIeAAIKA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIPMVVMDwgeAKADFTDAVI----DNaFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFmkamEEAMIKVP 160
Cdd:cd19968 80 GIPVVTVD---RRAEGAAPVPhvgaDN-VAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGF----HEELAAGP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESWIV---QGDFEPESGYRAMQQIL-SQPHRPTAVFCGGDIMAMGALCAADEMGLRVpQDVSLIGYDNVRNA-RYFTP-- 233
Cdd:cd19968 152 KIKVVfeqTGNFERDEGLTVMENILtSLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFDAVPDAlQAIKDge 230
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1943035 234 ALTTIHQPKDSLGETAFNMLLDRIvNKREEPQSIEVHPRLI 274
Cdd:cd19968 231 LYATVEQPPGGQARTALRILVDYL-KDKKAPKKVNLKPKLI 270
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
9-223 |
5.11e-13 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 67.37 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNL--EKQRAYLSMMAQKRVDGLLVmCSEYPEPLLAMLEEY- 85
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPESEEdvAGQNSLLEELINKKPDAIVV-APLDSEDLVDPLKDAk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 86 -RHIPMVVMDWGeAKADFTDAVI--DNaFEGGYMAGRYLIE--RGHREIGVIPGPLERNTGAGRLAGFMKAM-EEAMIKV 159
Cdd:cd06310 80 dKGIPVIVIDSG-IKGDAYLSYIatDN-YAAGRLAAQKLAEalGGKGKVAVLSLTAGNSTTDQREEGFKEYLkKHPGGIK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1943035 160 PESWIVQGDFEPEsGYRAMQQILSQphRPTA--VFCGGDIMAMGALCAADEMGLRvpQDVSLIGYD 223
Cdd:cd06310 158 VLASQYAGSDYAK-AANETEDLLGK--YPDIdgIFATNEITALGAAVAIKSRKLS--GQIKIVGFD 218
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
10-211 |
9.66e-12 |
|
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: 63.97 E-value: 9.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDgLLVMCSEYPEPLLAMLE--EYRH 87
Cdd:cd06318 2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVD-VLILNPVDPEGLTPAVKaaKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDWG-EAKADFTDAVIDNAFEGGYMAGRYLIER-GHREIGVI-----PGPLErntGAGRLAGFMKAMEEAMIKVP 160
Cdd:cd06318 81 IPVITVDSAlDPSANVATQVGRDNKQNGVLVGKEAAKAlGGDPGKIIelsgdKGNEV---SRDRRDGFLAGVNEYQLRKY 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1943035 161 ESW---IVQGDF---EPESGYRAMQQILsQPHrPTA--VFCGGDIMAMGALCAADEMGL 211
Cdd:cd06318 158 GKSnikVVAQPYgnwIRSGAVAAMEDLL-QAH-PDInvVYAENDDMALGAMKALKAAGM 214
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
9-223 |
1.03e-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 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: 63.85 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNC--FQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDgLLVMCSEYPEPLLAMLEEYR 86
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAaeINPGAKVTVVDARYDLAKQFSQIDDFIAQGVD-LILLNAADSAGIEPAIKRAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 H--IPMVVMDWGEAKADFTdaVIDNAFEGGYMAGRYLIER--GHREIGVIPGPleRNTGA-GRLAGFMKAMEEAM-IKVP 160
Cdd:cd06321 80 DagIIVVAVDVAAEGADAT--VTTDNVQAGYLACEYLVEQlgGKGKVAIIDGP--PVSAViDRVNGCKEALAEYPgIKLV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943035 161 EswIVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRvpqDVSLIGYD 223
Cdd:cd06321 156 D--DQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---DIVITSVD 213
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
10-223 |
1.10e-10 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 60.92 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMcseyPEPLLAM-----LEE 84
Cdd:cd19972 2 IGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYI----PAGATAAavpvkAAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 85 YRHIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEA--MIKVP 160
Cdd:cd19972 78 AAGIPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQtgGKGEIAILHGQLGTTPEVDRTKGFQEALAEApgIKVVA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943035 161 ESWivqGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLrvPQDVSLIGYD 223
Cdd:cd19972 158 EQT---ADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFD 215
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
60-228 |
8.07e-10 |
|
