|
Name |
Accession |
Description |
Interval |
E-value |
| PtsA |
COG1080 |
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate ... |
123-684 |
0e+00 |
|
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism];
Pssm-ID: 440698 [Multi-domain] Cd Length: 571 Bit Score: 669.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 123 VCSGSAGGILTPISSLDLNALGNLPAAKSVDAEQSALENGLTLV---LKNIEFRLLDSDGAT-SAILEAHRSLAGDTSLR 198
Cdd:COG1080 6 ASPGIAIGKAFLLREEDLEVPEYTISPEDVEAEIARLEAALAKAreeLEALREKAPEDLGEEeAAIFDAHLLLLEDPELI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 199 EHLLAGVSAGLSCAEAIVASA-NHFCEEFSRSSSSYLQERALDVRDVCFQLLQQIYGEQRfPAPGKLTQPAICMADELTP 277
Cdd:COG1080 86 EEVEELIREGRYNAEWALKEViEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGVEA-PDLSDLPEPVILVAHDLTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 278 SQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIYIDGNAGAIVVEPGEAVARYYQQEARV 357
Cdd:COG1080 165 SDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEYRERQAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 358 QDALREQQRVWLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESAN 437
Cdd:COG1080 245 YAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRAVAEAMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 438 GRSIIVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYEEYASLFTTQLRSILRASAHGSLKIMIPMISSMEEILWVKEK 517
Cdd:COG1080 325 GRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEELRQAKAL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 518 LAEAKQQLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRAL 597
Cdd:COG1080 405 LEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHPAVLRLI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 598 DYAVQAVHRQGKWIGLCGELGAK----------GsvlpllvglgLDELSMSAPSIPAAKARMAQLDSRECRKLLNQAMAC 667
Cdd:COG1080 485 KMVIDAAHKAGKPVGVCGEMAGDplatplllglG----------LDELSMSPSSIPAVKAIIRRLDLAEARALAEKALAL 554
|
570
....*....|....*..
gi 447096837 668 RTSLEVEHLLAQFRMTQ 684
Cdd:COG1080 555 DTAEEVRALLEEFLAEL 571
|
|
| PEP-utilizers_C |
pfam02896 |
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ... |
362-654 |
6.64e-147 |
|
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at the C terminus of a number of PEP (phosphoenolpyruvate)-utilizing proteins. In PPDK (Pyruvate phosphate dikinase) this C-terminal domain has been shown to be a PEP-binding domain.
Pssm-ID: 397163 [Multi-domain] Cd Length: 292 Bit Score: 433.66 E-value: 6.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 362 REQQRVWLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESANGRSI 441
Cdd:pfam02896 1 KAELGKLKDLPAPTADGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 442 IVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYEEYASLFTTQLRSILRASAHGSLKIMIPMISSMEEILWVKEKLAEA 521
Cdd:pfam02896 81 TVRTLDIGGDKELPYLEEPEEMNPFLGWRGIRIGLDRPELFRTQLRAILRASAFGNLRIMFPMVASVEELREAKAIIEEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 522 KQQLRNEhIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRALDYAV 601
Cdd:pfam02896 161 KEELDAE-VGFDKDIKVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447096837 602 QAVHRQGKWIGLCGELGAKGSVLPLLVGLGLDELSMSAPSIPAAKARMAQLDS 654
Cdd:pfam02896 240 RAAHRHGKWVGICGEMAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQIDR 292
|
|
| PTS_I_fam |
TIGR01417 |
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ... |
183-677 |
2.33e-133 |
|
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homolog of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homolog designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport.
Pssm-ID: 273611 [Multi-domain] Cd Length: 565 Bit Score: 409.18 E-value: 2.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 183 AILEAHRSLAGDTSLREHLLAGVSAGLSCAEAIVASA-NHFCEEFSRSSSSYLQERALDVRDVCFQLLQQIYGeQRFPAP 261
Cdd:TIGR01417 70 AIFEAHILILEDPELTEEVIELIKKDHKNAEFAAHEVfEGQAKSLEEMDDEYLKERAADIRDIGNRLLGHLLG-VKISDL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 262 GKLTQPAICMADELTPSQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIYIDGNAGAIVV 341
Cdd:TIGR01417 149 SEIQDEVILVAEDLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQVKNGDTVIIDGVKGIVIF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 342 EPGEAVARYYQQEARVQDALREQQRVWLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPG 421
Cdd:TIGR01417 229 NPSSETIDKYEAKQEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 422 ESELYNIFCQALESANGRSIIVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYEEYASLFTTQLRSILRASAHGSLKIM 501
Cdd:TIGR01417 309 EEEQFAAYKTVLEAMESDAVIVRTLDIGGDKELPYLNFPKEENPFLGYRAIRLALEREEILRTQLRAILRASAYGKLRIM 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 502 IPMISSMEEILWVKEKLAEAKQQLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAK 581
Cdd:TIGR01417 389 FPMVATVEEIRAVKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDL 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 582 VTRHYNSLNPAFLRALDYAVQAVHRQGKWIGLCGELGAKGSVLPLLVGLGLDELSMSAPSIPAAKARMAQLDSRECRKLL 661
Cdd:TIGR01417 469 ISNLYQPYNPAVLRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLA 548
|
490
....*....|....*.
