|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
173-532 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 721.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 173 GVLEILPDGFGFLRGSNYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPDTAIQRNAFE 252
Cdd:COG1158 11 GVLEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGEDPEEARKRPDFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 253 TLTPIFPEERLTLETNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPEEVT 332
Cdd:COG1158 91 NLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHLIVLLIDERPEEVT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 333 DMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGALHGP 412
Cdd:COG1158 171 DMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRTLSGGVDANALYKP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 413 KKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEK 492
Cdd:COG1158 251 KRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSGTRREELLLSPEEL 330
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489533121 493 TALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSIK 532
Cdd:COG1158 331 EKVWILRRALSGMDPVEAMEFLLDRLKKTKSNAEFLESMN 370
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
173-533 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 661.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 173 GVLEILPDGFGFLRGS--NYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPDTAIQRNA 250
Cdd:PRK09376 53 GVLEILPDGFGFLRSPdaNYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 251 FETLTPIFPEERLTLET-NRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPE 329
Cdd:PRK09376 133 FENLTPLYPNERLRLETgNPEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDERPE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 330 EVTDMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGAL 409
Cdd:PRK09376 213 EVTDMQRSVKGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLSGGVDANAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 410 HGPKKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDD 489
Cdd:PRK09376 293 HRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEELLLSP 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489533121 490 EEKTALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSIKN 533
Cdd:PRK09376 373 EELQKVWILRKILSPMDEVEAMEFLLDKLKKTKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
173-533 |
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: 577.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 173 GVLEILPDGFGFLRG--SNYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPDTAIQRNA 250
Cdd:TIGR00767 53 GVLEILPDGFGFLRSpdSSYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 251 FETLTPIFPEERLTLETNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPEE 330
Cdd:TIGR00767 133 FENLTPLYPNERLRLETSTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERPEE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 331 VTDMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGALH 410
Cdd:TIGR00767 213 VTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSGGVDANALH 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 411 GPKKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDE 490
Cdd:TIGR00767 293 RPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPE 372
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489533121 491 EKTALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSIKN 533
Cdd:TIGR00767 373 ELQKIWVLRKIISPMDSIEAMEFLISKLKKTKTNEEFLESMKR 415
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
271-519 |
7.56e-166 |
|
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: 469.76 E-value: 7.56e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 271 EIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPEEVTDMKESIEGDVIYSTFDQV 350
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKGEVVASTFDEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 351 SSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGALHGPKKFFGAARNIRQGGSLTI 430
Cdd:cd01128 81 PERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 431 LGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKTALWRLRREMSNNSVMEI 510
Cdd:cd01128 161 IATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIEA 240
|
....*....
gi 489533121 511 TDKVIELIK 519
Cdd:cd01128 241 MEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
173-243 |
1.87e-37 |
|
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: 132.50 E-value: 1.87e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489533121 173 GVLEILPDGFGFLRGSNYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPD 243
Cdd:pfam07497 2 GILEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGEDPE 72
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
173-231 |
1.94e-09 |
|
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: 53.76 E-value: 1.94e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489533121 173 GVLEILPDGFGFLRGSNYLStegDVYVSPSQI--RRFNMKTGDKIKGITRHPKSGEKFRAL 231
Cdd:smart00357 2 GVVKWFNKGFGFIRPDDGGK---DVFVHPSQIqgGLKSLREGDEVEFKVVSPEGGEKPEAE 59
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
16-56 |
1.60e-07 |
|
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: 47.76 E-value: 1.60e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489533121 16 LGSKTLVELREIAKELKIKSITTYKKNELI-EIINSKSKNEE 56
Cdd:pfam07498 2 LKEKTLSELREIAKELGIENYSRLRKQELIfAILKAQAEKGG 43
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
16-56 |
2.37e-07 |
|
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: 46.98 E-value: 2.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489533121 16 LGSKTLVELREIAKELKIKSITTYKKNELI-EIINSKSKNEE 56
Cdd:smart00959 2 LKKKTLSELLEIAKELGIENASRLRKQELIfAILKAQAKKGG 43
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
18-91 |
1.75e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 1.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489533121 18 SKTLVELREIAKELKI--KSITTYKKNELIEIINSKSKNEEKVNEETKEKNEDIKEdIKNRKENIEREsiEKEVEY 91
