|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
293-666 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 786.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 293 EFEGILTGTGVLEIMPDGYGFLRSsdYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLD 372
Cdd:COG1158 2 EDDGLIPVEGVLEILPDGYGFLRS--SNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 373 PGLVRDRVPFDHLTPLFPDEKFKLCKGgySDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYM 452
Cdd:COG1158 80 PEEARKRPDFDNLTPLYPDERLRLETT--PDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 453 IMLLIDERPEEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKV 532
Cdd:COG1158 158 IVLLIDERPEEVTDMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 533 LSGGVDANALHKPKRFFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASS 612
Cdd:COG1158 238 LSGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2796578243 613 TRRDDLLLDKTTLDRMWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLMSMNS 666
Cdd:COG1158 318 TRREELLLSPEELEKVWILRRALSGMDPVEAMEFLLDRLKKTKSNAEFLESMNK 371
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
295-666 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 745.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 295 EGILTGTGVLEIMPDGYGFLRSSDYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLDPG 374
Cdd:PRK09376 46 GGDIFGEGVLEILPDGFGFLRSPDANYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 375 LVRDRVPFDHLTPLFPDEKFKLCKGGySDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYMIM 454
Cdd:PRK09376 126 KARNRPLFENLTPLYPNERLRLETGN-PEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 455 LLIDERPEEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLS 534
Cdd:PRK09376 205 LLIDERPEEVTDMQRSVKGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 535 GGVDANALHKPKRFFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK09376 285 GGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTR 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2796578243 615 RDDLLLDKTTLDRMWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLMSMNS 666
Cdd:PRK09376 365 KEELLLSPEELQKVWILRKILSPMDEVEAMEFLLDKLKKTKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
293-666 |
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: 652.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 293 EFEGILTGTGVLEIMPDGYGFLRSSDYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLD 372
Cdd:TIGR00767 44 EQGGLIFGEGVLEILPDGFGFLRSPDSSYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 373 PGLVRDRVPFDHLTPLFPDEKFKLCKGgySDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYM 452
Cdd:TIGR00767 124 PEKAKNRVLFENLTPLYPNERLRLETS--TEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 453 IMLLIDERPEEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKV 532
Cdd:TIGR00767 202 IVLLIDERPEEVTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 533 LSGGVDANALHKPKRFFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASS 612
Cdd:TIGR00767 282 LSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSG 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2796578243 613 TRRDDLLLDKTTLDRMWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLMSMNS 666
Cdd:TIGR00767 362 TRKEELLLTPEELQKIWVLRKIISPMDSIEAMEFLISKLKKTKTNEEFLESMKR 415
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
404-652 |
2.15e-173 |
|
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: 494.03 E-value: 2.15e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 404 NLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYMIMLLIDERPEEVTDMARSVNAEVIASTFDEP 483
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKGEVVASTFDEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 484 AERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLSGGVDANALHKPKRFFGAARNIEGGGSLTI 563
Cdd:cd01128 81 PERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 564 IATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDRMWILRKYLADMNPIEA 643
Cdd:cd01128 161 IATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIEA 240
|
....*....
gi 2796578243 644 MDFVKSRLE 652
Cdd:cd01128 241 MEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
301-373 |
1.10e-44 |
|
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: 153.68 E-value: 1.10e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796578243 301 TGVLEIMPDGYGFLRSSdyNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLDP 373
Cdd:pfam07497 1 EGILEILPDGYGFLRSS--NYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGEDP 71
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
301-366 |
3.98e-16 |
|
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: 73.02 E-value: 3.98e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796578243 301 TGVLEIMPDGYGFLRSSDYNylsspDDIYVSQSQIK--LFGLKTGDVVEGSIRPPKEGEKYFPLVKVE 366
Cdd:smart00357 1 TGVVKWFNKGFGFIRPDDGG-----KDVFVHPSQIQggLKSLREGDEVEFKVVSPEGGEKPEAENVVK 63
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
6-44 |
2.86e-08 |
|
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: 50.07 E-value: 2.86e-08
10 20 30
....*....|....*....|....*....|....*....
gi 2796578243 6 QLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQA 44
Cdd:pfam07498 1 ELKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQA 39
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
6-47 |
9.57e-08 |
|
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: 48.53 E-value: 9.57e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2796578243 6 QLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQAIVG 47
Cdd:smart00959 1 ELKKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKKG 42
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
2-44 |
1.21e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 51.29 E-value: 1.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2796578243 2 YNIIQLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQA 44
Cdd:PRK09376 1 MNLSELKNKSLSELLELAEELGIENASRLRKQELIFAILKAQA 43
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
2-44 |
1.79e-04 |
|
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: 44.29 E-value: 1.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2796578243 2 YNIIQLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQA 44
Cdd:TIGR00767 1 YNIEELKNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHA 43
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
29-135 |
2.24e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 41.01 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 29 SLKKEElVYKILDEQAIVGATKKVAAAKVNEDRKENQPKKRsrisvkkegdKVYTATKDKAQKLEAATP-TTAAHIAEEA 107
Cdd:PRK12472 226 SLRKLE-RAKARADAELKRADKALAAAKTDEAKARAEERQQ----------KAAQQAAEAATQLDTAKAdAEAKRAAAAA 294
|
90 100
....*....|....*....|....*...
