|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
14-608 |
8.97e-135 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 408.09 E-value: 8.97e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 14 LLRNETLPQDELAQRLSVSTRTVRADITALNALLAQYGAQFTLNRGSGYQLKIDDrSRFQALEETAPKTQHvPRTAQERI 93
Cdd:COG3711 6 LKNNNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDD-EQKEKLLQLLEKSED-PLSPKERV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 94 HFLLVRFLTSAFSIKLENLADEWFVSRATLQNDMVEVRERFQRYQLTLETRPRHGMKLFGSEVSIRACLTDLLWELTLQG 173
Cdd:COG3711 84 AYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLSEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 174 GINPLISAEALEADVPAQLEPVLQETLTRHHIRLTDVGERFICLYGAVVVRRVSEGYPLADFSAEDV---AQNVRDAARD 250
Cdd:COG3711 164 DLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWeikKPKEYEIAKE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 251 LAGELQRLAGKPFSPAEEEWLCVHIA-ARQVQDVDPETISADDDEALVNYILRYINSQYNYNLLDDAQLHADLLTHIKTM 329
Cdd:COG3711 244 ILKLIEERLGISLPEDEIGYIALHLLgARLNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 330 ITRVRYQIMIPNPLLDNIKQHYPMAWDMTLAAVSSWGKYTPYTISENEIGFLVLHIGVGLERHYNIgyqRQPHVLLVCDT 409
Cdd:COG3711 324 INRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES---KKKRVLVVCSS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 410 SNAMVRMIEAILQRKYPQLAIAATISQREYEQREAIDEDFVISTVRIgeKDKPVVTIAPFPTDYQLDQIGKLVLvdrtrp 489
Cdd:COG3711 401 GIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPL--EDKPVIVVSPLLTEEDIEKIRKFLK------ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 490 wMLNKYFDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVI 569
Cdd:COG3711 473 -QIKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIVL 551
|
570 580 590
....*....|....*....|....*....|....*....
gi 1709388247 570 APQGIAWGDETAHIIFLLAISKSEYEEAMAIYDIFVTFL 608
Cdd:COG3711 552 AAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLL 590
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
496-628 |
8.19e-27 |
|
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation.
Pssm-ID: 238129 [Multi-domain] Cd Length: 136 Bit Score: 105.72 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 496 FDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVIAPQGIA 575
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709388247 576 WGDE---TAHIIFLLAISKSEyEEAMAIYDIFVTFLRERAMSRLAATRSFDEFKTV 628
Cdd:cd00211 81 FGSLdgqPVHLIFLLAAPDSN-EHLKALSQLARLLSDEEFVEQLLNAQSKEEILAL 135
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
495-625 |
9.49e-19 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 83.02 E-value: 9.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 495 YFDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVIAPQGI 574
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKEPV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1709388247 575 AWGDET---AHIIFLLAISKSEYEEAMAIYDIFVTFLRERAMSRLAATRSFDEF 625
Cdd:pfam00359 81 DFGSEDgkpVKLIFLLAAPDNEASHLKILSQLARLLQDEEFVEKLLKAKDPEEI 134
|
|
| PRK09863 |
PRK09863 |
putative frv operon regulatory protein; Provisional |
5-625 |
1.61e-13 |
|
putative frv operon regulatory protein; Provisional
Pssm-ID: 182121 [Multi-domain] Cd Length: 584 Bit Score: 73.73 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 5 NQRLAQLFTLLRNETLPQDELAQRLSVSTRTVRADITALNALLaQYGAQFTLNRGSGYQLKIDDRSRFQALEEtapktqh 84
Cdd:PRK09863 3 NERELKIVDLLEQQDRSGGELAQQLGVSRRTIVRDIAYINFTL-NGKAIGSISGSAKYHLEILNRRSLFQLLQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 85 vprTAQERIHFLLVRFLTSAFsIKLENLADEWFVSRATLQNDMVEVRERFQRYqLTLETRPRHGMKLFGSEVSIRACLTD 164
Cdd:PRK09863 75 ---KSDNEDRLLLLRLLLNTF-TPMAQLASALNLSRTWVAERLPRLNQRYERI-CCIASRPGLGHFIDETEEKRIDILAN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 165 LLWELTLqgginpLISAEALEADVPAQLEPVLQETLTRHHIR----LTDVGERFICLygAVVVRRVSEGYPladfsAEDV 240
Cdd:PRK09863 150 LIRKDPQ------LIPKAGPTRDNLQHLSRTACDNQHRWPLMqgdyLSSLILAIYAL--RNQLTDEWPQYP-----GDEI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 241 AQNVRDAArDLAGELQRLAGKPFSPAEEEwLCVHIAARQVQDvdpetisadddealvnyILRYINSQYNYNLLdDAQLHA 320
