|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1-672 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 920.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 1 MADSQDLSKMKLPELKEIAKELGLRGLSAKRKGDLVAAIEEARAKQSSAKSETAPAQAEQPAGhddavsvPVRKTGARRV 80
Cdd:PRK12678 17 RARGGGLAGMKLPELRALAKQLGIKGTSGMRKGELIAAIKEARGGGAAAAAATPAAPAAAARR-------AARAAAAARQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 81 VRKAGEPKAVEESAAEQPTQVKEEGHAALPAEEEMTQIRGRRVRGKRRQMESADQAATNGETSAAEQLLSTLNLPEHAER 160
Cdd:PRK12678 90 AEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEER 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 161 GGEQPRRRRGavdslpTRRRAGAAAVREPDAEAKPDLDDILSSLPLSANDDESDERHEEHAHRRGERGSRTNDRSNARAD 240
Cdd:PRK12678 170 DERRRRGDRE------DRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 241 RENRQHRRNRNERDYEEREEGNERRSRDERGNNRNERNNRNDRNERreenTEDLVEVGGIVDVLDSYAFIRTSGYLPGPN 320
Cdd:PRK12678 244 REDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPELRE----DDVLVPVAGILDVLDNYAFVRTSGYLPGPN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 321 DIYVSMGQIKKYGLRKGDAVRGYTRAPHEGERRNQRQKFMPLQSITLINGLSVEEAQDRPNFSKLTPLYPDERLRMETTP 400
Cdd:PRK12678 320 DVYVSMNQVRKNGLRKGDAVTGAVRAPREGEQGNQRQKFNPLVRLDSVNGMSPEEAKKRPEFGKLTPLYPNERLRLETEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 401 NRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVHLMVVLVDERPEEVTDMERTVKGEIISSTFDR 480
Cdd:PRK12678 400 KKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIANAITTNNPECHLMVVLVDERPEEVTDMQRSVKGEVIASTFDR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 481 PASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRILSGGVDAQALYPPKKFFGAARNIENGGSLT 560
Cdd:PRK12678 480 PPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASGRILSGGVDSTALYPPKRFFGAARNIENGGSLT 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 561 IISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRRLLGGLEPEQ 640
Cdd:PRK12678 560 IIATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTRKEELLLSPDELAIVHKLRRVLSGLDSQQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 501697128 641 AYQTLVPRLKKTMTNADFFKAIVQQGNSSLNG 672
Cdd:PRK12678 640 AIDLLISRLKKTKSNYEFLMQVSKTTPGAMDD 671
|
|
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
292-666 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 723.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 292 EDLVEVGGIVDVL-DSYAFIRTSGYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGErrnqrqKFMPLQSITLING 370
Cdd:COG1158 4 DGLIPVEGVLEILpDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGE------KYFALLRVESVNG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 371 LSVEEAQDRPNFSKLTPLYPDERLRMETTPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVHL 450
Cdd:COG1158 78 EDPEEARKRPDFDNLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 451 MVVLVDERPEEVTDMERTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRI 530
Cdd:COG1158 158 IVLLIDERPEEVTDMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 531 LSGGVDAQALYPPKKFFGAARNIENGGSLTIISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASG 610
Cdd:COG1158 238 LSGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 501697128 611 TRREELITNPQELPVLYSLRRLLGGLEPEQAYQTLVPRLKKTMTNADFFKAIVQQG 666
Cdd:COG1158 318 TRREELLLSPEELEKVWILRRALSGMDPVEAMEFLLDRLKKTKSNAEFLESMNKTT 373
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
292-662 |
0e+00 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 576.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 292 EDLVEVGGIVDVL-DSYAFIRT--SGYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGERrnqrqkFMPLQSITLI 368
Cdd:TIGR00767 46 GGLIFGEGVLEILpDGFGFLRSpdSSYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGER------YFALLKVESV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 369 NGLSVEEAQDRPNFSKLTPLYPDERLRMETTPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEV 448
Cdd:TIGR00767 120 NGDDPEKAKNRVLFENLTPLYPNERLRLETSTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 449 HLMVVLVDERPEEVTDMERTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASG 528
Cdd:TIGR00767 200 ELIVLLIDERPEEVTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 529 RILSGGVDAQALYPPKKFFGAARNIENGGSLTIISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINA 608
Cdd:TIGR00767 280 KVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKK 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 501697128 609 SGTRREELITNPQELPVLYSLRRLLGGLEPEQAYQTLVPRLKKTMTNADFFKAI 662
Cdd:TIGR00767 360 SGTRKEELLLTPEELQKIWVLRKIISPMDSIEAMEFLISKLKKTKTNEEFLESM 413
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
405-650 |
1.46e-154 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 446.27 E-value: 1.46e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 405 GRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVHLMVVLVDERPEEVTDMERTVKGEIISSTFDRPASD 484
Cdd:cd01128 4 TRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKGEVVASTFDEPPER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 485 HTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRILSGGVDAQALYPPKKFFGAARNIENGGSLTIISS 564
Cdd:cd01128 84 HVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLTIIAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 565 ALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRRLLGGLEPEQAYQT 644
Cdd:cd01128 164 ALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIEAMEF 243
|
....*.
gi 501697128 645 LVPRLK 650
Cdd:cd01128 244 LLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
299-374 |
7.59e-28 |
|
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It it thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers.
