|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
14-609 |
2.33e-138 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 417.34 E-value: 2.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 14 MLQNEALPQDELAQRLSVSTRTVRADITALNALLSQYGAQFVLSRGNGYQLKIDDPAsFHTLQTQQPDSllRIPRTSQER 93
Cdd:COG3711 6 LKNNNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQ-KEKLLQLLEKS--EDPLSPKER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 94 VHWLVVRFLTSAFSLKLEDLADEWFISRATLQNDMAEVREHLQRYHLTLETRPRHGMKLFGSEMAIRACLTDLLWMLAQQ 173
Cdd:COG3711 83 VAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 174 DPQHPLVTEEALNAGLPERLQPVLQDIFARFHIRLTDEGELFLRLYCAVAVRRISEGYPLPEFAAEEAE---QSVCLATR 250
Cdd:COG3711 163 NDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEikkPKEYEIAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 251 EIAAVLHRLADKPLSISEENWLQVHIAARQVQEI-APSAINADDDEALVNYILRFINSQYNYNLLNDKQLHADLLTHIKT 329
Cdd:COG3711 243 EILKLIEERLGISLPEDEIGYIALHLLGARLNNDnELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 330 MITRVRYQIMIPNPLLENIKQHYPMAWDMTLAAVSGWGKYTPYTISENEIGFLVLHIGVGLERSYNIgyqRQPKVLLVCD 409
Cdd:COG3711 323 AINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES---KKKRVLVVCS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 410 AGNAMARMIEAVLARKYPQIDIVDTVTLRDYEQRESISEDFVISTARLgeKDKPVVMIAPFPTDYQLEQIGKLVLvdrtr 489
Cdd:COG3711 400 SGIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPL--EDKPVIVVSPLLTEEDIEKIRKFLK----- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 490 pwMLNKFFDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKKTVVYTI 569
Cdd:COG3711 473 --QIKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIV 550
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2197300114 570 LAPQGIAWGDETAHVIFLLAISKSEYEEAMAIYDIFVTFL 609
Cdd:COG3711 551 LAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLL 590
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
497-629 |
2.93e-23 |
|
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: 95.71 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 497 FDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKKTVVYTILAPQGIA 576
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2197300114 577 WGDE---TAHVIFLLAISKSEyEEAMAIYDIFVTFLRERAMTRLCGCRNFTEFKTV 629
Cdd:cd00211 81 FGSLdgqPVHLIFLLAAPDSN-EHLKALSQLARLLSDEEFVEQLLNAQSKEEILAL 135
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
301-387 |
8.66e-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: 75.75 E-value: 8.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 301 ILRFINSQYNYNLLNDKQLHAdLLTHIKTMITRVRYQIMIPNPLLENIKQHYPMAWDMTLAAVSGWGKYTPYTISENEIG 380
Cdd:pfam00874 3 IIELIEKKLGITFDDDILYIR-LILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81
|
....*..