Cdd:PRK09863 217 KQIVEHSG-LFLGDNAVRTLTGLIEKQHQ-QAQVISADNVQQ-----------------LLQRVPGIASLNAI-DTQLVE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 321 DLLTHIktmitrVRyQIMIPNPL-------LDNIKQHYPMAWDMTLAAVSSWGKYTPYTISENEigFLVLHIGVGLERHY 393
Cdd:PRK09863 277 NIFGHL------LR-CLAFPVWIaehrqssINNLKAQNPAAFDMALHFITLLREQLDIPLFDSD--LIALYFACALERHQ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 394 NigyQRQPHVLLVcdTSNAMVRMIEAILQRKYPQLAIAATISQREYEQ-REAIDEDFVISTVR--IGEKD--KPVVTIAP 468
Cdd:PRK09863 348 N---ERVPILLLA--DQNSIATINQLIIEQKVLNIRVIIVRSLSELEAiREEIEPLLIINNSHylVDLQDaiNFYITFKN 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 469 FPTDYQLDQIGKLVLVDRTRPwMLNKYFDAAHFRVIDKPIDQ--QTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTML 546
Cdd:PRK09863 423 VITAAGIEQLKHLLATAYIRQ-NPERFLSAPGSFHYSNVRGEkwQHVTRQICAQLVAQHLLTADEAQRIIAREGAGNQLI 501
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709388247 547 GDGIALPHALGLLAKKTVVYTVIAPQGIAWGDETAHIIfLLAISKSEYEEAMAIYDIFVTFLRERAMSRLAATRSFDEF 625
Cdd:PRK09863 502 LNHLSIPHCWTEQERRYRGFAITLAQPIEVNNEVIYLV-LIVLAAADAAHELKIFSYLYSVLCQHPAEVIAGVTGYEAF 579
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
495-593 |
2.68e-11 |
|
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This model is specific for the IIA domain of the fructose PTS transporters. Also similar to the Enzyme IIA Fru subunits of the PTS, but included in TIGR01419 rather than this model, is enzyme IIA Ntr (nitrogen), also called PtsN, found in E. coli and other organisms, which may play a solely regulatory role. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
Pssm-ID: 273298 [Multi-domain] Cd Length: 129 Bit Score: 61.14 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 495 YFDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVD--AEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVIAPQ 572
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISdtEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80
|
90 100
....*....|....*....|....
gi 1709388247 573 GIAWGDE---TAHIIFLLAISKSE 593
Cdd:TIGR00848 81 GVDWQSLdgkPVKLIFLIAVPKDE 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
14-608 |
8.97e-135 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 408.09 E-value: 8.97e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 14 LLRNETLPQDELAQRLSVSTRTVRADITALNALLAQYGAQFTLNRGSGYQLKIDDrSRFQALEETAPKTQHvPRTAQERI 93
Cdd:COG3711 6 LKNNNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDD-EQKEKLLQLLEKSED-PLSPKERV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 94 HFLLVRFLTSAFSIKLENLADEWFVSRATLQNDMVEVRERFQRYQLTLETRPRHGMKLFGSEVSIRACLTDLLWELTLQG 173
Cdd:COG3711 84 AYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLSEN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 174 GINPLISAEALEADVPAQLEPVLQETLTRHHIRLTDVGERFICLYGAVVVRRVSEGYPLADFSAEDV---AQNVRDAARD 250
Cdd:COG3711 164 DLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWeikKPKEYEIAKE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 251 LAGELQRLAGKPFSPAEEEWLCVHIA-ARQVQDVDPETISADDDEALVNYILRYINSQYNYNLLDDAQLHADLLTHIKTM 329
Cdd:COG3711 244 ILKLIEERLGISLPEDEIGYIALHLLgARLNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 330 ITRVRYQIMIPNPLLDNIKQHYPMAWDMTLAAVSSWGKYTPYTISENEIGFLVLHIGVGLERHYNIgyqRQPHVLLVCDT 409
Cdd:COG3711 324 INRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES---KKKRVLVVCSS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 410 SNAMVRMIEAILQRKYPQLAIAATISQREYEQREAIDEDFVISTVRIgeKDKPVVTIAPFPTDYQLDQIGKLVLvdrtrp 489
Cdd:COG3711 401 GIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPL--EDKPVIVVSPLLTEEDIEKIRKFLK------ 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 490 wMLNKYFDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVI 569
Cdd:COG3711 473 -QIKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIVL 551
|
570 580 590
....*....|....*....|....*....|....*....
