|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-335 |
5.37e-125 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 361.82 E-value: 5.37e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 1 MVTIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSsanvaLQNPFFP 80
Cdd:COG1609 3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPD-----LSNPFFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 81 EILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLREQGFPFVMVGKPQEhDTEIT 160
Cdd:COG1609 78 ELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLP-DPGVP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 161 HVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIHTEFLKSGGREAVEHLMSL 240
Cdd:COG1609 157 SVGVDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 241 STPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEKTLNKNEPA 320
Cdd:COG1609 237 GPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPP 316
|
330
....*....|....*
gi 1896925672 321 KRIIIPYEIVYRDSV 335
Cdd:COG1609 317 ERVLLPPELVVREST 331
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
61-330 |
2.90e-116 |
|
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: 337.25 E-value: 2.90e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSSANVALQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd06294 1 TIGLVLPSSAEELFQNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDPLIEYLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPQEHDtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYK 220
Cdd:cd06294 81 EEGFPFVVIGKPLDDN-DVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYT 300
Cdd:cd06294 160 LLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPYE 239
|
250 260 270
....*....|....*....|....*....|
gi 1896925672 301 LGAQSAKALIEKTLNKNEPAKRIIIPYEIV 330
Cdd:cd06294 240 LGREAAKLLINLLEGPESLPKNVIVPHELI 269
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
62-330 |
1.25e-84 |
|
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: 256.29 E-value: 1.25e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLRE 141
Cdd:cd06267 2 IGLIVPD-----ISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 142 QGFPFVMVGKPQEHDtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKI 221
Cdd:cd06267 77 AGIPVVLIDRRLDGL-GVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 222 HTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTL 301
Cdd:cd06267 156 EGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEM 235
|
250 260
....*....|....*....|....*....
gi 1896925672 302 GAQSAKALIEKTLNKNEPAKRIIIPYEIV 330
Cdd:cd06267 236 GRAAAELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
61-334 |
3.33e-68 |
|
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: 214.71 E-value: 3.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNfLR 140
Cdd:cd06284 1 TILVLVPN-----ISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLS-EL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPQEhDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYK 220
Cdd:cd06284 75 SKRYPIVQCCEYIP-DSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYT 300
Cdd:cd06284 154 IEGDFSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYE 233
|
250 260 270
....*....|....*....|....*....|....
gi 1896925672 301 LGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06284 234 IGETAAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
61-334 |
1.59e-62 |
|
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: 200.19 E-value: 1.59e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSSANVAlQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd06292 1 LIGYVVPELPGGF-SDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPRVRYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPqEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYK 220
Cdd:cd06292 80 EAGVPFVAFGRA-NPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYT 300
Cdd:cd06292 159 VEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDE 238
|
250 260 270
....*....|....*....|....*....|....
gi 1896925672 301 LGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06292 239 IGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-335 |
1.18e-61 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 197.83 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd06285 1 TIGVLVSD-----LSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPQEHdTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYK 220
Cdd:cd06285 76 ARGVPVVLVDRRIGD-TALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYT 300
Cdd:cd06285 155 VPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYE 234
|
250 260 270
....*....|....*....|....*....|....*
gi 1896925672 301 LGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDSV 335
Cdd:cd06285 235 MGRRAAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-334 |
3.48e-61 |
|
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: 196.62 E-value: 3.48e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLS-TGETEKEILSEVQrMVYGSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd19975 2 IGVIIPD-----ISNSFFAEILKGIEDEARENGYSVILCnTGSDEEREKKYLQ-LLKEKRVDGIIFASGTLTEENKQLLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPQEHDtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVT-RDRESGYVAALEKAGIQECEGY 219
Cdd:cd19975 76 NMNIPVVLVSTESEDP-DIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAgYPRYEGYKKALKDAGLPIKENL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 220 KIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIY 299
Cdd:cd19975 155 IVEGDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFY 234
|
250 260 270
....*....|....*....|....*....|....*
gi 1896925672 300 TLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd19975 235 EMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-334 |
1.07e-60 |
|
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: 195.14 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd06290 1 TIGVLVPD-----IDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGfPFVMVGKpQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYK 220
Cdd:cd06290 76 EGI-PVVLVDR-ELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYT 300
Cdd:cd06290 154 VEGDFTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYE 233
|
250 260 270
....*....|....*....|....*....|....
gi 1896925672 301 LGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06290 234 MGKTAAEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
4-335 |
3.10e-59 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 193.38 E-value: 3.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 4 IKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSSANvalqnPFFPEIL 83
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTN-----PFYSELV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 84 RGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFL-REQGFPFVMVG-KPQEHDTEITH 161
Cdd:PRK10423 76 RGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREIMqRYPSVPTVMMDwAPFDGDSDLIQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 162 vdnDNVRAGKEI-TQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIHTEFLKSGGREAVEHLMSL 240
Cdd:PRK10423 156 ---DNSLLGGDLaTQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 241 STPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEKTLNKNEPA 320
Cdd:PRK10423 233 PLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQ 312
|
330
....*....|....*
gi 1896925672 321 KRIIIPYEIVYRDSV 335
Cdd:PRK10423 313 QRLQLTPELMERGSV 327
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
62-334 |
8.77e-59 |
|
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: 190.55 E-value: 8.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANvalqnPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLRE 141
Cdd:cd06275 2 IGLLVTSSEN-----PFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 142 QG-FPFVMVgkpqehDTEITH-----VDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQE 215
Cdd:cd06275 77 LRsIPVVVL------DREIAGdnadaVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 216 CEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVD 295
Cdd:cd06275 151 PPSWIVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIH 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 1896925672 296 IQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06275 231 QPKDELGELAVELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
61-330 |
2.62e-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: 189.30 E-value: 2.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSSANVALqNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd20010 1 AIGLVLPLDPGDLG-DPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPqEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYK 220
Cdd:cd20010 80 ERGIPFVVHGRS-ESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNV-YLSEITRPALTTVDIQIY 299
Cdd:cd20010 159 REGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLTTTRSSLR 238
|
250 260 270
....*....|....*....|....*....|.
gi 1896925672 300 TLGAQSAKALIEKTLNKNEPAKRIIIPYEIV 330
Cdd:cd20010 239 DAGRRLAEMLLALIDGEPAAELQELWPPELI 269
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
1-336 |
5.41e-58 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 190.71 E-value: 5.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 1 MVTIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSSanvalQNPFFP 80
Cdd:PRK10703 1 MATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSS-----EAPYFA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 81 EILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLRE-QGFPFVMV--GKPQEHDT 157
Cdd:PRK10703 76 EIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEyRHIPMVVMdwGEAKADFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 158 EIthVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIHTEFLKSGGREAVEHL 237
Cdd:PRK10703 156 DA--IIDNAFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 238 MSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEKTLNKN 317
Cdd:PRK10703 234 LSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKR 313
|
330
....*....|....*....
gi 1896925672 318 EPAKRIIIPYEIVYRDSVS 336
Cdd:PRK10703 314 EEPQTIEVHPRLVERRSVA 332
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
62-335 |
2.54e-56 |
|
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: 184.02 E-value: 2.54e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPssanvALQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLRE 141
Cdd:cd06296 2 IDLVLP-----QLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 142 QGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKI 221
Cdd:cd06296 77 AGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 222 HTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTL 301
Cdd:cd06296 157 EGDFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREM 236
|
250 260 270
....*....|....*....|....*....|....