gi 2796578243 108 EKEAVSTVETVQPIQEKAVTEAVEKSEP 135
Cdd:PRK12472 295 TKEAAKAAAAKKAETAKAATDAKLALEP 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
293-666 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 786.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 293 EFEGILTGTGVLEIMPDGYGFLRSsdYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLD 372
Cdd:COG1158 2 EDDGLIPVEGVLEILPDGYGFLRS--SNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 373 PGLVRDRVPFDHLTPLFPDEKFKLCKGgySDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYM 452
Cdd:COG1158 80 PEEARKRPDFDNLTPLYPDERLRLETT--PDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 453 IMLLIDERPEEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKV 532
Cdd:COG1158 158 IVLLIDERPEEVTDMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 533 LSGGVDANALHKPKRFFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASS 612
Cdd:COG1158 238 LSGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSG 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2796578243 613 TRRDDLLLDKTTLDRMWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLMSMNS 666
Cdd:COG1158 318 TRREELLLSPEELEKVWILRRALSGMDPVEAMEFLLDRLKKTKSNAEFLESMNK 371
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
295-666 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 745.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 295 EGILTGTGVLEIMPDGYGFLRSSDYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLDPG 374
Cdd:PRK09376 46 GGDIFGEGVLEILPDGFGFLRSPDANYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 375 LVRDRVPFDHLTPLFPDEKFKLCKGGySDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYMIM 454
Cdd:PRK09376 126 KARNRPLFENLTPLYPNERLRLETGN-PEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 455 LLIDERPEEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLS 534
Cdd:PRK09376 205 LLIDERPEEVTDMQRSVKGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 535 GGVDANALHKPKRFFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK09376 285 GGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTR 364
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2796578243 615 RDDLLLDKTTLDRMWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLMSMNS 666
Cdd:PRK09376 365 KEELLLSPEELQKVWILRKILSPMDEVEAMEFLLDKLKKTKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
293-666 |
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: 652.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 293 EFEGILTGTGVLEIMPDGYGFLRSSDYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLD 372
Cdd:TIGR00767 44 EQGGLIFGEGVLEILPDGFGFLRSPDSSYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 373 PGLVRDRVPFDHLTPLFPDEKFKLCKGgySDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYM 452
Cdd:TIGR00767 124 PEKAKNRVLFENLTPLYPNERLRLETS--TEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 453 IMLLIDERPEEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKV 532
Cdd:TIGR00767 202 IVLLIDERPEEVTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 533 LSGGVDANALHKPKRFFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASS 612
Cdd:TIGR00767 282 LSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSG 361
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2796578243 613 TRRDDLLLDKTTLDRMWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLMSMNS 666
Cdd:TIGR00767 362 TRKEELLLTPEELQKIWVLRKIISPMDSIEAMEFLISKLKKTKTNEEFLESMKR 415
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
7-662 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 589.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 7 LNDKDLSELQSIAKELGITKTESLKKEELVYKIldeQAIVGATKKVAAAKVNEDRKENQPKKRSRISVKKEGDKVYTATK 86
Cdd:PRK12678 23 LAGMKLPELRALAKQLGIKGTSGMRKGELIAAI---KEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 87 DKAQKLEAATPTTAAHIAEEAEKEAVSTVETVQPiQEKAVTEAVEKSEPKKRGRKPGTKNKTAAKTEEQPATTAEETNNT 166
Cdd:PRK12678 100 AKAEAAPAARAAAAAAAEAASAPEAAQARERRER-GEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 167 TPQKVSATNTPKEKEVilpeldfdsdtddfipiEDLPSEKIELPTELLGKFEATKNEAPvptvtpASKFQPRQPREQNPR 246
Cdd:PRK12678 179 EDRQAEAERGERGRRE-----------------ERGRDGDDRDRRDRREQGDRREERGR------RDGGDRRGRRRRRDR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 247 YNNPNQRNNNNYNNQRPTNNNNAEGLES-------------PQQPQQSAPERKpvekpyEFEGILTGTGVLEIMpDGYGF 313
Cdd:PRK12678 236 RDARGDDNREDRGDRDGDDGEGRGGRRGrrfrdrdrrgrrgGDGGNEREPELR------EDDVLVPVAGILDVL-DNYAF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 314 LRSSdyNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGE------KYFPLVKVEKINGLDPGLVRDRVPFDHLTP 387
Cdd:PRK12678 309 VRTS--GYLPGPNDVYVSMNQVRKNGLRKGDAVTGAVRAPREGEqgnqrqKFNPLVRLDSVNGMSPEEAKKRPEFGKLTP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 388 LFPDEKFKLckGGYSDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYMIMLLIDERPEEVTDM 467
Cdd:PRK12678 387 LYPNERLRL--ETEPKKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIANAITTNNPECHLMVVLVDERPEEVTDM 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 468 ARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLSGGVDANALHKPKR 547
Cdd:PRK12678 465 QRSVKGEVIASTFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASGRILSGGVDSTALYPPKR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 548 FFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDR 627
Cdd:PRK12678 545 FFGAARNIENGGSLTIIATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTRKEELLLSPDELAI 624
|
650 660 670
....*....|....*....|....*....|....*
gi 2796578243 628 MWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLM 662
Cdd:PRK12678 625 VHKLRRVLSGLDSQQAIDLLISRLKKTKSNYEFLM 659
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
301-666 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 554.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 301 TGVLEIMPDGYGFLRSSDYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPkegEKYFPLVKVEKINGLDPGLVRDRV 380
Cdd:PRK12608 20 LGVLEILGDGFGFLRSARRNYLPSPDDVFVPPALIRRFNLRTGDVVEGVARPR---ERYRVLVRVDSVNGTDPEKLARRP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 381 PFDHLTPLFPDEKFKLCKGgySDNLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYMIMLLIDER 460
Cdd:PRK12608 97 HFDDLTPLHPRERLRLETG--SDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLLIDER 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 461 PEEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLSGGVDAN 540
Cdd:PRK12608 175 PEEVTDMRRSVKGEVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSGGVDAR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 541 ALHKPKRFFGAARNIEGGGSLTIIATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLL 620
Cdd:PRK12608 255 ALQRPKRLFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRREELLL 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2796578243 621 DKTTLDRMWILRKYLADMNPIEAMDFVKSRLENTRDNEEFLMSMNS 666
Cdd:PRK12608 335 DSKELEKVRRLRRALASRKPVEAMEALLEKLRETPDNAEFLNSVQP 380
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
404-652 |
2.15e-173 |
|
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: 494.03 E-value: 2.15e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 404 NLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEVYMIMLLIDERPEEVTDMARSVNAEVIASTFDEP 483
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKGEVVASTFDEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 484 AERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLSGGVDANALHKPKRFFGAARNIEGGGSLTI 563
Cdd:cd01128 81 PERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 564 IATALIDTGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDRMWILRKYLADMNPIEA 643
Cdd:cd01128 161 IATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIEA 240
|
....*....
gi 2796578243 644 MDFVKSRLE 652
Cdd:cd01128 241 MEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
301-373 |
1.10e-44 |
|
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: 153.68 E-value: 1.10e-44
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2796578243 301 TGVLEIMPDGYGFLRSSdyNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEKINGLDP 373
Cdd:pfam07497 1 EGILEILPDGYGFLRSS--NYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGEDP 71
|
|
| Rho_CSD |
cd04459 |
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination ... |
300-367 |
4.06e-39 |
|
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: 138.14 E-value: 4.06e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796578243 300 GTGVLEIMPDGYGFLRSSDYNYLSSPDDIYVSQSQIKLFGLKTGDVVEGSIRPPKEGEKYFPLVKVEK 367
Cdd:cd04459 1 GSGVLEILPDGFGFLRSSGYNYLPGPDDIYVSPSQIRRFNLRTGDTVVGQIRPPKEGERYFALLKVEA 68
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
408-611 |
4.86e-27 |
|
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: 108.98 E-value: 4.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTD----------MARSVnaeVIA 477
Cdd:pfam00006 3 RAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD----VVVYALIGERGREVREfieellgsgaLKRTV---VVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPA-ERhvKIAGIVlekAKRMVE----CGHDVVIFLDSITRLARAYNTVSPASGKVLS-----GGVDanALHkPK- 546
Cdd:pfam00006 76 ATSDEPPlAR--YRAPYT---ALTIAEyfrdQGKDVLLIMDSLTRFAEALREISLALGEPPGregypPSVF--SLL-ARl 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2796578243 547 --RffgAARNIEGGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVAS 611
Cdd:pfam00006 148 leR---AGRVKGKGGSITALPTVLVP-GDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLAS 210
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
408-614 |
1.25e-23 |
|
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: 100.71 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAAnhpEVYMIMlLIDERPEEVTD----------MARSVnaeVIA 477
Cdd:cd01136 56 RAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARNTDA---DVNVIA-LIGERGREVREfiekdlgeegLKRSV---LVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVL-SGGVDANALHKPKRFFGAARNIE 556
Cdd:cd01136 129 ATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPtRRGYPPSVFALLPRLLERAGNGE 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2796578243 557 gGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:cd01136 209 -KGSITAFYTVLVE-GDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
408-614 |
2.18e-22 |
|
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: 97.53 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHPEvYMIMLLIDERPEEVTD----------MARSVnaeVIA 477