gi 1709388247 570 APQGIAWGDETAHIIFLLAISKSEYEEAMAIYDIFVTFL 608
Cdd:COG3711 552 AAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLL 590
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
496-628 |
8.19e-27 |
|
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. This family is one of four structurally and functionally distinct group IIA PTS system cytoplasmic enzymes, necessary for the uptake of carbohydrates across the cytoplasmic membrane and their phosphorylation.
Pssm-ID: 238129 [Multi-domain] Cd Length: 136 Bit Score: 105.72 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 496 FDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVIAPQGIA 575
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1709388247 576 WGDE---TAHIIFLLAISKSEyEEAMAIYDIFVTFLRERAMSRLAATRSFDEFKTV 628
Cdd:cd00211 81 FGSLdgqPVHLIFLLAAPDSN-EHLKALSQLARLLSDEEFVEQLLNAQSKEEILAL 135
|
|
| PTS_IIB_bgl_like |
cd05568 |
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ... |
401-483 |
7.14e-19 |
|
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory systems composed of a membrane-bound sugar-sensor (similar to BglF) and a transcription antiterminator (similar to BglG) which regulate expression of genes involved in sugar utilization. The domain architecture of the IIB-containing protein includes a region N-terminal to the IIB domain which is homologous to the BglG transcription antiterminator with an RNA-binding domain followed by two homologous domains, PRD1 and PRD2 (PTS Regulation Domains). C-terminal to the IIB domain is a domain similar to the PTS IIA domain. In this system, the BglG-like region and the IIB and IIA-like domains are all expressed together as a single multidomain protein. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include this sensory system with similarity to the bacterial bgl system, chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, and fructose systems.
Pssm-ID: 99910 Cd Length: 85 Bit Score: 81.40 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 401 PHVLLVCDTSNAMVRMIEAILQRKYPQLAIAATISQREYEQREAIDEDFVISTVRIGEKDKPVVTIAPFPTDYQLDQIGK 480
Cdd:cd05568 1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELEEVDLDDYDLIISTVPLEDTDKPVIVVSPILTEEDIKKIRK 80
|
...
gi 1709388247 481 LVL 483
Cdd:cd05568 81 FIK 83
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
495-625 |
9.49e-19 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 83.02 E-value: 9.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 495 YFDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVIAPQGI 574
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKEPV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1709388247 575 AWGDET---AHIIFLLAISKSEYEEAMAIYDIFVTFLRERAMSRLAATRSFDEF 625
Cdd:pfam00359 81 DFGSEDgkpVKLIFLLAAPDNEASHLKILSQLARLLQDEEFVEKLLKAKDPEEI 134
|
|
| PtsN |
COG1762 |
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ... |
491-628 |
1.51e-18 |
|
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate transport and metabolism, Signal transduction mechanisms];
Pssm-ID: 441368 [Multi-domain] Cd Length: 150 Bit Score: 82.59 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 491 MLNKYFDAAHFRVIDKPIDQQTLFAELCQQLQQEGFV--DAEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTV 568
Cdd:COG1762 2 MLSDLLTPELILLDLEASSKEEAIEELAELLAEKGYVldKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709388247 569 IAPQGIAWG---DETAHIIFLLAISKSEYEEAMAIYDIFVTFLR-ERAMSRLAATRSFDEFKTV 628
Cdd:COG1762 82 RLKEPVDFGamdGEPVDLVFLLAAPEDDSEEHLKLLAELARLLSdEEFREKLLNAKSPEEILEL 145
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
300-386 |
4.92e-17 |
|
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory domain found in bacterial transcriptional antiterminator such as BglG, SacY and LicT, as well as in activators such as MtlR and LevR. The PRD is phosphorylated on one or two conserved histidine residues. PRD-containing proteins are involved in the regulation of catabolic operons in Gram+ and Gram- bacteria and are often characterized by a short N-terminal effector domain that binds to either RNA (CAT-RBD for antiterminators pfam03123) or DNA (for activators), and a duplicated PRD module which is phosphorylated by the sugar phosphotransferase system (PTS) in response to the availability of carbon source. The phosphorylations modify the conformation and stability of the dimeric proteins and thereby the RNA- or DNA-binding activity of the effector domain. The structure of the LicT PRD domains has been solved in both the active (pdb:1h99) and inactive state (pdb:1tlv), revealing massive structural rearrangements upon activation.
