|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
55-427 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 721.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 55 MEKDGNYYMEGILDdIQPDGYGFLRTVNYSKGEKDIYISASQIRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHN 134
Cdd:COG1158 1 AEDDGLIPVEGVLE-ILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 135 AEEVKKRPHFQALTPLYPDERIKLETETQNYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFI 214
Cdd:COG1158 80 PEEARKRPDFDNLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 215 LLVGERPEEVTDLERSVEAaEVVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTL 294
Cdd:COG1158 160 LLIDERPEEVTDMQRSVKG-EVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 295 SGGLDPASLHKPKAFFGAARNIEAGGSLTILATALVDTGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSST 374
Cdd:COG1158 239 SGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSGT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 616687310 375 RKEELLISKSELDTLWQLRNLFT--DSTDFTERFIRKLKKSKNNEDFFKQLQKSA 427
Cdd:COG1158 319 RREELLLSPEELEKVWILRRALSgmDPVEAMEFLLDRLKKTKSNAEFLESMNKTT 373
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
18-425 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 719.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 18 YKNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDGNYYMEGILDdIQPDGYGFLRT--VNYSKGEKDIYISAS 95
Cdd:PRK09376 6 LKNKSLSELLELAEELGIENASRLRKQELIFAILKAQAEKGGDIFGEGVLE-ILPDGFGFLRSpdANYLPGPDDIYVSPS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 96 QIRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHNAEEVKKRPHFQALTPLYPDERIKLETET-QNYSTRIMDLVT 174
Cdd:PRK09376 85 QIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPLFENLTPLYPNERLRLETGNpEDLSTRIIDLIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 175 PIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVGERPEEVTDLERSVEAaEVVHSTFDEPPEHHVKVAEL 254
Cdd:PRK09376 165 PIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDERPEEVTDMQRSVKG-EVVASTFDEPAERHVQVAEM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 255 LLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPASLHKPKAFFGAARNIEAGGSLTILATALVDTGS 334
Cdd:PRK09376 244 VIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 335 RMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNLFT--DSTDFTERFIRKLKK 412
Cdd:PRK09376 324 RMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEELLLSPEELQKVWILRKILSpmDEVEAMEFLLDKLKK 403
|
410
....*....|...
gi 616687310 413 SKNNEDFFKQLQK 425
Cdd:PRK09376 404 TKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
19-425 |
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: 628.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 19 KNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDGNYYMEGILDdIQPDGYGFLRT--VNYSKGEKDIYISASQ 96
Cdd:TIGR00767 7 KNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHAEQGGLIFGEGVLE-ILPDGFGFLRSpdSSYLPGPDDIYVSPSQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 97 IRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHNAEEVKKRPHFQALTPLYPDERIKLETETQNYSTRIMDLVTPI 176
Cdd:TIGR00767 86 IRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVLFENLTPLYPNERLRLETSTEDLSTRVLDLFAPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 177 GLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVGERPEEVTDLERSVeAAEVVHSTFDEPPEHHVKVAELLL 256
Cdd:TIGR00767 166 GKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERPEEVTDMQRSV-KGEVVASTFDEPASRHVQVAEMVI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 257 ERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPASLHKPKAFFGAARNIEAGGSLTILATALVDTGSRM 336
Cdd:TIGR00767 245 EKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 337 DDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNLFT--DSTDFTERFIRKLKKSK 414
Cdd:TIGR00767 325 DEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRKIISpmDSIEAMEFLISKLKKTK 404
|
410
....*....|.
gi 616687310 415 NNEDFFKQLQK 425
Cdd:TIGR00767 405 TNEEFLESMKR 415
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
164-411 |
1.27e-162 |
|
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: 457.82 E-value: 1.27e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 164 NYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVGERPEEVTDLERSVEAaEVVHSTFDE 243
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKG-EVVASTFDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 244 PPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPASLHKPKAFFGAARNIEAGGSLT 323
Cdd:cd01128 80 PPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 324 ILATALVDTGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNLFTDSTDF- 402
Cdd:cd01128 160 IIATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIe 239
|
250
....*....|
gi 616687310 403 -TERFIRKLK 411
Cdd:cd01128 240 aMEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
64-136 |
9.36e-35 |
|
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: 123.64 E-value: 9.36e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616687310 64 EGILDdIQPDGYGFLRTVNYSKGEKDIYISASQIRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHNAE 136
Cdd:pfam07497 1 EGILE-ILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGEDPE 72
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
64-127 |
4.71e-11 |
|