gi 447096837 662 NQAMACRTSLEVEHLL 677
Cdd:TIGR01417 549 EKALAQPTTEEVHKLV 564
|
|
| PRK11177 |
PRK11177 |
phosphoenolpyruvate-protein phosphotransferase PtsI; |
182-680 |
1.78e-128 |
|
phosphoenolpyruvate-protein phosphotransferase PtsI;
Pssm-ID: 183017 [Multi-domain] Cd Length: 575 Bit Score: 396.69 E-value: 1.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 182 SAILEAHRSLAGDTSLREHLLAGVSAGLSCAEAIVASAnhfCEEFSRSSSS----YLQERALDVRDVCFQLLQQIYGeqr 257
Cdd:PRK11177 70 EAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHSV---IEGQAKALEElddeYLKERAADVRDIGKRLLKNILG--- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 258 fpAP----GKLTQPAICMADELTPSQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVD-------------ID 320
Cdd:PRK11177 144 --LKiidlSAIQEEVILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTGnitkqvkngdyliLD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 321 ALtpwqQQTIYIdgNAGAIVVEPGEAVARYYQQE----ARVQDAlreqqrvwltqQARTADGIRIEIAANIAHSVEAQAA 396
Cdd:PRK11177 222 AV----NNQIYV--NPTNEVIEELKAVQEQYASEkaelAKLKDL-----------PAITLDGHQVEVCANIGTVRDVEGA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 397 FGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESANGRSIIVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYE 476
Cdd:PRK11177 285 ERNGAEGVGLYRTEFLFMDRDALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLPKEENPFLGWRAIRIAM 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 477 EYASLFTTQLRSILRASAHGSLKIMIPMISSMEEILWVKEKLAEAKQQLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCE 556
Cdd:PRK11177 365 DRKEILHDQLRAILRASAFGKLRIMFPMIISVEEVRELKAEIEILKQELRDEGKAFDESIEIGVMVETPAAAVIARHLAK 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 557 EIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRALDYAVQAVHRQGKWIGLCGELGAKGSVLPLLVGLGLDELS 636
Cdd:PRK11177 445 EVDFFSIGTNDLTQYTLAVDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFS 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 447096837 637 MSAPSIPAAKARMAQLDSRECRKLLNQAMACRTSLEVEHLLAQF 680
Cdd:PRK11177 525 MSAISIPRIKKIIRNTNFEDAKALAEQALAQPTADELMTLVNKF 568
|
|
| PtsN |
COG1762 |
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ... |
687-831 |
4.60e-36 |
|
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: 133.05 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 687 APLVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARL 766
Cdd:COG1762 4 SDLLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVARL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447096837 767 QAPVRWG---DDEAQFIIMLTLNKHaAGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHEL 831
Cdd:COG1762 84 KEPVDFGamdGEPVDLVFLLAAPED-DSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKEAE 150
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
689-828 |
1.98e-34 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 128.09 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 689 LVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRypRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQA 768
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVE--PAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447096837 769 PVRWGD---DEAQFIIMLTLNKHAAGdqHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQ 828
Cdd:pfam00359 79 PVDFGSedgKPVKLIFLLAAPDNEAS--HLKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
690-827 |
1.52e-33 |
|
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: 125.37 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 690 VTAECITLESDWRSKEEVLKGMTDNLLLAGRCryPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQAP 769
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYV--EEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447096837 770 VRWGD---DEAQFIIMLTLNKhaaGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLL 827
Cdd:cd00211 79 VDFGSldgQPVHLIFLLAAPD---SNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
689-814 |
2.67e-28 |
|
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: 110.44 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 689 LVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQA 768
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 447096837 769 PVRWG--DDEA-QFIIMLTLNKHAAGDQHMRIFSRLARRIMHEEFRNAL 814
Cdd:TIGR00848 81 GVDWQslDGKPvKLIFLIAVPKDEAGNTHLKALSQLARLLLNDEFRAKL 129
|
|
| PTS-HPr_like |
cd00367 |
Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of ... |
6-84 |
3.77e-19 |
|
Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of the bacterial phosphoenolpyruvate sugar phosphotransferase system (PTS). The PTS catalyses the phosphorylation of sugar substrates during their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate is transferred to HPr by enzyme I (EI). Phospho-HPr then transfers the phosphoryl group to one of several sugar-specific phosphoprotein intermediates. The conserved histidine in the N-terminus of HPr serves as an acceptor for the phosphoryl group of EI. In addition to the phosphotransferase proteins HPr and E1, this family also includes the closely related Carbon Catabolite Repressor (CCR) proteins which use the same phosphorylation mechanism and interact with transcriptional regulators to control expression of genes coding for utilization of less favored carbon sources.
Pssm-ID: 238217 [Multi-domain] Cd Length: 77 Bit Score: 82.17 E-value: 3.77e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447096837 6 EFICELPNGVHARPASHVETLCNTFSSQIEWHNLrtDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWL 84
Cdd:cd00367 1 TVTITNPLGLHARPAALLVQLASKFKSDITLRKG--GRKANAKSILGLMSLGAKQGDEITLSAEGEDAEEALEALAELL 77
|
|
| PtsH |
COG1925 |
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ... |
6-88 |
3.48e-17 |
|
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport and metabolism];
Pssm-ID: 441528 [Multi-domain] Cd Length: 88 Bit Score: 77.07 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 6 EFICELPNGVHARPASHVETLCNTFSSQIEWHNlrTDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWLR 85
Cdd:COG1925 5 EVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALAALIE 82
|
...
gi 447096837 86 DEF 88
Cdd:COG1925 83 SGF 85
|
|
| PRK09765 |
PRK09765 |
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional |
695-830 |
9.39e-17 |
|
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
Pssm-ID: 182066 [Multi-domain] Cd Length: 631 Bit Score: 84.79 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 695 ITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQAPVRW-- 772
