|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
8-638 |
1.16e-71 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 243.23 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 8 IVLFLEHQNNWTTSKELSAEFQVSTRTIKKYISDI----SINYPNLIESSRQGYKIN-NSKLPIFRPALNQNPAIPQTPE 82
Cdd:COG3711 1 ILKILLKNNNVVTAKELAKKLNVSERTIRYDIKKInewlKKNGLEIISKKGIGFRLDiDDEQKEKLLQLLEKSEDPLSPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 83 ERMNYILKTLLIKKHSQNlanIYDFMDELYISESTFRADCQKINTICEKYNCSLQIVKDM-VSIDGSEKNKRKILNSYII 161
Cdd:COG3711 81 ERVAYILLRLLLAGDPIS---LDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYgIKLEGSELDIRKALAELLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 162 NESQNHFGDEQFLKSIFPNLDFALIKQTIQSTFEEHQYFINDFSLSNFVRHVAITINRIQNGCNEKSTDQQIDTT--TNE 239
Cdd:COG3711 158 ELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIkkPKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 240 YRISEDLTSKFASFFNISFTNTEIYELALLIICRGNSINETQSTKTEvatfvgDELIRFVTNICQNVKTLFAIDLDT-PE 318
Cdd:COG3711 238 YEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIIT------LEITKLIKEIINIIEEELGIDLDEdSL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 319 FIDRFSIHLHNLLIRNDNDLLNNNPLKNKIKMQCPFIYEVAVYIANQIQEQYKINLNDDEITYISFHIGGILELQKSLQs 398
Cdd:COG3711 312 LYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESK- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 399 KLSTILLIPEYYNLKKSLSTKIQNLFqDDLLILGIYTSIDHYLSYAQEHDLLLSSYSIDryiDKPNLYITPFLTEKDIKE 478
Cdd:COG3711 391 KKRVLVVCSSGIGTSRLLKSRLKKLF-PEIEIIDVISYRELEEIDLEDYDLIISTVPLE---DKPVIVVSPLLTEEDIEK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 479 IRNIINIVKQRKKKenrssyikkiFKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGNFAI 558
Cdd:COG3711 467 IRKFLKQIKKKLAK----------ILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVI 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 559 PHSLHINCLDTAIYVHIQEKPINWLNQYVNVVFLLSISDNDRTRFREIFEHITDTITSDDNLARIKKAKTYEELIDIFIN 638
Cdd:COG3711 537 AIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILL 616
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
502-636 |
2.91e-25 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 101.51 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 502 IFKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGN-FAIPHSLHINCLDTAIYVHIQEKPI 580
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNgIAIPHARSEAVKKPGIAVLTLKEPV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2601017576 581 NW---LNQYVNVVFLLSISDNDRTRFReIFEHITDTITSDDNLARIKKAKTYEELIDIF 636
Cdd:pfam00359 81 DFgseDGKPVKLIFLLAAPDNEASHLK-ILSQLARLLQDEEFVEKLLKAKDPEEILEIL 138
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
503-636 |
9.62e-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: 94.17 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 503 FKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGN-FAIPHSLHINCLDTAIYVHIQEKPIN 581
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNgIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2601017576 582 W---LNQYVNVVFLLSISDNDRTrfREIFEHITDTITSDDNLARIKKAKTYEELIDIF 636
Cdd:cd00211 81 FgslDGQPVHLIFLLAAPDSNEH--LKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
|
|
| PRK09765 |
PRK09765 |
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional |
499-635 |
1.15e-10 |
|
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
Pssm-ID: 182066 [Multi-domain] Cd Length: 631 Bit Score: 64.37 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 499 IKKIFKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSN--YVNEVKEREALSSTAFG-NFAIPHSLHINCLDTAIYVHI 575
Cdd:PRK09765 3 LTTLTHRDLLCLNARFTSREEAIHALAQRLAALGKISSTeqFLEEVYRRESLGPTALGeGLAVPHGKTAAVKEAAFAVAT 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2601017576 576 QEKPINWL----NQYVNVVFLLSISDNDR-TRFREIFEHITDTITSDDNLARIKKAKTYEELIDI 635
Cdd:PRK09765 83 LSEPLQWEgvdgPEAVDLIFLLAIPPNEAgTTHMQLLTALTTRLADDEIRARIQSATTPDELLSA 147
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| BglG |
COG3711 |
Transcriptional antiterminator [Transcription]; |
8-638 |
1.16e-71 |
|
Transcriptional antiterminator [Transcription];
Pssm-ID: 442925 [Multi-domain] Cd Length: 618 Bit Score: 243.23 E-value: 1.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 8 IVLFLEHQNNWTTSKELSAEFQVSTRTIKKYISDI----SINYPNLIESSRQGYKIN-NSKLPIFRPALNQNPAIPQTPE 82
Cdd:COG3711 1 ILKILLKNNNVVTAKELAKKLNVSERTIRYDIKKInewlKKNGLEIISKKGIGFRLDiDDEQKEKLLQLLEKSEDPLSPK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 83 ERMNYILKTLLIKKHSQNlanIYDFMDELYISESTFRADCQKINTICEKYNCSLQIVKDM-VSIDGSEKNKRKILNSYII 161
Cdd:COG3711 81 ERVAYILLRLLLAGDPIS---LDDLAEELFVSRSTILNDLKKIEKILKKYGLTLERKPNYgIKLEGSELDIRKALAELLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 162 NESQNHFGDEQFLKSIFPNLDFALIKQTIQSTFEEHQYFINDFSLSNFVRHVAITINRIQNGCNEKSTDQQIDTT--TNE 239
Cdd:COG3711 158 ELLSENDLLSLLLLKLIPEEDLELIEEIIEEAEKKLGIKLSDSIYINLTDHIAIAIKRIKKGKYIKLDNPLLWEIkkPKE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 240 YRISEDLTSKFASFFNISFTNTEIYELALLIICRGNSINETQSTKTEvatfvgDELIRFVTNICQNVKTLFAIDLDT-PE 318
Cdd:COG3711 238 YEIAKEILKLIEERLGISLPEDEIGYIALHLLGARLNNDNELSEIIT------LEITKLIKEIINIIEEELGIDLDEdSL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 319 FIDRFSIHLHNLLIRNDNDLLNNNPLKNKIKMQCPFIYEVAVYIANQIQEQYKINLNDDEITYISFHIGGILELQKSLQs 398
Cdd:COG3711 312 LYERLITHLKPAINRLKYGIPIRNPLLEEIKEKYPEAFELAKKIAKYLEKELGIEIPEDEIGYLTLHFGAALERQKESK- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 399 KLSTILLIPEYYNLKKSLSTKIQNLFqDDLLILGIYTSIDHYLSYAQEHDLLLSSYSIDryiDKPNLYITPFLTEKDIKE 478
Cdd:COG3711 391 KKRVLVVCSSGIGTSRLLKSRLKKLF-PEIEIIDVISYRELEEIDLEDYDLIISTVPLE---DKPVIVVSPLLTEEDIEK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 479 IRNIINIVKQRKKKenrssyikkiFKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGNFAI 558
Cdd:COG3711 467 IRKFLKQIKKKLAK----------ILFELLLLLLLLEEKEIIILLLLLLIEEALAADAIEELEEEEIEEELEEIIIIIVI 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 559 PHSLHINCLDTAIYVHIQEKPINWLNQYVNVVFLLSISDNDRTRFREIFEHITDTITSDDNLARIKKAKTYEELIDIFIN 638
Cdd:COG3711 537 AIPIIIIIIIAIIVLAAEEPGVIKLILVLLLLLILIILLEDDEALLVILLLLLLLIESSLLLLLLLELLLELELELLILL 616
|
|
| PtsN |
COG1762 |
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ... |
499-639 |
8.55e-26 |
|
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: 103.39 E-value: 8.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 499 IKKIFKKEFFSIDKTYADQSEAIEDICDILYQNKYVTS--NYVNEVKEREALSSTAFGN-FAIPHSLHINCLDTAIYVHI 575