Pssm-ID: 462182 [Multi-domain] Cd Length: 72 Bit Score: 106.69 E-value: 7.59e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501697128 299 GIVDVL-DSYAFIRTSGYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGErrnqrqKFMPLQSITLINGLSVE 374
Cdd:pfam07497 2 GILEILpDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGE------KYFALLRVESVNGEDPE 72
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
6-47 |
3.95e-11 |
|
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It it thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers. This domain is found to the N-terminus of the RNA binding domain.
Pssm-ID: 198027 [Multi-domain] Cd Length: 43 Bit Score: 58.16 E-value: 3.95e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 501697128 6 DLSKMKLPELKEIAKELGLRGLSAKRKGDLVAAIEEARAKQS 47
Cdd:smart00959 1 ELKKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKKG 42
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1-672 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 920.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 1 MADSQDLSKMKLPELKEIAKELGLRGLSAKRKGDLVAAIEEARAKQSSAKSETAPAQAEQPAGhddavsvPVRKTGARRV 80
Cdd:PRK12678 17 RARGGGLAGMKLPELRALAKQLGIKGTSGMRKGELIAAIKEARGGGAAAAAATPAAPAAAARR-------AARAAAAARQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 81 VRKAGEPKAVEESAAEQPTQVKEEGHAALPAEEEMTQIRGRRVRGKRRQMESADQAATNGETSAAEQLLSTLNLPEHAER 160
Cdd:PRK12678 90 AEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEEER 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 161 GGEQPRRRRGavdslpTRRRAGAAAVREPDAEAKPDLDDILSSLPLSANDDESDERHEEHAHRRGERGSRTNDRSNARAD 240
Cdd:PRK12678 170 DERRRRGDRE------DRQAEAERGERGRREERGRDGDDRDRRDRREQGDRREERGRRDGGDRRGRRRRRDRRDARGDDN 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 241 RENRQHRRNRNERDYEEREEGNERRSRDERGNNRNERNNRNDRNERreenTEDLVEVGGIVDVLDSYAFIRTSGYLPGPN 320
Cdd:PRK12678 244 REDRGDRDGDDGEGRGGRRGRRFRDRDRRGRRGGDGGNEREPELRE----DDVLVPVAGILDVLDNYAFVRTSGYLPGPN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 321 DIYVSMGQIKKYGLRKGDAVRGYTRAPHEGERRNQRQKFMPLQSITLINGLSVEEAQDRPNFSKLTPLYPDERLRMETTP 400
Cdd:PRK12678 320 DVYVSMNQVRKNGLRKGDAVTGAVRAPREGEQGNQRQKFNPLVRLDSVNGMSPEEAKKRPEFGKLTPLYPNERLRLETEP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 401 NRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVHLMVVLVDERPEEVTDMERTVKGEIISSTFDR 480
Cdd:PRK12678 400 KKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIANAITTNNPECHLMVVLVDERPEEVTDMQRSVKGEVIASTFDR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 481 PASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRILSGGVDAQALYPPKKFFGAARNIENGGSLT 560
Cdd:PRK12678 480 PPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASGRILSGGVDSTALYPPKRFFGAARNIENGGSLT 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 561 IISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRRLLGGLEPEQ 640
Cdd:PRK12678 560 IIATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTRKEELLLSPDELAIVHKLRRVLSGLDSQQ 639
|
650 660 670
....*....|....*....|....*....|..