gi 1896925672 302 GAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDSV 335
Cdd:cd06296 237 GAVAVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-334 |
4.81e-56 |
|
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: 183.22 E-value: 4.81e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPssaNVAlqNPFFPEILRGIGSVIHEAEYSMYL-STG---ETEKEILSEVQRmvYGsyVDGVILLYSRINDK-VT 136
Cdd:cd19976 2 IGLIVP---DIS--NPFFSELVRGIEDTLNELGYNIILcNTYndfEREKKYIQELKE--RN--VDGIIIASSNISDEaII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 137 NFLREQGFPFVMVG-KPQEHDTEITHVDNdnVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQE 215
Cdd:cd19976 73 KLLKEEKIPVVVLDrYIEDNDSDSVGVDD--YRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 216 CEGYKIHTEFLKSGGREAVEHLMSlSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVD 295
Cdd:cd19976 151 DESWIYSGESSLEGGYKAAEELLK-SKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIA 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 1896925672 296 IQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd19976 230 QPIFEMGQEAAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
61-334 |
5.66e-55 |
|
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: 180.44 E-value: 5.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVImpssANVALQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVIL--LYSRIndkVTNF 138
Cdd:cd06288 1 TIGLI----TDDIATTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYasMHHRE---VTLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMV-GKPQEHDteITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECE 217
Cdd:cd06288 74 PELTDIPLVLLnCFDDDPS--LPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 218 GYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQ 297
Cdd:cd06288 152 SLVVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALP 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1896925672 298 IYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06288 232 YYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-333 |
2.14e-54 |
|
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: 178.91 E-value: 2.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEV-QRMV-YGsyVDGVILLYSRINDKVT-NF 138
Cdd:cd06289 2 VGLIVPD-----LSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFlRRMLeQG--VDGLILSPAAGTTAELlRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMVGKPQEhDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEG 218
Cdd:cd06289 75 LKAWGIPVVLALRDVP-GSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDES 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 219 YKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQI 298
Cdd:cd06289 154 LIVPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHP 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1896925672 299 YTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRD 333
Cdd:cd06289 234 REIGRRAARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
57-334 |
3.81e-54 |
|
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: 178.60 E-value: 3.81e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 57 KSTKAIGVIMPSSANV--ALQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEilsEVQRMVYGSYVDGVILLYSRINDK 134
Cdd:cd06295 1 QRSRTIAVVVPMDPHGdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDAN---QLARLLDSGRADGLIVLGQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 135 VTNFLREQGFPFVMVGkPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVtRDRESGYVAALEKAGIQ 214
Cdd:cd06295 78 ALRELAQQGLPMVVWG-APEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEV-ADRLQGYRDALAEAGLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 215 ECEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTV 294
Cdd:cd06295 156 ADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1896925672 295 DIQIytlgAQSAKALIEKTLN--KNEPAKRIIIPYEIVYRDS 334
Cdd:cd06295 236 RQDL----ALAGRLLVEKLLAliAGEPVTSSMLPVELVVRES 273
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
62-325 |
4.30e-52 |
|
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380632 [Multi-domain] Cd Length: 264 Bit Score: 173.10 E-value: 4.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYS-MYLSTGE---TEKEILsevqRMVYGSYVDGVILLYSRINDKVTN 137
Cdd:cd19977 2 IGLIVAD-----ILNPFFTSVVRGIEDEAYKNGYHvILCNTDEdpeKEKKYI----EMLRAKQVDGIIIAPTGGNEDLIE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 138 FLREQGFPFVMVGKPQEhDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECE 217
Cdd:cd19977 73 KLVKSGIPVVFVDRYIP-GLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 218 GYkIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQ 297
Cdd:cd19977 152 EL-IKHVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQP 230
|
250 260
....*....|....*....|....*...
gi 1896925672 298 IYTLGAQSAKALIEKTLNKNEPAKRIII 325
Cdd:cd19977 231 TYEIGRKAAELLLDRIENKPKGPPRQIV 258
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
62-334 |
6.86e-52 |
|
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: 172.32 E-value: 6.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYL--STGETEKEIlsEVQRMVYGSYVDGVILL-YSRINDKvtnf 138
Cdd:cd06291 2 IGLIVPD-----ISNPFFAELAKYIEKELFKKGYKMILcnSNEDEEKEK--EYLEMLKRNKVDGIILGsHSLDIEE---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMVGKpqEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEG 218
Cdd:cd06291 71 YKKLNIPIVSIDR--YLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 219 YKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQI 298
Cdd:cd06291 149 EIDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPI 228
|
250 260 270
....*....|....*....|....*....|....*.
gi 1896925672 299 YTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06291 229 EEMAKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
62-332 |
7.41e-51 |
|
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: 169.75 E-value: 7.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYL-STGET-EKEilSEVQRMVYGSYVDGVILLYSRINDKVTNFL 139
Cdd:cd06280 2 IGLIVPD-----ITNPFFTTIARGIEDAAEKHGYQVILaNTDEDpEKE--KRYLDSLLSKQVDGIILAPSAGPSRELKRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 140 REQGFPFVMVGKPQEhDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGY 219
Cdd:cd06280 75 LKHGIPIVLIDREVE-GLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 220 KIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIY 299
Cdd:cd06280 154 IFEGDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAY 233
|
250 260 270
....*....|....*....|....*....|...