Cdd:cd19476 56 KVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAG-VVVFAGIGERGREVNDlyeeftksgaMERTV---VVA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLSG-GVDANALHKPKRFFG-AARNI 555
Cdd:cd19476 132 NTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALREMSALLGEPPGReGYPPYLFTKLATLYErAGKVK 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796578243 556 EGGGSLTIIATALIDTGSKMDEV---IFEEFKGTgnmeLQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:cd19476 212 DGGGSITAIPAVSTPGDDLTDPIpdnTFAILDGQ----IVLSRELARKGIYPAINVLDSTSR 269
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
408-614 |
4.56e-17 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 84.00 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTD----------MARSVnaeVIA 477
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSAD----LNVIALIGERGREVREfierdlgpegLKRSI---VVV 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASG-----KVLSGGVDANAlhkPKRFFGAA 552
Cdd:PRK07721 220 ATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAMAQREIGLAVGeppttKGYTPSVFAIL---PKLLERTG 296
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796578243 553 RNieGGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK07721 297 TN--ASGSITAFYTVLVD-GDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSR 355
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
301-366 |
3.98e-16 |
|
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: 73.02 E-value: 3.98e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796578243 301 TGVLEIMPDGYGFLRSSDYNylsspDDIYVSQSQIK--LFGLKTGDVVEGSIRPPKEGEKYFPLVKVE 366
Cdd:smart00357 1 TGVVKWFNKGFGFIRPDDGG-----KDVFVHPSQIQggLKSLREGDEVEFKVVSPEGGEKPEAENVVK 63
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
408-642 |
5.79e-16 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 80.63 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTDM----------ARSVnaeVIA 477
Cdd:PRK06820 152 RAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADSAAD----VMVLALIGERGREVREFleqvltpearARTV---VVV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKV-LSGGVDANALHKPKRFFGAARNIE 556
Cdd:PRK06820 225 ATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREIGLAAGEPpAAGSFPPSVFANLPRLLERTGNSD 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 557 gGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDRMWILRKYLA 636
Cdd:PRK06820 305 -RGSITAFYTVLVE-GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLA 382
|
....*.
gi 2796578243 637 DMNPIE 642
Cdd:PRK06820 383 CYQEIE 388
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
408-644 |
1.12e-15 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 80.00 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEV--------TDMARSVNAEVIAsT 479
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDAD----SNVLVLIGERGREVrefidftlSEETRKRCVIVVA-T 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 480 FDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLSGGVdanalHKPKRFFGAARNIEGG- 558
Cdd:PRK07594 219 SDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGE-----YPPGVFSALPRLLERTg 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 559 ----GSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDRMWILRKY 634
Cdd:PRK07594 294 mgekGSITAFYTVLVE-GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRC 372
|
250
....*....|
gi 2796578243 635 LADMNPIEAM 644
Cdd:PRK07594 373 LALYQEVELL 382
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
408-614 |
4.51e-14 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 74.65 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAAnhpEVYMIMLlIDERPEEVTD----MARSVNAE---VIASTF 480
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEA---DVFVIGL-IGERGREVTEfvesLRASSRREkcvLVYATS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 481 DEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKV-LSGGVDANA-------LHKPKRFfgaa 552
Cdd:PRK08149 216 DFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDVALAAGELpARRGYPASVfdslprlLERPGAT---- 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796578243 553 rnieGGGSLTIIATALIDTGSKMDeVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK08149 292 ----LAGSITAFYTVLLESEEEPD-PIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR 348
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
408-656 |
5.00e-13 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 71.57 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHpevyMIMLLIDERPEEVTD---------MARSVnaeVIAS 478
Cdd:PRK06002 154 RVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDT----VVIALVGERGREVREfledtladnLKKAV---AVVA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 479 TFDE-PAERhvKIAGIVlekAKRMVE----CGHDVVIFLDSITRLARAYNTVSPASGK-VLSGGVDANALHK-PKRFFGA 551
Cdd:PRK06002 227 TSDEsPMMR--RLAPLT---ATAIAEyfrdRGENVLLIVDSVTRFAHAAREVALAAGEpPVARGYPPSVFSElPRLLERA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 552 ARNIEGGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRrddlLLDKT-TLDRMWI 630
Cdd:PRK06002 302 GPGAEGGGSITGIFSVLVD-GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR----LARHAwTPEQRKL 376
|
250 260
....*....|....*....|....*.