Pssm-ID: 459973 [Multi-domain] Cd Length: 90 Bit Score: 76.52 E-value: 4.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 300 ILRYINSQYNYNLLDDaQLHADLLTHIKTMITRVRYQIMIPNPLLDNIKQHYPMAWDMTLAAVSSWGKYTPYTISENEIG 379
Cdd:pfam00874 3 IIELIEKKLGITFDDD-ILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81
|
....*..
gi 1709388247 380 FLVLHIG 386
Cdd:pfam00874 82 YIALHFL 88
|
|
| MtlA2 |
COG4668 |
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ... |
502-628 |
3.53e-15 |
|
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and metabolism];
Pssm-ID: 443705 [Multi-domain] Cd Length: 143 Bit Score: 72.89 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 502 RVIDKPIDQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALGlLAKKTVVYTVIA----PQGIAWG 577
Cdd:COG4668 10 RLNASAANKEEAIRLAGQLLVEAGYVEPEYIDAMLEREAQVSTYLGNGIAIPHGTN-EAKDLVLKTGISvlqfPDGVDWG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1709388247 578 D-ETAHIIFLLAiSKSeyEEAMAIY-DIFVTFLRERAMSRLAATRSFDEFKTV 628
Cdd:COG4668 89 DgNTVYLVIGIA-AKS--DEHLEILrQLARVLSDEENVEKLAKATDAEEILAL 138
|
|
| PRK09863 |
PRK09863 |
putative frv operon regulatory protein; Provisional |
5-625 |
1.61e-13 |
|
putative frv operon regulatory protein; Provisional
Pssm-ID: 182121 [Multi-domain] Cd Length: 584 Bit Score: 73.73 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 5 NQRLAQLFTLLRNETLPQDELAQRLSVSTRTVRADITALNALLaQYGAQFTLNRGSGYQLKIDDRSRFQALEEtapktqh 84
Cdd:PRK09863 3 NERELKIVDLLEQQDRSGGELAQQLGVSRRTIVRDIAYINFTL-NGKAIGSISGSAKYHLEILNRRSLFQLLQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 85 vprTAQERIHFLLVRFLTSAFsIKLENLADEWFVSRATLQNDMVEVRERFQRYqLTLETRPRHGMKLFGSEVSIRACLTD 164
Cdd:PRK09863 75 ---KSDNEDRLLLLRLLLNTF-TPMAQLASALNLSRTWVAERLPRLNQRYERI-CCIASRPGLGHFIDETEEKRIDILAN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 165 LLWELTLqgginpLISAEALEADVPAQLEPVLQETLTRHHIR----LTDVGERFICLygAVVVRRVSEGYPladfsAEDV 240
Cdd:PRK09863 150 LIRKDPQ------LIPKAGPTRDNLQHLSRTACDNQHRWPLMqgdyLSSLILAIYAL--RNQLTDEWPQYP-----GDEI 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 241 AQNVRDAArDLAGELQRLAGKPFSPAEEEwLCVHIAARQVQDvdpetisadddealvnyILRYINSQYNYNLLdDAQLHA 320
Cdd:PRK09863 217 KQIVEHSG-LFLGDNAVRTLTGLIEKQHQ-QAQVISADNVQQ-----------------LLQRVPGIASLNAI-DTQLVE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 321 DLLTHIktmitrVRyQIMIPNPL-------LDNIKQHYPMAWDMTLAAVSSWGKYTPYTISENEigFLVLHIGVGLERHY 393
Cdd:PRK09863 277 NIFGHL------LR-CLAFPVWIaehrqssINNLKAQNPAAFDMALHFITLLREQLDIPLFDSD--LIALYFACALERHQ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 394 NigyQRQPHVLLVcdTSNAMVRMIEAILQRKYPQLAIAATISQREYEQ-REAIDEDFVISTVR--IGEKD--KPVVTIAP 468
Cdd:PRK09863 348 N---ERVPILLLA--DQNSIATINQLIIEQKVLNIRVIIVRSLSELEAiREEIEPLLIINNSHylVDLQDaiNFYITFKN 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 469 FPTDYQLDQIGKLVLVDRTRPwMLNKYFDAAHFRVIDKPIDQ--QTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTML 546