Cdd:PRK05771 56 SEALDKLRSYLPKLNPlrEEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISE-LENEIKELEQE--IERLEP 128
|
|
| COG5124 |
COG5124 |
Protein predicted to be involved in meiotic recombination [Cell division and chromosome ... |
11-144 |
2.98e-03 |
|
Protein predicted to be involved in meiotic recombination [Cell division and chromosome partitioning / General function prediction only];
Pssm-ID: 227453 [Multi-domain] Cd Length: 209 Bit Score: 39.17 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 11 KVLEGLGSK---TLVELREIAKELKIKSITTYKKNELIEII----NSKSKNEEKVNEETKEKNEDIKEDIKNRKENIERE 83
Cdd:COG5124 29 KEVEKLGSKkqiVLMTVKDLLQQLVDDGVVSVEKCGTSNIYwsfkSQTLQKLYDSSELLKKKIQEVKQDIATYKEEIDKE 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489533121 84 SIEKEVEYKSPTKSYNKKEIDTQNISQNQEHRNQRNDYNKTTSVNDSNKSSNISNRMVRNN 144
Cdd:COG5124 109 KATRRKKFTEGQKNYNREALLEKRKKEQDEIKKKLNSLQKIEPIRWDAAKIQEKKKKVHLN 169
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
173-532 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 721.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 173 GVLEILPDGFGFLRGSNYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPDTAIQRNAFE 252
Cdd:COG1158 11 GVLEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGEDPEEARKRPDFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 253 TLTPIFPEERLTLETNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPEEVT 332
Cdd:COG1158 91 NLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHLIVLLIDERPEEVT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 333 DMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGALHGP 412
Cdd:COG1158 171 DMQRSVKGEVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRTLSGGVDANALYKP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 413 KKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEK 492
Cdd:COG1158 251 KRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSGTRREELLLSPEEL 330
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489533121 493 TALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSIK 532
Cdd:COG1158 331 EKVWILRRALSGMDPVEAMEFLLDRLKKTKSNAEFLESMN 370
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
173-533 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 661.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 173 GVLEILPDGFGFLRGS--NYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPDTAIQRNA 250
Cdd:PRK09376 53 GVLEILPDGFGFLRSPdaNYLPGPDDIYVSPSQIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 251 FETLTPIFPEERLTLET-NRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPE 329
Cdd:PRK09376 133 FENLTPLYPNERLRLETgNPEDLSTRIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDERPE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 330 EVTDMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGAL 409
Cdd:PRK09376 213 EVTDMQRSVKGEVVASTFDEPAERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLSGGVDANAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 410 HGPKKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDD 489
Cdd:PRK09376 293 HRPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEELLLSP 372
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 489533121 490 EEKTALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSIKN 533
Cdd:PRK09376 373 EELQKVWILRKILSPMDEVEAMEFLLDKLKKTKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
173-533 |
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: 577.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 173 GVLEILPDGFGFLRG--SNYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPDTAIQRNA 250
Cdd:TIGR00767 53 GVLEILPDGFGFLRSpdSSYLPGPDDIYVSPSQIRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 251 FETLTPIFPEERLTLETNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPEE 330
Cdd:TIGR00767 133 FENLTPLYPNERLRLETSTEDLSTRVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERPEE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 331 VTDMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGALH 410
Cdd:TIGR00767 213 VTDMQRSVKGEVVASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSGGVDANALH 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 411 GPKKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDE 490
Cdd:TIGR00767 293 RPKRFFGAARNIEEGGSLTIIATALIDTGSRMDEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPE 372
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 489533121 491 EKTALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSIKN 533
Cdd:TIGR00767 373 ELQKIWVLRKIISPMDSIEAMEFLISKLKKTKTNEEFLESMKR 415
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
99-531 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 571.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 99 NKKEIDTQNISQNQEHRNQRNDYNKTTSVNDSNKSSN--------ISNRMVRNNNKNYYMPKQVDESKIVDefNTSKEDE 170
Cdd:PRK12678 214 RREERGRRDGGDRRGRRRRRDRRDARGDDNREDRGDRdgddgegrGGRRGRRFRDRDRRGRRGGDGGNERE--PELREDD 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 171 VV----GVLEILpDGFGFLRGSNYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGE------KFRALLYVQKINDE 240
Cdd:PRK12678 292 VLvpvaGILDVL-DNYAFVRTSGYLPGPNDVYVSMNQVRKNGLRKGDAVTGAVRAPREGEqgnqrqKFNPLVRLDSVNGM 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 241 NPDTAIQRNAFETLTPIFPEERLTLETNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELI 320
Cdd:PRK12678 371 SPEEAKKRPEFGKLTPLYPNERLRLETEPKKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIANAITTNNPECHLM 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 321 VLLIDERPEEVTDMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTL 400
Cdd:PRK12678 451 VVLVDERPEEVTDMQRSVKGEVIASTFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASGRIL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 401 SGGIDPGALHGPKKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGT 480