gi 2796578243 631 LRKyladmnpIEAMdfvKSRLENTRD 656
Cdd:PRK06002 377 VSR-------LKSM---IARFEETRD 392
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
405-642 |
1.92e-12 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 69.78 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 405 LSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTD----------MARSVnae 474
Cdd:PRK06936 148 LGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD----VTVLALIGERGREVREfiesdlgeegLRKAV--- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 475 VIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKvlsggVDANALHKPKRFFGAARN 554
Cdd:PRK06936 221 LVVATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGE-----PPTRRGYPPSVFAALPRL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 555 IEGG-----GSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDRMW 629
Cdd:PRK06936 296 MERAgqsdkGSITALYTVLVE-GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAG 374
|
250
....*....|...
gi 2796578243 630 ILRKYLADMNPIE 642
Cdd:PRK06936 375 RLRELLAKYEEVE 387
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
405-614 |
4.12e-12 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 68.85 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 405 LSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAAnhpEVYMIMLlIDERPEEVTD----------MARSVnae 474
Cdd:PRK08927 144 LGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADA---DVSVIGL-IGERGREVQEflqddlgpegLARSV--- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 475 VIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASG-----KVLSGGVDANAlhkPKRFF 549
Cdd:PRK08927 217 VVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREIGLSAGeppttKGYTPTVFAEL---PRLLE 293
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2796578243 550 GAARNIEGGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK08927 294 RAGPGPIGEGTITGLFTVLVD-GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
408-644 |
8.33e-12 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 67.87 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAAnhpEVYMIMlLIDERPEEVTD----------MARSVnaeVIA 477
Cdd:PRK09099 152 RIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC---DVNVIA-LIGERGREVREfielilgedgMARSV---VVC 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKvlsggVDANALHKPKRFFGAARNIE- 556
Cdd:PRK09099 225 ATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARAQREIGLAAGE-----PPARRGFPPSVFAELPRLLEr 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 557 ----GGGSLTIIATALI--DTGSkmdEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDRMWI 630
Cdd:PRK09099 300 agmgETGSITALYTVLAedESGS---DPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQAAGR 376
|
250
....*....|....
gi 2796578243 631 LRKYLADMNPIEAM 644
Cdd:PRK09099 377 LRQLLAKHREVETL 390
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
408-611 |
2.27e-11 |
|
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: 66.21 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAAnhpEVYMIMLlIDERPEEVTD----------MARSVnaeVIA 477
Cdd:COG1157 146 RAIDGLLTVGRGQRIGIFAGSGVGKSTLLGMIARNTEA---DVNVIAL-IGERGREVREfieddlgeegLARSV---VVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAerhvkiagivLEKAK------------RmvECGHDVVIFLDSITRLARA----------------YntvsPAS 529
Cdd:COG1157 219 ATSDEPP----------LMRLRaaytataiaeyfR--DQGKNVLLLMDSLTRFAMAqreiglaageppatrgY----PPS 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 530 gkVLSggvdanALhkpkrffgaARNIE-----GGGSLTIIATALIDtGSKMDEVIFEEFKGT--GNmeLQLDRNLSNKRI 602
Cdd:COG1157 283 --VFA------LL---------PRLLEragngGKGSITAFYTVLVE-GDDMNDPIADAVRGIldGH--IVLSRKLAERGH 342
|
....*....