gi 2197300114 381 FLVLHIG 387
Cdd:pfam00874 82 YIALHFL 88
|
|
| PRK09863 |
PRK09863 |
putative frv operon regulatory protein; Provisional |
5-626 |
3.38e-16 |
|
putative frv operon regulatory protein; Provisional
Pssm-ID: 182121 [Multi-domain] Cd Length: 584 Bit Score: 82.21 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 5 NQRLAQLFGMLQNEALPQDELAQRLSVSTRTVRADITALNALLsQYGAQFVLSRGNGYQLKIDDPASFHTLQTQQPDS-- 82
Cdd:PRK09863 3 NERELKIVDLLEQQDRSGGELAQQLGVSRRTIVRDIAYINFTL-NGKAIGSISGSAKYHLEILNRRSLFQLLQKSDNEdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 83 --LLRIprtsqervhwLVVRFLTSAfslkleDLADEWFISRATLQNDMAEVRehlQRYHLTLETRPRHGMKLFGSEMAIR 160
Cdd:PRK09863 82 llLLRL----------LLNTFTPMA------QLASALNLSRTWVAERLPRLN---QRYERICCIASRPGLGHFIDETEEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 161 AclTDLLWMLAQQDPQhpLVTEEALNAGLPERLQPVLQDIFARFHIRLTD-EGELFLRLYC-AVAVRRISEGYPLPEFAA 238
Cdd:PRK09863 143 R--IDILANLIRKDPQ--LIPKAGPTRDNLQHLSRTACDNQHRWPLMQGDyLSSLILAIYAlRNQLTDEWPQYPGDEIKQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 239 EEAEQSVCLATREiAAVLHRLADKplsiseENWLQVHIAARQVQEiapsainadddealvnyILRFINSQYNYNLLnDKQ 318
Cdd:PRK09863 219 IVEHSGLFLGDNA-VRTLTGLIEK------QHQQAQVISADNVQQ-----------------LLQRVPGIASLNAI-DTQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 319 LHADLLTHIktmitrVRyQIMIPNPLLE-------NIKQHYPMAWDMTLAAVSGWGKYTPYTISENEigFLVLHIGVGLE 391
Cdd:PRK09863 274 LVENIFGHL------LR-CLAFPVWIAEhrqssinNLKAQNPAAFDMALHFITLLREQLDIPLFDSD--LIALYFACALE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 392 RSYNigyQRQPKVLLVcdAGNAMARMIEAVLARKYPQIDIVDTVTLRDYEQ-RESISEDFVISTAR-LGEKDKPVVMIAP 469
Cdd:PRK09863 345 RHQN---ERVPILLLA--DQNSIATINQLIIEQKVLNIRVIIVRSLSELEAiREEIEPLLIINNSHyLVDLQDAINFYIT 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 470 FP---TDYQLEQIGKLVLVDRTRPwMLNKFFDAAHFRVIDGPMDQ--QTLFNTLCRQLQDEGFVDAEFLDSVVEREAIVS 544
Cdd:PRK09863 420 FKnviTAAGIEQLKHLLATAYIRQ-NPERFLSAPGSFHYSNVRGEkwQHVTRQICAQLVAQHLLTADEAQRIIAREGAGN 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 545 TMLGDGIALPHSLGLLAKKTVVYTILAPQGIAWGDETAHVIfLLAISKSEYEEAMAIYDIFVTFLRERAMTRLCGCRNFT 624
Cdd:PRK09863 499 QLILNHLSIPHCWTEQERRYRGFAITLAQPIEVNNEVIYLV-LIVLAAADAAHELKIFSYLYSVLCQHPAEVIAGVTGYE 577
|
..
gi 2197300114 625 EF 626
Cdd:PRK09863 578 AF 579
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
496-594 |
1.52e-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: 61.91 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 496 FFDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFVD--AEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKK-TVVYTILAp 572
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISdtEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQpFVAIARLV- 79
|
90 100
....*....|....*....|....*
gi 2197300114 573 QGIAWGDE---TAHVIFLLAISKSE 594
Cdd:TIGR00848 80 KGVDWQSLdgkPVKLIFLIAVPKDE 104
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
14-609 |
2.33e-138 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 417.34 E-value: 2.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 14 MLQNEALPQDELAQRLSVSTRTVRADITALNALLSQYGAQFVLSRGNGYQLKIDDPAsFHTLQTQQPDSllRIPRTSQER 93
Cdd:COG3711 6 LKNNNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQ-KEKLLQLLEKS--EDPLSPKER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 94 VHWLVVRFLTSAFSLKLEDLADEWFISRATLQNDMAEVREHLQRYHLTLETRPRHGMKLFGSEMAIRACLTDLLWMLAQQ 173
Cdd:COG3711 83 VAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLSE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 174 DPQHPLVTEEALNAGLPERLQPVLQDIFARFHIRLTDEGELFLRLYCAVAVRRISEGYPLPEFAAEEAE---QSVCLATR 250
