|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
8-623 |
5.13e-94 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 304.09 E-value: 5.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 8 ILREIVLNP-TIHGKELESIFGLSRRQLGYRIQKINLWLEQEGYPKLERTSQGnFIVSSEIMTLFKRdvseQQMLNGNNV 86
Cdd:COG3711 1 ILKILLKNNnVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIG-FRLDIDDEQKEKL----LQLLEKSED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 87 IFSIETRRYYLMLMLFSKENAMSLNHFSIDLQVSKNTVIHDINHVKEQLEDHGLSLKYSRKHGYEIVGDEFEVRRFFIKL 166
Cdd:COG3711 76 PLSPKERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 167 IDQRLNHDITKSEVLKALnLTFEDIAYQKDKIKQVEQFLKSRFIDKSLSSLPYVLCVIRRRIQSGHVMNPLNINYQYLRD 246
Cdd:COG3711 156 LSELLSENDLLSLLLLKL-IPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIKK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 247 TKEYQ-----ATEIMTQHEPDLPEAEKLYLTLHLLSTSVQWTDLQESDNISNLTMAIAQMIHHFEQITFINIEDKEKLSQ 321
Cdd:COG3711 235 PKEYEiakeiLKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 322 QLLLHLTPAFYRIKYNLTDRDELINPLQGNYQSLFHMVKQSCQSLTEYFGKSLPDNEIAYLTMLFGGSLRRQDENfdGKI 401
Cdd:COG3711 315 RLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES--KKK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 402 KAIIVCTQGTSVSQMMLYELRNLFPEIIFLDAISLRTFENYTL-DYDIVFSPMFvLTHKKLFITKVALSENEQRKLRKEV 480
Cdd:COG3711 393 RVLVVCSSGIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLeDYDLIISTVP-LEDKPVIVVSPLLTEEDIEKIRKFL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 481 MKYINKES--ADIDKEINKLMALIERTTTVNDITELRDGLEDFIANYNSISTINGSIVTQNKTLDLADLIPARHVKRMHH 558
Cdd:COG3711 472 KQIKKKLAkiLFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIVL 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586176591 559 VENIDEAIAKASDVLVANHFIDIKYIHEMQQVFDDSYMVIMQNIAIPHAYSEKHVHKTAMSMLIL 623
Cdd:COG3711 552 AAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILL 616
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
547-683 |
2.72e-26 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 104.59 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 547 LIPARHVKRMHHVENIDEAIAKASDVLVANHFIDIKYIHEMQQVFDDSYMVIMQNIAIPHAYSEkHVHKTAMSMLILQEP 626
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNGIAIPHARSE-AVKKPGIAVLTLKEP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 627 IY--MSDGTAIHIIVPIAAVDK-VTHLRALLQLRDVAQDNDAIKRIIQSRKNSDVNEILK 683
Cdd:pfam00359 80 VDfgSEDGKPVKLIFLLAAPDNeASHLKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
548-683 |
5.19e-24 |
|
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: 98.02 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 548 IPARHVKRMHHVENIDEAIAKASDVLVANHFIDIKYIHEMQQVFDDSYMVIMQNIAIPHAYSEkHVHKTAMSMLILQEPI 627
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSE-AVKKPGIAVLRLKEPV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 586176591 628 YMS--DGTAIHIIVPIAAVDKVTHLRALLQLRDVAQDNDAIKRIIQSrknSDVNEILK 683
Cdd:cd00211 80 DFGslDGQPVHLIFLLAAPDSNEHLKALSQLARLLSDEEFVEQLLNA---QSKEEILA 134
|
|
| PRK10372 |
PRK10372 |
PTS ascorbate transporter subunit IIA; |
542-684 |
1.65e-09 |
|
PTS ascorbate transporter subunit IIA;