gi 2796578243 603 FPAVNIVAS 611
Cdd:COG1157 343 YPAIDVLAS 351
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
404-614 |
2.59e-11 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 66.07 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 404 NLSARVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTD----------MARSVna 473
Cdd:PRK07196 140 DVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD----VVVVGLIGERGREVKEfiehslqaagMAKSV-- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 474 eVIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGK-VLSGGVDANALHKPKRFFGAA 552
Cdd:PRK07196 214 -VVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREIALSLGEpPATKGYPPSAFSIIPRLAESA 292
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796578243 553 RNIEGGGSLTIIATALIDTGSKMDEVIfEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK07196 293 GNSSGNGTMTAIYTVLAEGDDQQDPIV-DCARAVLDGHIVLSRKLAEAGHYPAIDISQSISR 353
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
369-562 |
3.98e-10 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 62.61 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 369 NGLDPGlvrDRVPFDHLTPLFPDEKFKLCKGGYSDNLSA--RVVDMFAPIGKGQRALIVAQPKTGKTILMkdiaNAIAAN 446
Cdd:PRK05922 108 NPLDGK---EQLPKTHLKPLFSSPPSPMSRQPIQEIFPTgiKAIDAFLTLGKGQRIGVFSEPGSGKSSLL----STIAKG 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 447 HPEVYMIMLLIDERPEEVTDM----ARSVNAE---VIASTFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLA 519
Cdd:PRK05922 181 SKSTINVIALIGERGREVREYieqhKEGLAAQrtiIIASPAHETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWI 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2796578243 520 RAYNTVSPASGKVLSG-GVDANALHKPKRFFGAARNIEgGGSLT 562
Cdd:PRK05922 261 AALQEVALARGETLSAhHYAASVFHHVSEFTERAGNND-KGSIT 303
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
408-614 |
5.88e-10 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 61.92 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTDMARSVNAE-------VIASTF 480
Cdd:PRK06793 145 KSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD----INVISLVGERGREVKDFIRKELGEegmrksvVVVATS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 481 DEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGKVLSGG---VDANALHKPKRFFGAARNieg 557
Cdd:PRK06793 221 DESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVDIAVKELPIGGktlLMESYMKKLLERSGKTQK--- 297
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2796578243 558 gGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK06793 298 -GSITGIYTVLVD-GDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSR 352
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
408-636 |
8.80e-09 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 58.26 E-value: 8.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTD----------MARSVnaeVIA 477
Cdd:PRK07960 164 RAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARYTQAD----VIVVGLIGERGREVKDfienilgaegRARSV---VIA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGK-VLSGGVDANALHK-PKRFFGAARNI 555
Cdd:PRK07960 237 APADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEpPATKGYPPSVFAKlPALVERAGNGI 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 556 EGGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTRRDDLLLDKTTLDRMWILRKYL 635
Cdd:PRK07960 317 SGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLL 395
|
.
gi 2796578243 636 A 636
Cdd:PRK07960 396 S 396
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
6-44 |
2.86e-08 |
|
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: 50.07 E-value: 2.86e-08
10 20 30
....*....|....*....|....*....|....*....
gi 2796578243 6 QLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQA 44
Cdd:pfam07498 1 ELKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQA 39
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
6-47 |
9.57e-08 |
|
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: 48.53 E-value: 9.57e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2796578243 6 QLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQAIVG 47
Cdd:smart00959 1 ELKKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKKG 42
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
410-614 |
1.33e-07 |
|
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: 54.70 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 410 VDMFAPIGKGQRALIVAQPKTGKTILMKDiaNAIAANHPEVYMIMLLIDERPEEVTDMARSV-------NAEVIASTFDE 482
Cdd:TIGR00962 152 IDAMIPIGRGQRELIIGDRQTGKTAVAID--TIINQKDSDVYCIYVAIGQKASTVAQVVRKLeehgamaYTIVVAATASD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 483 PAERH--VKIAGIVLekAKRMVECGHDVVIFLDSITRLARAYNTVS-----PASGKVLSGGVdanalhkpkrFFGAARNI 555
Cdd:TIGR00962 230 SASLQylAPYTGCTM--GEYFRDNGKHALIIYDDLSKQAVAYRQISlllrrPPGREAFPGDV----------FYLHSRLL 297
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2796578243 556 E---------GGGSLT---IIAT------ALIDTG--SKMDEVIFeefkgtgnmelqLDRNLSNKRIFPAVNIVASSTR 614
Cdd:TIGR00962 298 EraaklndekGGGSLTalpIIETqagdvsAYIPTNviSITDGQIF------------LESDLFNSGIRPAINVGLSVSR 364
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
2-44 |
1.21e-06 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 51.29 E-value: 1.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2796578243 2 YNIIQLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQA 44
Cdd:PRK09376 1 MNLSELKNKSLSELLELAEELGIENASRLRKQELIFAILKAQA 43
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
417-614 |
1.32e-06 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 51.22 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 417 GKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTDMARS------VNAEVIASTFDEPAERHVKI 490
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMIVKGCLAP----IKVVALIGERGREIPEFIEKnlggdlENTVIVVATSDDSPLMRKYG 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 491 AGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGK-VLSGGVDANALHKPKRFFGAARNIEGGGSLTIIATALI 569
Cdd:PRK08472 231 AFCAMSVAEYFKNQGLDVLFIMDSVTRFAMAQREIGLALGEpPTSKGYPPSVLSLLPQLMERAGKEEGKGSITAFFTVLV 310
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2796578243 570 DtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK08472 311 E-GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASR 354
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
408-614 |
2.38e-06 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 50.50 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANhpevYMIMLLIDERPEEVTD----------MARSVnaeVIA 477
Cdd:PRK05688 157 RSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD----IIVVGLIGERGREVKEfiehilgeegLKRSV---VVA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 478 STFDEPAERHVKIAGIVLEKAKRMVECGHDVVIFLDSITRLARAYNTVSPASGK-VLSGGVDANALHKPKRFFGAARNIE 556
Cdd:PRK05688 230 SPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQREIALAIGEpPATKGYPPSVFAKLPKLVERAGNAE 309
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2796578243 557 -GGGSLTIIATALIDtGSKMDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PRK05688 310 pGGGSITAFYTVLSE-GDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISR 367
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
408-614 |
1.32e-05 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 48.37 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIanAIAANHPEVYMIMLLIDERP---EEVTDMARSVNAE-----VIAST 479
Cdd:PRK13343 151 KVVDALIPIGRGQRELIIGDRQTGKTAIAIDA--IINQKDSDVICVYVAIGQKAsavARVIETLREHGALeyttvVVAEA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 480 FDEPAERHVK-IAGIVLEKAKRmvECGHDVVIFLDSITRLARAYNTVS-----PASGKVLSGGVdanalhkpkrFFGAAR 553
Cdd:PRK13343 229 SDPPGLQYLApFAGCAIAEYFR--DQGQDALIVYDDLSKHAAAYRELSlllrrPPGREAYPGDI----------FYLHSR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 554 NIE---------GGGSLT---IIAT------ALIDTG--SKMDEVIFeefkgtgnmelqLDRNLSNKRIFPAVNIVASST 613
Cdd:PRK13343 297 LLEraaklspelGGGSLTalpIIETlagelsAYIPTNliSITDGQIY------------LDSDLFAAGQRPAVDVGLSVS 364
|
.