Cdd:PRK12678 531 SGGVDSTALYPPKRFFGAARNIENGGSLTIIATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGT 610
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 489533121 481 RRDDLLLDDEEKTALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSI 531
Cdd:PRK12678 611 RKEELLLSPDELAIVHKLRRVLSGLDSQQAIDLLISRLKKTKSNYEFLMQV 661
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
150-531 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 533.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 150 MPKQVDESKIVDEfntSKEDEVVGVLEILPDGFGFLRGS--NYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRhpkSGEK 227
Cdd:PRK12608 1 MATKTLELPTLQK---QSTEEVLGVLEILGDGFGFLRSArrNYLPSPDDVFVPPALIRRFNLRTGDVVEGVAR---PRER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 228 FRALLYVQKINDENPDTAIQRNAFETLTPIFPEERLTLETNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVA 307
Cdd:PRK12608 75 YRVLVRVDSVNGTDPEKLARRPHFDDLTPLHPRERLRLETGSDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 308 NSIAKNHPNVELIVLLIDERPEEVTDMKESIEGDVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLAR 387
Cdd:PRK12608 155 AAVAANHPEVHLMVLLIDERPEEVTDMRRSVKGEVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLAR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 388 AYNLTISPTGRTLSGGIDPGALHGPKKFFGAARNIRQGGSLTILGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEK 467
Cdd:PRK12608 235 AYNNEVESSGRTLSGGVDARALQRPKRLFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMEIVLDRELADK 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489533121 468 RIFPAIDIYKSGTRRDDLLLDDEEKTALWRLRREMSNNSVMEITDKVIELIKRTKDNKEFVKSI 531
Cdd:PRK12608 315 RVFPAIDIAKSGTRREELLLDSKELEKVRRLRRALASRKPVEAMEALLEKLRETPDNAEFLNSV 378
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
271-519 |
7.56e-166 |
|
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: 469.76 E-value: 7.56e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 271 EIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLLIDERPEEVTDMKESIEGDVIYSTFDQV 350
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKGEVVASTFDEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 351 SSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPGALHGPKKFFGAARNIRQGGSLTI 430
Cdd:cd01128 81 PERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 431 LGTALVETGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKTALWRLRREMSNNSVMEI 510
Cdd:cd01128 161 IATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIEA 240
|
....*....
gi 489533121 511 TDKVIELIK 519
Cdd:cd01128 241 MEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
173-243 |
1.87e-37 |
|
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: 132.50 E-value: 1.87e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489533121 173 GVLEILPDGFGFLRGSNYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQKINDENPD 243
Cdd:pfam07497 2 GILEILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGEDPE 72
|
|
| Rho_CSD |
cd04459 |
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination ... |
173-236 |
3.21e-26 |
|
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: 101.55 E-value: 3.21e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489533121 173 GVLEILPDGFGFLRGS--NYLSTEGDVYVSPSQIRRFNMKTGDKIKGITRHPKSGEKFRALLYVQK 236
Cdd:cd04459 3 GVLEILPDGFGFLRSSgyNYLPGPDDIYVSPSQIRRFNLRTGDTVVGQIRPPKEGERYFALLKVEA 68
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
275-478 |
4.85e-26 |
|
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: 105.52 E-value: 4.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHpnveLIVLLIDERPEEVTDMKESIEGD-------VIYSTF 347
Cdd:pfam00006 3 RAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADV----VVYALIGERGREVREFIEELLGSgalkrtvVVVATS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 348 DQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYnltisptgRTLSGGID--PG---------ALHGpkKFF 416
Cdd:pfam00006 79 DEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEAL--------REISLALGepPGregyppsvfSLLA--RLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489533121 417 -GAARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKS 478
Cdd:pfam00006 149 eRAGRVKGKGGSITALPTVLVP-GDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLAS 210
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
275-481 |
1.63e-24 |
|
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: 102.64 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLksvaNSIAKNhPNVELIVL-LIDERPEEVtdmKESIEGD----------VI 343
Cdd:cd01136 56 RAIDGLLTCGEGQRIGIFAGSGVGKSTLL----GMIARN-TDADVNVIaLIGERGREV---REFIEKDlgeeglkrsvLV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 344 YSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAY---NLTI--SPTgrtlSGGIDPGALHGPKKFFGA 418
Cdd:cd01136 128 VATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQrevGLAAgePPT----RRGYPPSVFALLPRLLER 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489533121 419 ARNIRQgGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTR 481
Cdd:cd01136 204 AGNGEK-GSITAFYTVLVE-GDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
245-481 |
1.37e-23 |
|
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: 100.22 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 245 AIQRNAFETLTPIFPEERLtletnrnEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVeLIVLLI 324
Cdd:cd19476 33 PIHLKAPNPIERLPPEEPL-------QTGIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGV-VVFAGI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 325 DERPEEVTD-MKESIEGD------VIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYnltisptg 397
Cdd:cd19476 105 GERGREVNDlYEEFTKSGamertvVVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEAL-------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 398 RTLSGGID--PGALHGPKKFFG--------AARNIRQGGSLTILGTALVETGSRMD---DVIFEEFKGTgnmeLHLDRKL 464
Cdd:cd19476 177 REMSALLGepPGREGYPPYLFTklatlyerAGKVKDGGGSITAIPAVSTPGDDLTDpipDNTFAILDGQ----IVLSREL 252
|
250
....*....|....*..