Pssm-ID: 182417 [Multi-domain] Cd Length: 154 Bit Score: 56.91 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 542 LDLADLIPARHVKRMH-HVENIDEAIAKASDVLVANHFIDIKYiheMQQVFDD-----SYMVIMQNIAIPHAYSEKHVHK 615
Cdd:PRK10372 1 MKLRDSLAENKSIRLQaEAETWQEAVKIGVDLLVAADVVEPRY---YQAILDGveqfgPYFVIAPGLAMPHGRPEEGVKK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586176591 616 TAMSMLILQEPIYMS--DGTAIHIIVPIAAVDKVTHLR-ALLQLRDVAQDNDAIKRIIQSRKNSDVNEILKN 684
Cdd:PRK10372 78 TGFALVTLKKPLEFNheDNDPVDILITMAAVDANTHQEvGIMQIVNLFEDEANFDRLRACRTEQEVLDLIDR 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
8-623 |
5.13e-94 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 304.09 E-value: 5.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 8 ILREIVLNP-TIHGKELESIFGLSRRQLGYRIQKINLWLEQEGYPKLERTSQGnFIVSSEIMTLFKRdvseQQMLNGNNV 86
Cdd:COG3711 1 ILKILLKNNnVVTAKELAKKLNVSERTIRYDIKKINEWLKKNGLEIISKKGIG-FRLDIDDEQKEKL----LQLLEKSED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 87 IFSIETRRYYLMLMLFSKENAMSLNHFSIDLQVSKNTVIHDINHVKEQLEDHGLSLKYSRKHGYEIVGDEFEVRRFFIKL 166
Cdd:COG3711 76 PLSPKERVAYILLRLLLAGDPISLDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYGIKLEGSELDIRKALAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 167 IDQRLNHDITKSEVLKALnLTFEDIAYQKDKIKQVEQFLKSRFIDKSLSSLPYVLCVIRRRIQSGHVMNPLNINYQYLRD 246
Cdd:COG3711 156 LSELLSENDLLSLLLLKL-IPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIKK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 247 TKEYQ-----ATEIMTQHEPDLPEAEKLYLTLHLLSTSVQWTDLQESDNISNLTMAIAQMIHHFEQITFINIEDKEKLSQ 321
Cdd:COG3711 235 PKEYEiakeiLKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIITLEITKLIKEIINIIEEELGIDLDEDSLLYE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 322 QLLLHLTPAFYRIKYNLTDRDELINPLQGNYQSLFHMVKQSCQSLTEYFGKSLPDNEIAYLTMLFGGSLRRQDENfdGKI 401
Cdd:COG3711 315 RLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKES--KKK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 402 KAIIVCTQGTSVSQMMLYELRNLFPEIIFLDAISLRTFENYTL-DYDIVFSPMFvLTHKKLFITKVALSENEQRKLRKEV 480
Cdd:COG3711 393 RVLVVCSSGIGTSRLLKSRLKKLFPEIEIIDVISYRELEEIDLeDYDLIISTVP-LEDKPVIVVSPLLTEEDIEKIRKFL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 481 MKYINKES--ADIDKEINKLMALIERTTTVNDITELRDGLEDFIANYNSISTINGSIVTQNKTLDLADLIPARHVKRMHH 558
Cdd:COG3711 472 KQIKKKLAkiLFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVIAIPIIIIIIIAIIVL 551
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586176591 559 VENIDEAIAKASDVLVANHFIDIKYIHEMQQVFDDSYMVIMQNIAIPHAYSEKHVHKTAMSMLIL 623
Cdd:COG3711 552 AAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILL 616
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
547-683 |
2.72e-26 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 104.59 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 547 LIPARHVKRMHHVENIDEAIAKASDVLVANHFIDIKYIHEMQQVFDDSYMVIMQNIAIPHAYSEkHVHKTAMSMLILQEP 626
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNGIAIPHARSE-AVKKPGIAVLTLKEP 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 627 IY--MSDGTAIHIIVPIAAVDK-VTHLRALLQLRDVAQDNDAIKRIIQSRKNSDVNEILK 683
Cdd:pfam00359 80 VDfgSEDGKPVKLIFLLAAPDNeASHLKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
548-683 |
5.19e-24 |
|