Cdd:PRK09765 12 LCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWeg 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 773 --GDDEAQFIIMLTLNKHAAGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHE 830
Cdd:PRK09765 92 vdGPEAVDLIFLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDK 151
|
|
| PTS-HPr |
pfam00381 |
PTS HPr component phosphorylation site; |
6-85 |
2.00e-13 |
|
PTS HPr component phosphorylation site;
Pssm-ID: 459792 [Multi-domain] Cd Length: 79 Bit Score: 66.25 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 6 EFICELPNGVHARPASHVETLCNTFSSQIEWHNLrtDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWLR 85
Cdd:pfam00381 2 TVTITNPLGLHARPAALLVQLASKFDSDITLEKG--GKKVNAKSIMGLMSLGAKQGDEITISAEGEDEEEALEALAALLE 79
|
|
| PTS_HPr_family |
TIGR01003 |
Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains ... |
12-82 |
3.46e-05 |
|
Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains of proteins) which function in phosphoryl transfer system (PTS) systems. They include energy-coupling components which catalyze sugar uptake via a group translocation mechanism. The functions of most of these proteins are not known, but they presumably function in PTS-related regulatory capacities. All seed members are stand-alone HPr proteins, although the model also recognizes HPr domains of PTS fusion proteins. This family includes the related NPr protein. [Signal transduction, PTS]
Pssm-ID: 273389 [Multi-domain] Cd Length: 82 Bit Score: 43.02 E-value: 3.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447096837 12 PNGVHARPASHVETLCNTFSSQIewHNLRTDRKGNAKSALALIgtdTLA---GDNCQLLISGADEQEAHQRLSQ 82
Cdd:TIGR01003 11 KVGLHARPAAILVKLASGFDSEI--TLTKNGKEVNAKSIMGIM---MLGagqGTEVTVSADGEDEAEALEALAK 79
|
|
| PRK13782 |
PRK13782 |
HPr family phosphocarrier protein; |
10-84 |
6.47e-05 |
|
HPr family phosphocarrier protein;
Pssm-ID: 172320 [Multi-domain] Cd Length: 82 Bit Score: 42.08 E-value: 6.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447096837 10 ELPNGVHARPASHVETLCNTFSSQIEWHnlRTDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWL 84
Cdd:PRK13782 9 SLKTGLQARPAALFVQEANRFHADIFIE--KDGKKVNAKSIMGLMSLAIGTGSMITIITEGSDEEEALEALAAYV 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PtsA |
COG1080 |
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate ... |
123-684 |
0e+00 |
|
Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism];
Pssm-ID: 440698 [Multi-domain] Cd Length: 571 Bit Score: 669.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 123 VCSGSAGGILTPISSLDLNALGNLPAAKSVDAEQSALENGLTLV---LKNIEFRLLDSDGAT-SAILEAHRSLAGDTSLR 198
Cdd:COG1080 6 ASPGIAIGKAFLLREEDLEVPEYTISPEDVEAEIARLEAALAKAreeLEALREKAPEDLGEEeAAIFDAHLLLLEDPELI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 199 EHLLAGVSAGLSCAEAIVASA-NHFCEEFSRSSSSYLQERALDVRDVCFQLLQQIYGEQRfPAPGKLTQPAICMADELTP 277
Cdd:COG1080 86 EEVEELIREGRYNAEWALKEViEELAAQFEALDDEYLRERAADIRDVGRRVLRNLLGVEA-PDLSDLPEPVILVAHDLTP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 278 SQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIYIDGNAGAIVVEPGEAVARYYQQEARV 357
Cdd:COG1080 165 SDTAQLDPSRVAGFVTDLGGRTSHTAILARSLGIPAVVGLGDALLLVKDGDLVIVDGDAGVVIVNPDEETLAEYRERQAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 358 QDALREQQRVWLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESAN 437
Cdd:COG1080 245 YAAERAELARLRDLPAVTLDGVRVELAANIGLPEDAAAALENGAEGVGLFRTEFLFMDRDDLPTEEEQFEAYRAVAEAMG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 438 GRSIIVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYEEYASLFTTQLRSILRASAHGSLKIMIPMISSMEEILWVKEK 517
Cdd:COG1080 325 GRPVTIRTLDIGGDKPLPYLPLPKEENPFLGLRAIRLCLDRPELFRTQLRAILRASAHGNLRIMFPMISSVEELRQAKAL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 518 LAEAKQQLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRAL 597
Cdd:COG1080 405 LEEAKAELRAEGIPFDEDIPVGIMIEVPAAALIADQLAKEVDFFSIGTNDLIQYTLAVDRGNEKVAYLYDPLHPAVLRLI 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 598 DYAVQAVHRQGKWIGLCGELGAK----------GsvlpllvglgLDELSMSAPSIPAAKARMAQLDSRECRKLLNQAMAC 667
Cdd:COG1080 485 KMVIDAAHKAGKPVGVCGEMAGDplatplllglG----------LDELSMSPSSIPAVKAIIRRLDLAEARALAEKALAL 554
|
570
....*....|....*..
gi 447096837 668 RTSLEVEHLLAQFRMTQ 684
Cdd:COG1080 555 DTAEEVRALLEEFLAEL 571
|
|
| PEP-utilizers_C |
pfam02896 |
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at ... |
362-654 |
6.64e-147 |
|
PEP-utilizing enzyme, PEP-binding domain; This entry represents a TIM barrel domain found at the C terminus of a number of PEP (phosphoenolpyruvate)-utilizing proteins. In PPDK (Pyruvate phosphate dikinase) this C-terminal domain has been shown to be a PEP-binding domain.
Pssm-ID: 397163 [Multi-domain] Cd Length: 292 Bit Score: 433.66 E-value: 6.64e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 362 REQQRVWLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESANGRSI 441
Cdd:pfam02896 1 KAELGKLKDLPAPTADGTKIKVAANIGTPDDAEAALANGAEGIGLYRTEFLFMDRDELPTEDEQFEAYKGVLEAMNGRPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 442 IVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYEEYASLFTTQLRSILRASAHGSLKIMIPMISSMEEILWVKEKLAEA 521
Cdd:pfam02896 81 TVRTLDIGGDKELPYLEEPEEMNPFLGWRGIRIGLDRPELFRTQLRAILRASAFGNLRIMFPMVASVEELREAKAIIEEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 522 KQQLRNEhIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRALDYAV 601
Cdd:pfam02896 161 KEELDAE-VGFDKDIKVGIMIEVPSAALLADQLAKEVDFFSIGTNDLTQYTLAVDRDNERVAYLYDPLHPAVLRLIKEVI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 447096837 602 QAVHRQGKWIGLCGELGAKGSVLPLLVGLGLDELSMSAPSIPAAKARMAQLDS 654
Cdd:pfam02896 240 RAAHRHGKWVGICGEMAGDPSAVPLLVGLGLDEFSMSPDSVPRARALLAQIDR 292
|
|
| PTS_I_fam |
TIGR01417 |
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of ... |
183-677 |
2.33e-133 |
|
phosphoenolpyruvate-protein phosphotransferase; This model recognizes a distinct clade of phophoenolpyruvate (PEP)-dependent enzymes. Most members are known or deduced to function as the phosphoenolpyruvate-protein phosphotransferase (or enzyme I) of PTS sugar transport systems. However, some species with both a member of this family and a homolog of the phosphocarrier protein HPr lack a IIC component able to serve as a permease. An HPr homolog designated NPr has been implicated in the regulation of nitrogen assimilation, which demonstrates that not all phosphotransferase system components are associated directly with PTS transport.
