|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
17-637 |
8.35e-140 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 421.19 E-value: 8.35e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 17 QTETLPQDELAKRFAVSTRTVRADITALNEILDKYGARFVHSRGAGYRLQVDNAALfsALQHQERRKQATPRSAQERVHY 96
Cdd:COG3711 8 NNNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQK--EKLLQLLEKSEDPLSPKERVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 97 LLVRFLTSAFSLKLEDLADEWFVSRGTLQNDMAEVRERLAHYQLTIETKPRYGMKLFGAEMAIRACLTDLLFQLQLADAE 176
Cdd:COG3711 86 ILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLSENDL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 177 NPLLNNEILLQPQVAAFAGLLHPLLSQYAIRLTDEGEQYLIFYCAVALRRINDGYPLPDF-----EVEDGDEavRQVSTR 251
Cdd:COG3711 166 LSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDnpllwEIKKPKE--YEIAKE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 252 LAAELRAASGKEISMAEEAYLRVNIAARRVQ-DVQPTEINADDEEALVDYILSYINAHYNYNLQGDEQLRADLLTHIKTM 330
Cdd:COG3711 244 ILKLIEERLGISLPEDEIGYIALHLLGARLNnDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 331 ITRVKYQINIPNPLLANIKQHYPMAYDVTLAAVSSWGKYTPYTLSENEIGYLVLHIGVGLERHYNigyERHPQVMLVCDT 410
Cdd:COG3711 324 INRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKE---SKKKRVLVVCSS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 411 GNSTVRMIQAQIARKYPQLVMTRIVSLRDYEMLAHIDEDFVISNARIgeKNKPVVVMSPFPTDYQLEQLGKLVLVDRTKp 490
Cdd:COG3711 401 GIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPL--EDKPVIVVSPLLTEEDIEKIRKFLKQIKKK- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 491 ymLEKFfdaeHFMVLNEPLTQAELFSRVCGQLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTLL 570
Cdd:COG3711 478 --LAKI----LFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIVL 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672091835 571 APQGVAWGEGEVAHVIFLLAISKSDYEEAMAIYELFVTFVRERSMSRLLGSDSFDSFKAVALDCLSR 637
Cdd:COG3711 552 AAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILLLL 618
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
497-630 |
9.72e-21 |
|
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: 88.39 E-value: 9.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 497 FDAEHFMVLNEPLTQAELFSRVCGQLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTLLAPQGVA 576
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 672091835 577 WG--EGEVAHVIFLLAISKSDyEEAMAIYELFVTFVRERSMSRLLGSDSFDSFKAV 630
Cdd:cd00211 81 FGslDGQPVHLIFLLAAPDSN-EHLKALSQLARLLSDEEFVEQLLNAQSKEEILAL 135
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
301-387 |
3.56e-18 |
|
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: 79.60 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 301 ILSYINAHYNYNLQgDEQLRADLLTHIKTMITRVKYQINIPNPLLANIKQHYPMAYDVTLAAVSSWGKYTPYTLSENEIG 380
Cdd:pfam00874 3 IIELIEKKLGITFD-DDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81
|
....*..
gi 672091835 381 YLVLHIG 387
Cdd:pfam00874 82 YIALHFL 88
|
|
| PRK11109 |
PRK11109 |
fused PTS fructose transporter subunit IIA/HPr protein; |
518-623 |
4.35e-10 |
|
fused PTS fructose transporter subunit IIA/HPr protein;
Pssm-ID: 236849 [Multi-domain] Cd Length: 375 Bit Score: 61.89 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 518 VCGQLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHslGL-----LAKKTVVVTLLAPQGVAWGEGEVAHVIFLLAiS 592
Cdd:PRK11109 25 VAAALTQAGNVAEGYVDGMLAREQQTSTFLGNGIAIPH--GTtdtrdLVLKTGVQVFQFPQGVTWGDGQTAYVAIGIA-A 101
|
90 100 110
....*....|....*....|....*....|.