gi 501697128 641 AYQTLVPRLKKTMTNADFFKAIVQQGNSSLNG 672
Cdd:PRK12678 640 AIDLLISRLKKTKSNYEFLMQVSKTTPGAMDD 671
|
|
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
292-666 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 723.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 292 EDLVEVGGIVDVL-DSYAFIRTSGYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGErrnqrqKFMPLQSITLING 370
Cdd:COG1158 4 DGLIPVEGVLEILpDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGE------KYFALLRVESVNG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 371 LSVEEAQDRPNFSKLTPLYPDERLRMETTPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVHL 450
Cdd:COG1158 78 EDPEEARKRPDFDNLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 451 MVVLVDERPEEVTDMERTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRI 530
Cdd:COG1158 158 IVLLIDERPEEVTDMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 531 LSGGVDAQALYPPKKFFGAARNIENGGSLTIISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASG 610
Cdd:COG1158 238 LSGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 501697128 611 TRREELITNPQELPVLYSLRRLLGGLEPEQAYQTLVPRLKKTMTNADFFKAIVQQG 666
Cdd:COG1158 318 TRREELLLSPEELEKVWILRRALSGMDPVEAMEFLLDRLKKTKSNAEFLESMNKTT 373
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
292-662 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 614.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 292 EDLVEVGGIVDVL-DSYAFIRTS--GYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGERrnqrqkFMPLQSITLI 368
Cdd:PRK09376 46 GGDIFGEGVLEILpDGFGFLRSPdaNYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGER------YFALLKVETV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 369 NGLSVEEAQDRPNFSKLTPLYPDERLRMET-TPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPE 447
Cdd:PRK09376 120 NGEDPEKARNRPLFENLTPLYPNERLRLETgNPEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 448 VHLMVVLVDERPEEVTDMERTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPAS 527
Cdd:PRK09376 200 VHLIVLLIDERPEEVTDMQRSVKGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSS 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 528 GRILSGGVDAQALYPPKKFFGAARNIENGGSLTIISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDIN 607
Cdd:PRK09376 280 GKVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIN 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 501697128 608 ASGTRREELITNPQELPVLYSLRRLLGGLEPEQAYQTLVPRLKKTMTNADFFKAI 662
Cdd:PRK09376 360 RSGTRKEELLLSPEELQKVWILRKILSPMDEVEAMEFLLDKLKKTKTNEEFFDSM 414
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
292-662 |
0e+00 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 576.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 292 EDLVEVGGIVDVL-DSYAFIRT--SGYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGERrnqrqkFMPLQSITLI 368
Cdd:TIGR00767 46 GGLIFGEGVLEILpDGFGFLRSpdSSYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGER------YFALLKVESV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 369 NGLSVEEAQDRPNFSKLTPLYPDERLRMETTPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEV 448
Cdd:TIGR00767 120 NGDDPEKAKNRVLFENLTPLYPNERLRLETSTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 449 HLMVVLVDERPEEVTDMERTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASG 528
Cdd:TIGR00767 200 ELIVLLIDERPEEVTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 529 RILSGGVDAQALYPPKKFFGAARNIENGGSLTIISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINA 608
Cdd:TIGR00767 280 KVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKK 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 501697128 609 SGTRREELITNPQELPVLYSLRRLLGGLEPEQAYQTLVPRLKKTMTNADFFKAI 662
Cdd:TIGR00767 360 SGTRKEELLLTPEELQKIWVLRKIISPMDSIEAMEFLISKLKKTKTNEEFLESM 413
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
292-663 |
2.49e-176 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 506.93 E-value: 2.49e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 292 EDLVEVGGIVDVL-DSYAFIRTS--GYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAphegerrnqRQKFMPLQSITLI 368
Cdd:PRK12608 14 QSTEEVLGVLEILgDGFGFLRSArrNYLPSPDDVFVPPALIRRFNLRTGDVVEGVARP---------RERYRVLVRVDSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 369 NGLSVEEAQDRPNFSKLTPLYPDERLRMETTPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEV 448
Cdd:PRK12608 85 NGTDPEKLARRPHFDDLTPLHPRERLRLETGSDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 449 HLMVVLVDERPEEVTDMERTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASG 528
Cdd:PRK12608 165 HLMVLLIDERPEEVTDMRRSVKGEVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 529 RILSGGVDAQALYPPKKFFGAARNIENGGSLTIISSALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINA 608
Cdd:PRK12608 245 RTLSGGVDARALQRPKRLFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAK 324
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 501697128 609 SGTRREELITNPQELPVLYSLRRLLGGLEPEQAYQTLVPRLKKTMTNADFFKAIV 663
Cdd:PRK12608 325 SGTRREELLLDSKELEKVRRLRRALASRKPVEAMEALLEKLRETPDNAEFLNSVQ 379
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
405-650 |
1.46e-154 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 446.27 E-value: 1.46e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 405 GRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVHLMVVLVDERPEEVTDMERTVKGEIISSTFDRPASD 484
Cdd:cd01128 4 TRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKGEVVASTFDEPPER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 485 HTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRILSGGVDAQALYPPKKFFGAARNIENGGSLTIISS 564
Cdd:cd01128 84 HVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLTIIAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 565 ALVETGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRRLLGGLEPEQAYQT 644
Cdd:cd01128 164 ALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIEAMEF 243
|
....*.
gi 501697128 645 LVPRLK 650
Cdd:cd01128 244 LLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
299-374 |
7.59e-28 |
|
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It it thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers.