gi 2796578243 614 R 614
Cdd:PRK13343 365 R 365
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
410-614 |
3.09e-05 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 46.01 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 410 VDMFAPIGKGQRALIVAQPKTGKTILMKD-IANAIAANhpeVYMIMLLIDERPEEVtdmARSVNA----------EVIAS 478
Cdd:cd01132 60 IDSLIPIGRGQRELIIGDRQTGKTAIAIDtIINQKGKK---VYCIYVAIGQKRSTV---AQIVKTleehgameytIVVAA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 479 TFDEPAERHVKI--AGIVLekAKRMVECGHDVVIFLDSITRLARAYNTVS-----PASGKVLSGgvDANALHK--PKRff 549
Cdd:cd01132 134 TASDPAPLQYLApyAGCAM--GEYFRDNGKHALIIYDDLSKQAVAYRQMSlllrrPPGREAYPG--DVFYLHSrlLER-- 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2796578243 550 gAAR--NIEGGGSLT---IIAT------ALIDTG--SKMDEVIFeefkgtgnmelqLDRNLSNKRIFPAVNIVASSTR 614
Cdd:cd01132 208 -AAKlsDELGGGSLTalpIIETqagdvsAYIPTNviSITDGQIF------------LESELFNKGIRPAINVGLSVSR 272
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
418-521 |
6.81e-05 |
|
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: 43.52 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 418 KGQRALIVAQPKTGKTILMKDIANAIAANHPEVYMIMLliderpeEVTDMARSVNAEVIASTFDEPAERHVKIAGIVLEK 497
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
|
90 100
....*....|....*....|....
gi 2796578243 498 AKRMVECghdvVIFLDSITRLARA 521
Cdd:smart00382 74 ARKLKPD----VLILDEITSLLDA 93
|
|
| RecA-like_superfamily |
cd01120 |
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ... |
423-578 |
7.28e-05 |
|
RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain] Cd Length: 119 Bit Score: 42.88 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 423 LIVAQPKTGKTILMKDIANAIAANHPEVYMIMLLIDerpeevtdmarsvnaeviastfdepaerhvkiagiVLEKAKRMV 502
Cdd:cd01120 2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFISFLDT-----------------------------------ILEAIEDLI 46
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2796578243 503 ECGHDVVIFLDSITRLARAYntvspasgkvlSGGVDANALHKPKRFFGAARNieggGSLTIIATALIDTGSKMDEV 578
Cdd:cd01120 47 EEKKLDIIIIDSLSSLARAS-----------QGDRSSELLEDLAKLLRAARN----TGITVIATIHSDKFDIDRGG 107
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
2-44 |
1.79e-04 |
|
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: 44.29 E-value: 1.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2796578243 2 YNIIQLNDKDLSELQSIAKELGITKTESLKKEELVYKILDEQA 44
Cdd:TIGR00767 1 YNIEELKNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHA 43
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
408-614 |
2.67e-04 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 44.26 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKT-ILMKDIANAIAANHP-----EVYMIMLLIDERPEEVTDMARSVNA-------E 474
Cdd:PTZ00185 178 KAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQVRINQQilsknAVISIYVSIGQRCSNVARIHRLLRSygalrytT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 475 VIASTFDEPA--ERHVKIAGIVLekAKRMVECGHDVVIFLDSITRLARAYNTVS-----PASGKVLSGgvDANALHkpKR 547
Cdd:PTZ00185 258 VMAATAAEPAglQYLAPYSGVTM--GEYFMNRGRHCLCVYDDLSKQAVAYRQISlllrrPPGREAYPG--DVFYLH--SR 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796578243 548 FFGAARNI---EGGGSLTiiATALIDTGSK-MDEVIFEEFKGTGNMELQLDRNLSNKRIFPAVNIVASSTR 614
Cdd:PTZ00185 332 LLERAAMLspgKGGGSVT--ALPIVETLSNdVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
409-433 |
3.55e-04 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 43.42 E-value: 3.55e-04