gi 1896925672 300 TLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYR 332
Cdd:cd06280 234 EIGRIAAQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
62-334 |
8.36e-50 |
|
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: 167.29 E-value: 8.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTG----ETEKEILsevqRMVYGSYVDGVILLYSRINDKVTN 137
Cdd:cd01575 2 VAVVVPS-----LSNSVFAETLQGLSDVLEPAGYQLLLGNTgyspEREEELI----RALLSRRPAGLILTGTEHTPATRK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 138 FLREQGFPFVMVGkpqehDTEITHVDN----DNVRAGKEITQHLIDMGHEKIGFIGGSRDLLV-TRDRESGYVAALEKAG 212
Cdd:cd01575 73 LLRAAGIPVVETW-----DLPDDPIDMavgfSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 213 IQECEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALT 292
Cdd:cd01575 148 LPLPLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1896925672 293 TVDIQIYTLGAQSAKALIEKtLNKNEPAKRII-IPYEIVYRDS 334
Cdd:cd01575 228 TVRVPRYEIGRKAAELLLAR-LEGEEPEPRVVdLGFELVRRES 269
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
62-334 |
7.10e-49 |
|
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: 164.62 E-value: 7.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANVALQNPFFPEILRGIGSVIHEAEYSM--YLSTGETEKEILSEVqrmvygsyvDGVILLySRINDKVTNFL 139
Cdd:cd01544 2 IGIIQWYSEEEELEDPYYLSIRLGIEKEAKKLGYEIktIFRDDEDLESLLEKV---------DGIIAI-GKFSKEEIEKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 140 REQGFPFVMVGKPQEHDtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRD-----RESGYVAALEKAGIQ 214
Cdd:cd01544 72 KKLNPNIVFVDSNPDPD-GFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEeiedpRLRAFREYMKEKGLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 215 ECEgYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTV 294
Cdd:cd01544 151 NEE-YIYIGEFSVESGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1896925672 295 DIQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd01544 230 HIPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-334 |
1.20e-48 |
|
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: 164.22 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGE--TEKEiLSEVQRMVyGSYVDGVILLYSRINDKVTNFL 139
Cdd:cd06273 2 IGAIVPT-----LDNAIFARAIQALQQTLAEAGYTLLLATSEydPARE-LEQVRALI-ERGVDGLILVGSDHDPELFELL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 140 REQGFPFVMVGKPQEhDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGG---SRDLlvTRDRESGYVAALEKAGIQEC 216
Cdd:cd06273 75 EQRQVPYVLTWSYDE-DSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGptaGNDR--ARARLAGIRDALAERGLELP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 217 EGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDI 296
Cdd:cd06273 152 EERVVEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRV 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1896925672 297 QIYTLGAQSAKALIEKtLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06273 232 PAREIGELAARYLLAL-LEGGPPPKSVELETELIVRES 268
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
27-335 |
2.01e-48 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 164.79 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 27 RISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEK 106
Cdd:PRK11041 3 KVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPD-----ICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 107 EILSEVQRMVYGSYVDGVILLYSRINDKVTnfLREQGF--PFVMVGK--PqehDTEITHVDNDNVRAGKEITQHLIDMGH 182
Cdd:PRK11041 78 QQEKTFVNLIITKQIDGMLLLGSRLPFDAS--KEEQRNlpPMVMANEfaP---ELELPTVHIDNLTAAFEAVNYLHELGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 183 EKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSML 262
Cdd:PRK11041 153 KRIACIAGPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896925672 263 ESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDSV 335
Cdd:PRK11041 233 KRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
62-334 |
2.74e-48 |
|
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: 163.50 E-value: 2.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGET-EKEILSEVQRMVYGSYVDGVILLySRI--NDKVTNF 138
Cdd:cd01545 2 IGLLYDN-----PSASYVSALQVGALRACREAGYHLVVEPCDSdDEDLADRLRRFLSRSRPDGVILT-PPLsdDPALLDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMVGkPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEG 218
Cdd:cd01545 76 LDELGIPYVRIA-PGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 219 YKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQI 298
Cdd:cd01545 155 LVVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPI 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1896925672 299 YTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd01545 235 AEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
62-333 |
2.66e-47 |
|
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: 160.76 E-value: 2.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTG----ETEKE-ILSEVQRMVygsyvDGVILLYSRINDKVT 136
Cdd:cd06270 2 IGLVVPD-----LSGPFFGSLLKGAERVARAHGKQLLITSGhhdaEEEREaIEFLLDRRC-----DAIILHSRALSDEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 137 NFLREQGFPFVMVGKpqeHDTEITH--VDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQ 214
Cdd:cd06270 72 ILIAEKIPPLVVINR---YIPGLADrcVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 215 ECEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTV 294
Cdd:cd06270 149 LDPSLIIEGDFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTV 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 1896925672 295 DIQIYTLGAQSAKALIEKTLNKNEPAKRIIIPyEIVYRD 333
Cdd:cd06270 229 HYPIEEMAQAAAELALNLAYGEPLPISHEFTP-TLIERD 266
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
61-334 |
8.57e-47 |
|
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: 159.68 E-value: 8.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSSANVALQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRmvygSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd06279 1 AIGVLLPDDLSYAFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRN----AAVDGFIVYGLSDDDPAVAALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGkpQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDL-----------------LVTRDRESG 203
Cdd:cd06279 77 RRGLPLVVVD--GPAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRgrergpvsaerlaaatnSVARERLAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 204 YVAALEKAGIQECEGYKIH-TEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVY 282
Cdd:cd06279 155 YRDALEEAGLDLDDVPVVEaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDIP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1896925672 283 LSEITRPALTTVDIQIYTLGAQSAKALIEktLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06279 235 EAAAADPGLTTVRQPAVEKGRAAARLLLG--LLPGAPPRPVILPTELVVRAS 284
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-334 |
9.39e-47 |
|
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: 159.25 E-value: 9.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANValQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLySRINDKVTNFLRE 141
Cdd:cd19974 2 IAVLIPERFFG--DNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIIL-GEISKEYLEKLKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 142 QGFPFVMVGKPQEHDtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGgsrDLLVTR---DRESGYVAALEKAGIQECEG 218
Cdd:cd19974 79 LGIPVVLVDHYDEEL-NADSVLSDNYYGAYKLTSYLIEKGHKKIGFVG---DINYTSsfmDRYLGYRKALLEAGLPPEKE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 219 YKIhtefLKsgGREAVEHLM-SLSTP-----PSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALT 292
Cdd:cd19974 155 EWL----LE--DRDDGYGLTeEIELPlklmlPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1896925672 293 TVDIQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd19974 229 TVEVDKEAMGRRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-334 |
2.32e-46 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 158.08 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVygSY-VDGVILLYSRINDKVTNFLR 140
Cdd:cd06278 2 VGVVVGD-----LSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDDALRQLL--QYrVDGVIVTSATLSSELAEECA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGkPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEgyK 220
Cdd:cd06278 75 RRGIPVVLFN-RVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPPA--V 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSML-ESYGLRVPQDISLVSFNNVYLSEitRPA--LTTVdiq 297
Cdd:cd06278 152 EAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAA--WPSydLTTV--- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1896925672 298 iytlgAQSAKALIEKTL--------NKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06278 227 -----RQPIEEMAEAAVdlllerieNPETPPERRVLPGELVERGS 266
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
62-330 |
2.71e-46 |
|
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: 157.66 E-value: 2.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPssanvALQNPFFPEILRGIGSVIHEAEYSMYL--STGETEKEI--LSEVQRMvygsYVDGVILLYSRINDKVTN 137
Cdd:cd01542 2 IGVIVP-----RLDSYSTSRVLEGIDEVLKENGYQPLIanTNLDEEREIeyLETLARQ----KVDGIILFATEITDEHRK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 138 FLREQGFPFVMVGkpQEHDtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGS-RDLLVTRDRESGYVAALEKAGIQEc 216
Cdd:cd01542 73 ALKKLKIPVVVLG--QEHE-GFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDeEDIAVGVARKQGYLDALKEHGIDE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 217 eGYKIHTEFLKSGGREAVEHLMSlSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDI 296
Cdd:cd01542 149 -VEIVETDFSMESGYEAAKELLK-ENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKF 226
|
250 260 270
....*....|....*....|....*....|....
gi 1896925672 297 QIYTLGAQSAKALIEkTLNKNEPAKRIIIPYEIV 330
Cdd:cd01542 227 DYEEAGEKAAELLLD-MIEGEKVPKKQKLPYELI 259
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
62-334 |
1.84e-45 |
|
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: 156.18 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLS-TG---ETEKEILSEVqrmvYGSYVDGVILLYSR-----IN 132
Cdd:cd01541 2 IGVITTY-----IDDYIFPSIIQGIESVLSENGYSLLLAlTNndvEKEREILESL----LDQNVDGLIIEPTKsalpnPN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 133 DKVTNFLREQGFPFVMV-GKPQEHDteITHVDNDNVRAGKEITQHLIDMGHEKIGFIGgSRDLLVTRDRESGYVAALEKA 211
Cdd:cd01541 73 LDLYEELQKKGIPVVFInSYYPELD--APSVSLDDEKGGYLATKHLIDLGHRRIAGIF-KSDDLQGVERYQGFIKALREA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 212 GIQECEGY--KIHTE-FLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITR 288
Cdd:cd01541 150 GLPIDDDRilWYSTEdLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1896925672 289 PALTTVDIQIYTLGAQSAKALIEKtLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd01541 230 PPLTSVVHPKEELGRKAAELLLRM-IEEGRKPESVIFPPELIERES 274
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
62-334 |
2.07e-45 |
|
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: 155.90 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLRE 141
Cdd:cd06299 2 IGLLVPD-----IRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 142 QGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKI 221
Cdd:cd06299 77 QGLPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 222 HTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTL 301
Cdd:cd06299 157 FGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERI 236
|
250 260 270
....*....|....*....|....*....|...