gi 489533121 465 AEKRIFPAIDIYKSGTR 481
Cdd:cd19476 253 ARKGIYPAINVLDSTSR 269
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
250-509 |
6.16e-20 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 92.52 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 250 AFETLTPIF-----PEERLTLETnrnEIAT--RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAknhPNVELIVL 322
Cdd:PRK09099 123 DCDELVPVIaappdPMSRRMVEA---PLPTgvRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQ---CDVNVIAL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 323 lIDERPEEVTDMKESIEGD-------VIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAynltisp 395
Cdd:PRK09099 197 -IGERGREVREFIELILGEdgmarsvVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARA------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 396 tGRT--LSGGiDPGALHG--PKKFFGAARNI-RQG----GSLTILGTALVE--TGSrmdDVIFEEFKGTGNMELHLDRKL 464
Cdd:PRK09099 269 -QREigLAAG-EPPARRGfpPSVFAELPRLLeRAGmgetGSITALYTVLAEdeSGS---DPIAEEVRGILDGHMILSREI 343
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489533121 465 AEKRIFPAIDIYKSGTRRDDLLLDDEEKTALWRLRREMSNNSVME 509
Cdd:PRK09099 344 AARNQYPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVE 388
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
275-516 |
5.39e-19 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 89.43 E-value: 5.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANsiaknHPNVELIVL-LIDERPEEVtdmKESIEGD----------VI 343
Cdd:PRK06936 151 RVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIR-----SAEVDVTVLaLIGERGREV---REFIESDlgeeglrkavLV 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 344 YSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNlTISptgrtLSGGIDPGALHGPKKFFGAARNI- 422
Cdd:PRK06936 223 VATSDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQR-EIG-----LAAGEPPTRRGYPPSVFAALPRLm 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 423 -RQG----GSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKTALWR 497
Cdd:PRK06936 297 eRAGqsdkGSITALYTVLVE-GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGR 375
|
250
....*....|....*....
gi 489533121 498 LRREMSNNSVMEITDKVIE 516
Cdd:PRK06936 376 LRELLAKYEEVELLLQIGE 394
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
271-503 |
1.59e-18 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 87.86 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 271 EIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLksvaNSIAKNhPNVEL-IVLLIDERPEEVtdmKESIEGD-------- 341
Cdd:PRK07721 143 EVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLM----GMIARN-TSADLnVIALIGERGREV---REFIERDlgpeglkr 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 342 --VIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLA---RAYNLTIS--PTGRtlsgGIDPGALHG-PK 413
Cdd:PRK07721 215 siVVVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAmaqREIGLAVGepPTTK----GYTPSVFAIlPK 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 414 KFFGAARNirQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKT 493
Cdd:PRK07721 291 LLERTGTN--ASGSITAFYTVLVD-GDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKE 367
|
250
....*....|
gi 489533121 494 ALWRLRREMS 503
Cdd:PRK07721 368 AANRFRELLS 377
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
275-503 |
2.35e-18 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 87.32 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSiaknhPNVELIVL-LIDERPEEVTDMKESIEGD-------VIYST 346
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNA-----PDADSNVLvLIGERGREVREFIDFTLSEetrkrcvIVVAT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 347 FDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLSGGIDPgalhgPKKFFGAARNI-RQG 425
Cdd:PRK07594 219 SDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYP-----PGVFSALPRLLeRTG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 426 ----GSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKTALWRLRRE 501
Cdd:PRK07594 294 mgekGSITAFYTVLVE-GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRC 372
|
..