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: 58.38 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 60 AQKRVDGLLVMcseyPE-----PLLAMLEEYRhIPMVVMDwgeakADFTDA------------------VIDNAFEGGYM 116
Cdd:cd06324 55 RPPKPDYLILV----NEkgvapELLELAEQAK-IPVFLIN-----NDLTDEerallgkprekfkywlgsIVPDNEQAGYL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 117 AGRYLIERGHREIGVIPGPL-----ERNTGAG--RLAGFMKAMEEA-MIKVPEswIVQGDFEPESGYRAMQQILSQPHRP 188
Cdd:cd06324 125 LAKALIKAARKKSDDGKIRVlaisgDKSTPASilREQGLRDALAEHpDVTLLQ--IVYANWSEDEAYQKTEKLLQRYPDI 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1943035 189 TAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNA 228
Cdd:cd06324 203 DIVWAANDAMALGAIDALEEAGLKPGKDVLVGGIDWSPEA 242
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
1-277 |
1.18e-09 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 57.97 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 1 SLKVNHTKSIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPE-PLL 79
Cdd:PRK11303 55 GLRAGRTRSIGLIIPDLENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEhPFY 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 80 AMLEEyRHIPMVVMDWGEAKADFTDAVIDNaFEGGYMAGRYLIERGHREIGVIpGPL-ERNTGAGRLAGFMKAMEEAMIK 158
Cdd:PRK11303 135 QRLQN-DGLPIIALDRALDREHFTSVVSDD-QDDAEMLAESLLKFPAESILLL-GALpELSVSFEREQGFRQALKDDPRE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 159 VPeswIVQGD-FEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVPQDVSLIGYDNVRNARYFTPALTT 237
Cdd:PRK11303 212 VH---YLYANsFEREAGAQLFEKWLETHPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGDNELLDFLPCPVNA 288
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1943035 238 IHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLIERR 277
Cdd:PRK11303 289 VAQQHRLIAERALELALAALDEPRKPKPGLTRIRRNLKRR 328
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
10-281 |
1.37e-09 |
|
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: 57.67 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYL-SMMAQKrVDGLLV--MCSEYPEPLLAMLEEyR 86
Cdd:cd06313 2 IGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVdTLIAQG-VDAIIVvpVDADALAPAVEKAKE-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEAM-IKVPESw 163
Cdd:cd06313 80 GIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQSAQIDRGKGIENVLKKYPdIKVLAE- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 164 iVQGDFEPESGYRAMQQILSQ-PHRPTAVFCGGDIMAMGALCAADEMGLrvpQDVSLIGYD-------NVRNARYftpaL 235
Cdd:cd06313 159 -QTANWSRDEAMSLMENWLQAyGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDgiedalqAVKSGEL----I 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1943035 236 TTIHQPKDSLGETAFNMLLDrIVNKREEPQSIEVHPRLIERRSVAD 281
Cdd:cd06313 231 ATVLQDAEAQGKGAVEVAVD-AVKGEGVEKKYYIPFVLVTKDNVDD 275
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
9-223 |
5.16e-09 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 55.87 E-value: 5.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLV--MCSEYPEPLLAMLEEyR 86
Cdd:PRK10653 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLInpTDSDAVGNAVKMANQ-A 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 87 HIPMVVMDWGEAKADFTDAVI-DNAFeGGYMAGRYLIERGHREIGVIPgpLE--RNTGAGRL--AGFMKAMEEAMIKVPE 161
Cdd:PRK10653 107 NIPVITLDRGATKGEVVSHIAsDNVA-GGKMAGDFIAKKLGEGAKVIQ--LEgiAGTSAARErgEGFKQAVAAHKFNVLA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1943035 162 SwivQ-GDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGlrvPQDVSLIGYD 223
Cdd:PRK10653 184 S---QpADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFD 240
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
88-270 |
5.24e-09 |
|
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: 55.79 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDW-----GEAKADFtdaVIDNaFEGGYMAGRYLIERGHREIGVIP--GPLERNTGAGRLAGFmkamEEAMIKVP 160
Cdd:cd19967 81 IPVFLIDReinaeGVAVAQI---VSDN-YQGAVLLAQYFVKLMGEKGLYVEllGKESDTNAQLRSQGF----HSVIDQYP 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 161 ESWIV---QGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLrvPQDVSLIGYD---NVRNARYFTPA 234
Cdd:cd19967 153 ELKMVaqqSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDgsnDVRDAIKEGKI 230
|
170 180 190
....*....|....*....|....*....|....*....