gi 1896925672 302 GAQSAKALIEKtLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06299 237 GRRAVELLLAL-IENGGRATSIRVPTELIPRES 268
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
62-334 |
4.56e-45 |
|
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: 154.76 E-value: 4.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLRE 141
Cdd:cd06298 2 VGVIIPD-----ISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 142 QGFPFVMVGKpQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRD-RESGYVAALEKAGIQECEGYK 220
Cdd:cd06298 77 SPVPVVLAGT-VDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDkKLQGYKRALEEAGLEFNEPLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDlISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYT 300
Cdd:cd06298 156 FEGDYDYDSGYELYEELLESGEPDAAIVVRDE-IAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYD 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1896925672 301 LGAQSAKALIEktLNKNEP--AKRIIIPYEIVYRDS 334
Cdd:cd06298 235 IGAVAMRLLTK--LMNKEEveETIVKLPHSIIWRQS 268
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
2-335 |
3.33e-44 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 154.77 E-value: 3.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 2 VTIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVImpsSANVALQNPffPE 81
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLA---TTSLALHAP--SQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 82 ILRGIGSVIHEAEYSMYLStgetekeilsevqrMVYGSYVDGvillysrINDKVTNfLREQGFPFVMVGKPQEHDT-EIT 160
Cdd:PRK09526 81 IAAAIKSRADQLGYSVVIS--------------MVERSGVEA-------CQAAVNE-LLAQRVSGVIINVPLEDADaEKI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 161 HVDNDNV------------------------RAGKEitqHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQEC 216
Cdd:PRK09526 139 VADCADVpclfldvspqspvnsvsfdpedgtRLGVE---HLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQPI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 217 EgyKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDI 296
Cdd:PRK09526 216 A--VREGDWSAMSGYQQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQ 293
|
330 340 350
....*....|....*....|....*....|....*....
gi 1896925672 297 QIYTLGAQSAKALIEKTLNKNEPAkRIIIPYEIVYRDSV 335
Cdd:PRK09526 294 DFRLLGKEAVDRLLALSQGQAVKG-SQLLPTSLVVRKST 331
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
1-336 |
1.15e-43 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 153.37 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 1 MVTIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMpssANVAlqNPFFP 80
Cdd:PRK10727 1 MATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVV---GDVS--DPFFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 81 EILRGIGSVIHEAEYSMYLSTG----ETEKEILSEVQRmvygSYVDGVILLYSRINDKVTNFLREQGFPFVMVGK--Pqe 154
Cdd:PRK10727 76 AMVKAVEQVAYHTGNFLLIGNGyhneQKERQAIEQLIR----HRCAALVVHAKMIPDAELASLMKQIPGMVLINRilP-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 155 hDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIHTEFLKSGGREAV 234
Cdd:PRK10727 150 -GFENRCIALDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 235 EHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIekTL 314
Cdd:PRK10727 229 TELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELAL--AL 306
|
330 340
....*....|....*....|....
gi 1896925672 315 NKNEPAKRIIIPYE--IVYRDSVS 336
Cdd:PRK10727 307 ADNRPLPEITNVFSptLVRRHSVS 330
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-334 |
1.36e-43 |
|
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: 151.27 E-value: 1.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANvalqnPFFPEILRGIGSVIHEAEYSMYL-STGE-TEKEilSEVQRMVYGSYVDGVILLYSRINDKVTNFL 139
Cdd:cd06293 2 IGLVVPDVSN-----PFFAEVARGVEDAARERGYAVVLcNSGRdPERE--RRYLEMLESQRVRGLIVTPSDDDLSHLARL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 140 REQGFPFVMVGKPQEHDtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEgy 219
Cdd:cd06293 75 RARGTAVVLLDRPAPGP-AGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDE-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 220 KIHTEFLKSG----GREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVD 295
Cdd:cd06293 152 VVRELSAPDAnaelGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVR 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 1896925672 296 IQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06293 232 QPSYELGRAAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
76-335 |
2.52e-42 |
|
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: 147.77 E-value: 2.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 76 NPFFPEILRGIGSVIHEAEYSMYL-STG---ETEKEILSEVQRMVygsyVDGVILLYSRINDKVTN-FLREQGFPFVMVG 150
Cdd:cd06281 11 NPLYARIVKAAEARLRAAGYTLLLaSTGndeERELELLSLFQRRR----VDGLILTPGDEDDPELAaALARLDIPVVLID 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 151 KpqEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIHTEFLKSGG 230
Cdd:cd06281 87 R--DLPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGSFSADSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 231 REAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALI 310
Cdd:cd06281 165 FREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRAAAELLL 244
|
250 260
....*....|....*....|....*.
gi 1896925672 311 EKTLNKNE-PAKRIIIPYEIVYRDSV 335
Cdd:cd06281 245 DRIEGPPAgPPRRIVVPTELILRDSC 270
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
77-334 |
5.47e-42 |
|
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: 147.00 E-value: 5.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 77 PFFPEILRGIGSVIHEAEYSMYLSTGETEKEILsEVQRMVYGSYVDGVILLYSRINDKVTNFLREQGFPFVMVGKpQEHD 156
Cdd:cd06277 19 PFFSELIDGIEREARKYGYNLLISSVDIGDDFD-EILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDN-YFED 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 157 TEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIhteFLKSGGREAVEH 236
Cdd:cd06277 97 LNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEF---VVSVGPEGAYKD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 237 LMSL----STPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEK 312
Cdd:cd06277 174 MKALldtgPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEK 253
|
250 260
....*....|....*....|..
gi 1896925672 313 TLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06277 254 IKDPDGGTLKILVSTKLVERGS 275
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-333 |
7.17e-42 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 148.70 E-value: 7.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 2 VTIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSsanvaLQNPFFPE 81
Cdd:PRK10014 7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRD-----LSAPFYAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 82 ILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSR-INDKVTNFLREQGFPFVMVGKPQEHDtEIT 160
Cdd:PRK10014 82 LTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAgSSDDLREMAEEKGIPVVFASRASYLD-DVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 161 HVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAG-------IQECEGYKihteflKSGGrEA 233
Cdd:PRK10014 161 TVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGlpfhsewVLECTSSQ------KQAA-EA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 234 VEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRV---------PQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQ 304
Cdd:PRK10014 234 ITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQSgesgvdryfEQQVALAAFTDVPEAELDDPPLTWASTPAREIGRT 313
|
330 340
....*....|....*....|....*....