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: 57.99 E-value: 4.71e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616687310 64 EGILDdIQPDGYGFLRTVNyskGEKDIYISASQI--RRFEIKRGDKVTGKVRKPKDNEKYYGLLQV 127
Cdd:smart00357 1 TGVVK-WFNKGFGFIRPDD---GGKDVFVHPSQIqgGLKSLREGDEVEFKVVSPEGGEKPEAENVV 62
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
18-59 |
3.39e-09 |
|
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: 52.00 E-value: 3.39e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 616687310 18 YKNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDG 59
Cdd:pfam07498 2 LKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQAEKGG 43
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
19-59 |
7.09e-09 |
|
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: 51.22 E-value: 7.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 616687310 19 KNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDG 59
Cdd:smart00959 3 KKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKKGG 43
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Rho |
COG1158 |
Transcription termination factor Rho [Transcription]; |
55-427 |
0e+00 |
|
Transcription termination factor Rho [Transcription];
Pssm-ID: 440772 [Multi-domain] Cd Length: 373 Bit Score: 721.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 55 MEKDGNYYMEGILDdIQPDGYGFLRTVNYSKGEKDIYISASQIRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHN 134
Cdd:COG1158 1 AEDDGLIPVEGVLE-ILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDAVTGQVRPPKEGEKYFALLRVESVNGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 135 AEEVKKRPHFQALTPLYPDERIKLETETQNYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFI 214
Cdd:COG1158 80 PEEARKRPDFDNLTPLYPDERLRLETTPDDLSTRVIDLVAPIGKGQRGLIVAPPKAGKTTLLQDIANAITANHPEVHLIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 215 LLVGERPEEVTDLERSVEAaEVVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTL 294
Cdd:COG1158 160 LLIDERPEEVTDMQRSVKG-EVIASTFDEPAERHVQVAELVIERAKRLVELGKDVVILLDSITRLARAYNLVVPASGRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 295 SGGLDPASLHKPKAFFGAARNIEAGGSLTILATALVDTGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSST 374
Cdd:COG1158 239 SGGVDANALYKPKRFFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINKSGT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 616687310 375 RKEELLISKSELDTLWQLRNLFT--DSTDFTERFIRKLKKSKNNEDFFKQLQKSA 427
Cdd:COG1158 319 RREELLLSPEELEKVWILRRALSgmDPVEAMEFLLDRLKKTKSNAEFLESMNKTT 373
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
18-425 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 719.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 18 YKNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDGNYYMEGILDdIQPDGYGFLRT--VNYSKGEKDIYISAS 95
Cdd:PRK09376 6 LKNKSLSELLELAEELGIENASRLRKQELIFAILKAQAEKGGDIFGEGVLE-ILPDGFGFLRSpdANYLPGPDDIYVSPS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 96 QIRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHNAEEVKKRPHFQALTPLYPDERIKLETET-QNYSTRIMDLVT 174
Cdd:PRK09376 85 QIRRFNLRTGDTVEGKIRPPKEGERYFALLKVETVNGEDPEKARNRPLFENLTPLYPNERLRLETGNpEDLSTRIIDLIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 175 PIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVGERPEEVTDLERSVEAaEVVHSTFDEPPEHHVKVAEL 254
Cdd:PRK09376 165 PIGKGQRGLIVAPPKAGKTVLLQNIANSITTNHPEVHLIVLLIDERPEEVTDMQRSVKG-EVVASTFDEPAERHVQVAEM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 255 LLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPASLHKPKAFFGAARNIEAGGSLTILATALVDTGS 334
Cdd:PRK09376 244 VIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 335 RMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNLFT--DSTDFTERFIRKLKK 412
Cdd:PRK09376 324 RMDEVIFEEFKGTGNMELHLDRKLAEKRIFPAIDINRSGTRKEELLLSPEELQKVWILRKILSpmDEVEAMEFLLDKLKK 403
|
410
....*....|...
gi 616687310 413 SKNNEDFFKQLQK 425
Cdd:PRK09376 404 TKTNEEFFDSMNR 416
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
19-425 |
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: 628.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 19 KNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDGNYYMEGILDdIQPDGYGFLRT--VNYSKGEKDIYISASQ 96
Cdd:TIGR00767 7 KNMPLEELRKLAEQLGVENTSSLKKQELIFAILKAHAEQGGLIFGEGVLE-ILPDGFGFLRSpdSSYLPGPDDIYVSPSQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 97 IRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHNAEEVKKRPHFQALTPLYPDERIKLETETQNYSTRIMDLVTPI 176
Cdd:TIGR00767 86 IRRFNLRTGDTIEGQIRSPKEGERYFALLKVESVNGDDPEKAKNRVLFENLTPLYPNERLRLETSTEDLSTRVLDLFAPI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 177 GLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVGERPEEVTDLERSVeAAEVVHSTFDEPPEHHVKVAELLL 256
Cdd:TIGR00767 166 GKGQRGLIVAPPKAGKTVLLQKIAQAITRNHPEVELIVLLIDERPEEVTDMQRSV-KGEVVASTFDEPASRHVQVAEMVI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 257 ERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPASLHKPKAFFGAARNIEAGGSLTILATALVDTGSRM 336
Cdd:TIGR00767 245 EKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSGGVDANALHRPKRFFGAARNIEEGGSLTIIATALIDTGSRM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 337 DDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNLFT--DSTDFTERFIRKLKKSK 414
Cdd:TIGR00767 325 DEVIFEEFKGTGNMELHLDRKLADRRIFPAIDIKKSGTRKEELLLTPEELQKIWVLRKIISpmDSIEAMEFLISKLKKTK 404
|
410
....*....|.