Pssm-ID: 462182 [Multi-domain] Cd Length: 72 Bit Score: 106.69 E-value: 7.59e-28
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501697128 299 GIVDVL-DSYAFIRTSGYLPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGErrnqrqKFMPLQSITLINGLSVE 374
Cdd:pfam07497 2 GILEILpDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGE------KYFALLRVESVNGEDPE 72
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
406-609 |
1.31e-25 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 105.13 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNnpevHLMVVLVDERPEEVTD----------MERTVkgeIIS 475
Cdd:pfam00006 3 RAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD----VVVYALIGERGREVREfieellgsgaLKRTV---VVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 476 STFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRILS-GGvdaqalYPPKKFF------- 547
Cdd:pfam00006 76 ATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGrEG------YPPSVFSllarlle 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501697128 548 GAARNIENGGSLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINAS 609
Cdd:pfam00006 150 RAGRVKGKGGSITALPTVLVP-GDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLAS 210
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
406-633 |
3.01e-22 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 100.03 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAiavnnPEVHLMV-VLVDERPEEVTD-MERTVKGE------IISST 477
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNA-----PDADSNVlVLIGERGREVREfIDFTLSEEtrkrcvIVVAT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 478 FDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRILSGGVdaqalYPPKKFFGAARNIENGG 557
Cdd:PRK07594 219 SDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGE-----YPPGVFSALPRLLERTG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 558 -----SLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRRL 632
Cdd:PRK07594 294 mgekgSITAFYTVLVE-GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRC 372
|
.
gi 501697128 633 L 633
Cdd:PRK07594 373 L 373
|
|
| Rho_CSD |
cd04459 |
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination ... |
299-353 |
9.37e-20 |
|
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination factor in most bacteria. In bacteria, there are two distinct mechanisms for mRNA transcription termination. In intrinsic termination, RNA polymerase and nascent mRNA are released from DNA template by an mRNA stem loop structure, which resembles the transcription termination mechanism used by eukaryotic pol III. The second mechanism is mediated by Rho factor. Rho factor terminates transcription by using energy from ATP hydrolysis to forcibly dissociate the transcripts from RNA polymerase. Rho protein contains an N-terminal S1-like domain, which binds single-stranded RNA. Rho has a C-terminal ATPase domain which hydrolyzes ATP to provide energy to strip RNA polymerase and mRNA from the DNA template. Rho functions as a homohexamer.
Pssm-ID: 239906 [Multi-domain] Cd Length: 68 Bit Score: 83.44 E-value: 9.37e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 501697128 299 GIVDVL-DSYAFIRTSGY--LPGPNDIYVSMGQIKKYGLRKGDAVRGYTRAPHEGERR 353
Cdd:cd04459 3 GVLEILpDGFGFLRSSGYnyLPGPDDIYVSPSQIRRFNLRTGDTVVGQIRPPKEGERY 60
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
406-612 |
1.27e-19 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 89.16 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIAnaiavNNPEVHLMVV-LVDERPEEVTD-MERTVKGE------IISST 477
Cdd:cd01136 56 RAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIA-----RNTDADVNVIaLIGERGREVREfIEKDLGEEglkrsvLVVAT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 478 FDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRIL-SGGvdaqalYPPKKFFGAARNIE-- 554
Cdd:cd01136 131 SDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPtRRG------YPPSVFALLPRLLEra 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501697128 555 ---NGGSLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTR 612
Cdd:cd01136 205 gngEKGSITAFYTVLVE-GDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
387-612 |
1.07e-18 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 86.74 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 387 PLYPDERLRMETTPNRIIGRL------------IDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVhLMVVL 454
Cdd:cd19476 25 PIKTKQRRPIHLKAPNPIERLppeeplqtgikvIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGV-VVFAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 455 VDERPEEVTD----------MERTVkgeIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAA 524
Cdd:cd19476 104 IGERGREVNDlyeeftksgaMERTV---VVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALREMS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 525 PASGRilsggVDAQALYPPKKFFG-------AARNIENGGSLTIISSALVETGSKMDEVIFEEFKGTgNMELRLSRELAD 597
Cdd:cd19476 181 ALLGE-----PPGREGYPPYLFTKlatlyerAGKVKDGGGSITAIPAVSTPGDDLTDPIPDNTFAIL-DGQIVLSRELAR 254
|
250
....*....|....*
gi 501697128 598 KRLFPAVDINASGTR 612
Cdd:cd19476 255 KGIYPAINVLDSTSR 269
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
406-633 |
8.71e-18 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 86.41 E-value: 8.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANaiavnNPEVHLMVV-LVDERPEEVTD-MERTVKGE------IISST 477
Cdd:PRK06820 152 RAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA-----DSAADVMVLaLIGERGREVREfLEQVLTPEarartvVVVAT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 478 FDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLAR-AYNIAAPASGRILSGGvdaqalYPPKKFFGAARNIENG 556
Cdd:PRK06820 227 SDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARaAREIGLAAGEPPAAGS------FPPSVFANLPRLLERT 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 557 G-----SLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRR 631
Cdd:PRK06820 301 GnsdrgSITAFYTVLVE-GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRR 379
|
..