gi 672091835 593 KSDyeEAMAIYelfvtfvreRSMSRLLGSDS 623
Cdd:PRK11109 102 KSD--EHLGLL---------RQLTHVLSDDS 121
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
496-624 |
1.04e-08 |
|
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: 53.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 496 FFDAEHFMVLNEPLTQAELFSRVCGQLEREGYVG--ADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTLLAPQ 573
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISdtEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 672091835 574 GVAWG--EGEVAHVIFLLAISKSdyEEAMAIYELFVTFvrersmSRLLGSDSF 624
Cdd:TIGR00848 81 GVDWQslDGKPVKLIFLIAVPKD--EAGNTHLKALSQL------ARLLLNDEF 125
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
17-637 |
8.35e-140 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 421.19 E-value: 8.35e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 17 QTETLPQDELAKRFAVSTRTVRADITALNEILDKYGARFVHSRGAGYRLQVDNAALfsALQHQERRKQATPRSAQERVHY 96
Cdd:COG3711 8 NNNVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIGFRLDIDDEQK--EKLLQLLEKSEDPLSPKERVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 97 LLVRFLTSAFSLKLEDLADEWFVSRGTLQNDMAEVRERLAHYQLTIETKPRYGMKLFGAEMAIRACLTDLLFQLQLADAE 176
Cdd:COG3711 86 ILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAELLSELLSENDL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 177 NPLLNNEILLQPQVAAFAGLLHPLLSQYAIRLTDEGEQYLIFYCAVALRRINDGYPLPDF-----EVEDGDEavRQVSTR 251
Cdd:COG3711 166 LSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDnpllwEIKKPKE--YEIAKE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 252 LAAELRAASGKEISMAEEAYLRVNIAARRVQ-DVQPTEINADDEEALVDYILSYINAHYNYNLQGDEQLRADLLTHIKTM 330
Cdd:COG3711 244 ILKLIEERLGISLPEDEIGYIALHLLGARLNnDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYERLITHLKPA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 331 ITRVKYQINIPNPLLANIKQHYPMAYDVTLAAVSSWGKYTPYTLSENEIGYLVLHIGVGLERHYNigyERHPQVMLVCDT 410
Cdd:COG3711 324 INRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKE---SKKKRVLVVCSS 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 411 GNSTVRMIQAQIARKYPQLVMTRIVSLRDYEMLAHIDEDFVISNARIgeKNKPVVVMSPFPTDYQLEQLGKLVLVDRTKp 490
Cdd:COG3711 401 GIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLEDYDLIISTVPL--EDKPVIVVSPLLTEEDIEKIRKFLKQIKKK- 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 491 ymLEKFfdaeHFMVLNEPLTQAELFSRVCGQLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTLL 570
Cdd:COG3711 478 --LAKI----LFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIVL 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672091835 571 APQGVAWGEGEVAHVIFLLAISKSDYEEAMAIYELFVTFVRERSMSRLLGSDSFDSFKAVALDCLSR 637
Cdd:COG3711 552 AAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILLLL 618
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
497-630 |
9.72e-21 |
|
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: 88.39 E-value: 9.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 497 FDAEHFMVLNEPLTQAELFSRVCGQLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTLLAPQGVA 576
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 672091835 577 WG--EGEVAHVIFLLAISKSDyEEAMAIYELFVTFVRERSMSRLLGSDSFDSFKAV 630
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 |
1.62e-20 |
|
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: 86.02 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 402 PQVMLVCDTGNSTVRMIQAQIARKYPQLVMTRIVSLRDYEMLAHIDEDFVISNARIGEKNKPVVVMSPFPTDYQLEQLGK 481
Cdd:cd05568 1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELEEVDLDDYDLIISTVPLEDTDKPVIVVSPILTEEDIKKIRK 80
|
...
gi 672091835 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 |
3.56e-18 |
|
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: 79.60 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 301 ILSYINAHYNYNLQgDEQLRADLLTHIKTMITRVKYQINIPNPLLANIKQHYPMAYDVTLAAVSSWGKYTPYTLSENEIG 380
Cdd:pfam00874 3 IIELIEKKLGITFD-DDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEIG 81
|
....*..