gi 616687310 415 NNEDFFKQLQK 425
Cdd:TIGR00767 405 TNEEFLESMKR 415
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
65-427 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 588.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 65 GILDDIqpDGYGFLRTVNYSKGEKDIYISASQIRRFEIKRGDKVTGKVRKPKDNE------KYYGLLQVDFVNDHNAEEV 138
Cdd:PRK12678 298 GILDVL--DNYAFVRTSGYLPGPNDVYVSMNQVRKNGLRKGDAVTGAVRAPREGEqgnqrqKFNPLVRLDSVNGMSPEEA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 139 KKRPHFQALTPLYPDERIKLETETQNYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVG 218
Cdd:PRK12678 376 KKRPEFGKLTPLYPNERLRLETEPKKLTTRVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIANAITTNNPECHLMVVLVD 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 219 ERPEEVTDLERSVEAaEVVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGL 298
Cdd:PRK12678 456 ERPEEVTDMQRSVKG-EVIASTFDRPPSDHTTVAELAIERAKRLVELGKDVVVLLDSITRLGRAYNLAAPASGRILSGGV 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 299 DPASLHKPKAFFGAARNIEAGGSLTILATALVDTGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEE 378
Cdd:PRK12678 535 DSTALYPPKRFFGAARNIENGGSLTIIATALVETGSKMDEVIFEEFKGTGNMELKLDRKLADKRIFPAVDVNASGTRKEE 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 616687310 379 LLISKSELDTLWQLRNLFT--DSTDFTERFIRKLKKSKNNEDFFKQLQKSA 427
Cdd:PRK12678 615 LLLSPDELAIVHKLRRVLSglDSQQAIDLLISRLKKTKSNYEFLMQVSKTT 665
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
64-424 |
0e+00 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 512.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 64 EGILDdIQPDGYGFLRTV--NYSKGEKDIYISASQIRRFEIKRGDKVTGKVRKpkdNEKYYGLLQVDFVNDHNAEEVKKR 141
Cdd:PRK12608 20 LGVLE-ILGDGFGFLRSArrNYLPSPDDVFVPPALIRRFNLRTGDVVEGVARP---RERYRVLVRVDSVNGTDPEKLARR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 142 PHFQALTPLYPDERIKLETETQNYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVGERP 221
Cdd:PRK12608 96 PHFDDLTPLHPRERLRLETGSDDLSMRVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLLIDERP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 222 EEVTDLERSVEAaEVVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPA 301
Cdd:PRK12608 176 EEVTDMRRSVKG-EVYASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLSGGVDAR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 302 SLHKPKAFFGAARNIEAGGSLTILATALVDTGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLI 381
Cdd:PRK12608 255 ALQRPKRLFGAARNIEEGGSLTIIATALVDTGSRMDEVIFEEFKGTGNMEIVLDRELADKRVFPAIDIAKSGTRREELLL 334
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 616687310 382 SKSELDTLWQLRNLFT--DSTDFTERFIRKLKKSKNNEDFFKQLQ 424
Cdd:PRK12608 335 DSKELEKVRRLRRALAsrKPVEAMEALLEKLRETPDNAEFLNSVQ 379
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
164-411 |
1.27e-162 |
|
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: 457.82 E-value: 1.27e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 164 NYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFILLVGERPEEVTDLERSVEAaEVVHSTFDE 243
Cdd:cd01128 1 ELSTRVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLLIDERPEEVTDMRRSVKG-EVVASTFDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 244 PPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPASLHKPKAFFGAARNIEAGGSLT 323
Cdd:cd01128 80 PPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSGGVDANALHKPKRFFGAARNIEEGGSLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 324 ILATALVDTGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNLFTDSTDF- 402
Cdd:cd01128 160 IIATALVDTGSRMDEVIFEEFKGTGNMELVLDRKLAEKRIFPAIDILKSGTRKEELLLTPEELQKIWLLRRILSPMDPIe 239
|
250
....*....|
gi 616687310 403 -TERFIRKLK 411
Cdd:cd01128 240 aMEFLLKKLK 249
|
|
| Rho_RNA_bind |
pfam07497 |
Rho termination factor, RNA-binding domain; The Rho termination factor disengages newly ... |
64-136 |
9.36e-35 |
|
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: 123.64 E-value: 9.36e-35
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616687310 64 EGILDdIQPDGYGFLRTVNYSKGEKDIYISASQIRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVDFVNDHNAE 136
Cdd:pfam07497 1 EGILE-ILPDGYGFLRSSNYLPGPDDIYVSPSQIRRFGLRTGDIVEGQVRPPKEGEKYFALLRVESVNGEDPE 72
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
168-372 |
1.40e-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: 106.29 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLlkeiANAISTNKPDAKLFILLVGERPEEVTD----------LERSVeaaeVV 237