Cdd:PRK09863 423 VITAAGIEQLKHLLATAYIRQ-NPERFLSAPGSFHYSNVRGEkwQHVTRQICAQLVAQHLLTADEAQRIIAREGAGNQLI 501
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709388247 547 GDGIALPHALGLLAKKTVVYTVIAPQGIAWGDETAHIIfLLAISKSEYEEAMAIYDIFVTFLRERAMSRLAATRSFDEF 625
Cdd:PRK09863 502 LNHLSIPHCWTEQERRYRGFAITLAQPIEVNNEVIYLV-LIVLAAADAAHELKIFSYLYSVLCQHPAEVIAGVTGYEAF 579
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
495-593 |
2.68e-11 |
|
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family Bacterial PTS transporters transport and concomitantly phosphorylate their sugar substrates, and typically consist of multiple subunits or protein domains. The Fru family is a large and complex family which includes several sequenced fructose and mannitol-specific permeases as well as several putative PTS permeases of unknown specificities. The fructose permeases of this family phosphorylate fructose on the 1-position. Those of family 4.6 phosphorylate fructose on the 6-position. The Fru family PTS systems typically have 3 domains, IIA, IIB and IIC, which may be found as 1 or more proteins. The fructose and mannitol transporters form separate phylogenetic clusters in this family. This model is specific for the IIA domain of the fructose PTS transporters. Also similar to the Enzyme IIA Fru subunits of the PTS, but included in TIGR01419 rather than this model, is enzyme IIA Ntr (nitrogen), also called PtsN, found in E. coli and other organisms, which may play a solely regulatory role. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids, Signal transduction, PTS]
Pssm-ID: 273298 [Multi-domain] Cd Length: 129 Bit Score: 61.14 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 495 YFDAAHFRVIDKPIDQQTLFAELCQQLQQEGFVD--AEFHDSVVEREAIVSTMLGDGIALPHALGLLAKKTVVYTVIAPQ 572
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISdtEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80
|
90 100
....*....|....*....|....
gi 1709388247 573 GIAWGDE---TAHIIFLLAISKSE 593
Cdd:TIGR00848 81 GVDWQSLdgkPVKLIFLIAVPKDE 104
|
|
| PTS_IIB |
cd00133 |
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ... |
402-482 |
1.39e-10 |
|
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS). In the multienzyme PTS complex, EII is a carbohydrate-specific permease consisting of two cytoplasmic domains (IIA and IIB) and a transmembrane channel IIC domain. The IIB domain fold includes a central four-stranded parallel open twisted beta-sheet flanked by alpha-helices on both sides. The seven major PTS systems with this IIB fold include chitobiose/lichenan, ascorbate, lactose, galactitol, mannitol, fructose, and a sensory system with similarity to the bacterial bgl system. The PTS is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, polyols, amino sugars, and other sugar derivatives. The four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB), can phosphorylate or interact with numerous non-PTS proteins thereby regulating their activity.