gi 672091835 381 YLVLHIG 387
Cdd:pfam00874 82 YIALHFL 88
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
496-630 |
6.30e-18 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 80.71 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 496 FFDAEHFMVLNEPLTQAELFSRVCGQLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTLLAPQGV 575
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKEPV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 672091835 576 AWG--EGEVAHVIFLLAISKSDYEEAMAIYELFVTFVRERSMSRLLGSDSFDSFKAV 630
Cdd:pfam00359 81 DFGseDGKPVKLIFLLAAPDNEASHLKILSQLARLLQDEEFVEKLLKAKDPEEILEI 137
|
|
| PtsN |
COG1762 |
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ... |
492-630 |
1.96e-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: 76.81 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 492 MLEKFFDAEHFMVLNEPLTQAELFSRVCGQLEREGYVG--ADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTL 569
Cdd:COG1762 2 MLSDLLTPELILLDLEASSKEEAIEELAELLAEKGYVLdkEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672091835 570 LAPQGVAWG--EGEVAHVIFLLAISKSDYEEAMAIY-ELFVTFVRERSMSRLLGSDSFDSFKAV 630
Cdd:COG1762 82 RLKEPVDFGamDGEPVDLVFLLAAPEDDSEEHLKLLaELARLLSDEEFREKLLNAKSPEEILEL 145
|
|
| MtlA2 |
COG4668 |
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ... |
517-623 |
1.50e-15 |
|
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and metabolism];
Pssm-ID: 443705 [Multi-domain] Cd Length: 143 Bit Score: 74.04 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 517 RVCGQ-LEREGYVGADFYPSVVEREAIVSTLLGEGIALPHslGLLA-----KKTVVVTLLAPQGVAWGEGEVAHVIFLLA 590
Cdd:COG4668 23 RLAGQlLVEAGYVEPEYIDAMLEREAQVSTYLGNGIAIPH--GTNEakdlvLKTGISVLQFPDGVDWGDGNTVYLVIGIA 100
|
90 100 110
....*....|....*....|....*....|....
gi 672091835 591 iSKSDyeEAMAIY-ELFVTFVRERSMSRLLGSDS 623
Cdd:COG4668 101 -AKSD--EHLEILrQLARVLSDEENVEKLAKATD 131
|
|
| PRK11109 |
PRK11109 |
fused PTS fructose transporter subunit IIA/HPr protein; |
518-623 |
4.35e-10 |
|
fused PTS fructose transporter subunit IIA/HPr protein;
Pssm-ID: 236849 [Multi-domain] Cd Length: 375 Bit Score: 61.89 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 518 VCGQLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHslGL-----LAKKTVVVTLLAPQGVAWGEGEVAHVIFLLAiS 592
Cdd:PRK11109 25 VAAALTQAGNVAEGYVDGMLAREQQTSTFLGNGIAIPH--GTtdtrdLVLKTGVQVFQFPQGVTWGDGQTAYVAIGIA-A 101
|
90 100 110
....*....|....*....|....*....|.
gi 672091835 593 KSDyeEAMAIYelfvtfvreRSMSRLLGSDS 623
Cdd:PRK11109 102 KSD--EHLGLL---------RQLTHVLSDDS 121
|
|
| PRK09863 |
PRK09863 |
putative frv operon regulatory protein; Provisional |
14-627 |
7.67e-10 |
|
putative frv operon regulatory protein; Provisional
Pssm-ID: 182121 [Multi-domain] Cd Length: 584 Bit Score: 61.79 E-value: 7.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 14 DALQTETLPQDELAKRFAVSTRTVRADITALNEILDKyGARFVHSRGAGYRLQVDNAALFSALQHQERRKQatprsaqer 93