gi 1896925672 305 SAKALIEKTLNKNEPAKRIIIPYEIVYRD 333
Cdd:PRK10014 314 LADRMMQRITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
62-334 |
1.40e-40 |
|
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: 143.11 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANvalqnpFFP-EILRGIGSVIHEAEYSMYLST--GETEKEILSEVQRMVyGSYVDGVILLYSRINDKVTNF 138
Cdd:cd01574 2 IGVIATGLSL------YGPaSTLAGIERAARERGYSVSIATvdEDDPASVREALDRLL-SQRVDGIIVIAPDEAVLEALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMVGKPQEHDteITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQecEG 218
Cdd:cd01574 75 RLPPGLPVVIVGSGPSPG--VPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLP--PP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 219 YKIHTEFLKSGGREAVEHLmSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQI 298
Cdd:cd01574 151 PVVEGDWSAASGYRAGRRL-LDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDF 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 1896925672 299 YTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd01574 230 AELGRRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
61-320 |
1.66e-40 |
|
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: 142.95 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSSANvaLQNPFFPEILRGIGSVIHEAEYSMYLsTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLR 140
Cdd:cd06271 1 VIALVFPVTET--ELNGTVSE*VSGITEEAGTTGYHLLV-WPFEEAES*VPIRDLVETGSADGVILSEIEPNDPRVQFLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKpQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIqecEGYK 220
Cdd:cd06271 78 KQNFPFVAHGR-SD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGL---TGYP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNV-YLSEITRPALTTVDIQIY 299
Cdd:cd06271 154 LDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSApFLGAMITPPLTTVHAPIA 233
|
250 260
....*....|....*....|.
gi 1896925672 300 TLGAQSAKALIEKtLNKNEPA 320
Cdd:cd06271 234 EAGRELAKALLAR-IDGEDPE 253
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
61-329 |
2.44e-40 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380505 [Multi-domain] Cd Length: 267 Bit Score: 142.42 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRI-NDKVTNFL 139
Cdd:cd06282 1 TIGVLIPS-----LNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAqGSEALELL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 140 REQGFPFVMVGKPQEHDTEIThVDNDNVRAGKEITQHLIDMGHEKIGFIGGS-----RdllvTRDRESGYVAALEKAGIQ 214
Cdd:cd06282 76 EEEGVPYVLLFNQTENSSHPF-VSVDNRLASYDVAEYLIALGHRRIAMVAGDfsasdR----ARLRYQGYRDALKEAGLK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 215 ECEgyKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTV 294
Cdd:cd06282 151 PIP--IVEVDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATV 228
|
250 260 270
....*....|....*....|....*....|....*
gi 1896925672 295 DIQIYTLGAQSAKALIEKtLNKNEPAKRIIIPYEI 329
Cdd:cd06282 229 VQPSRDMGRAAADLLLAE-IEGESPPTSIRLPHHL 262
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
1-337 |
1.92e-33 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 126.43 E-value: 1.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 1 MVTIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMpssanVALQNPFFP 80
Cdd:PRK10401 1 MITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVV-----MDVSDAFFG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 81 EILRGIGSVIHeaEYSMYLSTG----ETEKE--------------------ILSEVQRMVYGSYVDGVILlysrINDKVT 136
Cdd:PRK10401 76 ALVKAVDLVAQ--QHQKYVLIGnsyhEAEKErhaievlirqrcnalivhskALSDDELAQFMDQIPGMVL----INRVVP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 137 NFlreqgfpfvmvgkpqEHDTeithVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQEC 216
Cdd:PRK10401 150 GY---------------AHRC----VCLDNVSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 217 EGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDI 296
Cdd:PRK10401 211 ESWIGTGTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRY 290
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1896925672 297 QIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDSVSQ 337
Cdd:PRK10401 291 PIASMAKLATELALQGAAGNLDPRASHCFMPTLVRRHSVAT 331
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
62-332 |
2.89e-33 |
|
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: 123.81 E-value: 2.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEY--SMYLSTGETEKEIlsEVQRMVYGSYVDGVILLySRIND--KVTN 137
Cdd:cd06286 2 IGVVVPY-----IDHPYFSQLINGIAEAAFKKGYqvLLLQTNYDKEKEL--RALELLKTKQIDGLIIT-SRENDweVIEP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 138 FLREqgFPFVMVGKPQehDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDL--LVTRDRESGYVAALEKAGIQe 215
Cdd:cd06286 74 YAKY--GPIVLCEETD--SPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESssASTQARLKAYQDVLGEHGLS- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 216 cegykIHTEFLKSG------GREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEItrP 289
Cdd:cd06286 149 -----LREEWIFTNchtiedGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--L 221
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1896925672 290 ALTTVDIQIYTLGAQSAKALIEKtLNKNEPaKRIIIPYEIVYR 332
Cdd:cd06286 222 NLTTIDQPLEEMGKEAFELLLSQ-LESKEP-TKKELPSKLIER 262
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
176-335 |
9.85e-33 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 119.37 E-value: 9.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 176 HLIDMGHEKIGFIG--GSRDLLVTRDRESGYVAALEKAGIQECEGYKIHTEFlkSGGREAVEHLMSLSTPPSGLVVSDDL 253
Cdd:pfam13377 1 HLAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDE--AEAAAARERLRWLGALPTAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 254 ISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRD 333
Cdd:pfam13377 79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158
|
..
gi 1896925672 334 SV 335
Cdd:pfam13377 159 ST 160
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
62-332 |
4.32e-31 |
|
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: 118.04 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMpssANVAlqNPFFPEILRGIGSVIHEAEYSMYL--STGETEKEiLSEVQRMVygSY-VDGVILLYSRINDKVTNF 138
Cdd:cd06283 2 IGVIV---ADIT--NPFSSLLLKGIEDVCREAGYQLLIcnSNNDPEKE-RDYIESLL--SQrVDGLILQPTGNNNDAYLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMVGKPQEhDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTR-DRESGYVAALEKAGIqECE 217
Cdd:cd06283 74 LAQKGLPVVLVDRQIE-PLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRrERLQGFLDALARYNI-EGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 218 GYKIHTEfLKSGGREAVEHLMSLST-PPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDI 296
Cdd:cd06283 152 VYVIEIE-DTEDLQQALAAFLSQHDgGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQ 230
|
250 260 270
....*....|....*....|....*....|....*.
gi 1896925672 297 QIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYR 332
Cdd:cd06283 231 PTYEIGKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
2-71 |
1.73e-30 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 110.37 E-value: 1.73e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 2 VTIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSSAN 71
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
62-310 |
2.20e-30 |
|
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: 116.10 E-value: 2.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANValqNPFFPEILRGIGSVIHEAEYSMYL---STGETEkeiLSEVQRMVYGSYVDGVILLYSRINDKVTNF 138
Cdd:cd20009 2 IALVLPTEDEI---DGFTSQLISGISEALRGTPYHLVVtpeFPGDDP---LEPVRYIVENRLADGIIISHTEPQDPRVRY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMVGKpQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEG 218
Cdd:cd20009 76 LLERGFPFVTHGR-TELSTPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 219 YKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQI 298
Cdd:cd20009 155 LIVTLDSSAEAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDI 234
|
250
....*....|..