Cdd:pfam00006 3 RAIDGLLPIGRGQRIGIFGGSGVGKTVL----AGMIARQASADVVVYALIGERGREVREfieellgsgaLKRTV----VV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 238 HSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVI-----PPSGRTLSGGLdpASLHkPKAFFGA 312
Cdd:pfam00006 75 VATSDEPPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISlalgePPGREGYPPSV--FSLL-ARLLERA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 313 ARNIEAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRS 372
Cdd:pfam00006 152 GRVKGKGGSITALPTVLVP-GDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLAS 210
|
|
| Rho_CSD |
cd04459 |
Rho_CSD: Rho protein cold-shock domain (CSD). Rho protein is a transcription termination ... |
63-128 |
2.48e-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: 100.78 E-value: 2.48e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616687310 63 MEGILDdIQPDGYGFLRTV--NYSKGEKDIYISASQIRRFEIKRGDKVTGKVRKPKDNEKYYGLLQVD 128
Cdd:cd04459 1 GSGVLE-ILPDGFGFLRSSgyNYLPGPDDIYVSPSQIRRFNLRTGDTVVGQIRPPKEGERYFALLKVE 67
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
168-375 |
5.49e-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: 100.33 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAistnkPDAKLFIL-LVGERPEEVTD----------LERSVeaaeV 236
Cdd:cd01136 56 RAIDGLLTCGEGQRIGIFAGSGVGKSTLLGMIARN-----TDADVNVIaLIGERGREVREfiekdlgeegLKRSV----L 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 237 VHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTL-SGGLDPASLHKPKAFFGAARN 315
Cdd:cd01136 127 VVATSDESPLLRVRAAYTATAIAEYFRDQGKKVLLLMDSLTRFAMAQREVGLAAGEPPtRRGYPPSVFALLPRLLERAGN 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 316 IEAgGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:cd01136 207 GEK-GSITAFYTVLVE-GDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
140-375 |
2.57e-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: 95.99 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 140 KRPHFQALTPlypdERIKLETetqnySTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTNKPDAKLFIlLVGE 219
Cdd:cd19476 37 KAPNPIERLP----PEEPLQT-----GIKVIDLLAPYGRGQKIGIFGGSGVGKTVLAMQLARNQAKAHAGVVVFA-GIGE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 220 RPEEVTDL----------ERSVeaaeVVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYN----- 284
Cdd:cd19476 107 RGREVNDLyeeftksgamERTV----VVANTANDPPGARMRVPYTGLTIAEYFRDNGQHVLLIIDDISRYAEALRemsal 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 285 LVIPPSGRTLSGGLdpASLHkPKAFFGAARNIEAGGSLTILATALVDTGSRMD---DMIYEEFKGTgnmeLHLDRKLSER 361
Cdd:cd19476 183 LGEPPGREGYPPYL--FTKL-ATLYERAGKVKDGGGSITAIPAVSTPGDDLTDpipDNTFAILDGQ----IVLSRELARK 255
|
250
....*....|....
gi 616687310 362 RIFPAIDIGRSSTR 375
Cdd:cd19476 256 GIYPAINVLDSTSR 269
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
168-395 |
3.20e-18 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 86.41 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAistnkPDAKLFIL-LVGERPEEVTDLERSVEAAE------VVHST 240
Cdd:PRK06820 152 RAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCAD-----SAADVMVLaLIGERGREVREFLEQVLTPEarartvVVVAT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 241 FDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVippsgrTLSGGLDPASLHKPKAFFG-AARNIE-- 317
Cdd:PRK06820 227 SDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYARAAREI------GLAAGEPPAAGSFPPSVFAnLPRLLErt 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 318 ---AGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRN 394
Cdd:PRK06820 301 gnsDRGSITAFYTVLVE-GDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRR 379
|
.
gi 616687310 395 L 395
Cdd:PRK06820 380 M 380
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
168-408 |
3.62e-18 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 86.16 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAistnkPDAKLFIL-LVGERPEEVTDL------ERSVEAAEVVHST 240
Cdd:PRK07594 144 RAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNA-----PDADSNVLvLIGERGREVREFidftlsEETRKRCVIVVAT 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 241 FDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPaslhkPKAFFGAARNIE-AG 319
Cdd:PRK07594 219 SDRPALERVRALFVATTIAEFFRDNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYP-----PGVFSALPRLLErTG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 320 ----GSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNL 395
Cdd:PRK07594 294 mgekGSITAFYTVLVE-GDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRC 372
|
250
....*....|...