10 20
....*....|....*....|....*
gi 2796578243 409 VVDMFAPIGKGQRALIVAQPKTGKT 433
Cdd:PRK07165 133 AIDLLIPIGKGQRELIIGDRQTGKT 157
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
408-534 |
1.68e-03 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 40.67 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 408 RVVDMFAPIGKGQRALIVAQPKTGKTILMKDIANAIAANHpEVYMIMLLIDERPEEVTD----MARS--VNAEVIAST-- 479
Cdd:cd01133 56 KVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNIAKAH-GGYSVFAGVGERTREGNDlyheMKESgvINLDGLSKVal 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2796578243 480 ----FDEP--AERHVKIAGIVLEKAKRMVEcGHDVVIFLDSITRLARAYNTVSPASGKVLS 534
Cdd:cd01133 135 vygqMNEPpgARARVALTGLTMAEYFRDEE-GQDVLLFIDNIFRFTQAGSEVSALLGRIPS 194
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
29-135 |
2.24e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 41.01 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 29 SLKKEElVYKILDEQAIVGATKKVAAAKVNEDRKENQPKKRsrisvkkegdKVYTATKDKAQKLEAATP-TTAAHIAEEA 107
Cdd:PRK12472 226 SLRKLE-RAKARADAELKRADKALAAAKTDEAKARAEERQQ----------KAAQQAAEAATQLDTAKAdAEAKRAAAAA 294
|
90 100
....*....|....*....|....*...
gi 2796578243 108 EKEAVSTVETVQPIQEKAVTEAVEKSEP 135
Cdd:PRK12472 295 TKEAAKAAAAKKAETAKAATDAKLALEP 322
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
423-522 |
2.54e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 39.90 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 423 LIVAQPKTGKTILMKDIANAIAANHPEVYMIMLliDERPEEVTDMARSVN---AEVIAST----FDEPAERHVKIAGIVL 495
Cdd:COG0467 24 LLSGPPGTGKTTLALQFLAEGLRRGEKGLYVSF--EESPEQLLRRAESLGldlEEYIESGllriIDLSPEELGLDLEELL 101
|
90 100
....*....|....*....|....*..
gi 2796578243 496 EKAKRMVECGHDVVIFLDSITRLARAY 522
Cdd:COG0467 102 ARLREAVEEFGAKRVVIDSLSGLLLAL 128
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
10-181 |
2.75e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 10 KDLSELQSIAKELGITKTESLKKEELVYKILDEQAIVGATKKVAAAKVNED--RKENQPKKRSRISVKKEGDKvytATKD 87
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEakKKAEEAKKKADEAKKAAEAK---KKAD 1513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 88 KAQKLEAATPTTAAHIAEEAEK-EAVSTVETVQPIQEKAVTEAVEKSEPKKRG---------RKPGTKNKTAAKTEEQPA 157
Cdd:PTZ00121 1514 EAKKAEEAKKADEAKKAEEAKKaDEAKKAEEKKKADELKKAEELKKAEEKKKAeeakkaeedKNMALRKAEEAKKAEEAR 1593
|
170 180
....*....|....*....|....
gi 2796578243 158 TTAEETNNTTPQKVSATNTPKEKE 181
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEE 1617
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
10-154 |
5.70e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 10 KDLSELQSIAKELGITKTESLKKEELVYKILDEQAIVGATKKVAAAKVNEDRKENQPKKRSRISVKKEGDKVYTATKDKA 89
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 90 QKLEAATPTTAAHIAEEAEKEAvstVETVQPIQEKAVTEAVEKSEPKKRG---RKPGTKNKT--AAKTEE 154
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKA---DEAKKAAEAKKKADEAKKAEEAKKAdeaKKAEEAKKAdeAKKAEE 1544
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
9-155 |
8.94e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2796578243 9 DKDLSELQSIAKELGITKTESLKKEELVYKILDEQAIVGATKKVAAAKVN-EDRKENQPKKRSRISVKKEGDKVYTATKD 87
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2796578243 88 KAQKLEAATPTTAAHIAEEAEK--EAVSTVETVQPIQE--KAVTEAVEKSEPKKRGRKPGTKNKTAAKTEEQ 155
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEakKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
|
| |