Pssm-ID: 99904 Cd Length: 84 Bit Score: 58.04 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 402 HVLLVCDTSNAMVRMIEAILQRKYPQLAIAATISQREYEQREAIDE-DFVISTVRIGEK--DKPVVTIAPFPTDYQLDQI 478
Cdd:cd00133 1 KILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVEAQGLSEVIDLADaDLIISTVPLAARflGKPVIVVSPLLNEKDGEKI 80
|
....
gi 1709388247 479 GKLV 482
Cdd:cd00133 81 LEKL 84
|
|
| PRK15083 |
PRK15083 |
PTS system mannitol-specific transporter subunit IICBA; Provisional |
519-625 |
2.17e-09 |
|
PTS system mannitol-specific transporter subunit IICBA; Provisional
Pssm-ID: 237905 [Multi-domain] Cd Length: 639 Bit Score: 60.45 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 519 QQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHALgLLAKKTVVYTVIA----PQGIAWGDETAHIIFL-LAISKSE 593
Cdd:PRK15083 520 EQLVKGGYVEPEYVDAMLDREKLTSTYLGESIAVPHGT-VEAKDRVLKTGVVfcqyPEGVRFGEEEDDIARLvIGIAARN 598
|
90 100 110
....*....|....*....|....*....|..
gi 1709388247 594 YEEAMAIYDIFVTFLRERAMSRLAATRSFDEF 625
Cdd:PRK15083 599 NEHIQVITSLTNALDDESVIERLAHTTSVDEV 630
|
|
| PRK13779 |
PRK13779 |
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional |
521-630 |
9.35e-08 |
|
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional
Pssm-ID: 237502 [Multi-domain] Cd Length: 503 Bit Score: 54.88 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 521 LQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHA---LGLLAKKTVVYTVIAPQGIAWGD-ETAHIIFLLAISKSEYee 596
Cdd:PRK13779 29 LEQAGNVENGYLQGMLARELQTSTFLGNGIAIPHGtldTRHMVKNTGVQIFQFPQGIEWGEgNIAYVVIGIAARSDEH-- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1709388247 597 amaiydifVTFLR--------ERAMSRLAATRSFDEFKTVAM 630
Cdd:PRK13779 107 --------LSLLRqlthvlsdEDTAAKLATLTDVKEFRAILM 140
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
10-62 |
1.55e-07 |
|
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
Pssm-ID: 429896 [Multi-domain] Cd Length: 52 Bit Score: 48.20 E-value: 1.55e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1709388247 10 QLFTLLRN--ETLPQDELAQRLSVSTRTVRADITALNALlaqyGAQFTLNRGSGY 62
Cdd:pfam08279 2 QILQLLLEarGPISGQELAEKLGVSRRTIRRDIKILEEL----GVPIEAEPGRGY 52
|
|
| PRK11109 |
PRK11109 |
fused PTS fructose transporter subunit IIA/HPr protein; |
509-578 |
1.73e-07 |
|
fused PTS fructose transporter subunit IIA/HPr protein;
Pssm-ID: 236849 [Multi-domain] Cd Length: 375 Bit Score: 53.80 E-value: 1.73e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709388247 509 DQQTLFAELCQQLQQEGFVDAEFHDSVVEREAIVSTMLGDGIALPHalGL-----LAKKTVVYTVIAPQGIAWGD 578
Cdd:PRK11109 17 NKEEAIRQVAAALTQAGNVAEGYVDGMLAREQQTSTFLGNGIAIPH--GTtdtrdLVLKTGVQVFQFPQGVTWGD 89
|
|
| Mga |
pfam05043 |
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a ... |
90-166 |
9.88e-07 |
|
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a DNA-binding protein that activates the expression of several important virulence genes in group A streptococcus in response to changing environmental conditions. This domain is found in the centre of the Mga proteins. This family also contains a number of bacterial RofA transcriptional regulators that seem to be largely restricted to streptococci. These proteins have been shown to regulate the expression of important bacterial adhesins. This is presumably a DNA-binding domain.
Pssm-ID: 428276 [Multi-domain] Cd Length: 87 Bit Score: 46.83 E-value: 9.88e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709388247 90 QERIHFLLVRFLTSAFSIKLENLADEWFVSRATLQNDMVEVRERFQRYQLTLETRPrhgMKLFGSEVSIRACLTDLL 166
Cdd:pfam05043 14 KESLKFQLLKYLFFEEFVSIKSLAQKLYISESTLYRKIKELNKLLKEFDLSIKKKN---LKLIGDEKQIRYFYALLF 87
|
|
| LevR |
COG3933 |
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]; |
283-383 |
1.55e-06 |
|
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
Pssm-ID: 443134 [Multi-domain] Cd Length: 916 Bit Score: 51.27 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 283 VDPETISadddeaLVNYILRYINSQYNYNLlDDAQLHAdLLTHIKTMITRVRYQIMIPNPLLDNIKQHYPMAWDMTLAAV 362
Cdd:COG3933 453 VDEDIIN------VVEEILELAEKKLGRKF-SENFIYA-LSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIK 524
|
90 100
....*....|....*....|.