Cdd:PRK09863 11 DLLEQQDRSGGELAQQLGVSRRTIVRDIAYINFTLNG-KAIGSISGSAKYHLEILNRRSLFQLLQKSDNED--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 94 vHYLLVRFLTSAFsLKLEDLADEWFVSRGTLQNDMAEVRERLAHYqLTIETKPRYGMKLFGAEMAIRACLTDLLFQL-QL 172
Cdd:PRK09863 81 -RLLLLRLLLNTF-TPMAQLASALNLSRTWVAERLPRLNQRYERI-CCIASRPGLGHFIDETEEKRIDILANLIRKDpQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 173 ADAENPLLNN---------EILLQPQVAAFAGLLHPLLSQYAIR--LTDEGEQYlifycavalrrindgyplPDFEVEDg 241
Cdd:PRK09863 158 IPKAGPTRDNlqhlsrtacDNQHRWPLMQGDYLSSLILAIYALRnqLTDEWPQY------------------PGDEIKQ- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 242 deaVRQVSTRLAAELRAASGKEISMAEEAYLRVNIAARRVQDVQPTeinADdeealvDYILSYInahynynlqgDEQLRA 321
Cdd:PRK09863 219 ---IVEHSGLFLGDNAVRTLTGLIEKQHQQAQVISADNVQQLLQRV---PG------IASLNAI----------DTQLVE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 322 DLLTHI-------KTMITRVKYQINipnpllaNIKQHYPMAYDVTLAAVSSWGKYTPYTLSENEigYLVLHIGVGLERHy 394
Cdd:PRK09863 277 NIFGHLlrclafpVWIAEHRQSSIN-------NLKAQNPAAFDMALHFITLLREQLDIPLFDSD--LIALYFACALERH- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 395 nigyERHPQVMLVCDTGNSTVRMIQAQIARKYPQLVMTRIVSLRDYE-MLAHIDEDFVISNAR-IGEKNKPVVVMSPFP- 471
Cdd:PRK09863 347 ----QNERVPILLLADQNSIATINQLIIEQKVLNIRVIIVRSLSELEaIREEIEPLLIINNSHyLVDLQDAINFYITFKn 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 472 --TDYQLEQLGKLVlvdrTKPYM---LEKFFDAEHFmvLNEPLTQAELFSRV----CGQLEREGYVGADFYPSVVEREAI 542
Cdd:PRK09863 423 viTAAGIEQLKHLL----ATAYIrqnPERFLSAPGS--FHYSNVRGEKWQHVtrqiCAQLVAQHLLTADEAQRIIAREGA 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 543 VSTLLGEGIALPHSLGLLAK--KTVVVTLLAPQGVawgEGEVAHVIfLLAISKSDYEEAMAIYELFVTFVRERSMSRLLG 620
Cdd:PRK09863 497 GNQLILNHLSIPHCWTEQERryRGFAITLAQPIEV---NNEVIYLV-LIVLAAADAAHELKIFSYLYSVLCQHPAEVIAG 572
|
....*..
gi 672091835 621 SDSFDSF 627
Cdd:PRK09863 573 VTGYEAF 579
|
|
| PRK13779 |
PRK13779 |
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional |
522-630 |
8.99e-10 |
|
bifunctional PTS system fructose-specific transporter subunit IIA/HPr protein; Provisional
Pssm-ID: 237502 [Multi-domain] Cd Length: 503 Bit Score: 61.43 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 522 LEREGYVGADFYPSVVEREAIVSTLLGEGIALPH---SLGLLAKKTVVVTLLAPQGVAWGEGEVAHVIFLLAiSKSDyEE 598
Cdd:PRK13779 29 LEQAGNVENGYLQGMLARELQTSTFLGNGIAIPHgtlDTRHMVKNTGVQIFQFPQGIEWGEGNIAYVVIGIA-ARSD-EH 106
|
90 100 110
....*....|....*....|....*....|..
gi 672091835 599 AMAIYELFVTFVRERSMSRLLGSDSFDSFKAV 630
Cdd:PRK13779 107 LSLLRQLTHVLSDEDTAAKLATLTDVKEFRAI 138
|
|
| PTS_IIB |
cd00133 |
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ... |
404-483 |
1.50e-09 |
|
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: 54.95 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 404 VMLVCDTGNSTVRMIQAQIARKYPQLVMTRIVSLRDYEMLAHIDE-DFVISNARIGEK--NKPVVVMSPFPTDYQLEQLG 480
Cdd:cd00133 2 ILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVEAQGLSEVIDLADaDLIISTVPLAARflGKPVIVVSPLLNEKDGEKIL 81
|
...