gi 489533121 502 MS 503
Cdd:PRK07594 373 LA 374
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
275-519 |
1.14e-16 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 82.17 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANsiaknHPNVELIVL-LIDERPEEVtdmKESIEGD----------VI 343
Cdd:PRK06820 152 RAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCA-----DSAADVMVLaLIGERGREV---REFLEQVltpearartvVV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 344 YSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNlTISptgrtLSGGIDPGALHGPKKFFGAARNI- 422
Cdd:PRK06820 224 VATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAR-EIG-----LAAGEPPAAGSFPPSVFANLPRLl 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 423 -RQG----GSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKTALWR 497
Cdd:PRK06820 298 eRTGnsdrGSITAFYTVLVE-GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQK 376
|
250 260
....*....|....*....|..
gi 489533121 498 LRREMSNNSVMEITDKVIELIK 519
Cdd:PRK06820 377 LRRMLACYQEIELLVRVGEYQA 398
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
275-503 |
1.34e-16 |
|
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: 82.00 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQR-GlIVAPPKAGKTVLLksvaNSIAKNhPNVELIVL-LIDERPEEVtdmKESIEGD----------V 342
Cdd:COG1157 146 RAIDGLLTVGRGQRiG-IFAGSGVGKSTLL----GMIARN-TEADVNVIaLIGERGREV---REFIEDDlgeeglarsvV 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 343 IYSTFDQVSSHHVKVAEMvlnrAQRLVEH----GKDVVILLDSITRLARAynltisptGR--TLSGGiDPGALHG-PKKF 415
Cdd:COG1157 217 VVATSDEPPLMRLRAAYT----ATAIAEYfrdqGKNVLLLMDSLTRFAMA--------QReiGLAAG-EPPATRGyPPSV 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 416 F----------GAArnirQGGSLTILGTALVEtGSRMDDVIFEEFKGT--GnmelH--LDRKLAEKRIFPAIDIYKSGTR 481
Cdd:COG1157 284 FallprlleraGNG----GKGSITAFYTVLVE-GDDMNDPIADAVRGIldG----HivLSRKLAERGHYPAIDVLASISR 354
|
250 260
....*....|....*....|..
gi 489533121 482 RDDLLLDDEEKTALWRLRREMS 503
Cdd:COG1157 355 VMPDIVSPEHRALARRLRRLLA 376
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
168-481 |
1.80e-15 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 78.50 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 168 EDEVVGVLEILpdgfGFLRGSNYLSTEGD-------VYVSPSQiRRFNMKTGDKIKGITRHPKSG--EKFRAllyvqkin 238
Cdd:PRK08149 39 SNEVIARAQVV----GFQRERTILSLIGNaqglsrqVVLKPTG-KPLSVWVGEALLGAVLDPTGKivERFDA-------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 239 DENPDTAIQRNAFETLTPIFpEERLTLETnrnEIATRI--IDLISPIGKGQRGLIVAPPKAGKTVLLksvanSIAKNHPN 316
Cdd:PRK08149 106 PPTVGPISEERVIDVAPPSY-AERRPIRE---PLITGVraIDGLLTCGVGQRMGIFASAGCGKTSLM-----NMLIEHSE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 317 VELIVL-LIDERPEEVTDMKESIEGD-------VIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARA 388
Cdd:PRK08149 177 ADVFVIgLIGERGREVTEFVESLRASsrrekcvLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 389 YnltisptgR--TLSGGIDPGALHGPKKFFGAARNI--RQG----GSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHL 460
Cdd:PRK08149 257 L--------RdvALAAGELPARRGYPASVFDSLPRLleRPGatlaGSITAFYTVLLE-SEEEPDPIGDEIRSILDGHIYL 327
|
330 340
....*....|....*....|.