gi 1896925672 299 YTLGAQSAKALI 310
Cdd:cd20009 235 EEAGRFLAEALL 246
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
1-334 |
7.54e-30 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 116.40 E-value: 7.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 1 MVTIKDVAKVSGVSPSTVSRVIANNPRIS--EDTKKKVRKAMKELGYHPNVNARNLV-AKSTKAIGVIMPSSANVALQNP 77
Cdd:PRK10339 1 MATLKDIAIEAGVSLATVSRVLNDDPTLNvkEETKHRILEIAEKLEYKTSSARKLQTgAVNQHHILAIYSYQQELEINDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 78 FFPEILRGIGSVIHEAEYSMylsTGETEKEILSEVQRmvygsyVDGvILLYSRINDKVTNFLREQGFPFVMVgKPQEHDT 157
Cdd:PRK10339 81 YYLAIRHGIETQCEKLGIEL---TNCYEHSGLPDIKN------VTG-ILIVGKPTPALRAAASALTDNICFI-DFHEPGS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 158 EITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGI-QECEGYKihTEFLKSGGREAVEH 236
Cdd:PRK10339 150 GYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQVvREEDIWR--GGFSSSSGYELAKQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 237 LMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEKTLNK 316
Cdd:PRK10339 228 MLAREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKARDG 307
|
330
....*....|....*...
gi 1896925672 317 NEPAKRIIIPYEIVYRDS 334
Cdd:PRK10339 308 RALPLLVFVPSKLKLRGT 325
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
62-334 |
1.56e-27 |
|
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: 108.71 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANvalqnPFFPEILRGIGSVIHEA--EYSMYLSTGETEKEILSEVQRMVYgsYVDGVILLYSRINDKVTNFL 139
Cdd:cd06297 2 ISLLVPEVMT-----PFYMRLLTGVERALDENryDLAIFPLLSEYRLEKYLRNSTLAY--QCDGLVMASLDLTELFEEVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 140 REQGFPFVMVGKPQEHdteITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRD----RESGYVAALEKAGIQE 215
Cdd:cd06297 75 VPTEKPVVLIDANSMG---YDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTETvfreREQGFLEALNKAGRPI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 216 CEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEitRPALTTVD 295
Cdd:cd06297 152 SSSRMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVR 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 1896925672 296 IQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06297 230 QPVEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
4-312 |
2.82e-26 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 106.65 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 4 IKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSsanvaLQNPFFPEIL 83
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPS-----LTNQVFAEVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 84 RGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRINDKVTNFLREQGFPFVMVGKPQEHDTEIThVD 163
Cdd:PRK14987 83 RGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIA-VG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 164 NDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLvTRDRESGYVAALEKAG-------IQECEGYKIHTEFLKSGGREAVEH 236
Cdd:PRK14987 162 FDNFEAARQMTTAIIARGHRHIAYLGARLDER-TIIKQKGYEQAMLDAGlvpysvmVEQSSSYSSGIELIRQARREYPQL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896925672 237 lmslstppSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIEK 312
Cdd:PRK14987 241 --------DGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLAR 308
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
61-333 |
1.35e-23 |
|
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: 97.83 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 61 AIGVIMPSSAN-VALQNpffpeILRGIGSVIHEAEYSMYLSTGE-------TEKEILSEVQrmvygsyVDGVILLYSRIN 132
Cdd:cd06272 1 TIGLYWPSVGErVALTR-----LLSGINEAISKQGYNINLSICPykvghlcTAKGLFSENR-------FDGVIVFGISDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 133 DKVTNFLREQGFPFVMVGKPQEhdtEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAG 212
Cdd:cd06272 69 DIEYLNKNKPKIPIVLYNRESP---KYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 213 IQECEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALT 292
Cdd:cd06272 146 IHLSDSIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLT 225
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1896925672 293 TVDIQIYTLGAQSAKaLIEKTLNK--NEPAKRIIIPyEIVYRD 333
Cdd:cd06272 226 VVGVPIEKIAEESLR-LILKLIEGreNEIQQLILYP-ELIFRE 266
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
122-334 |
5.96e-22 |
|
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: 93.42 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 122 DGVIllySRINDKVTN-FLREQGFPFVMVGkPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIgGSRDLLVTRDR 200
Cdd:cd01543 52 DGII---ARLDDPELAeALRRLGIPVVNVS-GSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFC-GFRNAAWSRER 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 201 ESGYVAALEKAGIqECEGYKIHTEFLKSGGREAVEHLMS-LST--PPSGLVVSDDLISLGILSMLESYGLRVPQDISLVS 277
Cdd:cd01543 127 GEGFREALREAGY-ECHVYESPPSGSSRSWEEEREELADwLKSlpKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLG 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 278 FNN-VYLSEITRPALTTVDIQIYTLGAQSAKALiEKTLNKNEPAKRIII--PYEIVYRDS 334
Cdd:cd01543 206 VDNdELICELSSPPLSSIALDAEQIGYEAAELL-DRLMRGERVPPEPILipPLGVVTRQS 264
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
5-56 |
1.28e-21 |
|
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.
Pssm-ID: 143331 [Multi-domain] Cd Length: 52 Bit Score: 86.31 E-value: 1.28e-21
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1896925672 5 KDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPNVNARNLVA 56
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
3-48 |
2.50e-19 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 79.99 E-value: 2.50e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1896925672 3 TIKDVAKVSGVSPSTVSRVIANNPRISEDTKKKVRKAMKELGYHPN 48
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
62-327 |
6.50e-19 |
|
Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.
Pssm-ID: 380479 [Multi-domain] Cd Length: 265 Bit Score: 84.99 E-value: 6.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANvalqnPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLYSRIN-DKVTNFLR 140
Cdd:cd01537 2 IGVTIYSYDD-----NFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAaAGVAEKAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYK 220
Cdd:cd01537 77 GQNVPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 221 IHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVDIQIYT 300
Cdd:cd01537 157 DTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANN 236
|
250 260
....*....|....*....|....*..
gi 1896925672 301 LGAQSAKALIEKTLNKNEPAKRIIIPY 327
Cdd:cd01537 237 LGKTTFDLLLNLADNWKIDNKVVRVPY 263
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
62-330 |
9.67e-19 |
|
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: 84.18 E-value: 9.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYS-MYLSTG---ETEKEIlseVQRMVYGSyVDGVILLYSRINDKVTN 137
Cdd:cd06274 2 IGLIVPD-----LANRFFARLAEALERLARERGLQlLIACSDddpEQERRL---VENLIARQ-VDGLIVAPSTPPDDIYY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 138 FLREQGFPFVMVGKPQeHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECE 217
Cdd:cd06274 73 LCQAAGLPVVFLDRPF-SGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 218 GYKIHTEFLKSGGREAVEHLM-SLSTPPSGLVVSdDLISL-GILSMLESYGLRVPQDISLVSFNNVYLSEITRPALTTVD 295
Cdd:cd06274 152 DWILAEGYDRESGYQLMAELLaRLGGLPQALFTS-SLTLLeGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVR 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1896925672 296 iQIYTLGAQSAKALIEKTLNKNEPAKRIIIPYEIV 330
Cdd:cd06274 231 -QDHDEIAEHAFELLDALIEGQPEPGVIIIPPELI 264
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
3-332 |
4.07e-18 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 83.77 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 3 TIKDVAKVSGVSPSTVSRVI---ANNPRISEDTKKKVRKAMKELGYHPNVNARNLVAKSTKAIGVIMPSsanvaLQNPFF 79
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVIngkAKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPD-----LENTSY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 80 PEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVIL---------LYSRINDKvtnflreqGFPFVMVG 150
Cdd:PRK11303 77 ARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVstslppehpFYQRLQND--------GLPIIALD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 151 KP--QEHdteITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYKIHteFLKS 228
Cdd:PRK11303 149 RAldREH---FTSVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREVHYLYANS--FERE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 229 GGREAVEHLMSLSTPPSGLVVSDDLISLGIL-SMLESYGlRVPQDISLVSFNNVYLSEITR-PALTTVdiQIYTLGAQSA 306
Cdd:PRK11303 224 AGAQLFEKWLETHPMPDALFTTSYTLLQGVLdVLLERPG-ELPSDLAIATFGDNELLDFLPcPVNAVA--QQHRLIAERA 300
|
330 340 350
....*....|....*....|....*....|.