gi 616687310 396 FTDSTDfTERFIR 408
Cdd:PRK07594 373 LALYQE-VELLIR 384
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
168-372 |
2.35e-17 |
|
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: 83.54 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQR-GlIVAPPKAGKTSLLKEIA-NAistnkpDAKLFIL-LVGERPEEVTD----------LERSVeaa 234
Cdd:COG1157 146 RAIDGLLTVGRGQRiG-IFAGSGVGKSTLLGMIArNT------EADVNVIaLIGERGREVREfieddlgeegLARSV--- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 235 eVVHSTFDEPPehhvkvaellLERAK------RLVEI----GEDVIILMDSITRLARAynlvippsGR--TLSGGLDPAS 302
Cdd:COG1157 216 -VVVATSDEPP----------LMRLRaaytatAIAEYfrdqGKNVLLLMDSLTRFAMA--------QReiGLAAGEPPAT 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 303 LHKPKAFFGA-ARNIE-AG----GSLTILATALVDtGSRMDDMIYEEFKGT--GnmelH--LDRKLSERRIFPAIDIGRS 372
Cdd:COG1157 277 RGYPPSVFALlPRLLErAGnggkGSITAFYTVLVE-GDDMNDPIADAVRGIldG----HivLSRKLAERGHYPAIDVLAS 351
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
142-375 |
6.41e-17 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 82.25 E-value: 6.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 142 PHFQALTPLYPDERIKLETETQNYSTRIMDLVTpIGLGQRGLIVAPPKAGKTSLLKEIanaisTNKPDAKLFIL-LVGER 220
Cdd:PRK07196 119 PLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLT-IGKGQRVGLMAGSGVGKSVLLGMI-----TRYTQADVVVVgLIGER 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 221 PEEVTD-LERSVEAAEVVHSTF-----DEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVippsgrTL 294
Cdd:PRK07196 193 GREVKEfIEHSLQAAGMAKSVVvaapaDESPLMRIKATELCHAIATYYRDKGHDVLLLVDSLTRYAMAQREI------AL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 295 SGGLDPASLHKPKAFFG-------AARNIEAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAI 367
Cdd:PRK07196 267 SLGEPPATKGYPPSAFSiiprlaeSAGNSSGNGTMTAIYTVLAE-GDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAI 345
|
....*...
gi 616687310 368 DIGRSSTR 375
Cdd:PRK07196 346 DISQSISR 353
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
149-430 |
1.09e-16 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 81.56 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 149 PLYPDERIKLeTETQNYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIA-NAistnKPDAKLfILLVGERPEEVTDL 227
Cdd:PRK06793 127 PIHAFEREEI-TDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAkNA----KADINV-ISLVGERGREVKDF 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 228 ------ERSVEAAEVVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLV------IPPSGRTLs 295
Cdd:PRK06793 201 irkelgEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMMDSVTRFADARRSVdiavkeLPIGGKTL- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 296 ggLDPASLHKPKAFFGAARNieagGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:PRK06793 280 --LMESYMKKLLERSGKTQK----GSITGIYTVLVD-GDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSR 352
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 616687310 376 KEELLISKSEldtlWQLRNLftdstdfterfIRK-LKKSKNNEDFFK--QLQKSAEES 430
Cdd:PRK06793 353 IMEEIVSPNH----WQLANE-----------MRKiLSIYKENELYFKlgTIQENAENA 395
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
168-398 |
1.11e-16 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 81.69 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANaistnKPDAKL-FILLVGERPEEVTD----------LERSVeaaeV 236
Cdd:PRK07721 147 RAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIAR-----NTSADLnVIALIGERGREVREfierdlgpegLKRSI----V 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 237 VHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLA---RAYNLVI--PPSGRtlsgGLDP---ASLhkPKA 308
Cdd:PRK07721 218 VVATSDQPALMRIKGAYTATAIAEYFRDQGLNVMLMMDSVTRVAmaqREIGLAVgePPTTK----GYTPsvfAIL--PKL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 309 FFGAARNieAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDT 388
Cdd:PRK07721 292 LERTGTN--ASGSITAFYTVLVD-GDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSPEHKEA 368
|
250
....*....|
gi 616687310 389 LWQLRNLFTD 398
Cdd:PRK07721 369 ANRFRELLST 378
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
168-375 |
2.00e-16 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 80.81 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAistnkpDA--KLFILLVGERPEEVTD---------LERSVeaaeV 236
Cdd:PRK06002 154 RVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARA------DAfdTVVIALVGERGREVREfledtladnLKKAV----A 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 237 VHSTFDE-------PPEHHVKVAELLLERakrlveiGEDVIILMDSITRLARAYNLVI-----PPSGRTLsggldPASLH 304
Cdd:PRK06002 224 VVATSDEspmmrrlAPLTATAIAEYFRDR-------GENVLLIVDSVTRFAHAAREVAlaagePPVARGY-----PPSVF 291
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 616687310 305 K--PKAFFGAARNIEAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:PRK06002 292 SelPRLLERAGPGAEGGGSITGIFSVLVD-GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISR 363
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
168-395 |
1.54e-15 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 78.26 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIanaisTNKPDAKLFIL-LVGERPEEV-----TDL-ERSVEAAEVVHST 240
Cdd:PRK06936 151 RVIDGLLTCGEGQRMGIFAAAGGGKSTLLASL-----IRSAEVDVTVLaLIGERGREVrefieSDLgEEGLRKAVLVVAT 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 241 FDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVippsgrTLSGGLDPASLHKPKAFFGA-ARNIE-A 318
Cdd:PRK06936 226 SDRPSMERAKAGFVATSIAEYFRDQGKRVLLLMDSVTRFARAQREI------GLAAGEPPTRRGYPPSVFAAlPRLMErA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 319 G----GSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRN 394
Cdd:PRK06936 300 GqsdkGSITALYTVLVE-GDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRE 378
|
.