gi 1943035 235 LTTIHQPKDSLGETAFNM---LLDRIVNKREEPQSIEVH 270
Cdd:cd19967 231 SATVLQPAKLIARLAVEQadqYLKGGSTGKEEKQLFDCV 269
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
52-280 |
1.43e-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: 54.58 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 52 QRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEY--RHIPMVVMDWG-------EAKADFTDAVIDNAFEGGYMAGRYLI 122
Cdd:cd06320 46 QLNLLETMLNKGYDAILVSPIS-DTNLIPPIEKAnkKGIPVINLDDAvdadalkKAGGKVTSFIGTDNVAAGALAAEYIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 123 ER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEAM-IKVPESwiVQGDFEPESGYRAMQQILSQPHRPTAVFCGGDIMA 199
Cdd:cd06320 125 EKlpGGGKVAIIEGLPGNAAAEARTKGFKETFKKAPgLKLVAS--QPADWDRTKALDAATAILQAHPDLKGIYAANDTMA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 200 MGALCAADEMGLRvpQDVSLIGYDNVRNARYFTPA--LT-TIHQPKDSLGETAFNMLLdRIVNKREEPQSIEVHPRLIER 276
Cdd:cd06320 203 LGAVEAVKAAGKT--GKVLVVGTDGIPEAKKSIKAgeLTaTVAQYPYLEGAMAVEAAL-RLLQGQKVPAVVATPQALITK 279
|
....
gi 1943035 277 RSVA 280
Cdd:cd06320 280 DNVD 283
|
|
| PBP1_TorT-like |
cd06306 |
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ... |
37-274 |
3.06e-08 |
|
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: 53.35 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 37 GYTLILGNA--WNNLEKQRAYLSMMAQKRVDGLLVMCSEYP--EPLLAMLEEyRHIPMVVMDWGEAKADFTDAVIDNAFE 112
Cdd:cd06306 29 GVKLTVYEAggYTNLSKQISQLEDCVASGADAILLGAISFDglDPKVAEAAA-AGIPVIDLVNGIDSPKVAARVLVDFYD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 113 GGYMAGRYLIERGHR---EIGVIPGPlERNTGA-GRLAGFMKAMEEAMIKVPEswIVQGDFEPESGYRAMQQILsQPHRP 188
Cdd:cd06306 108 MGYLAGEYLVEHHPGkpvKVAWFPGP-AGAGWAeDREKGFKEALAGSNVEIVA--TKYGDTGKAVQLNLVEDAL-QAHPD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 189 TAVFCGGDIMAMGALCAADEMGLRvpQDVSLI-------GYDNVRNAR-YFTPALTTIHQpkdslGETAFNMLLdRIVNK 260
Cdd:cd06306 184 IDYIVGNAVAAEAAVGALREAGLT--GKVKVVstyltpgVYRGIKRGKiLAAPSDQPVLQ-----GRIAVDQAV-RALEG 255
|
250
....*....|....