gi 501697128 632 LL 633
Cdd:PRK06820 380 ML 381
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
395-633 |
1.30e-14 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 76.71 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 395 RMETTPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIanaiaVNNPEVHLMVV-LVDERPEEVTDM-------E 466
Cdd:PRK06936 140 RLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASL-----IRSAEVDVTVLaLIGERGREVREFiesdlgeE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 467 RTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRilsggVDAQALYPPKKF 546
Cdd:PRK06936 215 GLRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGE-----PPTRRGYPPSVF 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 547 FGAARNIENGG-----SLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQ 621
Cdd:PRK06936 290 AALPRLMERAGqsdkgSITALYTVLVE-GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKE 368
|
250
....*....|..
gi 501697128 622 ELPVLYSLRRLL 633
Cdd:PRK06936 369 HKTWAGRLRELL 380
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
390-645 |
3.15e-14 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 75.42 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 390 PDERLRMETTPNRIIG-RLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIanaiaVNNPEVHLMVV-LVDERPEEVTD--- 464
Cdd:PRK08149 123 PSYAERRPIREPLITGvRAIDGLLTCGVGQRMGIFASAGCGKTSLMNML-----IEHSEADVFVIgLIGERGREVTEfve 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 465 -MERTVKGE---IISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRIlsggvDAQAL 540
Cdd:PRK08149 198 sLRASSRREkcvLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGEL-----PARRG 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 541 YPPKKFFGAARNIEN-----GGSLTIISSALVETGSKMDeVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREE 615
Cdd:PRK08149 273 YPASVFDSLPRLLERpgatlAGSITAFYTVLLESEEEPD-PIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG 351
|
250 260 270
....*....|....*....|....*....|
gi 501697128 616 LITNPQELPVLYSLRRLLGGLEPEQAYQTL 645
Cdd:PRK08149 352 QVTDPKHRQLAAAFRKLLTRLEELQLFIDL 381
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
393-653 |
4.70e-13 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 71.57 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 393 RLRMETtPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNpevhLMVVLVDERPEEVTDM-ERTV-- 469
Cdd:PRK06002 142 RARVET-GLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDT----VVIALVGERGREVREFlEDTLad 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 470 ---KGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGR--ILSGgvdaqalYPPK 544
Cdd:PRK06002 217 nlkKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLLIVDSVTRFAHAAREVALAAGEppVARG-------YPPS 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 545 KFFGAAR-------NIENGGSLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELI 617
Cdd:PRK06002 290 VFSELPRlleragpGAEGGGSITGIFSVLVD-GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501697128 618 TNPQELPVLYSLR------------RLLGGLEP------EQAYQtLVPRLKKTM 653
Cdd:PRK06002 369 WTPEQRKLVSRLKsmiarfeetrdlRLIGGYRAgsdpdlDQAVD-LVPRIYEAL 421
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
361-633 |
9.18e-13 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 70.91 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 361 PLQSITLINGLS-VEEAQDRPNfskltplyPDERLRMETtPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIAN 439
Cdd:PRK07721 110 PLDGSALPKGLApVSTDQDPPN--------PLKRPPIRE-PMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIAR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 440 aiavnNPEVHLMVV-LVDERPEEVTD-MERTVKGE------IISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLD 511
Cdd:PRK07721 181 -----NTSADLNVIaLIGERGREVREfIERDLGPEglkrsiVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMD 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 512 SMTRLARAYNIAAPASGRilsggVDAQALYPPKKFFGAARNIENGG-----SLTIISSALVEtGSKMDEVIFEEFKGTGN 586
Cdd:PRK07721 256 SVTRVAMAQREIGLAVGE-----PPTTKGYTPSVFAILPKLLERTGtnasgSITAFYTVLVD-GDDMNEPIADTVRGILD 329
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 501697128 587 MELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRRLL 633
Cdd:PRK07721 330 GHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEAANRFRELL 376
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
350-660 |
7.53e-12 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 67.70 E-value: 7.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 350 GERRNQRQKFMPLQSITLinglsveeaqDRPnfskltPLYPDERLRMETTPNRIIgRLIDIVSPIGKGQRGLIVSPPKAG 429
Cdd:PRK06793 106 GEVLNEEAENIPLQKIKL----------DAP------PIHAFEREEITDVFETGI-KSIDSMLTIGIGQKIGIFAGSGVG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 430 KTITLQNIA-NAIAVNNpevhlMVVLVDERPEEVTDMERTVKGE-------IISSTFDRPASDHTIVAELAIERAKRLVE 501
Cdd:PRK06793 169 KSTLLGMIAkNAKADIN-----VISLVGERGREVKDFIRKELGEegmrksvVVVATSDESHLMQLRAAKLATSIAEYFRD 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 502 LGQDVVVLLDSMTRLARAYNIAAPASGRILSGGVDAQALYPPKKFFGAARNIENGgSLTIISSALVEtGSKMDEVIFEEF 581
Cdd:PRK06793 244 QGNNVLLMMDSVTRFADARRSVDIAVKELPIGGKTLLMESYMKKLLERSGKTQKG-SITGIYTVLVD-GDDLNGPVPDLA 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501697128 582 KGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRRLLGGLEPEQAYQTLvPRLKKTMTNADFFK 660
Cdd:PRK06793 322 RGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKL-GTIQENAENAYIFE 399
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
406-633 |
2.00e-11 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 66.72 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIA--VNnpevhlMVVLVDERPEEVTDMERTVKGE-------IISS 476
Cdd:PRK09099 152 RIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQcdVN------VIALIGERGREVREFIELILGEdgmarsvVVCA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 477 TFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRilsggVDAQALYPPKKFFGAARNIENG 556
Cdd:PRK09099 226 TSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGE-----PPARRGFPPSVFAELPRLLERA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 557 G-----SLTIISSALVETGSKMDEVIfEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLRR 631
Cdd:PRK09099 301 GmgetgSITALYTVLAEDESGSDPIA-EEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQ 379
|
..