gi 616687310 395 L 395
Cdd:PRK06936 379 L 379
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
168-375 |
4.52e-15 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 76.94 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTnkpDAKLfILLVGERPEEVTD----------LERSVeaaeVV 237
Cdd:PRK08927 147 RALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADA---DVSV-IGLIGERGREVQEflqddlgpegLARSV----VV 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 238 HSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVippsgrTLSGGLDPASL-HKPKAFFGAARNI 316
Cdd:PRK08927 219 VATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFAMAQREI------GLSAGEPPTTKgYTPTVFAELPRLL 292
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616687310 317 E-AG------GSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:PRK08927 293 ErAGpgpigeGTITGLFTVLVD-GDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSR 357
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
168-395 |
5.93e-15 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 76.35 E-value: 5.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAISTnkpDAKLfILLVGERPEEVTD----------LERSVeaaeVV 237
Cdd:PRK09099 152 RIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQC---DVNV-IALIGERGREVREfielilgedgMARSV----VV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 238 HSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAynlvippsGRT--LSGGLDPASLHKPKAFFGA-AR 314
Cdd:PRK09099 224 CATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMMDSLTRFARA--------QREigLAAGEPPARRGFPPSVFAElPR 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 315 NIE-----AGGSLTILATALV--DTGSrmdDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELD 387
Cdd:PRK09099 296 LLEragmgETGSITALYTVLAedESGS---DPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQ 372
|
....*...
gi 616687310 388 TLWQLRNL 395
Cdd:PRK09099 373 AAGRLRQL 380
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
168-375 |
2.79e-13 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 71.18 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIanaisTNKPDAKLF-ILLVGERPEEVTD----LERSVEAAEV--VHST 240
Cdd:PRK08149 140 RAIDGLLTCGVGQRMGIFASAGCGKTSLMNML-----IEHSEADVFvIGLIGERGREVTEfvesLRASSRREKCvlVYAT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 241 FDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYNLVippsgrTLSGGLDPASLHKPKAFF---------- 310
Cdd:PRK08149 215 SDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSMTRYARALRDV------ALAAGELPARRGYPASVFdslprllerp 288
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616687310 311 GAARNieagGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:PRK08149 289 GATLA----GSITAFYTVLLE-SEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSR 348
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
169-375 |
9.75e-13 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 69.76 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 169 IMDLVTpIGLGQRGLIVAPPKAGKTSLLkeianAISTNKPDAKLFIL-LVGERPEEVTD----------LERSVeaaeVV 237
Cdd:PRK05688 159 INGLLT-VGRGQRLGLFAGTGVGKSVLL-----GMMTRFTEADIIVVgLIGERGREVKEfiehilgeegLKRSV----VV 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 238 HSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARAYN---LVI--PPSGRtlsgGLDPASLHK-PKAFFG 311
Cdd:PRK05688 229 ASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDSLTRFAQAQReiaLAIgePPATK----GYPPSVFAKlPKLVER 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616687310 312 AARNIEAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:PRK05688 305 AGNAEPGGGSITAFYTVLSE-GDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISR 367
|
|
| CSP |
smart00357 |
Cold shock protein domain; RNA-binding domain that functions as a RNA-chaperone in bacteria ... |
64-127 |
4.71e-11 |
|
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: 57.99 E-value: 4.71e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 616687310 64 EGILDdIQPDGYGFLRTVNyskGEKDIYISASQI--RRFEIKRGDKVTGKVRKPKDNEKYYGLLQV 127
Cdd:smart00357 1 TGVVK-WFNKGFGFIRPDD---GGKDVFVHPSQIqgGLKSLREGDEVEFKVVSPEGGEKPEAENVV 62
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
148-397 |
7.32e-11 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 63.65 E-value: 7.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 148 TPLYPDERIKLeTETQNYSTRIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIANaisTNKPDAkLFILLVGERPEEVTDL 227
Cdd:PRK07960 145 PPFNPLQRTPI-EHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMAR---YTQADV-IVVGLIGERGREVKDF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 228 ERSVEAAE------VVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLA---RAYNLVI--PPSGRtlsg 296
Cdd:PRK07960 220 IENILGAEgrarsvVIAAPADVSPLLRMQGAAYATRIAEDFRDRGQHVLLIMDSLTRYAmaqREIALAIgePPATK---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 297 GLDPASLHKPKAFFGAARN-IEAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:PRK07960 296 GYPPSVFAKLPALVERAGNgISGGGSITAFYTVLTE-GDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISR 374
|
250 260
....*....|....*....|..
gi 616687310 376 KEELLISKSELDTLWQLRNLFT 397
Cdd:PRK07960 375 AMTALIDEQHYARVRQFKQLLS 396
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
177-397 |
3.71e-10 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 61.63 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 177 GLGQRGLIVAPPKAGKTSLLKEIanaISTNKPDAKLfILLVGERPEEVT---------DLERSVeaaeVVHSTFDEPPEH 247
Cdd:PRK08472 155 GKGQKLGIFAGSGVGKSTLMGMI---VKGCLAPIKV-VALIGERGREIPefieknlggDLENTV----IVVATSDDSPLM 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 248 H-------VKVAELLLERakrlveiGEDVIILMDSITRLA---RAYNLVI--PPSgrtlSGGLDPASLHKPKAFFGAARN 315
Cdd:PRK08472 227 RkygafcaMSVAEYFKNQ-------GLDVLFIMDSVTRFAmaqREIGLALgePPT----SKGYPPSVLSLLPQLMERAGK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 316 IEAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNL 395
Cdd:PRK08472 296 EEGKGSITAFFTVLVE-GDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISPEHKLAARKFKRL 374
|
..