gi 1943035 261 REEPQSIEVHPRLI 274
Cdd:cd06306 256 KPVPKHVGPPILVV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
20-210 |
6.21e-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: 52.75 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 20 AYFAEiieAVEKNCFQKGYTLILGNawnNLEKQRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEYRH--IPMVVMDWGE 97
Cdd:cd06311 18 AYYAE---KQAKELADLEYKLVTSS---NANEQVSQLEDLIAQKVDAIVILPQD-SEELTVAAQKAKDagIPVVNFDRGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 98 AKADFTDAVIDNAFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEE-AMIKVPESWivQGDFEPESG 174
Cdd:cd06311 91 NVLIYDLYVAGDNPGMGVVSAEYIGKKlgGKGNVVVLEVPSSGSVNEERVAGFKEVIKGnPGIKILAMQ--AGDWTREDG 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 1943035 175 YRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMG 210
Cdd:cd06311 169 LKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAG 204
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
21-214 |
1.13e-07 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 51.86 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKnCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVmCSEYPEPLLAMLEEYRH--IPMVVMDWGEA 98
Cdd:cd19996 17 MIAEFEAEAAK-LKKLIKELIYTDAQGDTQKQIADIQDLIAQGVDAIIV-SPNSPTALLPAIEKAAAagIPVVLFDSGVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 99 KADFTDAVIDNAFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEEAM-IKVPESwiVQGDFEPESGY 175
Cdd:cd19996 95 SDKYTAFVGVDDAAFGRVGAEWLVKQlgGKGNIIALRGIAGVSVSEDRWAGAKEVFKEYPgIKIVGE--VYADWDYAKAK 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1943035 176 RAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVP 214
Cdd:cd19996 173 QAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLV 211
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
62-274 |
9.48e-07 |
|
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: 9.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 62 KRVDGLLVMCSEYPEpLLAMLEEYRH--IPMVVMDwgeakADFTDAV------IDNAFEG---GYMAGRYLIERGHReIG 130
Cdd:cd06307 57 AGCDGVALVAPDHPL-VRAAIDELAArgIPVVTLV-----SDLPGSRrlayvgIDNRAAGrtaAWLMGRFLGRRPGK-VL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 131 VIPGPLERNTGAGRLAGFMKAMEE--AMIKVPESWIVQGDfePESGYRAMQQILSQPHRPTAVFC-GGDIMAMGAlcAAD 207
Cdd:cd06307 130 VILGSHRFRGHEEREAGFRSVLRErfPDLTVLEVLEGLDD--DELAYELLRELLARHPDLVGIYNaGGGNEGIAR--ALR 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943035 208 EMGLrvPQDVSLIGYD-NVRNARyftpAL------TTIHQPKDSLGETAFNMLLDRIVNKREEPQSIEVHPRLI 274
Cdd:cd06307 206 EAGR--ARRVVFIGHElTPETRR----LLrdgtidAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEII 273
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
21-265 |
2.81e-06 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 47.96 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQ-KGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSE--YPEPLLAMLEEYRhIPMV------ 91
Cdd:cd01539 14 FISSVRKALEKAAKAgGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDrtAAQTIIDKAKAAN-IPVIffnrep 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 92 ----VMDWGeaKADFTDAvidNAFEGGYMAGRYLIE--RGHREI-----GVI--------PGplerNTGA-GRLAGFMKA 151
Cdd:cd01539 93 sredLKSYD--KAYYVGT---DAEESGIMQGEIIADywKANPEIdkngdGKIqyvmlkgePG----HQDAiARTKYSVKT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 152 MEEAMIKVPESWIVQGDFEPESGYRAMQQILSQPH-RPTAVFCGGDIMAMGALCAADEMGL---RVPQDVSLIGYDNVrn 227
Cdd:cd01539 164 LNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYGdKIELVIANNDDMALGAIEALKAAGYntgDGDKYIPVFGVDAT-- 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1943035 228 aryfTPALT---------TIHQPKDSLGETAFNMLLDrIVNKREEPQ 265
Cdd:cd01539 242 ----PEALEaikegkmlgTVLNDAKAQAKAIYELAKN-LANGKEPLE 283
|
|
| PBP1_ABC_sugar_binding-like |
cd20005 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
47-223 |
3.60e-06 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380660 [Multi-domain] Cd Length: 274 Bit Score: 47.24 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 47 NNLEKQRAYLSMMAQKRVDGLLVMCSEYpEPLLAMLEEYRH--IPMVVMDWGeAKADFTDAVI--DNAFEGGyMAGRYLI 122
Cdd:cd20005 41 SDVDKQIEMLDNAIAKKPDAIALAALDT-NALLPQLEKAKEkgIPVVTFDSG-VPSDLPLATVatDNYAAGA-LAADHLA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 123 E--RGHREIGVIPGPLERNTGAGRLAGFMKAMEEamiKVPESWIVQGDFEPESGYRAM---QQILSQPHRPTAVFCGGDI 197
Cdd:cd20005 118 EliGGKGKVAIVAHDATSETGIDRRDGFKDEIKE---KYPDIKVVNVQYGVGDHAKAAdiaKAILQANPDLKGIYATNEG 194
|
170 180
....*....|....*....|....*.