gi 1896925672 307 KALiekTLNKNEPAKR-----IIIPYEIVYR 332
Cdd:PRK11303 301 LEL---ALAALDEPRKpkpglTRIRRNLKRR 328
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
115-334 |
1.39e-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: 81.31 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 115 MVYGSYVDGVILLYSRINDKVTNFLREQGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEKIGFIGGSRDL 194
Cdd:cd06287 51 MLDALDVDGAIVVEPTVEDPILARLRQRGVPVVSIGRAPGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 195 LVTRDRESGYVAALEKAGiQECEGYKIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRVPQDIS 274
Cdd:cd06287 131 NSSLESEAAYLRFAQEYG-TTPVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLM 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 275 LVSFNNVYLSEITRPALTTVDIQIYTLGAQSAKALIeKTLNKNEPAKRIIIPYEIVYRDS 334
Cdd:cd06287 210 VVTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLF-ASLSGEERSVEVGPAPELVVRAS 268
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
59-326 |
1.51e-17 |
|
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: 81.40 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 59 TKAIGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEILSEVQRMVYGSYVDGVILLySRIN--DKVT 136
Cdd:pfam00532 1 TLKLGALVPQ-----LDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIIT-TPAPsgDDIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 137 NFLREQGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDMGHEK-IGFIGGSRDLLVTRDRESGYVAALEKAGIQe 215
Cdd:pfam00532 75 AKAEGYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGRE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 216 cegYKIHTEFLKS----GGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYG-LRVPQDI-----SLVSFNNVYLSE 285
Cdd:pfam00532 154 ---VKIYHVATGDndipDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVgiginSVVGFDGLSKAQ 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1896925672 286 IT---RPALTTVDIQIYTLGAQSAKALIEKTLNKNEPAKRIIIP 326
Cdd:pfam00532 231 DTglyLSPLTVIQLPRQLLGIKASDMVYQWIPKFREHPRVLLIP 274
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
56-335 |
8.47e-14 |
|
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: 70.72 E-value: 8.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 56 AKSTKAIGVIMPSsanvaLQNPFFPEILRGIGSVIHE--AEYSMYLSTGETEKEIlSEVQRMVyGSYVDGVILLysrIND 133
Cdd:COG1879 30 AAKGKTIGFVVKT-----LGNPFFVAVRKGAEAAAKElgVELIVVDAEGDAAKQI-SQIEDLI-AQGVDAIIVS---PVD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 134 -----KVTNFLREQGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDM--GHEKIGFIGGSRDLLVTRDRESGYVA 206
Cdd:COG1879 100 pdalaPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 207 ALEKAGiqeceGYKI----HTEFLKSGGREAVEHLmsLSTPPS--GLVVSDDLISLGILSMLESYGLrvPQDISLVSFNn 280
Cdd:COG1879 180 ALKEYP-----GIKVvaeqYADWDREKALEVMEDL--LQAHPDidGIFAANDGMALGAAQALKAAGR--KGDVKVVGFD- 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896925672 281 vyLSEITRPAL------TTVDIQIYTLGAQSAKALIeKTLNKNEPAKRIIIPYEIVYRDSV 335
Cdd:COG1879 250 --GSPEALQAIkdgtidATVAQDPYLQGYLAVDAAL-KLLKGKEVPKEILTPPVLVTKENV 307
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
74-335 |
3.87e-10 |
|
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: 59.68 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 74 LQNPFFPEILRGIGSVIHEAEYSMY-LSTGETEKEILSEVQRmVYGSYVDGVIL--LYSRINDKVTNFLREQGFPFVMVG 150
Cdd:cd06319 9 LDNPFWQIMERGVQAAAEELGYEFVtYDQKNSANEQVTNAND-LIAQGVDGIIIspTNSSAAPTVLDLANEAKIPVVIAD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 151 KPQEHDTEITHVDNDN----VRAGKEITQHLIDMGHE--KIGFIGGSRDLLVTRDRESGYVAALEKAGIQECeGYKIHTE 224
Cdd:cd06319 88 IGTGGGDYVSYIISDNydggYQAGEYLAEALKENGWGggSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEV-ALRQTPN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 225 FLKSGGREAVEHLmsLSTPPS--GLVVSDDLISLGILSMLESYGLRvpQDISLVSFN--NVYLSEITRPALT-TVDIQIY 299
Cdd:cd06319 167 STVEETYSAAQDL--LAANPDikGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDgdPEALDLIKDGKLDgTVAQQPF 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 1896925672 300 TLGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDSV 335
Cdd:cd06319 243 GMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV 278
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
159-335 |
3.71e-09 |
|
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: 56.84 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 159 ITHVDNDNVRAGKEITQHLID---MGHEKIGFIGGSRDLLVTRDRESGYVAALEKAGiqeceGYKIHT----EFLKSGGR 231
Cdd:cd06309 99 VTFIGSDFVEEGRRAAEWLVKnykGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHP-----NIKIVAsqsgNFTREKGQ 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 232 EAVEHLmsLSTPPSGLVV----SDDLIsLGILSMLESYGLRVPQDISLVSFNNvylseiTRPALTTV-------DIQIYT 300
Cdd:cd06309 174 KVMENL--LQAGPGDIDViyahNDDMA-LGAIQALKEAGLKPGKDVLVVGIDG------QKDALEAIkagelnaTVECNP 244
|
170 180 190
....*....|....*....|....*....|....*
gi 1896925672 301 LGAQSAKALIEKTLNKNEPAKRIIIPYEIVYRDSV 335
Cdd:cd06309 245 LFGPTAFDTIAKLLAGEKVPKLIIVEERLFDKDNA 279
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
121-279 |
2.87e-07 |
|
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: 51.45 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 121 VDGVILL-YSRINDKVTNFLREQGFPFVMV------------GKPQEHDT----EITHvdnDNVRAGKEITQHLIDMGHE 183
Cdd:cd06324 59 PDYLILVnEKGVAPELLELAEQAKIPVFLInndltdeerallGKPREKFKywlgSIVP---DNEQAGYLLAKALIKAARK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 184 -------KIGFIGGSRDLLVTRDRESGYVAALEKAGIQECEGYkIHTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISL 256
Cdd:cd06324 136 ksddgkiRVLAISGDKSTPASILREQGLRDALAEHPDVTLLQI-VYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMAL 214
|
170 180
....*....|....*....|...