gi 501697128 632 LL 633
Cdd:PRK09099 380 LL 381
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
6-47 |
3.95e-11 |
|
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It it thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers. This domain is found to the N-terminus of the RNA binding domain.
Pssm-ID: 198027 [Multi-domain] Cd Length: 43 Bit Score: 58.16 E-value: 3.95e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 501697128 6 DLSKMKLPELKEIAKELGLRGLSAKRKGDLVAAIEEARAKQS 47
Cdd:smart00959 1 ELKKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKKG 42
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
6-46 |
1.58e-10 |
|
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It it thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers. This domain is found to the N-terminus of the RNA binding domain (pfam07497).
Pssm-ID: 429493 [Multi-domain] Cd Length: 43 Bit Score: 56.62 E-value: 1.58e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 501697128 6 DLSKMKLPELKEIAKELGLRGLSAKRKGDLVAAIEEARAKQ 46
Cdd:pfam07498 1 ELKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQAEK 41
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
406-634 |
5.37e-10 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 61.97 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQR-GlIVSPPKAGKTITLQNIA-NAIA-VNnpevhlmVV-LVDERPEEVTD----------MERTVkg 471
Cdd:COG1157 146 RAIDGLLTVGRGQRiG-IFAGSGVGKSTLLGMIArNTEAdVN-------VIaLIGERGREVREfieddlgeegLARSV-- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 472 eIISSTFDRPAsdhtivaelaIERAK------------RlvELGQDVVVLLDSMTRLARAY-NIA-----APASGrilsG 533
Cdd:COG1157 216 -VVVATSDEPP----------LMRLRaaytataiaeyfR--DQGKNVLLLMDSLTRFAMAQrEIGlaagePPATR----G 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 534 gvdaqalYPPKKFFGAARNIE-----NGGSLTIISSALVEtGSKMDEVIFEefkgtgnmELR--------LSRELADKRL 600
Cdd:COG1157 279 -------YPPSVFALLPRLLEragngGKGSITAFYTVLVE-GDDMNDPIAD--------AVRgildghivLSRKLAERGH 342
|
250 260 270
....*....|....*....|....*....|....
gi 501697128 601 FPAVDINASGTRREELITNPQELPVLYSLRRLLG 634
Cdd:COG1157 343 YPAIDVLASISRVMPDIVSPEHRALARRLRRLLA 376
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
406-633 |
4.46e-09 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 59.33 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLqnianAIAVNNPEVHLMVV-LVDERPEEVTDMERTVKGE---IISSTFDRP 481
Cdd:PRK08972 151 RAINAMLTVGKGQRMGLFAGSGVGKSVLL-----GMMTRGTTADVIVVgLVGERGREVKEFIEEILGEegrARSVVVAAP 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 482 ASDHTIVAELAIERAKRLVE----LGQDVVVLLDSMTRLARAYNIAAPASGRilsggVDAQALYPPKKFFGAARNIE--- 554
Cdd:PRK08972 226 ADTSPLMRLKGCETATTIAEyfrdQGLNVLLLMDSLTRYAQAQREIALAVGE-----PPATKGYPPSVFAKLPALVErag 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 555 NG----GSLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLR 630
Cdd:PRK08972 301 NGgpgqGSITAFYTVLTE-GDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVK 379
|
...