Pssm-ID: 273611 [Multi-domain] Cd Length: 565 Bit Score: 409.18 E-value: 2.33e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 183 AILEAHRSLAGDTSLREHLLAGVSAGLSCAEAIVASA-NHFCEEFSRSSSSYLQERALDVRDVCFQLLQQIYGeQRFPAP 261
Cdd:TIGR01417 70 AIFEAHILILEDPELTEEVIELIKKDHKNAEFAAHEVfEGQAKSLEEMDDEYLKERAADIRDIGNRLLGHLLG-VKISDL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 262 GKLTQPAICMADELTPSQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIYIDGNAGAIVV 341
Cdd:TIGR01417 149 SEIQDEVILVAEDLTPSETAQLNLKYVKGFLTDAGGKTSHTAIMARSLEIPAIVGTKSVTSQVKNGDTVIIDGVKGIVIF 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 342 EPGEAVARYYQQEARVQDALREQQRVWLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPG 421
Cdd:TIGR01417 229 NPSSETIDKYEAKQEAVSSEKAELAKLKDKPAITLDGHQVELAANIGTVDDVEGAERNGGEGIGLFRTEFLYMSRDQLPT 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 422 ESELYNIFCQALESANGRSIIVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYEEYASLFTTQLRSILRASAHGSLKIM 501
Cdd:TIGR01417 309 EEEQFAAYKTVLEAMESDAVIVRTLDIGGDKELPYLNFPKEENPFLGYRAIRLALEREEILRTQLRAILRASAYGKLRIM 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 502 IPMISSMEEILWVKEKLAEAKQQLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAK 581
Cdd:TIGR01417 389 FPMVATVEEIRAVKQELEEEKQELNDEGKAFDENIEVGVMIEIPSAALIADHLAKEVDFFSIGTNDLTQYTLAVDRGNDL 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 582 VTRHYNSLNPAFLRALDYAVQAVHRQGKWIGLCGELGAKGSVLPLLVGLGLDELSMSAPSIPAAKARMAQLDSRECRKLL 661
Cdd:TIGR01417 469 ISNLYQPYNPAVLRLIKLVIDAAKAEGIWVGMCGEMAGDERAIPLLLGLGLRELSMSASSILRIKMIIRKLNIEECKSLA 548
|
490
....*....|....*.
gi 447096837 662 NQAMACRTSLEVEHLL 677
Cdd:TIGR01417 549 EKALAQPTTEEVHKLV 564
|
|
| PRK11177 |
PRK11177 |
phosphoenolpyruvate-protein phosphotransferase PtsI; |
182-680 |
1.78e-128 |
|
phosphoenolpyruvate-protein phosphotransferase PtsI;
Pssm-ID: 183017 [Multi-domain] Cd Length: 575 Bit Score: 396.69 E-value: 1.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 182 SAILEAHRSLAGDTSLREHLLAGVSAGLSCAEAIVASAnhfCEEFSRSSSS----YLQERALDVRDVCFQLLQQIYGeqr 257
Cdd:PRK11177 70 EAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHSV---IEGQAKALEElddeYLKERAADVRDIGKRLLKNILG--- 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 258 fpAP----GKLTQPAICMADELTPSQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVD-------------ID 320
Cdd:PRK11177 144 --LKiidlSAIQEEVILVAADLTPSETAQLNLKKVLGFITDIGGRTSHTSIMARSLELPAIVGTGnitkqvkngdyliLD 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 321 ALtpwqQQTIYIdgNAGAIVVEPGEAVARYYQQE----ARVQDAlreqqrvwltqQARTADGIRIEIAANIAHSVEAQAA 396
Cdd:PRK11177 222 AV----NNQIYV--NPTNEVIEELKAVQEQYASEkaelAKLKDL-----------PAITLDGHQVEVCANIGTVRDVEGA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 397 FGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESANGRSIIVRTMDIGGDKPVDYLNIPAEANPFLGYRAVRIYE 476
Cdd:PRK11177 285 ERNGAEGVGLYRTEFLFMDRDALPTEEEQFQAYKAVAEAMGSQAVIVRTMDIGGDKELPYMNLPKEENPFLGWRAIRIAM 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 477 EYASLFTTQLRSILRASAHGSLKIMIPMISSMEEILWVKEKLAEAKQQLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCE 556
Cdd:PRK11177 365 DRKEILHDQLRAILRASAFGKLRIMFPMIISVEEVRELKAEIEILKQELRDEGKAFDESIEIGVMVETPAAAVIARHLAK 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 557 EIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRALDYAVQAVHRQGKWIGLCGELGAKGSVLPLLVGLGLDELS 636
Cdd:PRK11177 445 EVDFFSIGTNDLTQYTLAVDRGNELISHLYNPMSPSVLNLIKQVIDASHAEGKWTGMCGELAGDERATLLLLGMGLDEFS 524
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 447096837 637 MSAPSIPAAKARMAQLDSRECRKLLNQAMACRTSLEVEHLLAQF 680
Cdd:PRK11177 525 MSAISIPRIKKIIRNTNFEDAKALAEQALAQPTADELMTLVNKF 568
|
|
| PRK11061 |
PRK11061 |
phosphoenolpyruvate--protein phosphotransferase; |
134-686 |
2.32e-102 |
|
phosphoenolpyruvate--protein phosphotransferase;
Pssm-ID: 182937 [Multi-domain] Cd Length: 748 Bit Score: 333.50 E-value: 2.32e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 134 PISSLDlnalgnlpaaksVDAEQSALENGLTLVLKniEFRLL------DSDGATSAILEAHRSLAGDTSLREHLLAGVSA 207
Cdd:PRK11061 199 PASTLD------------PALERERLTGALEEAAN--EFRRYskrfaaGAQKETAAIFDLYSHLLNDPRLRRELFAEVDK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 208 GLSCAEAIVASANHFCEEFSRSSSSYLQERALDVRDVCFQLLQQIYGEQRFPApgKLTQPAICMADELTPSQFLELDKNH 287
Cdd:PRK11061 265 GSVAEWAVKQVIEKFAEQFAALSDNYLRERAGDLRALGQRLLFHLDDSEQGPN--AWPERFILVADELTATLLAELPQDR 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 288 LKGLLLKSGGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIyIDGNAGAIVVEPGEAVARYYQQ---EARVQDALREQ 364
Cdd:PRK11061 343 LAGVVVRDGAANSHAAILVRALGIPTVMGADIQPSLLHQRLLI-VDGYRGELLVDPEPVLLQEYQRlisEEIELSRLAED 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 365 QrvwLTQQARTADGIRIEIAANIAHSVEAQAAFGNGAEGVGLFRTEMLYMDRTSAPGESELYNIFCQALESANGRSIIVR 444
Cdd:PRK11061 422 D---VNLPAQLKSGERIKVMLNAGLSAEHEEKLGSRVDGVGLYRTEIPFMLQSGFPSEEEQVAQYQGMLQMFPDKPVTLR 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 445 TMDIGGDKPVDYLNIpAEANPFLGYRAVRIYEEYASLFTTQLRSILRASA-HGSLKIMIPMISSMEEILWVKEKLAEAKQ 523
Cdd:PRK11061 499 TLDIGADKQLPYMPI-SEENPCLGWRGIRITLDQPEIFLIQVRAMLRANAaTGNLSILLPMVTSIDEVDEARRLIDRAGR 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 524 QLRNEHIPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQYLLAVDRDNAKVTRHYNSLNPAFLRALDYAVQA 603
Cdd:PRK11061 578 EVEEMLGYEIPKPRIGIMIEVPSMVFMLPHLASRVDFISVGTNDLTQYLLAVDRNNTRVASLYDSLHPAMLRALKMIADE 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 604 VHRQGKWIGLCGELGAKGSVLPLLVGLGLDELSMSAPSIPAAKARMAQLDSRECRKLLNQAMACRTSLEVEHLLAQFrMT 683
Cdd:PRK11061 658 AEQHGLPVSLCGEMAGDPMGALLLIGLGYRHLSMNGRSVARVKYLLRHIDLAEAENLAQRSLEAQLATEVRHQVAAF-ME 736
|
...