gi 489533121 461 DRKLAEKRIFPAIDIYKSGTR 481
Cdd:PRK08149 328 SRKLAAKGHYPAIDVLKSVSR 348
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
242-490 |
7.49e-14 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 73.66 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 242 PDTAiQRNAFETlTPIFPEERlTLETNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANsiaknHPNVELIV 321
Cdd:PRK07960 134 PDTG-ETGALIT-PPFNPLQR-TPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR-----YTQADVIV 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 322 L-LIDERPEEVTDMKESIEGD-------VIYSTFD-------QVSSHHVKVAEMVLNRaqrlvehGKDVVILLDSITRLA 386
Cdd:PRK07960 206 VgLIGERGREVKDFIENILGAegrarsvVIAAPADvspllrmQGAAYATRIAEDFRDR-------GQHVLLIMDSLTRYA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 387 RAYnltisptgRTLSGGI-DPGALHG-PKKFFG--------AARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNM 456
Cdd:PRK07960 279 MAQ--------REIALAIgEPPATKGyPPSVFAklpalverAGNGISGGGSITAFYTVLTE-GDDQQDPIADSARAILDG 349
|
250 260 270
....*....|....*....|....*....|....
gi 489533121 457 ELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDE 490
Cdd:PRK07960 350 HIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQ 383
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
254-502 |
8.36e-14 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 73.39 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 254 LTPIFPEERLTLETNRnEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANsiaknHPNVELIVL-LIDERPEEVT 332
Cdd:PRK07196 124 LPQIHPLQRRAVDTPL-DVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITR-----YTQADVVVVgLIGERGREVK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 333 DMKESIEGD-------VIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTisptgrTLSGGID 405
Cdd:PRK07196 198 EFIEHSLQAagmaksvVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREI------ALSLGEP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 406 PGALHGPKKFFG-------AARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKS 478
Cdd:PRK07196 272 PATKGYPPSAFSiiprlaeSAGNSSGNGTMTAIYTVLAE-GDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQS 350
|
250 260
....*....|....*....|....
gi 489533121 479 GTRRDDLLLDDEEkTALWRLRREM 502
Cdd:PRK07196 351 ISRCMSQVIGSQQ-AKAASLLKQC 373
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
271-481 |
1.40e-12 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 69.76 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 271 EIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLksvanSIAKNHPNVELIVL-LIDERPEEVTDMKESIEGD-------V 342
Cdd:PRK05688 153 DVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLL-----GMMTRFTEADIIVVgLIGERGREVKEFIEHILGEeglkrsvV 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 343 IYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYnltisptgRTLSGGI-DPGALHG-PKKFFG--- 417
Cdd:PRK05688 228 VASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQ--------REIALAIgEPPATKGyPPSVFAklp 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489533121 418 -----AARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTR 481
Cdd:PRK05688 300 klverAGNAEPGGGSITAFYTVLSE-GDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISR 367
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
275-519 |
4.95e-12 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 68.08 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAknhpnVELIVL-LIDERPEEVtdmKESIEGD----------VI 343
Cdd:PRK08927 147 RALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD-----ADVSVIgLIGERGREV---QEFLQDDlgpeglarsvVV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 344 YSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNlTISptgrtLSGGiDPGALHG---------PKK 414
Cdd:PRK08927 219 VATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQR-EIG-----LSAG-EPPTTKGytptvfaelPRL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 415 FFGAARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKTA 494
Cdd:PRK08927 292 LERAGPGPIGEGTITGLFTVLVD-GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDPEENPL 370
|
250 260
....*....|....*....|....*
gi 489533121 495 LWRLRREMSNNSVMEitdkviELIK 519
Cdd:PRK08927 371 VRRARQLMATYADME------ELIR 389
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
275-499 |
1.10e-10 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 63.86 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSIAKNhpnvELIVLLIDERPEEVTDMKESIEGD------VIYSTFD 348
Cdd:PRK06002 154 RVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFD----TVVIALVGERGREVREFLEDTLADnlkkavAVVATSD 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 349 QvSSHHVKVAEmvlNRAQRLVEH----GKDVVILLDSITRLARAynltisptGR--TLSGGIDPGALHGPKKFFG----- 417
Cdd:PRK06002 230 E-SPMMRRLAP---LTATAIAEYfrdrGENVLLIVDSVTRFAHA--------ARevALAAGEPPVARGYPPSVFSelprl 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 418 ---AARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFPAIDIYKSGTRRDDLLLDDEEKTA 494
Cdd:PRK06002 298 lerAGPGAEGGGSITGIFSVLVD-GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHAWTPEQRKL 376
|
....*
gi 489533121 495 LWRLR 499
Cdd:PRK06002 377 VSRLK 381
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
237-502 |
1.48e-10 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 63.46 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 237 INDENPDTAIQRNAFETlTPIFPEERLTLeTNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSiAKNHPN 316
Cdd:PRK06793 109 LNEEAENIPLQKIKLDA-PPIHAFEREEI-TDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKN-AKADIN 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 317 VeliVLLIDERPEEVTD----------MKESIegdVIYSTFDQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLA 386
Cdd:PRK06793 186 V---ISLVGERGREVKDfirkelgeegMRKSV---VVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 387 RAYNlTISPTGRTLSGGIDPGALHGPKKFFGAARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAE 466
Cdd:PRK06793 260 DARR-SVDIAVKELPIGGKTLLMESYMKKLLERSGKTQKGSITGIYTVLVD-GDDLNGPVPDLARGILDGHIVLKRELAT 337
|
250 260 270
....*....|....*....|....*....|....*.