gi 501697128 631 RLL 633
Cdd:PRK08972 380 QVY 382
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
378-612 |
9.70e-09 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 57.98 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 378 DRPNFSKLTPLYPDERlRMETTPNRIIGRLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIavnnpEVHLMVV-LVD 456
Cdd:PRK07196 117 STPLQQQLPQIHPLQR-RAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYT-----QADVVVVgLIG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 457 ERPEEVTDM-------ERTVKGEIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGR 529
Cdd:PRK07196 191 ERGREVKEFiehslqaAGMAKSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 530 ilsggVDAQALYPPKKF------FGAARNIENGGSLTIISSALVETGSKMDEVIfEEFKGTGNMELRLSRELADKRLFPA 603
Cdd:PRK07196 271 -----PPATKGYPPSAFsiiprlAESAGNSSGNGTMTAIYTVLAEGDDQQDPIV-DCARAVLDGHIVLSRKLAEAGHYPA 344
|
....*....
gi 501697128 604 VDINASGTR 612
Cdd:PRK07196 345 IDISQSISR 353
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
383-532 |
5.76e-08 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 55.68 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 383 SKLTPLYPDERLRMETTPNRIIG----RLIDIVSPIGKGQRGLIVSPPKAGKTITLqniaNAIAVNNPEVHLMVVLVDER 458
Cdd:PRK05922 119 THLKPLFSSPPSPMSRQPIQEIFptgiKAIDAFLTLGKGQRIGVFSEPGSGKSSLL----STIAKGSKSTINVIALIGER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 459 PEEVTD----------MERTVkgeIISSTFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASG 528
Cdd:PRK05922 195 GREVREyieqhkeglaAQRTI---IIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARG 271
|
....
gi 501697128 529 RILS 532
Cdd:PRK05922 272 ETLS 275
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
408-670 |
7.19e-08 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 55.46 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 408 IDIVSPIGKGQRGLIVSPPKAGKTITLQNIanaiaVNNPEVHLMVV-LVDERPEEVT---------DMERTVkgeIISST 477
Cdd:PRK08472 148 IDGLLTCGKGQKLGIFAGSGVGKSTLMGMI-----VKGCLAPIKVVaLIGERGREIPefieknlggDLENTV---IVVAT 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 478 FDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRI-LSGGvdaqalYPPKKF------FGAA 550
Cdd:PRK08472 220 SDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEPpTSKG------YPPSVLsllpqlMERA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 551 RNIENGGSLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQELPVLYSLR 630
Cdd:PRK08472 294 GKEEGKGSITAFFTVLVE-GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFK 372
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 501697128 631 RLLGGLEPEQ------AYQTLV-PRLKKTMTNADFFKAIVQQGNSSL 670
Cdd:PRK08472 373 RLYSLLKENEvlirigAYQKGNdKELDEAISKKEFMEQFLKQNPNEL 419
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
406-623 |
1.95e-07 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 53.97 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLqnianAIAVNNPEVHLMVV-LVDERPEEVTDMERTVKGE-------IISSt 477
Cdd:PRK05688 157 RSINGLLTVGRGQRLGLFAGTGVGKSVLL-----GMMTRFTEADIIVVgLIGERGREVKEFIEHILGEeglkrsvVVAS- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 478 fdrPASDHTIVAELAIERAKRLVE----LGQDVVVLLDSMTRLARAYNIAAPASGRilsggVDAQALYPPKKFFGAARNI 553
Cdd:PRK05688 231 ---PADDAPLMRLRAAMYCTRIAEyfrdKGKNVLLLMDSLTRFAQAQREIALAIGE-----PPATKGYPPSVFAKLPKLV 302
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501697128 554 E-------NGGSLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTRREELITNPQEL 623
Cdd:PRK05688 303 EragnaepGGGSITAFYTVLSE-GDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHL 378
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
406-612 |
9.89e-07 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 51.71 E-value: 9.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 406 RLIDIVSPIGKGQRGLIVSPPKAGKTITLQNIANAIAVNNpevhLMVVLVDERPEEVTDMERTVKGE-------IISSTF 478
Cdd:PRK07960 164 RAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQADV----IVVGLIGERGREVKDFIENILGAegrarsvVIAAPA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 479 DRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAYNIAAPASGRilsggVDAQALYPPKKFFG-------AAR 551
Cdd:PRK07960 240 DVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGE-----PPATKGYPPSVFAKlpalverAGN 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501697128 552 NIENGGSLTIISSALVEtGSKMDEVIFEEFKGTGNMELRLSRELADKRLFPAVDINASGTR 612
Cdd:PRK07960 315 GISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR 374
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
299-353 |
9.74e-06 |
|
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria and is involved in regulating translation in eukaryotes. Contains sub-family of RNA-binding domains in the Rho transcription termination factor.