gi 447096837 684 QQD 686
Cdd:PRK11061 737 RRG 739
|
|
| PRK06464 |
PRK06464 |
phosphoenolpyruvate synthase; Validated |
296-615 |
1.23e-41 |
|
phosphoenolpyruvate synthase; Validated
Pssm-ID: 235809 [Multi-domain] Cd Length: 795 Bit Score: 163.76 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 296 GGTTSHTVILARSFNIPTLVGVDiDA---LTPWQQQTIYI-DGNAGaiVVEPGEAVAryyqqearvqdalrEQQRVWLTQ 371
Cdd:PRK06464 413 GGRTCHAAIIARELGIPAVVGTG-NAtevLKDGQEVTVSCaEGDTG--YVYEGLLEF--------------EVEEVSLEE 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 372 QARTAdgirIEIAANIAHSVEAQAAFGNGAEGVGLFRTEM----------LYMDRTSAPGESELYNIFCQALESANG--- 438
Cdd:PRK06464 476 MPETP----TKIMMNVGNPERAFDFAALPNDGVGLARLEFiinnmigvhpLALLEFDQQDADLKAEIEELTAGYASPeef 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 439 ------------------RSIIVRTMD---------IGGDkpvDYLniPAEANPFLGYRAVRIY--EEYASLFTTQLRSI 489
Cdd:PRK06464 552 yvdklaegiatvaaafypKPVIVRLSDfksneyanlIGGE---RYE--PEEENPMLGFRGASRYlsESFREAFALECEAI 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 490 LRA-SAHG--SLKIMIPMISSMEEILWVKEKLAEakQQLRnehiPFDEKIQLGIMLEVPSVMFIIDQCCEEIDFFSIGSN 566
Cdd:PRK06464 627 KRVrEEMGltNVEVMIPFVRTVEEAEKVIELLAE--NGLK----RGENGLKVIMMCEIPSNALLAEEFLEYFDGFSIGSN 700
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 447096837 567 DLTQYLLAVDRDNAKVTRHYNSLNPAFLRALDYAVQAVHRQGKWIGLCG 615
Cdd:PRK06464 701 DLTQLTLGLDRDSGLVAHLFDERNPAVKKLISMAIKAAKKAGKYVGICG 749
|
|
| PEP_synth |
TIGR01418 |
phosphoenolpyruvate synthase; Also called pyruvate,water dikinase and PEP synthase. The member ... |
296-616 |
6.44e-41 |
|
phosphoenolpyruvate synthase; Also called pyruvate,water dikinase and PEP synthase. The member from Methanococcus jannaschii contains a large intein. This enzyme generates phosphoenolpyruvate (PEP) from pyruvate, hydrolyzing ATP to AMP and releasing inorganic phosphate in the process. The enzyme shows extensive homology to other enzymes that use PEP as substrate or product. This enzyme may provide PEP for gluconeogenesis, for PTS-type carbohydrate transport systems, or for other processes. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273612 [Multi-domain] Cd Length: 786 Bit Score: 161.44 E-value: 6.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 296 GGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIYIDGNAGAI-VVEPGEAvaRYyqqearvqdalrEQQRVWLTQQAR 374
Cdd:TIGR01418 412 GGMTCHAAIVARELGIPAVVGTGDATKTLKDGMEVTVDCAEGDTgYVYAGKL--EH------------EVKEVELSNMPV 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 375 TAdgirIEIAANIAHSVEAQAAFGNGAEGVGLFRTEM-------------LYMDRTSAPGESELYNI--------FCQAL 433
Cdd:TIGR01418 478 TA----TKIYMNVGNPEVAFRFAALPNDGVGLARIEFiilnwigkhplalIDDDDLESVEKNEIEELmagnprdfFVDKL 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 434 esANG----------RSIIVRTMDIggdKPVDYLNI-------PAEANPFLGYRAVRIY--EEYASLFTTQLRSILRASA 494
Cdd:TIGR01418 554 --AEGiakvaaafypKPVIVRTSDF---KSNEYRNLiggeeyePDEENPMLGWRGASRYysESYEEAFRLECRAIKRVRE 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 495 HGSLK---IMIPMISSMEEilwvkekLAEAKQQLRNEHIPFDEK-IQLGIMLEVPSVMFIIDQCCEEIDFFSIGSNDLTQ 570
Cdd:TIGR01418 629 EMGLTnveVMIPFVRTPEE-------GKRALEIMAEEGLRRGKNgLEVYVMCEVPSNALLADEFAKEFDGFSIGSNDLTQ 701
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 447096837 571 YLLAVDRDNAKVTRHYNSLNPAFLRALDYAVQAVHRQGKWIGLCGE 616
Cdd:TIGR01418 702 LTLGVDRDSGLVAHLFDERNPAVLRLIEMAIKAAKEHGKKVGICGQ 747
|
|
| PtsN |
COG1762 |
Phosphotransferase system mannitol/fructose-specific IIA domain (Ntr-type) [Carbohydrate ... |
687-831 |
4.60e-36 |
|
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: 133.05 E-value: 4.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 687 APLVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARL 766
Cdd:COG1762 4 SDLLTPELILLDLEASSKEEAIEELAELLAEKGYVLDKEEYLEALLEREELGSTGIGPGIAIPHARPEGVKKPGIAVARL 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447096837 767 QAPVRWG---DDEAQFIIMLTLNKHaAGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHEL 831
Cdd:COG1762 84 KEPVDFGamdGEPVDLVFLLAAPED-DSEEHLKLLAELARLLSDEEFREKLLNAKSPEEILELLKEAE 150
|
|
| PTS_EIIA_2 |
pfam00359 |
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2; |
689-828 |
1.98e-34 |
|
Phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 2;
Pssm-ID: 459780 [Multi-domain] Cd Length: 139 Bit Score: 128.09 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 689 LVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRypRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQA 768
Cdd:pfam00359 1 LLDKELIFLNLEAKSKEEAIEFLADKLVEAGYVE--PAYLEAILEREKEGSTGIGNGIAIPHARSEAVKKPGIAVLTLKE 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447096837 769 PVRWGD---DEAQFIIMLTLNKHAAGdqHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQ 828