gi 616687310 396 FT 397
Cdd:PRK08472 375 YS 376
|
|
| Rho_N |
pfam07498 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
18-59 |
3.39e-09 |
|
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: 52.00 E-value: 3.39e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 616687310 18 YKNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDG 59
Cdd:pfam07498 2 LKEKTLSELREIAKELGIENYSRLRKQELIFAILKAQAEKGG 43
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
147-397 |
5.31e-09 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 57.79 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 147 LTPLYPDERIKLETETQNYSTR-------------IMDLVTpIGLGQRGLIVAPPKAGKTSLLkeianAISTNKPDAKLF 213
Cdd:PRK08972 118 LGPIYTDQRASRHSPPINPLSRrpitepldvgvraINAMLT-VGKGQRMGLFAGSGVGKSVLL-----GMMTRGTTADVI 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 214 IL-LVGERPEEVTDL----------ERSVeaaeVVHSTFDEPPEHHVKVAELLLERAKRLVEIGEDVIILMDSITRLARA 282
Cdd:PRK08972 192 VVgLVGERGREVKEFieeilgeegrARSV----VVAAPADTSPLMRLKGCETATTIAEYFRDQGLNVLLLMDSLTRYAQA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 283 YNLVippsgrTLSGGLDPASLHKPKAFFG--------AARNIEAGGSLTILATALVDtGSRMDDMIYEEFKGTGNMELHL 354
Cdd:PRK08972 268 QREI------ALAVGEPPATKGYPPSVFAklpalverAGNGGPGQGSITAFYTVLTE-GDDLQDPIADASRAILDGHIVL 340
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 616687310 355 DRKLSERRIFPAIDIGRSSTRKEELLISKSELDTLWQLRNLFT 397
Cdd:PRK08972 341 SRELADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYS 383
|
|
| Rho_N |
smart00959 |
Rho termination factor, N-terminal domain; The Rho termination factor disengages newly ... |
19-59 |
7.09e-09 |
|
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: 51.22 E-value: 7.09e-09
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 616687310 19 KNYTTKELTQKAKTLKLTNYSKLNKKELVLAIMEAQMEKDG 59
Cdd:smart00959 3 KKKTLSELLEIAKELGIENASRLRKQELIFAILKAQAKKGG 43
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
168-329 |
6.32e-08 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 54.52 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSLLKEIAnaiSTNKPDAKLfILLVGERPEEVTD-LERSVEAAEVVHSTFDEPPE 246
Cdd:PRK05922 146 KAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIA---KGSKSTINV-IALIGERGREVREyIEQHKEGLAAQRTIIIASPA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 247 HHVKVAELLLERAKRLV-----EIGEDVIILMDSITRLARAYNLVIPPSGRTLSGGLDPASL-HKPKAFFGAARNIEAgG 320
Cdd:PRK05922 222 HETAPTKVIAGRAAMTIaeyfrDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVfHHVSEFTERAGNNDK-G 300
|
....*....
gi 616687310 321 SLTILATAL 329
Cdd:PRK05922 301 SITALYAIL 309
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
167-375 |
3.23e-07 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 52.61 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 167 TRIMDLVTPIGLGQRGLIVAPPKAGKTSllkeIA-NAISTNK-PDAKLFILLVGERP---EEVTDLERSVEAAE----VV 237
Cdd:PRK13343 150 IKVVDALIPIGRGQRELIIGDRQTGKTA----IAiDAIINQKdSDVICVYVAIGQKAsavARVIETLREHGALEyttvVV 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 238 HSTFDEPPEHHV------KVAELLLERakrlveiGEDVIILMDSITRLARAYN----LVIPPSGRTLSGGlDPASLHkpk 307
Cdd:PRK13343 226 AEASDPPGLQYLapfagcAIAEYFRDQ-------GQDALIVYDDLSKHAAAYRelslLLRRPPGREAYPG-DIFYLH--- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 308 affgaARNIE---------AGGSLTILATALVDTG-----------SRMDDMIYeefkgtgnmelhLDRKLSERRIFPAI 367
Cdd:PRK13343 295 -----SRLLEraaklspelGGGSLTALPIIETLAGelsayiptnliSITDGQIY------------LDSDLFAAGQRPAV 357
|
....*...
gi 616687310 368 DIGRSSTR 375
Cdd:PRK13343 358 DVGLSVSR 365
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
179-282 |
3.30e-06 |
|
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: 46.60 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 179 GQRGLIVAPPKAGKTSLLKEIANAIstnKPDAKLFILLVGERPEEVTDLERsveaaEVVHSTFDEPPEHHVKVAELLLER 258
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAREL---GPPGGGVIYIDGEDILEEVLDQL-----LLIIVGGKKASGSGELRLRLALAL 73
|
90 100
....*....|....*....|....