gi 1896925672 257 GILSMLESYGLRVPQDISLVSFN 279
Cdd:cd06324 215 GAIDALEEAGLKPGKDVLVGGID 237
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
62-329 |
5.79e-07 |
|
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: 50.26 E-value: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEA--EYSMYLSTGETEKEIlSEVQRMVyGSYVDGVIL------LYSRIND 133
Cdd:cd01536 2 IGVVVKD-----LTNPFWVAVKKGAEAAAKELgvELVVLDAQGDVAKQI-SQIEDLI-AQGVDAIIIapvdseALVPAVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 134 KVtnflREQGFPFVMVG-KPQEHDTEITHVDNDNVRAGKEITQHLID-MGHE-KIGFIGGSRDLLVTRDRESGYVAALEK 210
Cdd:cd01536 75 KA----NAAGIPVVAVDtDIDGGGDVVAFVGTDNYEAGKLAGEYLAEaLGGKgKVAILEGPPGSSTAIDRTKGFKEALKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 211 AGiqeceGYKI----HTEFLKSGGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLrvPQDISLVSFNNV--YLS 284
Cdd:cd01536 151 YP-----DIEIvaeqPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTpeALK 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1896925672 285 EITRPALT-TVDIQIYTLGAQSAKALIeKTLNKNEPAKRIIIPYEI 329
Cdd:cd01536 224 AIKDGELDaTVAQDPYLQGYLAVEAAV-KLLNGEKVPKEILTPVTL 268
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
62-318 |
1.08e-06 |
|
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: 49.57 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANVAlqNPFFPEILRGIGSVIHE----AEYSMYLSTGETEKEILSEVQRMVYGsyvdGVILLYS-RINDKVT 136
Cdd:cd01391 2 IGVVTSSLHQIR--EQFGIQRVEAIFHTADKlgasVEIRDSCWHGSVALEQSIEFIRDNIA----GVIGPGSsSVAIVIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 137 NFLREQGFPFVMVGKPQEHDTEITHVDN------DNVRAGKEITQHLIDMGHEKIGFIGGsRDLLVTRDRESGYVAALEK 210
Cdd:cd01391 76 NLAQLFDIPQLALDATSQDLSDKTLYKYflsvvfSDTLGARLGLDIVKRKNWTYVAAIHG-EGLNSGELRMAGFKELAKQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 211 AGIQECEGYKIHTEFLKSGGREAVEHLMSlSTPPSGLVVSDDLISLGILSMLESYGLRvpQDISLVSFNN------VYLS 284
Cdd:cd01391 155 EGICIVASDKADWNAGEKGFDRALRKLRE-GLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGwadrdeVGYE 231
|
250 260 270
....*....|....*....|....*....|....
gi 1896925672 285 EITrPALTTVDIQIYTLGAQSAKALIEKTLNKNE 318
Cdd:cd01391 232 VEA-NGLTTIKQQKMGFGITAIKAMADGSQNMHE 264
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
141-281 |
1.82e-05 |
|
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: 45.46 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 141 EQGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDM--GHEKIGFIGGSRDLLVTRDRESGYVAALEKAGiqeceG 218
Cdd:cd19968 78 KAGIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGFHEELAAGP-----K 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1896925672 219 YKIHTE----FLKSGGREAVEH-LMSLSTPPSGLVVSDDLISLGILSMLESYGLRVpQDISLVSFNNV 281
Cdd:cd19968 153 IKVVFEqtgnFERDEGLTVMENiLTSLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFDAV 219
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
124-332 |
7.13e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 43.74 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 124 VILL----YSRINDKVTNfLREQGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDMGHE--KIGFIGGSRDLLVT 197
Cdd:cd20006 62 AIVLaasdYDRLVEAVER-AKKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEkgKVAIVSFVKGSSTA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 198 RDRESGYVAALEKAGIqecegYKIH-TEFLKS---GGREAVEHLMSLSTPPSGLVVSDDLISLGILSMLESYGLRvpQDI 273
Cdd:cd20006 141 IEREEGFKQALAEYPN-----IKIVeTEYCDSdeeKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLG--GKV 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896925672 274 SLVSF-NNVYlsEITrpALTTVDIQI------YTLGAQSAKALIEKtLNKNEPAKRIIIPYEIVYR 332
Cdd:cd20006 214 KVVGFdSSVE--EIQ--LLEEGIIDAlvvqnpFNMGYLSVQAAVDL-LNGKKIPKRIDTGSVVITK 274
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
62-330 |
5.60e-04 |
|
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: 41.01 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSSANvalqnPFFPEILRGIGSVIHEAEY-----SMYLSTGETEKEILSEVQRMVYGsyVDGVILL---YSRIND 133
Cdd:cd06307 2 FGFLLPSPEN-----PFYELLRRAIEAAAAALRDrrvrlRIHFVDSLDPEALAAALRRLAAG--CDGVALVapdHPLVRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 134 KVtNFLREQGFPFVMVGKPQEHDTEITHVDNDNVRAGK---EITQHLIDMGHEKIGFIGGSRDLLVTRDRESGYVAALEK 210
Cdd:cd06307 75 AI-DELAARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRtaaWLMGRFLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 211 -------AGIQECEGykihtefLKSGGREAVEHLMSLSTPPSGLVVsddlI---SLGILSMLESYGLrvPQDISLVSFNn 280
Cdd:cd06307 154 rfpdltvLEVLEGLD-------DDELAYELLRELLARHPDLVGIYN----AgggNEGIARALREAGR--ARRVVFIGHE- 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1896925672 281 vyLSEITRPALT--TVDIQI----YTLGAQSAKALIEKTLNKNEPAKRIIIPYEIV 330
Cdd:cd06307 220 --LTPETRRLLRdgTIDAVIdqdpELQARRAIEVLLAHLGGKGPAPPQPPIPIEII 273
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
139-311 |
1.23e-03 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 39.99 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 139 LREQGFPFVMVGKPQEHDTEITHVDNDNVRAGKEITQHLIDM--GHEKIGFIGGSRDLLVTRDRESGYVAALEKagiqEC 216
Cdd:pfam13407 76 AKDAGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKE----KY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 217 EGYKIHTEFLKSG-----GREAVEHLMS-LSTPPSGLVVSDDLISLGILSMLESYGLRvpQDISLVSFNnvyLSEITRPA 290
Cdd:pfam13407 152 PGIKVVAEVEGTNwdpekAQQQMEALLTaYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFD---ATPEALEA 226
|
170 180
....*....|....*....|....*..
gi 1896925672 291 L------TTVDIQIYTLGAQSAKALIE 311
Cdd:pfam13407 227 IkdgtidATVLQDPYGQGYAAVELAAA 253
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-210 |
1.94e-03 |
|
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: 39.18 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896925672 62 IGVIMPSsanvaLQNPFFPEILRGIGSVIHEAEYSMYLSTGETEKEI-LSEVQRMVyGSYVDGVILLYSRINDKVT--NF 138
Cdd:cd06322 2 IGVSLLT-----LQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKqLSQIEDFI-QQGVDAIILAPVDSGGIVPaiEA 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896925672 139 LREQGFPFVMVGKPQEHDTEITHVDNDNV----RAGKEITQHLIDmGHEKIGFIgGSRDLLVTRDRESGYVAALEK 210
Cdd:cd06322 76 ANEAGIPVFTVDVKADGAKVVTHVGTDNYaggkLAGEYALKALLG-GGGKIAII-DYPEVESVVLRVNGFKEAIKK 149
|
|
| |