Cdd:pfam00359 79 PVDFGSedgKPVKLIFLLAAPDNEAS--HLKILSQLARLLQDEEFVEKLLKAKDPEEILEILK 139
|
|
| PTS_IIA_fru |
cd00211 |
PTS_IIA, PTS system, fructose/mannitol specific IIA subunit. The bacterial phosphoenolpyruvate: ... |
690-827 |
1.52e-33 |
|
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: 125.37 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 690 VTAECITLESDWRSKEEVLKGMTDNLLLAGRCryPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQAP 769
Cdd:cd00211 1 LTKENIRLNLKAKSKEEAIEELAQLLVAAGYV--EEEYIEALLEREKEGSTGIGNGIAIPHAKSEAVKKPGIAVLRLKEP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447096837 770 VRWGD---DEAQFIIMLTLNKhaaGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLL 827
Cdd:cd00211 79 VDFGSldgQPVHLIFLLAAPD---SNEHLKALSQLARLLSDEEFVEQLLNAQSKEEILALL 136
|
|
| fruA |
TIGR00848 |
PTS system, fructose subfamily, IIA component; 4.A.2 The PTS Fructose-Mannitol (Fru) Family ... |
689-814 |
2.67e-28 |
|
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: 110.44 E-value: 2.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 689 LVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQA 768
Cdd:TIGR00848 1 LLNKDLIFLDQQFTSKEDVIKFLANKLLENGYISDTEEFLEDLLKREEEGTTGIGDGVAIPHAKSAAVKQPFVAIARLVK 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 447096837 769 PVRWG--DDEA-QFIIMLTLNKHAAGDQHMRIFSRLARRIMHEEFRNAL 814
Cdd:TIGR00848 81 GVDWQslDGKPvKLIFLIAVPKDEAGNTHLKALSQLARLLLNDEFRAKL 129
|
|
| PTS-HPr_like |
cd00367 |
Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of ... |
6-84 |
3.77e-19 |
|
Histidine-containing phosphocarrier protein (HPr)-like proteins. HPr is a central component of the bacterial phosphoenolpyruvate sugar phosphotransferase system (PTS). The PTS catalyses the phosphorylation of sugar substrates during their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate is transferred to HPr by enzyme I (EI). Phospho-HPr then transfers the phosphoryl group to one of several sugar-specific phosphoprotein intermediates. The conserved histidine in the N-terminus of HPr serves as an acceptor for the phosphoryl group of EI. In addition to the phosphotransferase proteins HPr and E1, this family also includes the closely related Carbon Catabolite Repressor (CCR) proteins which use the same phosphorylation mechanism and interact with transcriptional regulators to control expression of genes coding for utilization of less favored carbon sources.
Pssm-ID: 238217 [Multi-domain] Cd Length: 77 Bit Score: 82.17 E-value: 3.77e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447096837 6 EFICELPNGVHARPASHVETLCNTFSSQIEWHNLrtDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWL 84
Cdd:cd00367 1 TVTITNPLGLHARPAALLVQLASKFKSDITLRKG--GRKANAKSILGLMSLGAKQGDEITLSAEGEDAEEALEALAELL 77
|
|
| PRK11377 |
PRK11377 |
dihydroxyacetone kinase subunit M; Provisional |
12-339 |
6.25e-19 |
|
dihydroxyacetone kinase subunit M; Provisional
Pssm-ID: 183108 [Multi-domain] Cd Length: 473 Bit Score: 90.58 E-value: 6.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 12 PNGVHARPASH-VETLcNTFSS--QIEwhnlRTDRKGNAKS--ALALIgtDTLAGDNCQLLISGADEQEAHQRLSQWLRD 86
Cdd:PRK11377 165 RNGLHVRPASRlVYTL-STFNAdmLLE----KNGKCVTPESlnQIALL--QVRYNDTLRLIAKGPEAEEALIAFRQLAED 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 87 EFphcdaplaevkSDELEPLPVSLTNLnPQIIRARTVCSGSAggILTPISsldlnalgnlPAAKSVDAEQSALENGLTLV 166
Cdd:PRK11377 238 NF-----------GETEEVAPPTLRPV-PSPVSGKAFYYQPV--LCTVQA----------KSTLTVEEEQERLRQAIDFT 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 167 LKNIEfRLLDSDGAT-----SAILEAHRSLAGDTSLREHLLAGVSAGLSCAE-AIVASANHFCEEFSRSSSSYLQERALD 240
Cdd:PRK11377 294 LLDLM-TLTAKAEASglddiAAIFSGHHTLLDDPELLAAASERLQHEHCTAEyAWQQVLKELSQQYQQLDDEYLQARYID 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 241 VRDVCFQLLQQIYGEQrfPAPGKLTQPAICMADELTPSQFLELDKNHLKGLLLKSGGTTSHTVILARSFNIPTLVGVD-- 318
Cdd:PRK11377 373 VDDLLHRTLVHLTQTK--EELPQFNSPTILLAENIYPSTVLQLDPAVVKGICLSAGSPLSHSAIIARELGIGWICQQGek 450
|
330 340
....*....|....*....|.
gi 447096837 319 IDALTPwqQQTIYIDGNAGAI 339
Cdd:PRK11377 451 LYAIQP--EETLTLDVKTQRL 469
|
|
| PtsH |
COG1925 |
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport ... |
6-88 |
3.48e-17 |
|
HPr or related phosphotransfer protein [Signal transduction mechanisms, Carbohydrate transport and metabolism];
Pssm-ID: 441528 [Multi-domain] Cd Length: 88 Bit Score: 77.07 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 6 EFICELPNGVHARPASHVETLCNTFSSQIEWHNlrTDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWLR 85
Cdd:COG1925 5 EVTIVNKLGLHARPAAKLVQLASKFDSEITVEK--GGKEVNAKSIMGLMSLGAKKGDEVTITAEGPDAEEALDALAALIE 82
|
...