Pssm-ID: 214633 [Multi-domain] Cd Length: 64 Bit Score: 43.74 E-value: 9.74e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 501697128 299 GIVDVL-DSYAFIRTSGylpGPNDIYVSMGQIKK--YGLRKGDAVRGYTRAPHEGERR 353
Cdd:smart00357 2 GVVKWFnKGFGFIRPDD---GGKDVFVHPSQIQGglKSLREGDEVEFKVVSPEGGEKP 56
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
5-47 |
1.68e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 47.83 E-value: 1.68e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 501697128 5 QDLSKMKLPELKEIAKELGLRGLSAKRKGDLVAAIEEARAKQS 47
Cdd:PRK09376 4 SELKNKSLSELLELAEELGIENASRLRKQELIFAILKAQAEKG 46
|
|
| SAP |
pfam02037 |
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding ... |
7-42 |
3.69e-04 |
|
SAP domain; The SAP (after SAF-A/B, Acinus and PIAS) motif is a putative DNA/RNA binding domain found in diverse nuclear and cytoplasmic proteins.
Pssm-ID: 460424 [Multi-domain] Cd Length: 35 Bit Score: 38.15 E-value: 3.69e-04
10 20 30
....*....|....*....|....*....|....*.
gi 501697128 7 LSKMKLPELKEIAKELGLRglSAKRKGDLVAAIEEA 42
Cdd:pfam02037 1 LSKLTVAELKEELRKRGLP--TSGKKAELIERLQEY 34
|
|
| PRK14537 |
PRK14537 |
50S ribosomal protein L20/unknown domain fusion protein; Provisional |
3-46 |
9.55e-04 |
|
50S ribosomal protein L20/unknown domain fusion protein; Provisional
Pssm-ID: 237748 [Multi-domain] Cd Length: 230 Bit Score: 41.13 E-value: 9.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 501697128 3 DSQDLSKMKLPELKEIAKELGLRGLSAKRKGDLVAAIEEARAKQ 46
Cdd:PRK14537 187 EHIDLSKMLLKELKKLAKEHKIPNFNKLKKTEIIKALKKALKKK 230
|
|
| spore_III_AA |
TIGR02858 |
stage III sporulation protein AA; Members of this protein are the stage III sporulation ... |
421-460 |
1.29e-03 |
|
stage III sporulation protein AA; Members of this protein are the stage III sporulation protein AA, encoded by one of several genes in the spoIIIA locus. It seems that this protein is found in a species if and only if that species is capable of endospore formation. [Cellular processes, Sporulation and germination]
Pssm-ID: 274324 Cd Length: 270 Bit Score: 41.17 E-value: 1.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 501697128 421 LIVSPPKAGKTITLQNIANAIAVNNPEVHLM---VVLVDERPE 460
Cdd:TIGR02858 115 LIISPPQCGKTTLLRDLARILSTGISQLGLRgkkVGIVDERSE 157
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
408-439 |
1.38e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 41.88 E-value: 1.38e-03
10 20 30
....*....|....*....|....*....|...
gi 501697128 408 IDIVSPIGKGQRGLIVSPPKAGKT-ITLQNIAN 439
Cdd:PRK07165 134 IDLLIPIGKGQRELIIGDRQTGKThIALNTIIN 166
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
416-519 |
1.48e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 39.66 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 416 KGQRGLIVSPPKAGKTITLQNIANAIAVNNPEVhlmVVLVDERPEEVTDMERTVKGEIISSTFDRPASDhtivAELAIER 495
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV---IYIDGEDILEEVLDQLLLIIVGGKKASGSGELR----LRLALAL 73
|
90 100
....*....|....*....|....
gi 501697128 496 AKRLvelgQDVVVLLDSMTRLARA 519
Cdd:smart00382 74 ARKL----KPDVLILDEITSLLDA 93
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
408-520 |
4.00e-03 |
|
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. The alpha-subunit contains a highly conserved adenine-specific noncatalytic nucleotide-binding domain. The conserved amino acid sequence is Gly-X-X-X-X-Gly-Lys. Proton translocating ATP synthase F1, alpha subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), B subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273365 [Multi-domain] Cd Length: 501 Bit Score: 40.06 E-value: 4.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501697128 408 IDIVSPIGKGQRGLIVSPPKAGKT-ITLQNIAN-----------AIAVNNPEVHLMVvlvdERPEEVTDMERTVkgeIIS 475
Cdd:TIGR00962 152 IDAMIPIGRGQRELIIGDRQTGKTaVAIDTIINqkdsdvyciyvAIGQKASTVAQVV----RKLEEHGAMAYTI---VVA 224
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 501697128 476 STFDRPASDHTIVAELAIERAKRLVELGQDVVVLLDSMTRLARAY 520
Cdd:TIGR00962 225 ATASDSASLQYLAPYTGCTMGEYFRDNGKHALIIYDDLSKQAVAY 269
|
|
| |