gi 616687310 259 AKRLVeigeDVIILMDSITRLARA 282
Cdd:smart00382 74 ARKLK----PDVLILDEITSLLDA 93
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
171-375 |
2.61e-04 |
|
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: 42.55 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 171 DLVTPIGLGQRGLIVAPPKAGKTSLlkeianAIST--NKPDAKLFILLV--GERPEEVTDLERSVE---AAE---VVHST 240
Cdd:cd01132 61 DSLIPIGRGQRELIIGDRQTGKTAI------AIDTiiNQKGKKVYCIYVaiGQKRSTVAQIVKTLEehgAMEytiVVAAT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 241 FDEP-------PEHHVKVAELLLERakrlveiGEDVIILMDSITRLARAYN----LVIPPSGRTLSGGlDPASLHkPKAF 309
Cdd:cd01132 135 ASDPaplqylaPYAGCAMGEYFRDN-------GKHALIIYDDLSKQAVAYRqmslLLRRPPGREAYPG-DVFYLH-SRLL 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616687310 310 FGAAR--NIEAGGSLTIL---------ATALVDTG--SRMDDMIYeefkgtgnmelhLDRKLSERRIFPAIDIGRSSTR 375
Cdd:cd01132 206 ERAAKlsDELGGGSLTALpiietqagdVSAYIPTNviSITDGQIF------------LESELFNKGIRPAINVGLSVSR 272
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
170-325 |
3.50e-04 |
|
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: 42.76 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 170 MDLVTPIGLGQRGLIVAPPKAGKTSLlkeianAIST--NKPDAKLFILLV--GERPEEVTDLERSVEAAE------VVHS 239
Cdd:TIGR00962 152 IDAMIPIGRGQRELIIGDRQTGKTAV------AIDTiiNQKDSDVYCIYVaiGQKASTVAQVVRKLEEHGamaytiVVAA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 240 TFDEP-------PEHHVKVAELLLERakrlveiGEDVIILMDSITRLARAYN----LVIPPSGRTLSGGlDPASLHKpKA 308
Cdd:TIGR00962 226 TASDSaslqylaPYTGCTMGEYFRDN-------GKHALIIYDDLSKQAVAYRqislLLRRPPGREAFPG-DVFYLHS-RL 296
|
170
....*....|....*....
gi 616687310 309 FFGAARNIEA--GGSLTIL 325
Cdd:TIGR00962 297 LERAAKLNDEkgGGSLTAL 315
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
168-375 |
6.63e-04 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 41.95 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 168 RIMDLVTPIGLGQRGLIVAPPKAGKTSL-LKEIANAISTNK----PDAKLFILL-VGERPEEVTDLERSVEA------AE 235
Cdd:PTZ00185 178 KAVDTMIPIGRGQRELIVGDRQTGKTSIaVSTIINQVRINQqilsKNAVISIYVsIGQRCSNVARIHRLLRSygalryTT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 236 VVHSTFDEP-------PEHHVKVAELLLERakrlveiGEDVIILMDSITRLARAYN----LVIPPSGRTLSGGlDPASLH 304
Cdd:PTZ00185 258 VMAATAAEPaglqylaPYSGVTMGEYFMNR-------GRHCLCVYDDLSKQAVAYRqislLLRRPPGREAYPG-DVFYLH 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616687310 305 KpKAFFGAARNIEAGGSLTILATALVDTGSR-MDDMIYEEFKGTGNMELHLDRKLSERRIFPAIDIGRSSTR 375
Cdd:PTZ00185 330 S-RLLERAAMLSPGKGGGSVTALPIVETLSNdVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR 400
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
171-263 |
1.46e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 39.94 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 171 DLVTPIGLGQRGLIVAPPKAGKTSLLKEIANAIStNKPDAKLFILLVGERPEEVTDLER------SVEAAEVVHS----- 239
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK-GTPVAGCVDVPDNQFGREASLIDAigrkgdFKDAVELLNAvglsd 126
|
90 100 110
....*....|....*....|....*....|...
gi 616687310 240 --TFDEPPEH-------HVKVAELLLERAKRLV 263
Cdd:COG2401 127 avLWLRRFKElstgqkfRFRLALLLAERPKLLV 159
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
176-279 |
4.63e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 38.73 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687310 176 IGLGQRGLIVAPPKAGKTSLLKEIANAISTNKP------DAKLFILLVGERPEEvtDLERSVEAAEVVHSTFDEPPEHHV 249
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFLALQLAAAVAAGGPwlgrrvPPGKVLYLAAEDDRG--ELRRRLKALGADLGLPFADLDGRL 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 616687310 250 KVAEL--------LLER-AKRLVEIGEDVIILmDSITRL 279
Cdd:COG3598 88 RLLSLagdlddtdDLEAlERAIEEEGPDLVVI-DPLARV 125
|
|
| |