gi 1709388247 363 SSWGKYTPYTISENEIGFLVL 383
Cdd:COG3933 525 ELIEQELDIEIPEDEVGFLTL 545
|
|
| PRK11564 |
PRK11564 |
stationary phase inducible protein CsiE; Provisional |
88-352 |
6.03e-06 |
|
stationary phase inducible protein CsiE; Provisional
Pssm-ID: 236932 [Multi-domain] Cd Length: 426 Bit Score: 48.85 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 88 TAQERIHFLLVRFLtSAFSIKLENLADEWFVSRATLQNDMVEVRERFQRY-QLTLETRPRHGMKLFGSEVSIRACL---- 162
Cdd:PRK11564 13 APQRRCQILLMLFQ-PGLTVTLETFSQLNGVDDDTARQDIAETGREIQRYhRLTLTTGADGSYRIEGTALDQRLCLlhwl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 163 ---------------TDLLWELTLQGGI-NPLISAEALEADVpAQLEPVLQETLTRHhirltDVgeRFICLYGAVVVRRV 226
Cdd:PRK11564 92 rrglrlcpsfitqqfTPALKSELKQRGIaRNLYDDTNLQALI-NLCSRRLNRQFEER-----DR--QFLQLYLQYCLLQH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 227 SEGYPlADFSAEDVAQNVRDAARDLAGEL----QRLAGKPfSPAEEEWLCVhIAARQVQDVDPETISADDDEALVNYILR 302
Cdd:PRK11564 164 HAGIT-PQFNPLQQQWLESKAEFQLAQEIgrhwQRRVLQP-PPLDEPLFLA-LLFSMLRAPDPLRDAHQRDRRLRQAIKR 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1709388247 303 YIN---SQYNYNLLDDAQLHADLLTHIKTMITRVRYQIMIPNPLLDNIKQHYP 352
Cdd:PRK11564 241 LVNrfrELGGVRFSDEQGLCDQLYTHLAQALERSLFAIGIDNTLPEEFARLYP 293
|
|
| PRK09765 |
PRK09765 |
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional |
517-593 |
1.01e-05 |
|
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
Pssm-ID: 182066 [Multi-domain] Cd Length: 631 Bit Score: 48.58 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709388247 517 LCQQLQQEG-FVDAE-FHDSVVEREAIVSTMLGDGIALPHALGLLAKKT--VVYTVIAPqgIAW----GDETAHIIFLLA 588
Cdd:PRK09765 28 LAQRLAALGkISSTEqFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAafAVATLSEP--LQWegvdGPEAVDLIFLLA 105
|
....*
gi 1709388247 589 ISKSE 593
Cdd:PRK09765 106 IPPNE 110
|
|
| YobV |
COG2378 |
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ... |
7-64 |
2.91e-04 |
|
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];
Pssm-ID: 441945 [Multi-domain] Cd Length: 314 Bit Score: 43.53 E-value: 2.91e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709388247 7 RLAQLFTLLRN-ETLPQDELAQRLSVSTRTVRADItalnALLAQYGAQFTLNRGS--GYQL 64
Cdd:COG2378 6 RLLALLQLLQSrRGVTAAELAERLEVSERTIYRDI----DALRELGVPIEAERGRggGYRL 62
|
|
| PRK09772 |
PRK09772 |
transcriptional antiterminator BglG; Provisional |
318-385 |
1.70e-03 |
|
transcriptional antiterminator BglG; Provisional
Pssm-ID: 170086 [Multi-domain] Cd Length: 278 Bit Score: 40.84 E-value: 1.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709388247 318 LHADLLTHIKTMITRVRYQIMIPNPLLDNIKQHYPMAWDMTLAAVSSWGKYTPYTISENEIGFLVLHI 385
Cdd:PRK09772 94 IYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161
|
|
| |