Cdd:COG1762 3 LSDLLTPELILLDLEASSKEEAIEELAELLAEKGYVLDkeEYLEALLEREELGSTGIGPgIAIPHARPEGVKKPGIAVAR 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2601017576 576 QEKPINWL---NQYVNVVFLLSISDNDRTRFREIFEHITDTITSDDNLARIKKAKTYEELIDIFINA 639
Cdd:COG1762 83 LKEPVDFGamdGEPVDLVFLLAAPEDDSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKEA 149
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
502-636 |
2.91e-25 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 101.51 E-value: 2.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 502 IFKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGN-FAIPHSLHINCLDTAIYVHIQEKPI 580
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVEPAYLEAILEREKEGSTGIGNgIAIPHARSEAVKKPGIAVLTLKEPV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2601017576 581 NW---LNQYVNVVFLLSISDNDRTRFReIFEHITDTITSDDNLARIKKAKTYEELIDIF 636
Cdd:pfam00359 81 DFgseDGKPVKLIFLLAAPDNEASHLK-ILSQLARLLQDEEFVEKLLKAKDPEEILEIL 138
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
503-636 |
9.62e-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: 94.17 E-value: 9.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 503 FKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGN-FAIPHSLHINCLDTAIYVHIQEKPIN 581
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYVEEEYIEALLEREKEGSTGIGNgIAIPHAKSEAVKKPGIAVLRLKEPVD 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2601017576 582 W---LNQYVNVVFLLSISDNDRTrfREIFEHITDTITSDDNLARIKKAKTYEELIDIF 636
Cdd:cd00211 81 FgslDGQPVHLIFLLAAPDSNEH--LKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
|
|
| MtlA2 |
COG4668 |
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ... |
510-636 |
1.44e-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: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 510 IDKTYADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGNF-AIPHSL-----HIncLDTAIYVHIQEKPINWL 583
Cdd:COG4668 11 LNASAANKEEAIRLAGQLLVEAGYVEPEYIDAMLEREAQVSTYLGNGiAIPHGTneakdLV--LKTGISVLQFPDGVDWG 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2601017576 584 -NQYVNVVFLLSISDNDRTrfrEIFEHITDTITSDDNLARIKKAKTYEELIDIF 636
Cdd:COG4668 89 dGNTVYLVIGIAAKSDEHL---EILRQLARVLSDEENVEKLAKATDAEEILALL 139
|
|
| PRK09765 |
PRK09765 |
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional |
499-635 |
1.15e-10 |
|
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
Pssm-ID: 182066 [Multi-domain] Cd Length: 631 Bit Score: 64.37 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 499 IKKIFKKEFFSIDKTYADQSEAIEDICDILYQNKYVTSN--YVNEVKEREALSSTAFG-NFAIPHSLHINCLDTAIYVHI 575
Cdd:PRK09765 3 LTTLTHRDLLCLNARFTSREEAIHALAQRLAALGKISSTeqFLEEVYRRESLGPTALGeGLAVPHGKTAAVKEAAFAVAT 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2601017576 576 QEKPINWL----NQYVNVVFLLSISDNDR-TRFREIFEHITDTITSDDNLARIKKAKTYEELIDI 635
Cdd:PRK09765 83 LSEPLQWEgvdgPEAVDLIFLLAIPPNEAgTTHMQLLTALTTRLADDEIRARIQSATTPDELLSA 147
|
|
| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
300-388 |
4.66e-09 |
|
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: 53.80 E-value: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 300 TNICQNVKTLFAIDLDTPEFIDRFSIHLHNLLIRNDNDLLNNNPLKNKIKMQCPFIYEVAVYIANQIQEQYKINLNDDEI 379
Cdd:pfam00874 1 EEIIELIEKKLGITFDDDILYIRLILHLAFAIERIKEGITIENPLLEEIKEKYPKEFEIAKKILEILEEELGIELPEDEI 80
|
....*....