gi 489533121 467 KRIFPAIDIYKSGTRrddlLLDDEEKTALWRLRREM 502
Cdd:PRK06793 338 LSHYPAISVLDSVSR----IMEEIVSPNHWQLANEM 369
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
173-231 |
1.94e-09 |
|
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: 53.76 E-value: 1.94e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489533121 173 GVLEILPDGFGFLRGSNYLStegDVYVSPSQI--RRFNMKTGDKIKGITRHPKSGEKFRAL 231
Cdd:smart00357 2 GVVKWFNKGFGFIRPDDGGK---DVFVHPSQIqgGLKSLREGDEVEFKVVSPEGGEKPEAE 59
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
255-500 |
4.15e-08 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 55.46 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 255 TPIFPEERLTLEtNRNEIATRIIDLISPIGKGQRGLIVAPPKAGKTVLLksvaNSIAKNHPNVELIVLLIDERPEEVTDM 334
Cdd:PRK08472 127 APIAAMKRGLID-EVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLM----GMIVKGCLAPIKVVALIGERGREIPEF 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 335 KE-----SIEGDVI-------------YSTFDQVSshhvkVAEMVLNRaqrlvehGKDVVILLDSITRLA---RAYNLTI 393
Cdd:PRK08472 202 IEknlggDLENTVIvvatsddsplmrkYGAFCAMS-----VAEYFKNQ-------GLDVLFIMDSVTRFAmaqREIGLAL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 394 S--PTgrtlSGGIDPGALHGPKKFFGAARNIRQGGSLTILGTALVEtGSRMDDVIFEEFKGTGNMELHLDRKLAEKRIFP 471
Cdd:PRK08472 270 GepPT----SKGYPPSVLSLLPQLMERAGKEEGKGSITAFFTVLVE-GDDMSDPIADQSRSILDGHIVLSRELTDFGIYP 344
|
250 260
....*....|....*....|....*....
gi 489533121 472 AIDIYKSGTRRDDLLLDDEEKTALWRLRR 500
Cdd:PRK08472 345 PINILNSASRVMNDIISPEHKLAARKFKR 373
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
16-56 |
1.60e-07 |
|
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: 47.76 E-value: 1.60e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489533121 16 LGSKTLVELREIAKELKIKSITTYKKNELI-EIINSKSKNEE 56
Cdd:pfam07498 2 LKEKTLSELREIAKELGIENYSRLRKQELIfAILKAQAEKGG 43
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
16-56 |
2.37e-07 |
|
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: 46.98 E-value: 2.37e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 489533121 16 LGSKTLVELREIAKELKIKSITTYKKNELI-EIINSKSKNEE 56
Cdd:smart00959 2 LKKKTLSELLEIAKELGIENASRLRKQELIfAILKAQAKKGG 43
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
275-401 |
6.31e-07 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 51.83 E-value: 6.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 275 RIIDLISPIGKGQRGLIVAPPKAGKTVLLKSVANSiAKNHPNVeliVLLIDERPEEVTDM----KESIEGD---VIYSTF 347
Cdd:PRK05922 146 KAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKG-SKSTINV---IALIGERGREVREYieqhKEGLAAQrtiIIASPA 221
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 489533121 348 DQVSSHHVKVAEMVLNRAQRLVEHGKDVVILLDSITRLARAYNLTISPTGRTLS 401
Cdd:PRK05922 222 HETAPTKVIAGRAAMTIAEYFRDQGHRVLFIMDSLSRWIAALQEVALARGETLS 275
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
256-398 |
3.94e-05 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 46.06 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 256 PIFPEERLTLETNRNEIATR------------IIDLISPIGKGQRGLIVAPPKAGKTVLlkSVANSIAKNHPNVELIVLL 323
Cdd:PRK13343 120 PLQATARRPLERPAPAIIERdfvteplqtgikVVDALIPIGRGQRELIIGDRQTGKTAI--AIDAIINQKDSDVICVYVA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 324 IDERPEEVTDMKESIE--GDVIYSTfdqvsshhVKVAE---------------MVLnrAQRLVEHGKDVVILLDSITRLA 386
Cdd:PRK13343 198 IGQKASAVARVIETLRehGALEYTT--------VVVAEasdppglqylapfagCAI--AEYFRDQGQDALIVYDDLSKHA 267
|
170
....*....|....*.