gi 447096837 86 DEF 88
Cdd:COG1925 83 SGF 85
|
|
| PRK09765 |
PRK09765 |
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional |
695-830 |
9.39e-17 |
|
PTS system 2-O-a-mannosyl-D-glycerate specific transporter subunit IIABC; Provisional
Pssm-ID: 182066 [Multi-domain] Cd Length: 631 Bit Score: 84.79 E-value: 9.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 695 ITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQAPVRW-- 772
Cdd:PRK09765 12 LCLNARFTSREEAIHALAQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWeg 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 773 --GDDEAQFIIMLTLNKHAAGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHE 830
Cdd:PRK09765 92 vdGPEAVDLIFLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDK 151
|
|
| MtlA2 |
COG4668 |
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and ... |
691-830 |
6.10e-16 |
|
Mannitol/fructose-specific phosphotransferase system, IIA domain [Carbohydrate transport and metabolism];
Pssm-ID: 443705 [Multi-domain] Cd Length: 143 Bit Score: 75.58 E-value: 6.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 691 TAECITLESDWRSKEEVLKgMTDNLLLAGRCRYPRKLEAdLWAREAVFSTGLGFSFAIPHSKSE---HIEQSTISVARLQ 767
Cdd:COG4668 5 TKENIRLNASAANKEEAIR-LAGQLLVEAGYVEPEYIDA-MLEREAQVSTYLGNGIAIPHGTNEakdLVLKTGISVLQFP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447096837 768 APVRWGDDE-AQFIIMLTlnkhAAGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHE 830
Cdd:COG4668 83 DGVDWGDGNtVYLVIGIA----AKSDEHLEILRQLARVLSDEENVEKLAKATDAEEILALLTGE 142
|
|
| PRK09913 |
PRK09913 |
PTS fructose transporter subunit IIA; |
688-831 |
9.39e-16 |
|
PTS fructose transporter subunit IIA;
Pssm-ID: 182141 [Multi-domain] Cd Length: 148 Bit Score: 74.92 E-value: 9.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 688 PLVTAECITLESDWRSKEEVLKGMTDNLLLAGRCRYPRKLEADLWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQ 767
Cdd:PRK09913 2 AALTASCIDLNIQGNGAYSILKQLATIALQNGFITDSHQFLQTLLLREKMHSTGFGSGVAVPHGKSACVKQPFVLFARKA 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447096837 768 APVRW----GDDEAQFIIMLTlnKHAAGDQHMRIFSRLARRIMHEEFRNALVNaASADAIASLLQHEL 831
Cdd:PRK09913 82 QAIDWqasdGEDVNCWICLGV--PQSGEEDQVKIIGTLCRKIIHQDFIHQLKQ-GDTDQVLALLNQTL 146
|
|
| PEP-utilizers |
pfam00391 |
PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain ... |
263-337 |
1.54e-15 |
|
PEP-utilizing enzyme, mobile domain; This domain is a "swivelling" beta/beta/alpha domain which is thought to be mobile in all proteins known to contain it.
Pssm-ID: 459796 [Multi-domain] Cd Length: 73 Bit Score: 72.06 E-value: 1.54e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447096837 263 KLTQPAICMADELTPSQFLELDKnhLKGLLLKSGGTTSHTVILARSFNIPTLVGVDIDALTPWQQQTIYIDGNAG 337
Cdd:pfam00391 1 KLPEGVILVAPDTTPSDTAGLDK--AAGIVTERGGMTSHAAIVARELGIPAVVGVGDATILLKEGDLVTVDGSTG 73
|
|
| PTS-HPr |
pfam00381 |
PTS HPr component phosphorylation site; |
6-85 |
2.00e-13 |
|
PTS HPr component phosphorylation site;
Pssm-ID: 459792 [Multi-domain] Cd Length: 79 Bit Score: 66.25 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 6 EFICELPNGVHARPASHVETLCNTFSSQIEWHNLrtDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWLR 85
Cdd:pfam00381 2 TVTITNPLGLHARPAALLVQLASKFDSDITLEKG--GKKVNAKSIMGLMSLGAKQGDEITISAEGEDEEEALEALAALLE 79
|
|
| nitro_reg_IIA |
TIGR01419 |
PTS IIA-like nitrogen-regulatory protein PtsN; This model describes a full-length protein of ... |
689-827 |
1.22e-10 |
|
PTS IIA-like nitrogen-regulatory protein PtsN; This model describes a full-length protein of about 160 residues closely related to the fructose-specific phosphotransferase (PTS) system IIA component. It is a regulatory protein found only in species with a phosphoenolpyruvate-protein phosphotransferase (enzyme I of PTS systems) and an HPr-like phosphocarrier protein, but not all species have a IIC-like permease. Members of this family are found in Proteobacteria, Chlamydia, and the spirochete Treponema pallidum. [Signal transduction, PTS]
Pssm-ID: 162350 [Multi-domain] Cd Length: 145 Bit Score: 60.12 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 689 LVTAECITLESDWRSKEEVLKGMTdnLLLAGRCRYPRKLEAD-LWAREAVFSTGLGFSFAIPHSKSEHIEQSTISVARLQ 767
Cdd:TIGR01419 5 LLLPEAIRVAMECGSKKRLLEIIS--LLAARELSLPEQDVFEcLLAREKLGSTGVGNGIAIPHGRLSGLKQPVGVFIRLD 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447096837 768 APVRWG--DDEAQFIIMLTLNKHAAGDQHMRIFSRLARRIMHEEFRNALvNAASADAIASLL 827
Cdd:TIGR01419 83 APVDFDalDGKPVDLLFALLVPENATAEHLEALSRIARKLSDKTICRRL-RAASAEEIYQIL 143
|
|
| PEP-utilizers_N |
pfam05524 |
PEP-utilizing enzyme, N-terminal; |
145-237 |
6.39e-09 |
|
PEP-utilizing enzyme, N-terminal;
Pssm-ID: 461671 [Multi-domain] Cd Length: 125 Bit Score: 54.93 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 145 NLPAAKSVDAEQSALENGLTLV---LKNIEFRLLDSDGAT-SAILEAHRSLAGDTSLREHLLAGVSAGLSCAEAIVASA- 219
Cdd:pfam05524 28 REVPADDVEAEIARLEAALEAAreeLEALAERAAGELGEEeAAIFEAHLMMLEDPELLEEVEELIREGGLNAEAAVKEVv 107
|
90
....*....|....*...