Cdd:COG3711 163 NDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEikkPKEYEIAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 251 EIAAVLHRLADKPLSISEENWLQVHIAARQVQEI-APSAINADDDEALVNYILRFINSQYNYNLLNDKQLHADLLTHIKT 329
Cdd:COG3711 243 EILKLIEERLGISLPEDEIGYIALHLLGARLNNDnELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 330 MITRVRYQIMIPNPLLENIKQHYPMAWDMTLAAVSGWGKYTPYTISENEIGFLVLHIGVGLERSYNIgyqRQPKVLLVCD 409
Cdd:COG3711 323 AINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES---KKKRVLVVCS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 410 AGNAMARMIEAVLARKYPQIDIVDTVTLRDYEQRESISEDFVISTARLgeKDKPVVMIAPFPTDYQLEQIGKLVLvdrtr 489
Cdd:COG3711 400 SGIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPL--EDKPVIVVSPLLTEEDIEKIRKFLK----- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 490 pwMLNKFFDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKKTVVYTI 569
Cdd:COG3711 473 --QIKKKLAKILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIV 550
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2197300114 570 LAPQGIAWGDETAHVIFLLAISKSEYEEAMAIYDIFVTFL 609
Cdd:COG3711 551 LAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLL 590
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
497-629 |
2.93e-23 |
|
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: 95.71 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 497 FDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKKTVVYTILAPQGIA 576
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2197300114 577 WGDE---TAHVIFLLAISKSEyEEAMAIYDIFVTFLRERAMTRLCGCRNFTEFKTV 629
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 ... |
402-484 |
1.12e-21 |
|
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: 89.49 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 402 PKVLLVCDAGNAMARMIEAVLARKYPQIDIVDTVTLRDYEQRESISEDFVISTARLGEKDKPVVMIAPFPTDYQLEQIGK 481
Cdd:cd05568 1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELEEVDLDDYDLIISTVPLEDTDKPVIVVSPILTEEDIKKIRK 80
|
...
gi 2197300114 482 LVL 484
Cdd:cd05568 81 FIK 83
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
301-387 |
8.66e-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: 75.75 E-value: 8.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 301 ILRFINSQYNYNLLNDKQLHAdLLTHIKTMITRVRYQIMIPNPLLENIKQHYPMAWDMTLAAVSGWGKYTPYTISENEIG 380
Cdd:pfam00874 3 IIELIEKKLGITFDDDILYIR-LILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81
|
....*..
gi 2197300114 381 FLVLHIG 387
Cdd:pfam00874 82 YIALHFL 88
|
|
| PRK09863 |
PRK09863 |
putative frv operon regulatory protein; Provisional |
5-626 |
3.38e-16 |
|
putative frv operon regulatory protein; Provisional
Pssm-ID: 182121 [Multi-domain] Cd Length: 584 Bit Score: 82.21 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 5 NQRLAQLFGMLQNEALPQDELAQRLSVSTRTVRADITALNALLsQYGAQFVLSRGNGYQLKIDDPASFHTLQTQQPDS-- 82
Cdd:PRK09863 3 NERELKIVDLLEQQDRSGGELAQQLGVSRRTIVRDIAYINFTL-NGKAIGSISGSAKYHLEILNRRSLFQLLQKSDNEdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 83 --LLRIprtsqervhwLVVRFLTSAfslkleDLADEWFISRATLQNDMAEVRehlQRYHLTLETRPRHGMKLFGSEMAIR 160
Cdd:PRK09863 82 llLLRL----------LLNTFTPMA------QLASALNLSRTWVAERLPRLN---QRYERICCIASRPGLGHFIDETEEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 161 AclTDLLWMLAQQDPQhpLVTEEALNAGLPERLQPVLQDIFARFHIRLTD-EGELFLRLYC-AVAVRRISEGYPLPEFAA 238