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: 98.02 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 548 IPARHVKRMHHVENIDEAIAKASDVLVANHFIDIKYIHEMQQVFDDSYMVIMQNIAIPHAYSEkHVHKTAMSMLILQEPI 627
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNGIAIPHAKSE-AVKKPGIAVLRLKEPV 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 586176591 628 YMS--DGTAIHIIVPIAAVDKVTHLRALLQLRDVAQDNDAIKRIIQSrknSDVNEILK 683
Cdd:cd00211 80 DFGslDGQPVHLIFLLAAPDSNEHLKALSQLARLLSDEEFVEQLLNA---QSKEEILA 134
|
|
| PTS_IIB_bgl_like |
cd05568 |
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ... |
401-483 |
9.20e-17 |
|
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: 75.62 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 401 IKAIIVCTQGTSVSQMMLYELRNLFPEIIFLDAISLRTFENYTL-DYDIVFSPMFV-LTHKKLFITKVALSENEQRKLRK 478
Cdd:cd05568 1 KKALVVCPSGIGTSRLLKSKLKKLFPEIEIIDVISLRELEEVDLdDYDLIISTVPLeDTDKPVIVVSPILTEEDIKKIRK 80
|
....*
gi 586176591 479 EVMKY 483
Cdd:cd05568 81 FIKKL 85
|
|
| PtsN |
COG1762 |
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ... |
543-685 |
9.67e-17 |
|
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: 77.58 E-value: 9.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 543 DLADLIPARHVKRMHHVENIDEAIAKASDVLVANHFIDIK--YIHEMQQVFDDSYMVIMQNIAIPHAYSEkHVHKTAMSM 620
Cdd:COG1762 2 MLSDLLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKeeYLEALLEREELGSTGIGPGIAIPHARPE-GVKKPGIAV 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586176591 621 LILQEPIYMS--DGTAIHIIVPIAA--VDKVTHLRALLQLRDVAQDNDAIKRIIQSRKNSDVNEILKNY 685
Cdd:COG1762 81 ARLKEPVDFGamDGEPVDLVFLLAApeDDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKEA 149
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
300-389 |
8.10e-15 |
|
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: 70.36 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 300 QMIHHFEQITFINIEDkEKLSQQLLLHLTPAFYRIKYNLTDRDELINPLQGNYQSLFHMVKQSCQSLTEYFGKSLPDNEI 379
Cdd:pfam00874 2 EIIELIEKKLGITFDD-DILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80
|
90
....*....|
gi 586176591 380 AYLTMLFGGS 389
Cdd:pfam00874 81 GYIALHFLSA 90
|
|
| MtlA2 |
COG4668 |
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ... |
546-683 |
3.84e-14 |
|
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and metabolism];
Pssm-ID: 443705 [Multi-domain] Cd Length: 143 Bit Score: 69.80 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 546 DLIPARHVKRMHHVENIDEAIAKASDVLVANHFIDIKYIHEMQQVfDDSYMVIMQN-IAIPHAYSE--KHVHKTAMSMLI 622
Cdd:COG4668 2 LILTKENIRLNASAANKEEAIRLAGQLLVEAGYVEPEYIDAMLER-EAQVSTYLGNgIAIPHGTNEakDLVLKTGISVLQ 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586176591 623 LQEPIYMSDGTAIHIIVPIAAVDKvTHLRALLQLRDVAQDNDAIKRIIQSrknSDVNEILK 683
Cdd:COG4668 81 FPDGVDWGDGNTVYLVIGIAAKSD-EHLEILRQLARVLSDEENVEKLAKA---TDAEEILA 137
|
|
| PRK10372 |
PRK10372 |
PTS ascorbate transporter subunit IIA; |
542-684 |
1.65e-09 |
|
PTS ascorbate transporter subunit IIA;
Pssm-ID: 182417 [Multi-domain] Cd Length: 154 Bit Score: 56.91 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 542 LDLADLIPARHVKRMH-HVENIDEAIAKASDVLVANHFIDIKYiheMQQVFDD-----SYMVIMQNIAIPHAYSEKHVHK 615