gi 1943035 198 MAMGALCAADEMGLRvpQDVSLIGYD 223
Cdd:cd20005 195 AAIGVANALKEMGKL--GKIKVVGFD 218
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
10-224 |
2.07e-05 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 44.88 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFaeiiEAVEKNCFQK----GYTLI-LGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYP--EPLLAML 82
Cdd:cd06314 2 FALVPKGLNNPFW----DLAEAGAEKAakelGVNVEfVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEavTPVINKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 83 EEyRHIPMVVMDwgeakadfTDAV---------IDNaFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKA 151
Cdd:cd06314 78 AD-KGIPVITFD--------SDAPdskrlayigTDN-YEAGREAGELMKKAlpGGGKVAIITGGLGADNLNERIQGFKDA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1943035 152 MEEAM-IKVPESWIVQGDfePESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRvpQDVSLIGYDN 224
Cdd:cd06314 148 LKGSPgIEIVDPLSDNDD--IAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKV--GKVKIVGFDT 217
|
|
| PBP1_ABC_sugar_binding-like |
cd19969 |
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ... |
62-224 |
4.81e-05 |
|
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380624 [Multi-domain] Cd Length: 278 Bit Score: 43.87 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 62 KRVDGLLVMCSEyPEPLLAMLEEYRH--IPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER--GHREIGVIPGPLE 137
Cdd:cd19969 55 KNPDGIAVSAID-PEALTPTINKAVDagIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELlgGKGKVAVLTGPGQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 138 RNTGAgRLAGFMKAMEE-AMIKVPESWIVQGDfePESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRVpqD 216
Cdd:cd19969 134 PNHEE-RVEGFKEAFAEyPGIEVVAVGDDNDD--PEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTG--K 208
|
....*...
gi 1943035 217 VSLIGYDN 224
Cdd:cd19969 209 VKIVAFDD 216
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
47-223 |
5.92e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 43.76 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 47 NNLEKQRAYLSMMAQKRVDGLlVMCSEYPEPLLAMLEEYRH--IPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIER 124
Cdd:cd20004 41 DDVEAQIQIIEYFIDQGVDGI-VLAPLDRKALVAPVERARAqgIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 125 GHREIGVIPGPLERNTG--AGRLAGFMKAMEEAMikvPESWIVQ----GDFEPESGYRAmQQILSQPHRPTAVFCGGDIM 198
Cdd:cd20004 120 LNGKGKVALLRLAKGSAstTDRERGFLEALKKLA---PGLKVVDdqyaGGTVGEARSSA-ENLLNQYPDVDGIFTPNEST 195
|
170 180
....*....|....*....|....*
gi 1943035 199 AMGALCAADEMGLRVpqDVSLIGYD 223
Cdd:cd20004 196 TIGALRALRRLGLAG--KVKFIGFD 218
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
9-223 |
4.53e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 40.82 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 9 SIGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEYPEPLLAMLE-EYRH 87
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRaSEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDwGEAKADFTDAVI--DNAfEGGYMAGRYLIE------RGHREIGVIpGPLERNTGAGRLAGFmkamEEAMIKV 159
Cdd:cd06317 81 IPVIAYD-AVIPSDFQAAQVgvDNL-EGGKEIGKYAADyikaelGGQAKIGVV-GALSSLIQNQRQKGF----EEALKAN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1943035 160 PESWIVQ---GDFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRvpQDVSLIGYD 223
Cdd:cd06317 154 PGVEIVAtvdGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQ--GKIKVFGWD 218
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
10-251 |
4.85e-04 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 41.03 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDgLLVMCSEYPEPLLAMLEeYRH-- 87
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGID-VLIIAPVDAGAAANIVD-KAKaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 -IPMVVMDWGEAKADFTDAVIDNAFEGGYMAGRYLIERGHR-EIGVIPGPlERNTGAGRL-AGFMKAMEEAM----IK-V 159
Cdd:cd19992 80 gVPVISYDRLILNADVDLYVGRDNYKVGQLQAEYALEAVPKgNYVILSGD-PGDNNAQLItAGAMDVLQPAIdsgdIKiV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 160 PESWIVqgDFEPESGYRAMQQILSQPH-RPTAVFCGGDIMAMGALCAADEMGLrvPQDVSLIGYD-NVRNARYF---TPA 234
Cdd:cd19992 159 LDQYVK--GWSPDEAMKLVENALTANNnNIDAVLAPNDGMAGGAIQALKAQGL--AGKVFVTGQDaELAALKRIvegTQT 234
|
250
....*....|....*..