gi 672091835 481 KLV 483
Cdd:cd00133 82 EKL 84
|
|
| PRK15083 |
PRK15083 |
PTS system mannitol-specific transporter subunit IICBA; Provisional |
521-581 |
7.61e-09 |
|
PTS system mannitol-specific transporter subunit IICBA; Provisional
Pssm-ID: 237905 [Multi-domain] Cd Length: 639 Bit Score: 58.53 E-value: 7.61e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672091835 521 QLEREGYVGADFYPSVVEREAIVSTLLGEGIALPHslGLLA-----KKTVVVTLLAPQGVAWGEGE 581
Cdd:PRK15083 521 QLVKGGYVEPEYVDAMLDREKLTSTYLGESIAVPH--GTVEakdrvLKTGVVFCQYPEGVRFGEEE 584
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
496-624 |
1.04e-08 |
|
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: 53.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 496 FFDAEHFMVLNEPLTQAELFSRVCGQLEREGYVG--ADFYPSVVEREAIVSTLLGEGIALPHSLGLLAKKTVVVTLLAPQ 573
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISdtEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 672091835 574 GVAWG--EGEVAHVIFLLAISKSdyEEAMAIYELFVTFvrersmSRLLGSDSF 624
Cdd:TIGR00848 81 GVDWQslDGKPVKLIFLIAVPKD--EAGNTHLKALSQL------ARLLLNDEF 125
|
|
| Mga |
pfam05043 |
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a ... |
91-167 |
1.59e-08 |
|
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: 52.23 E-value: 1.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672091835 91 QERVHYLLVRFLTSAFSLKLEDLADEWFVSRGTLQNDMAEVRERLAHYQLTIETKPrygMKLFGAEMAIRACLTDLL 167
Cdd:pfam05043 14 KESLKFQLLKYLFFEEFVSIKSLAQKLYISESTLYRKIKELNKLLKEFDLSIKKKN---LKLIGDEKQIRYFYALLF 87
|
|
| LevR |
COG3933 |
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]; |
297-384 |
1.65e-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: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 297 LVDYILSYINAHYNYNLqgDEQLRADLLTHIKTMITRVKYQINIPNPLLANIKQHYPMAYDVTLAAVSSWGKYTPYTLSE 376
Cdd:COG3933 460 VVEEILELAEKKLGRKF--SENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEIKELIEQELDIEIPE 537
|
....*...
gi 672091835 377 NEIGYLVL 384
Cdd:COG3933 538 DEVGFLTL 545
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
17-63 |
5.14e-06 |
|
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: 43.96 E-value: 5.14e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 672091835 17 QTETLPQDELAKRFAVSTRTVRADITALNEIldkyGARFVHSRGAGY 63
Cdd:pfam08279 10 ARGPISGQELAEKLGVSRRTIRRDIKILEEL----GVPIEAEPGRGY 52
|
|
| PRK09765 |
PRK09765 |
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional |
510-633 |
1.10e-04 |
|
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
Pssm-ID: 182066 [Multi-domain] Cd Length: 631 Bit Score: 45.11 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672091835 510 TQAELFSRVCGQLEREG--YVGADFYPSVVEREAIVSTLLGEGIALPH--SLGLLAKKTVVVTLLAPqgVAW---GEGEV 582
Cdd:PRK09765 20 SREEAIHALAQRLAALGkiSSTEQFLEEVYRRESLGPTALGEGLAVPHgkTAAVKEAAFAVATLSEP--LQWegvDGPEA 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 672091835 583 AHVIFLLAISKSdyeEAMAIY-----ELFVTFVRERSMSRLLGSDSFDSFKAvALD 633
Cdd:PRK09765 98 VDLIFLLAIPPN---EAGTTHmqlltALTTRLADDEIRARIQSATTPDELLS-ALD 149
|
|
| YobV |
COG2378 |
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains ... |
8-65 |
7.70e-04 |
|
Predicted DNA-binding transcriptional regulator YobV, contains HTH and WYL domains [Transcription];
Pssm-ID: 441945 [Multi-domain] Cd Length: 314 Bit Score: 41.99 E-value: 7.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672091835 8 RLAYLFDALQT-ETLPQDELAKRFAVSTRTVRADITALNEildkYGARFVHSRGA--GYRL 65
Cdd:COG2378 6 RLLALLQLLQSrRGVTAAELAERLEVSERTIYRDIDALRE----LGVPIEAERGRggGYRL 62
|
|
| PRK09772 |
PRK09772 |
transcriptional antiterminator BglG; Provisional |
323-386 |
6.85e-03 |
|
transcriptional antiterminator BglG; Provisional
Pssm-ID: 170086 [Multi-domain] Cd Length: 278 Bit Score: 38.92 E-value: 6.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672091835 323 LLTHIKTMITRVKYQINIPNPLLANIKQHYPMAYDVTLAAVSSWGKYTPYTLSENEIGYLVLHI 386
Cdd:PRK09772 98 LTDHCQFAIKRFQQNVLLPNPLLWDIQRLYPKEFQLGEEALTIIDKRLGVQLPKDEVGFIAMHL 161
|
|
| |