Cdd:PRK10372 1 MKLRDSLAENKSIRLQaEAETWQEAVKIGVDLLVAADVVEPRY---YQAILDGveqfgPYFVIAPGLAMPHGRPEEGVKK 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586176591 616 TAMSMLILQEPIYMS--DGTAIHIIVPIAAVDKVTHLR-ALLQLRDVAQDNDAIKRIIQSRKNSDVNEILKN 684
Cdd:PRK10372 78 TGFALVTLKKPLEFNheDNDPVDILITMAAVDANTHQEvGIMQIVNLFEDEANFDRLRACRTEQEVLDLIDR 149
|
|
| cmtB |
PRK09854 |
PTS mannitol transporter subunit IIA; |
544-682 |
4.18e-09 |
|
PTS mannitol transporter subunit IIA;
Pssm-ID: 182114 [Multi-domain] Cd Length: 147 Bit Score: 55.77 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 544 LADLIPARHVKRMHHVENIDEAIAKASDVLVANHFIDIKYIHEMQQ--VFDDSYMVIMQNIAIPHAYSEKHVHKTAMSML 621
Cdd:PRK09854 3 LSDYFPESSISVIHSAKDWQEAIDFSMVSLLDKNYISENYIQAIKDstINNGPYYILAPGVAMPHARPECGALKTGMSLT 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586176591 622 ILQEPIYMSDG-TAIHIIVPIAAVDKVTHLRALLQLRDVAQDNDAIKRIIQSRKNSDVNEIL 682
Cdd:PRK09854 83 LLEQGVYFPGNdEPIKLLIGLSAADADSHIGAIQALSELLCEEEILEQLLTASSEKQLADII 144
|
|
| PRK11564 |
PRK11564 |
stationary phase inducible protein CsiE; Provisional |
87-390 |
1.23e-07 |
|
stationary phase inducible protein CsiE; Provisional
Pssm-ID: 236932 [Multi-domain] Cd Length: 426 Bit Score: 54.63 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 87 IFSIETRRYYLMLMLFSKENAMSLNHFSIDLQVSKNTVIHDINHV-KEQLEDHGLSLKYSRKHGYEIVGDEFEVR----- 160
Cdd:PRK11564 10 VLSAPQRRCQILLMLFQPGLTVTLETFSQLNGVDDDTARQDIAETgREIQRYHRLTLTTGADGSYRIEGTALDQRlcllh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 161 --RFFIKLIDQRLNHDIT---KSEvLKALNLtfEDIAYQKDKIKQVEQFLkSRFIDKSLSS---------LPYVLCVIRR 226
Cdd:PRK11564 90 wlRRGLRLCPSFITQQFTpalKSE-LKQRGI--ARNLYDDTNLQALINLC-SRRLNRQFEErdrqflqlyLQYCLLQHHA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 227 RIQSGhvMNPLNinYQYLRDTKEYQATEIMTQH-------EPDLPEAEKLYLTLHLLSTSVQWTDLQESDniSNLTMAIA 299
Cdd:PRK11564 166 GITPQ--FNPLQ--QQWLESKAEFQLAQEIGRHwqrrvlqPPPLDEPLFLALLFSMLRAPDPLRDAHQRD--RRLRQAIK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 300 QMIHHFEQITFINIEDKEKLSQQLLLHLTPAFYRIKYNLTDRDELINPLQGNYQSLFHMVKQSCQSLTEYFGKSLPDNEI 379
Cdd:PRK11564 240 RLVNRFRELGGVRFSDEQGLCDQLYTHLAQALERSLFAIGIDNTLPEEFARLYPRLLRTTRAALAGFEQEYGVHFSDEEV 319
|
330
....*....|.
gi 586176591 380 AYLTMLFGGSL 390
Cdd:PRK11564 320 GLVAVIFGAWL 330
|
|
| PTS_IIB |
cd00133 |
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ... |
402-480 |
6.82e-07 |
|
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: 47.64 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586176591 402 KAIIVCTQGTSVSQMMLYELRNLFPEIIFLDAISLRTFENYTL--DYDIVFSPMFV---LTHKKLFITKVALSENEQRKL 476
Cdd:cd00133 1 KILVVCGSGIGSSSMLAEKLEKAAKELGIEVKVEAQGLSEVIDlaDADLIISTVPLaarFLGKPVIVVSPLLNEKDGEKI 80
|
....
gi 586176591 477 RKEV 480
Cdd:cd00133 81 LEKL 84
|
|
| Mga |
pfam05043 |
Mga helix-turn-helix domain; M regulator protein trans-acting positive regulator (Mga) is a ... |
96-163 |
1.97e-03 |
|
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: 37.59 E-value: 1.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586176591 96 YLMLMLFSKENAMSLNHFSIDLQVSKNTVIHDINHVKEQLEDHGLSLkysRKHGYEIVGDEFEVRRFF 163
Cdd:pfam05043 19 FQLLKYLFFEEFVSIKSLAQKLYISESTLYRKIKELNKLLKEFDLSI---KKKNLKLIGDEKQIRYFY 83
|
|
| |