gi 1943035 235 LtTIHQPKDSLGETAFN 251
Cdd:cd19992 235 M-TVWKDLKELARAAAD 250
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
21-224 |
5.62e-04 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr 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: 380621 [Multi-domain] Cd Length: 278 Bit Score: 40.77 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 21 YFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEYRH---IPMVVMDW-- 95
Cdd:cd19966 14 FWTVVYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAIMGHP-GDGAYTPLIEAAKkagIIVTSFNTdl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 96 --GEAKADFTDAVIDNAFEGGYMAGRYLIER-----GHReiGVIPGPLERNTGAG-RLAGFMKAMEEAMIKVPESWIVQG 167
Cdd:cd19966 93 pkLEYGDCGLGYVGADLYAAGYTLAKELVKRgglktGDR--VFVPGLLPGQPYRVlRTKGVIDALKEAGIKVDYLEISLE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1943035 168 DFEPESGYRAMQQILSQPHRPTAVFCGGDIMAMGALCAADEMGLRvPQDVSLIGYDN 224
Cdd:cd19966 171 PNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKK-PGEIPVAGFDL 226
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
109-223 |
1.12e-03 |
|
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: 39.91 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 109 NAFEGGYMAGRYLIER--GHREIGVIPGPLERNTGAGRLAGFMKAMEeamiKVPESWIVQ---GDFEPESGYRAMQQILS 183
Cdd:cd06301 105 DDIESGELQMEYLAKLlgGKGNIAILDGVLGHEAQILRTEGNKDVLA----KYPGMKIVAeqtANWSREKAMDIVENWLQ 180
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1943035 184 QPHRPTAVFCGGDIMAMGALCAADEMGLRVpqDVSLIGYD 223
Cdd:cd06301 181 SGDKIDAIVANNDEMAIGAILALEAAGKKD--DILVAGID 218
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
10-252 |
2.88e-03 |
|
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380646 [Multi-domain] Cd Length: 284 Bit Score: 38.37 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 10 IGLLATSSEAAYFAEIIEAVEKNCFQKGYTLILGNAWNNLEKQRAYLSMMAQKRVDGLLVMCSEyPEPLLAMLEEYRH-- 87
Cdd:cd19991 2 IGFSMDSLRVERWQRDRDYFVKKAKELGAEVIVQSANGDDEKQISQAEELIEQGVDVLVVVPNN-GEALAPIVKEAKKag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 88 IPMVVMDWGEAKADFtDAVI--DNaFEGGYMAGRYLIERGHR-EIGVIPGPLERNTGAGRLAGFMKA----MEEAMIK-V 159
Cdd:cd19991 81 VPVLAYDRLILNADV-DLYVsfDN-EKVGELQAEALVKAKPKgNYVLLGGSPTDNNAKLFREGQMKVlqplIDSGDIKvV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1943035 160 PESWIvqGDFEPESGYRAMQQILSQ-PHRPTAVFCGGDIMAMGALCAADEMGL--RVP---QDVSLIGYDNVRNARyftp 233
Cdd:cd19991 159 GDQWV--DDWDPEEALKIMENALTAnNNKIDAVIASNDGTAGGAIQALAEQGLagKVAvsgQDADLAACQRIVEGT---- 232
|
250
....*....|....*....
gi 1943035 234 ALTTIHQPKDSLGETAFNM 252
Cdd:cd19991 233 QTMTIYKPIKELAEKAAEL 251
|
|
| |