gi 2601017576 380 TYISFHIGG 388
Cdd:pfam00874 81 GYIALHFLS 89
|
|
| PRK09913 |
PRK09913 |
PTS fructose transporter subunit IIA; |
517-582 |
2.19e-05 |
|
PTS fructose transporter subunit IIA;
Pssm-ID: 182141 [Multi-domain] Cd Length: 148 Bit Score: 44.88 E-value: 2.19e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2601017576 517 QSEAIEDICDILYQNKYVT--SNYVNEVKEREALSSTAFGN-FAIPHSLHINCLDTAIYVHIQEKPINW 582
Cdd:PRK09913 18 AYSILKQLATIALQNGFITdsHQFLQTLLLREKMHSTGFGSgVAVPHGKSACVKQPFVLFARKAQAIDW 86
|
|
| PRK11109 |
PRK11109 |
fused PTS fructose transporter subunit IIA/HPr protein; |
515-635 |
2.14e-04 |
|
fused PTS fructose transporter subunit IIA/HPr protein;
Pssm-ID: 236849 [Multi-domain] Cd Length: 375 Bit Score: 44.17 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 515 ADQSEAIEDICDILYQNKYVTSNYVNEVKEREALSSTAFGN-FAIPH------SLhinCLDTAIYVHIQEKPINWLNQyv 587
Cdd:PRK11109 16 GNKEEAIRQVAAALTQAGNVAEGYVDGMLAREQQTSTFLGNgIAIPHgttdtrDL---VLKTGVQVFQFPQGVTWGDG-- 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2601017576 588 NVVFL-LSI---SDndrtrfreifEH--ITDTIT---SDDNLA-RIKKAKTYEELIDI 635
Cdd:PRK11109 91 QTAYVaIGIaakSD----------EHlgLLRQLThvlSDDSVAeQLKSATTAEELRAL 138
|
|
| PTS_IIB_bgl_like |
cd05568 |
PTS_IIB_bgl_like: the PTS (phosphotransferase system) IIB domain of a family of sensory ... |
416-484 |
3.78e-04 |
|
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: 39.79 E-value: 3.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2601017576 416 LSTKIQNLFQDdLLILGIYTSIDHYLSYAQEHDLLLSSYSIDrYIDKPNLYITPFLTEKDIKEIRNIIN 484
Cdd:cd05568 17 LKSKLKKLFPE-IEIIDVISLRELEEVDLDDYDLIISTVPLE-DTDKPVIVVSPILTEEDIKKIRKFIK 83
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
6-57 |
4.38e-04 |
|
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: 38.57 E-value: 4.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2601017576 6 NKIVLFLEHQNNWTTSKELSAEFQVSTRTIKKYISDI-SINYPnlIESSR-QGY 57
Cdd:pfam08279 1 LQILQLLLEARGPISGQELAEKLGVSRRTIRRDIKILeELGVP--IEAEPgRGY 52
|
|
| LevR |
COG3933 |
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription]; |
283-382 |
1.32e-03 |
|
Transcriptional regulatory protein LevR, contains PRD, AAA+ and EIIA domains [Transcription];
Pssm-ID: 443134 [Multi-domain] Cd Length: 916 Bit Score: 42.03 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2601017576 283 TKTEVATFVGDELIRFVTNICQNVKTLFAIDLDtPEFIDRFSIHLHNLLIRNDNDLLNNNPLKNKIKMQCPFIYEVAVYI 362
Cdd:COG3933 445 NKEELAKIVDEDIINVVEEILELAEKKLGRKFS-ENFIYALSLHLSSFIERIKEGKEIINPNLNEIKKKYPKEFKVAKEI 523
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90 100
....*....|....*....|
gi 2601017576 363 ANQIQEQYKINLNDDEITYI 382
Cdd:COG3933 524 KELIEQELDIEIPEDEVGFL 543
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| PTS_IIB |
cd00133 |
PTS_IIB: subunit IIB of enzyme II (EII) is the central energy-coupling domain of the ... |
416-483 |
6.78e-03 |
|
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: 36.08 E-value: 6.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2601017576 416 LSTKIQNLFQDdlliLGIYTSIDHY----LSYAQEHDLLLSSYSID-RYIDKPNLYITPFLTEKDIKEIRNII 483
Cdd:cd00133 16 LAEKLEKAAKE----LGIEVKVEAQglseVIDLADADLIISTVPLAaRFLGKPVIVVSPLLNEKDGEKILEKL 84
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| PRD |
pfam00874 |
PRD domain; The PRD domain (for PTS Regulation Domain), is the phosphorylatable regulatory ... |
200-271 |
9.10e-03 |
|
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: 35.69 E-value: 9.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2601017576 200 FINDFSLSNFVRHVAITINRIQNGCNEKSTDQQI--DTTTNEYRISEDLTSKFASFFNISFTNTEIYELALLII 271
Cdd:pfam00874 15 FDDDILYIRLILHLAFAIERIKEGITIENPLLEEikEKYPKEFEIAKKILEILEEELGIELPEDEIGYIALHFL 88
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