gi 447096837 220 NHFCEEFSRSSSSYLQER 237
Cdd:pfam05524 108 DEFAAMFEAMDDPYLRER 125
|
|
| PTS_HPr_family |
TIGR01003 |
Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains ... |
12-82 |
3.46e-05 |
|
Phosphotransferase System HPr (HPr) Family; The HPr family are bacterial proteins (or domains of proteins) which function in phosphoryl transfer system (PTS) systems. They include energy-coupling components which catalyze sugar uptake via a group translocation mechanism. The functions of most of these proteins are not known, but they presumably function in PTS-related regulatory capacities. All seed members are stand-alone HPr proteins, although the model also recognizes HPr domains of PTS fusion proteins. This family includes the related NPr protein. [Signal transduction, PTS]
Pssm-ID: 273389 [Multi-domain] Cd Length: 82 Bit Score: 43.02 E-value: 3.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447096837 12 PNGVHARPASHVETLCNTFSSQIewHNLRTDRKGNAKSALALIgtdTLA---GDNCQLLISGADEQEAHQRLSQ 82
Cdd:TIGR01003 11 KVGLHARPAAILVKLASGFDSEI--TLTKNGKEVNAKSIMGIM---MLGagqGTEVTVSADGEDEAEALEALAK 79
|
|
| PRK09665 |
PRK09665 |
PTS galactitol transporter subunit IIA; |
703-832 |
3.92e-05 |
|
PTS galactitol transporter subunit IIA;
Pssm-ID: 182023 [Multi-domain] Cd Length: 150 Bit Score: 44.41 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 703 SKEEVLKGMTDNLLLAGRCR--YPrkleADLWAREAVFSTGLGF---SFAIPHSKSEHIEQSTISVARLQAPV---RWGD 774
Cdd:PRK09665 14 DRSEALTHIGNEMLAKGVVHdtYP----QALIAREAEFPTGIMLeqhAVAIPHCEAIHAKSPAIYLIRPDKKVhfqQADD 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447096837 775 DE---AQFIIMLTLNKHAagdQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHELE 832
Cdd:PRK09665 90 DNdvaVSLVIALIVENPQ---QQLKLLRCLFGKLQQPDIVETLLTLPETQLKEYFTKYVLD 147
|
|
| PRK13782 |
PRK13782 |
HPr family phosphocarrier protein; |
10-84 |
6.47e-05 |
|
HPr family phosphocarrier protein;
Pssm-ID: 172320 [Multi-domain] Cd Length: 82 Bit Score: 42.08 E-value: 6.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447096837 10 ELPNGVHARPASHVETLCNTFSSQIEWHnlRTDRKGNAKSALALIGTDTLAGDNCQLLISGADEQEAHQRLSQWL 84
Cdd:PRK13782 9 SLKTGLQARPAALFVQEANRFHADIFIE--KDGKKVNAKSIMGLMSLAIGTGSMITIITEGSDEEEALEALAAYV 81
|
|
| PykA2 |
COG3848 |
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms]; |
296-349 |
1.26e-03 |
|
Phosphohistidine swiveling domain of PEP-utilizing enzymes [Signal transduction mechanisms];
Pssm-ID: 443058 Cd Length: 321 Bit Score: 41.81 E-value: 1.26e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 447096837 296 GGTTSHTVILARSFNIPTLVGVDiDALTPWQQ-QTIYIDGNAGaiVVEPGEAVAR 349
Cdd:COG3848 270 GGLTSHAAIVGLELGIPVIVGAE-GATEILKDgQVVTVDAERG--VVYRGAVNVL 321
|
|
| PRK15083 |
PRK15083 |
PTS system mannitol-specific transporter subunit IICBA; Provisional |
690-801 |
1.79e-03 |
|
PTS system mannitol-specific transporter subunit IICBA; Provisional
Pssm-ID: 237905 [Multi-domain] Cd Length: 639 Bit Score: 41.96 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 690 VTAECITLESDWRSKEEVLKgMTDNLLLAGRCRYPRKLEAdLWAREAVFSTGLGFSFAIPHSKSE---HIEQSTISVARL 766
Cdd:PRK15083 497 LGAENIFLGLKAATKEEAIR-FAGEQLVKGGYVEPEYVDA-MLDREKLTSTYLGESIAVPHGTVEakdRVLKTGVVFCQY 574
|
90 100 110
....*....|....*....|....*....|....*...
gi 447096837 767 QAPVRWGDDE---AQFIIMLTlnkhAAGDQHMRIFSRL 801
Cdd:PRK15083 575 PEGVRFGEEEddiARLVIGIA----ARNNEHIQVITSL 608
|
|
| PRK11109 |
PRK11109 |
fused PTS fructose transporter subunit IIA/HPr protein; |
680-830 |
3.90e-03 |
|
fused PTS fructose transporter subunit IIA/HPr protein;
Pssm-ID: 236849 [Multi-domain] Cd Length: 375 Bit Score: 40.32 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447096837 680 FRMTQQDaplvtaecITLESDWRSKEEVLKGMTDNLLLAGrcryprKLEA----DLWAREAVFSTGLGFSFAIPHSKSEH 755
Cdd:PRK11109 2 FQLSVQD--------IHLGQQAGNKEEAIRQVAAALTQAG------NVAEgyvdGMLAREQQTSTFLGNGIAIPHGTTDT 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447096837 756 IEQ-STISVARLQAP--VRWGDDEaqfIIMLTLNKHAAGDQHMRIFSRLARRIMHEEFRNALVNAASADAIASLLQHE 830
Cdd:PRK11109 68 RDLvLKTGVQVFQFPqgVTWGDGQ---TAYVAIGIAAKSDEHLGLLRQLTHVLSDDSVAEQLKSATTAEELRALLMGE 142
|
|
| PRK06241 |
PRK06241 |
phosphoenolpyruvate synthase; Validated |
289-339 |
5.09e-03 |
|
phosphoenolpyruvate synthase; Validated
Pssm-ID: 235751 [Multi-domain] Cd Length: 871 Bit Score: 40.64 E-value: 5.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 447096837 289 KGLLLKSGGTTSHTVILARSFNIPTLVGVDiDALTPWQQ-QTIYIDGNAGAI 339
Cdd:PRK06241 816 KGLVTEVGGLMTHGAVIAREYGIPAVVGVE-NATKLIKDgQRIRVDGTEGYV 866
|
|
| |