Cdd:PRK09863 143 R--IDILANLIRKDPQ--LIPKAGPTRDNLQHLSRTACDNQHRWPLMQGDyLSSLILAIYAlRNQLTDEWPQYPGDEIKQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 239 EEAEQSVCLATREiAAVLHRLADKplsiseENWLQVHIAARQVQEiapsainadddealvnyILRFINSQYNYNLLnDKQ 318
Cdd:PRK09863 219 IVEHSGLFLGDNA-VRTLTGLIEK------QHQQAQVISADNVQQ-----------------LLQRVPGIASLNAI-DTQ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 319 LHADLLTHIktmitrVRyQIMIPNPLLE-------NIKQHYPMAWDMTLAAVSGWGKYTPYTISENEigFLVLHIGVGLE 391
Cdd:PRK09863 274 LVENIFGHL------LR-CLAFPVWIAEhrqssinNLKAQNPAAFDMALHFITLLREQLDIPLFDSD--LIALYFACALE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 392 RSYNigyQRQPKVLLVcdAGNAMARMIEAVLARKYPQIDIVDTVTLRDYEQ-RESISEDFVISTAR-LGEKDKPVVMIAP 469
Cdd:PRK09863 345 RHQN---ERVPILLLA--DQNSIATINQLIIEQKVLNIRVIIVRSLSELEAiREEIEPLLIINNSHyLVDLQDAINFYIT 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 470 FP---TDYQLEQIGKLVLVDRTRPwMLNKFFDAAHFRVIDGPMDQ--QTLFNTLCRQLQDEGFVDAEFLDSVVEREAIVS 544
Cdd:PRK09863 420 FKnviTAAGIEQLKHLLATAYIRQ-NPERFLSAPGSFHYSNVRGEkwQHVTRQICAQLVAQHLLTADEAQRIIAREGAGN 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 545 TMLGDGIALPHSLGLLAKKTVVYTILAPQGIAWGDETAHVIfLLAISKSEYEEAMAIYDIFVTFLRERAMTRLCGCRNFT 624
Cdd:PRK09863 499 QLILNHLSIPHCWTEQERRYRGFAITLAQPIEVNNEVIYLV-LIVLAAADAAHELKIFSYLYSVLCQHPAEVIAGVTGYE 577
|
..
gi 2197300114 625 EF 626
Cdd:PRK09863 578 AF 579
|
|
| PtsN |
COG1762 |
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ... |
492-629 |
4.67e-16 |
|
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: 75.66 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 492 MLNKFFDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFV--DAEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKKTVVYTI 569
Cdd:COG1762 2 MLSDLLTPELILLDLEASSKEEAIEELAELLAEKGYVldKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2197300114 570 LAPQGIAWG---DETAHVIFLLAISKSEYEEAMAIYDIFVTFLR-ERAMTRLCGCRNFTEFKTV 629
Cdd:COG1762 82 RLKEPVDFGamdGEPVDLVFLLAAPEDDSEEHLKLLAELARLLSdEEFREKLLNAKSPEEILEL 145
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
496-626 |
5.66e-16 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 74.93 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 496 FFDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKKTVVYTILAPQGI 575
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKEPV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2197300114 576 AWGDET---AHVIFLLAISKSEYEEAMAIYDIFVTFLRERAMTRLCGCRNFTEF 626
Cdd:pfam00359 81 DFGSEDgkpVKLIFLLAAPDNEASHLKILSQLARLLQDEEFVEKLLKAKDPEEI 134
|
|
| MtlA2 |
COG4668 |
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ... |
520-617 |
2.41e-13 |
|
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and metabolism];
Pssm-ID: 443705 [Multi-domain] Cd Length: 143 Bit Score: 67.49 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 520 RQLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHslGLL-AKKTVVYTILA----PQGIAWGD-ETAHVIFLLAiSKS 593
Cdd:COG4668 27 QLLVEAGYVEPEYIDAMLEREAQVSTYLGNGIAIPH--GTNeAKDLVLKTGISvlqfPDGVDWGDgNTVYLVIGIA-AKS 103
|
90 100
....*....|....*....|....*
gi 2197300114 594 eyEEAMAIY-DIFVTFLRERAMTRL 617
Cdd:COG4668 104 --DEHLEILrQLARVLSDEENVEKL 126
|
|
| PTS_IIB |
cd00133 |
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ... |
403-483 |
1.66e-12 |
|
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: 63.43 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 403 KVLLVCDAGNAMARMIEAVLARKYPQIDIVDTVTLRDYEQRESISE-DFVISTARLGEK--DKPVVMIAPFPTDYQLEQI 479
Cdd:cd00133 1 KILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVEAQGLSEVIDLADaDLIISTVPLAARflGKPVIVVSPLLNEKDGEKI 80
|
....