gi 489533121 387 RAYN----LTISPTGR 398
Cdd:PRK13343 268 AAYRelslLLRRPPGR 283
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
285-388 |
4.44e-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: 43.90 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 285 KGQRGLIVAPPKAGKTVLLKSVANSIAKNHPNVELIVLliderpeEVTDMKESIEGDVIYSTFDQVSSHHVKVAEMVLNR 364
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG-------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL 73
|
90 100
....*....|....*....|....
gi 489533121 365 AQRLvehgKDVVILLDSITRLARA 388
Cdd:smart00382 74 ARKL----KPDVLILDEITSLLDA 93
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
18-91 |
1.75e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.15 E-value: 1.75e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489533121 18 SKTLVELREIAKELKI--KSITTYKKNELIEIINSKSKNEEKVNEETKEKNEDIKEdIKNRKENIEREsiEKEVEY 91
Cdd:PRK05771 56 SEALDKLRSYLPKLNPlrEEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISE-LENEIKELEQE--IERLEP 128
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
235-300 |
2.09e-03 |
|
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: 40.23 E-value: 2.09e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489533121 235 QKINDENPDTAIQRNAFETLTP-IFPEERLT--LETnrneiATRIIDLISPIGKGQRGLIVAPPKAGKT 300
Cdd:cd01132 20 NPIDGKGPIQTKERRRVESKAPgIIPRQSVNepLQT-----GIKAIDSLIPIGRGQRELIIGDRQTGKT 83
|
|
| COG5124 |
COG5124 |
Protein predicted to be involved in meiotic recombination [Cell division and chromosome ... |
11-144 |
2.98e-03 |
|
Protein predicted to be involved in meiotic recombination [Cell division and chromosome partitioning / General function prediction only];
Pssm-ID: 227453 [Multi-domain] Cd Length: 209 Bit Score: 39.17 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 11 KVLEGLGSK---TLVELREIAKELKIKSITTYKKNELIEII----NSKSKNEEKVNEETKEKNEDIKEDIKNRKENIERE 83
Cdd:COG5124 29 KEVEKLGSKkqiVLMTVKDLLQQLVDDGVVSVEKCGTSNIYwsfkSQTLQKLYDSSELLKKKIQEVKQDIATYKEEIDKE 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489533121 84 SIEKEVEYKSPTKSYNKKEIDTQNISQNQEHRNQRNDYNKTTSVNDSNKSSNISNRMVRNN 144
Cdd:COG5124 109 KATRRKKFTEGQKNYNREALLEKRKKEQDEIKKKLNSLQKIEPIRWDAAKIQEKKKKVHLN 169
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
277-398 |
9.45e-03 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 38.80 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489533121 277 IDLISPIGKGQRGLIVAPPKAGKT-VLLKSVANSIAKnhpNVELIVLLIDERPEEVTDMKESI-EGDVIYST-------- 346
Cdd:PRK07165 134 IDLLIPIGKGQRELIIGDRQTGKThIALNTIINQKNT---NVKCIYVAIGQKRENLSRIYETLkEHDALKNTiiidapst 210
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 489533121 347 --FDQVSSHHVKVAEmvlnrAQRLvEHGKDVVILLDSITRLARAYN----LTISPTGR 398
Cdd:PRK07165 211 spYEQYLAPYVAMAH-----AENI-SYNDDVLIVFDDLTKHANIYReialLTNKPVGK 262
|
|
| VacB |
COG0557 |
Exoribonuclease R [Transcription]; |
166-216 |
9.70e-03 |
|
Exoribonuclease R [Transcription];
Pssm-ID: 440323 [Multi-domain] Cd Length: 711 Bit Score: 38.55 E-value: 9.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489533121 166 SKEDEVVGVLEILPDGFGFLRGSNylsTEGDVYVSPSQIRR-FNmktGDKIK 216
Cdd:COG0557 65 EKLDLVEGRVRGHRDGFGFVIPDD---GEEDIFIPPRELNGaLH---GDRVL 110
|
|
| |