gi 2197300114 480 GKLV 483
Cdd:cd00133 81 LEKL 84
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
496-594 |
1.52e-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: 61.91 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 496 FFDAAHFRVIDGPMDQQTLFNTLCRQLQDEGFVD--AEFLDSVVEREAIVSTMLGDGIALPHSLGLLAKK-TVVYTILAp 572
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISdtEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQpFVAIARLV- 79
|
90 100
....*....|....*....|....*
gi 2197300114 573 QGIAWGDE---TAHVIFLLAISKSE 594
Cdd:TIGR00848 80 KGVDWQSLdgkPVKLIFLIAVPKDE 104
|
|
| PRK15083 |
PRK15083 |
PTS system mannitol-specific transporter subunit IICBA; Provisional |
520-580 |
2.37e-08 |
|
PTS system mannitol-specific transporter subunit IICBA; Provisional
Pssm-ID: 237905 [Multi-domain] Cd Length: 639 Bit Score: 56.99 E-value: 2.37e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2197300114 520 RQLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHSLgLLAKKTVVYTILA----PQGIAWGDE 580
Cdd:PRK15083 520 EQLVKGGYVEPEYVDAMLDREKLTSTYLGESIAVPHGT-VEAKDRVLKTGVVfcqyPEGVRFGEE 583
|
|
| PRK11109 |
PRK11109 |
fused PTS fructose transporter subunit IIA/HPr protein; |
521-595 |
4.96e-08 |
|
fused PTS fructose transporter subunit IIA/HPr protein;
Pssm-ID: 236849 [Multi-domain] Cd Length: 375 Bit Score: 55.34 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 521 QLQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPHslGL-----LAKKTVVYTILAPQGIAWGD-ETAHVIFLLAISKSE 594
Cdd:PRK11109 28 ALTQAGNVAEGYVDGMLAREQQTSTFLGNGIAIPH--GTtdtrdLVLKTGVQVFQFPQGVTWGDgQTAYVAIGIAAKSDE 105
|
.
gi 2197300114 595 Y 595
Cdd:PRK11109 106 H 106
|
|
| LevR |
COG3933 |
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]; |
297-384 |
2.19e-07 |
|
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
Pssm-ID: 443134 [Multi-domain] Cd Length: 916 Bit Score: 54.35 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 297 LVNYILRFINSQYNYNLlNDKQLHAdLLTHIKTMITRVRYQIMIPNPLLENIKQHYPMAWDMTLAAVSGWGKYTPYTISE 376
Cdd:COG3933 460 VVEEILELAEKKLGRKF-SENFIYA-LSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPE 537
|
....*...
gi 2197300114 377 NEIGFLVL 384
Cdd:COG3933 538 DEVGFLTL 545
|
|
| Mga |
pfam05043 |
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a ... |
91-167 |
2.26e-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: 48.76 E-value: 2.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2197300114 91 QERVHWLVVRFLTSAFSLKLEDLADEWFISRATLQNDMAEVREHLQRYHLTLETRPrhgMKLFGSEMAIRACLTDLL 167
Cdd:pfam05043 14 KESLKFQLLKYLFFEEFVSIKSLAQKLYISESTLYRKIKELNKLLKEFDLSIKKKN---LKLIGDEKQIRYFYALLF 87
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
14-62 |
3.33e-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: 47.04 E-value: 3.33e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 2197300114 14 MLQNEALPQDELAQRLSVSTRTVRADITALNALlsqyGAQFVLSRGNGY 62
Cdd:pfam08279 8 LEARGPISGQELAEKLGVSRRTIRRDIKILEEL----GVPIEAEPGRGY 52
|
|
| PRK13779 |
PRK13779 |
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional |
522-595 |
8.05e-07 |
|
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional
Pssm-ID: 237502 [Multi-domain] Cd Length: 503 Bit Score: 52.18 E-value: 8.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2197300114 522 LQDEGFVDAEFLDSVVEREAIVSTMLGDGIALPH---SLGLLAKKTVVYTILAPQGIAWGD-ETAHVIFLLAISKSEY 595
Cdd:PRK13779 29 LEQAGNVENGYLQGMLARELQTSTFLGNGIAIPHgtlDTRHMVKNTGVQIFQFPQGIEWGEgNIAYVVIGIAARSDEH 106
|
|
| PRK09765 |
PRK09765 |
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional |
518-594 |
3.92e-06 |
|
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
Pssm-ID: 182066 [Multi-domain] Cd Length: 631 Bit Score: 50.12 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 518 LCRQLQDEG-FVDAE-FLDSVVEREAIVSTMLGDGIALPH--SLGLLAKKTVVYTILAPqgIAW----GDETAHVIFLLA 589
Cdd:PRK09765 28 LAQRLAALGkISSTEqFLEEVYRRESLGPTALGEGLAVPHgkTAAVKEAAFAVATLSEP--LQWegvdGPEAVDLIFLLA 105
|
....*
gi 2197300114 590 ISKSE 594
Cdd:PRK09765 106 IPPNE 110
|
|
| PRK11564 |
PRK11564 |
stationary phase inducible protein CsiE; Provisional |
80-419 |
5.69e-06 |
|
stationary phase inducible protein CsiE; Provisional
Pssm-ID: 236932 [Multi-domain] Cd Length: 426 Bit Score: 49.24 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 80 PDSLLRiprTSQERVHWLVVRFLtSAFSLKLEDLADEWFISRATLQNDMAEVREHLQRYH-LTLETRPRHGMKLFGSEMA 158
Cdd:PRK11564 7 PPSVLS---APQRRCQILLMLFQ-PGLTVTLETFSQLNGVDDDTARQDIAETGREIQRYHrLTLTTGADGSYRIEGTALD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 159 IRACLtdLLWM----------------------LAQQDPQHPLVTEEALNAgLPERLQPVLQDIFarfhirlTDEGELFL 216
Cdd:PRK11564 83 QRLCL--LHWLrrglrlcpsfitqqftpalkseLKQRGIARNLYDDTNLQA-LINLCSRRLNRQF-------EERDRQFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 217 RLYCAVAVRRISEGYPlPEFAAEE-------AEQsvcLATREIAAVLHRLADKPLSISEENWL-----QVHiaarqvqei 284
Cdd:PRK11564 153 QLYLQYCLLQHHAGIT-PQFNPLQqqwleskAEF---QLAQEIGRHWQRRVLQPPPLDEPLFLallfsMLR--------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2197300114 285 APSAINADDDE------ALVNYILRFiNSQYNYNLLNDKQLHADLLTHIKTMITRVRYQIMIPNPLLENIKQHYPMAWDM 358
Cdd:PRK11564 220 APDPLRDAHQRdrrlrqAIKRLVNRF-RELGGVRFSDEQGLCDQLYTHLAQALERSLFAIGIDNTLPEEFARLYPRLLRT 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2197300114 359 TLAAVSGWGKYTPYTISENEIGFLVLHIGVGLERSyNIGYQRQpkVLLVCDAGNAMARMIE 419
Cdd:PRK11564 299 TRAALAGFEQEYGVHFSDEEVGLVAVIFGAWLMQE-NDLHEKQ--ILLLTGDNPELEAQIE 356
|
|
| YobV |
COG2378 |
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ... |
7-64 |
3.10e-04 |
|
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];
Pssm-ID: 441945 [Multi-domain] Cd Length: 314 Bit Score: 43.14 E-value: 3.10e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2197300114 7 RLAQLFGMLQN-EALPQDELAQRLSVSTRTVRADItalnALLSQYGAQFVLSRG--NGYQL 64
Cdd:COG2378 6 RLLALLQLLQSrRGVTAAELAERLEVSERTIYRDI----DALRELGVPIEAERGrgGGYRL 62
|
|
| PRK09772 |
PRK09772 |
transcriptional antiterminator BglG; Provisional |
319-386 |
1.71e-03 |
|
transcriptional antiterminator BglG; Provisional
Pssm-ID: 170086 [Multi-domain] Cd Length: 278 Bit Score: 40.84 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2197300114 319 LHADLLTHIKTMITRVRYQIMIPNPLLENIKQHYPMAWDMTLAAVSGWGKYTPYTISENEIGFLVLHI 386
Cdd:PRK09772 94 IYISLTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161
|
|
| |
